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Human Metabolome Database Version 2.5

 

Showing metabocard for Estradiol (HMDB00151)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-04-26 12:11:55
Accession Number HMDB00151
Secondary Accession Numbers HMDB04448; HMDB04481
Common Name Estradiol
Description Estradiol is the most potent form of mammalian estrogenic steroids. Estradiol is produced in the ovaries. The ovary requires both luteinizing hormone (LH) and follicle-stimulating hormone (FSH) to produce sex steroids. LH stimulates the cells surrounding the follicle to produce progesterone and androgens. The androgens diffuse across the basement membrane to the granulosa cell layer, where, under the action of FSH, they are aromatized to estrogens, mainly estradiol. The ovary shows cyclical activity, unlike the testis that is maintained in a more or less constant state of activity. Hormone secretions vary according to the phase of the menstrual cycle. In the developing follicle LH receptors (LH-R) are only located on the thecal cells and FSH receptors (FSHR) on the granulosa cells. The dominant pre-ovulatory follicle develops LH-Rs on the granulosa cells prior to the LH surge. Thecal cells of the preovulatory follicle also develop the capacity to synthesize estradiol and this persists when the thecal cells become incorporated into the corpus luteum. After ovulation, the empty follicle is remodelled and plays an important role in the second half or luteal phase of the menstrual cycle. This phase is dominated by progesterone and, to a lesser extent, estradiol secretion by the corpus luteum. estradiol is also synthesized locally from cholesterol through testosterone in the hippocampus and acts rapidly to modulate neuronal synaptic plasticity. Localization of estrogen receptor alpha (ERalpha) in spines in addition to nuclei of principal neurons implies that synaptic ERalpha is responsible for rapid modulation of synaptic plasticity by endogenous estradiol. estradiol is a potent endogenous antioxidant which suppresses hepatic fibrosis in animal models, and attenuates induction of redox sensitive transcription factors, hepatocyte apoptosis and hepatic stellate cells activation by inhibiting a generation of reactive oxygen species in primary cultures. This suggests that the greater progression of hepatic fibrosis and hepatocellular carcinoma in men and postmenopausal women may be due, at least in part, to lower production of estradiol and a reduced response to the action of estradiol. estradiol has been reported to induce the production of interferon (INF)-gamma in lymphocytes, and augments an antigen-specific primary antibody response in human peripheral blood mononuclear cells. IFN-gamma is a potent cytokine with immunomodulatory and antiproliferative properties. Therefore, female subjects, particularly before menopause, may produce antibodies against hepatitis B virus e antigen and hepatitis B virus surface antigen at a higher frequency than males with chronic hepatitis B virus infection. The estradiol-Dihydrotestosterone model of prostate cancer (PC) proposes that the first step in the development of most PC and breast cancer (BC) occurs when aromatase converts testosterone to estradiol. (PMID: 17708600, 17678531, 17644764)
Synonyms
  1. (+)-3,17b-Estradiol
  2. (17b)-Estra-1,3,5(10)-triene-3,17-diol
  3. 13b-Methyl-1,3,5(10)-gonatriene-3,17b-ol
  4. 17b-Estradiol
  5. 17b-Oestradiol
  6. 3,17-Epidihydroxyestratriene
  7. 3,17b-Dihydroxyestra-1,3,5(10)-triene
  8. 3,17b-Estradiol
  9. Aerodiol
  10. Agofollin
  11. Altrad
  12. Amnestrogen
  13. Aquadiol
  14. Bardiol
  15. Beta-estradiol
  16. Climaderm
  17. Climara
  18. Compudose
  19. Corpagen
  20. D-Estradiol
  21. D-Oestradiol
  22. Dermestril
  23. Dihydrofollicular hormone
  24. Dihydrofolliculin
  25. Dihydromenformon
  26. Dihydrotheelin
  27. Dihydroxyestrin
  28. Dimenformon
  29. Diogyn
  30. Diogynets
  31. Divigel
  32. Encore
  33. Epiestriol 50
  34. Estra-1,3,5(10)-triene-3,17b-diol
  35. Estrace
  36. Estradiol
  37. Estradot
  38. Estraldine
  39. Estring Vaginal Ring
  40. Estroclim
  41. Estroclim 50
  42. Estrogel
  43. Estrogel HBF
  44. Estrovite
  45. Evorel
  46. Femestral
  47. Femogen
  48. Follicyclin
  49. Gelestra
  50. Ginosedol
  51. Gynergon
  52. Gynoestryl
  53. Lamdiol
  54. Macrodiol
  55. Menorest
  56. Nordicol
  57. Oesclim
  58. Oestergon
  59. Oestra-1,3,5(10)-triene-3,17b-diol
  60. Oestradiol
  61. Oestrogel
  62. Oestroglandol
  63. Ovahormon
  64. Ovasterol
  65. Ovastevol
  66. Ovocyclin
  67. Ovocylin
  68. Perlatanol
  69. Primofol
  70. Profoliol
  71. Profoliol B
  72. Progynon
  73. Progynon DH
  74. Sandrena 1
  75. Syndiol
  76. Systen
  77. Vivelle
  78. Zumenon
  79. b-Estradiol
  80. dihydro-Theelin
  81. Estraderm TTS
  82. delta-Estradiol
  83. delta-Oestradiol;Estradiol-17-beta
Chemical IUPAC Name 13-methyl-6,7,8,9,11,12,14,15,16,17-decahydrocyclopenta[a]phenanthrene-3,17-diol
Chemical Formula C18H24O2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Cholesterols and derivatives
Class
  • Steroids and Steroid Derivatives
Sub Class
  • Ketosteroids
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • phenol or hydroxyhetarene
  • aromatic compound
Biofunction
  • Component of Androgen and estrogen metabolism
Application
Source
  • Endogenous
Average Molecular Weight 272.382
Monoisotopic Molecular Weight 272.177643
Isomeric SMILES C[C@]12CC[C@H]3[C@@H](CCC4=C3C=CC(O)=C4)[C@@H]1CC[C@@H]2O
Canonical SMILES CC12CCC3C(CCC4=C3C=CC(O)=C4)C1CCC2O
KEGG Compound ID C00951 Link Image
BioCyc ID CPD-352 Link Image
BiGG ID 36456 Link Image
Wikipedia Link Estradiol Link Image
NuGOwiki Link HMDB00151 Link Image
Metagene Link HMDB00151 Link Image
METLIN ID 263 Link Image
PubChem Compound 5757 Link Image
PubChem Substance 8028360 Link Image
ChEBI ID 16469 Link Image
CAS Registry Number 50-28-2
InChI Identifier InChI=1/C18H24O2/c1-18-9-8-14-13-5-3-12(19)10-11(13)2-4-15(14)16(18)6-7-17(18)20/h3,5,10,14-17,19-20H,2,4,6-9H2,1H3/t14-,15-,16+,17+,18+/m1/s1
Synthesis Reference Vasiljeva, L. L.; Demin, P. M.; Kochev, D. M.; Lapitskaya, M. A.; Pivnitskya, K. K. New synthesis of estradiol from androsta-1,4-diene-3,17-dione. Russian Chemical Bulletin (Translation of Izvestiya Akademii Nauk, Seriya Khimicheskaya) (1999), 48(3), 593-595.
Melting Point (Experimental) 178.5 oC
Experimental Water Solubility 0.0036 mg/mL [YALKOWSKY,SH & DANNENFELSER,RM (1992)] Source: PhysProp
Predicted Water Solubility 0.021300001 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity 4.01 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity 3.57 [Predicted by ALOGPS]; 4.2 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 1A27 Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Membrane (Predicted from LogP)
  • Cytoplasm
  • endoplasmic reticulum
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Saliva
  • Urine
Tissue Location
Tissue References
Adipose Tissue
Adrenal Cortex
Adrenal Gland
Brain
Epidermis
Fibroblasts
Gonads
Muscle
Neuron
Placenta
Platelet
Prostate
Spleen
Stratum Corneum
Testes
Uterus
Concentrations (Normal)
Biofluid Blood
Value 0.00009 (0.0-0.00018) 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 CSF
Value 0.0000007 - 0.000011 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Murakami K, Nakagawa T, Shozu M, Uchide K, Koike K, Inoue M: Changes with aging of steroidal levels in the cerebrospinal fluid of women. Maturitas. 1999 Sep 24;33(1):71-80. [PubMed Link Image]
Biofluid CSF
Value 0.0000011 +/- 0.0000003 uM
Age Adult:>18 yrs old
Sex Female
Patient information Postmenopause
Comments Not Available
References
  • Murakami K, Nakagawa T, Shozu M, Uchide K, Koike K, Inoue M: Changes with aging of steroidal levels in the cerebrospinal fluid of women. Maturitas. 1999 Sep 24;33(1):71-80. [PubMed Link Image]
Biofluid Saliva
Value <1.00 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Gibney MJ, Walsh M, Brennan L, Roche HM, German B, van Ommen B: Metabolomics in human nutrition: opportunities and challenges. Am J Clin Nutr. 2005 Sep;82(3):497-503. [PubMed Link Image]
Biofluid Urine
Value 0.0011 +/- 0.00061 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Bai SW, Jung BH, Chung BC, Kim SU, Kim JY, Rha KH, Cho JS, Park YW, Park KH: Relationship between urinary profile of the endogenous steroids and postmenopausal women with stress urinary incontinence. Neurourol Urodyn. 2003;22(3):198-205. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 0.00039 (0.000037-0.00073) uM
Age Adult:>18 yrs old
Sex Female
Condition Menstrual cycle
Comments Follicular phase
References
  • The Merck Manual, 17th ed. Mark H. Beers, MD, Robert Berkow, MD, eds. Whitehouse Station, NJ: Merck Research Labs, 1999.
Biofluid Blood
Value 0.00092 (0.00037-0.0015) uM
Age Adult:>18 yrs old
Sex Female
Condition Menstrual cycle
Comments Midcycle
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 (0.000055-0.00095) uM
Age Adult:>18 yrs old
Sex Female
Condition Menstrual cycle
Comments Luteal phase
References
  • The Merck Manual, 17th ed. Mark H. Beers, MD, Robert Berkow, MD, eds. Whitehouse Station, NJ: Merck Research Labs, 1999.
Biofluid Blood
Value 0.00009 (0.0-0.00018) 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 0.000095 +/- 0.000036 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 0.00011 +/- 0.00005 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 0.00015 +/- 0.000075 uM
Age Adult:>18 yrs old
Sex Female
Condition Abnormal
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 CSF
Value 0.000006 (0.0000007-0.000011) uM
Age Adult:>18 yrs old
Sex Female
Condition Benign gynecological diseases
Comments Not Available
References
  • Murakami K, Nakagawa T, Shozu M, Uchide K, Koike K, Inoue M: Changes with aging of steroidal levels in the cerebrospinal fluid of women. Maturitas. 1999 Sep 24;33(1):71-80. [PubMed Link Image]
Biofluid Urine
Value 0.00059 +/- 0.00025 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Condition Abnormal
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 0.0016 +/- 0.0011 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Comments Not Available
References
  • Bai SW, Jung BH, Chung BC, Kim SU, Kim JY, Rha KH, Cho JS, Park YW, Park KH: Relationship between urinary profile of the endogenous steroids and postmenopausal women with stress urinary incontinence. Neurourol Urodyn. 2003;22(3):198-205. [PubMed Link Image]
Associated Disorders
Condition References
Benign gynecological diseases
  • Murakami K, Nakagawa T, Shozu M, Uchide K, Koike K, Inoue M: Changes with aging of steroidal levels in the cerebrospinal fluid of women. Maturitas. 1999 Sep 24;33(1):71-80. [PubMed Link Image]
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
General References
  1. Schaap LA, Pluijm SM, Smit JH, van Schoor NM, Visser M, Gooren LJ, Lips P: The association of sex hormone levels with poor mobility, low muscle strength and incidence of falls among older men and women. Clin Endocrinol (Oxf). 2005 Aug;63(2):152-60. [PubMed Link Image]
  2. Evagelatou M, Webster AD, Farrant J: Effects of 17 beta-oestradiol on function of lymphocytes from normal donors and patients with common variable immunodeficiency (CVID). Clin Exp Immunol. 1994 Nov;98(2):203-9. [PubMed Link Image]
  3. Gibney MJ, Walsh M, Brennan L, Roche HM, German B, van Ommen B: Metabolomics in human nutrition: opportunities and challenges. Am J Clin Nutr. 2005 Sep;82(3):497-503. [PubMed Link Image]
  4. Carnevale V, Scillitani A, Vecci E, D'Erasmo E, Romagnoli E, Paglia F, Pepe J, Baldini V, Santori C, De Geronimo S, Minisola S: Dehydroepiandrosterone sulfate and bone resorption rates as reflected by serum levels of C-terminal telopeptide of type I collagen: a study in healthy men. J Endocrinol Invest. 2005 Feb;28(2):102-5. [PubMed Link Image]
  5. Jojua T, Sumbadze TS, Papava M: Secretion of sex hormones in patients with open angle glaucoma. Georgian Med News. 2005 Jul-Aug;(124-125):33-7. [PubMed Link Image]
  6. Hamden KE, Ford PW, Whitman AG, Dyson OF, Cheng SY, McCubrey JA, Akula SM: Raf-induced vascular endothelial growth factor augments Kaposi's sarcoma-associated herpesvirus infection. J Virol. 2004 Dec;78(23):13381-90. [PubMed Link Image]
  7. Lahdes-Vasama TT, Koskimaki JE, Streng TK, Fisch RD, Nilson EA, Santti RS, Tammela TL: Urodynamic findings in men operated on for an undescended testicle. BJU Int. 2003 Dec;92(9):972-6. [PubMed Link Image]
  8. Martina V, Benso A, Gigliardi VR, Masha A, Origlia C, Granata R, Ghigo E: Short-term dehydroepiandrosterone treatment increases platelet cGMP production in elderly male subjects. Clin Endocrinol (Oxf). 2006 Mar;64(3):260-4. [PubMed Link Image]
  9. Iranmanesh A, Veldhuis JD: Combined inhibition of types I and II 5 alpha-reductase selectively augments the basal (nonpulsatile) mode of testosterone secretion in young men. J Clin Endocrinol Metab. 2005 Jul;90(7):4232-7. Epub 2005 Apr 5. [PubMed Link Image]
  10. Stabile LP, Davis AL, Gubish CT, Hopkins TM, Luketich JD, Christie N, Finkelstein S, Siegfried JM: Human non-small cell lung tumors and cells derived from normal lung express both estrogen receptor alpha and beta and show biological responses to estrogen. Cancer Res. 2002 Apr 1;62(7):2141-50. [PubMed Link Image]
  11. Chabbert-Buffet N, Bouchard P: [Physiology and exploration of the gonadotropic axis] Rev Prat. 1999 Jun 15;49(12):1270-6. [PubMed Link Image]
  12. Schonknecht P, Henze M, Hunt A, Klinga K, Haberkorn U, Schroder J: Hippocampal glucose metabolism is associated with cerebrospinal fluid estrogen levels in postmenopausal women with Alzheimer's disease. Psychiatry Res. 2003 Oct 30;124(2):125-7. [PubMed Link Image]
  13. Elliott KJ, Cable NT, Reilly T: Does oral contraceptive use affect maximum force production in women? Br J Sports Med. 2005 Jan;39(1):15-9. [PubMed Link Image]
  14. Blomquist CH, D'Ascoli PT: Gestational development of human placental 17 beta-hydroxysteroid oxidoreductase types 1 and 2. Hum Reprod. 1995 Oct;10(10):2685-9. [PubMed Link Image]
  15. Fraser D, Padwick ML, Whitehead M, Coffer A, King RJ: Presence of an oestradiol receptor-related protein in the skin: changes during the normal menstrual cycle. Br J Obstet Gynaecol. 1991 Dec;98(12):1277-82. [PubMed Link Image]
  16. Greb RR, Grieshaber K, Gromoll J, Sonntag B, Nieschlag E, Kiesel L, Simoni M: A common single nucleotide polymorphism in exon 10 of the human follicle stimulating hormone receptor is a major determinant of length and hormonal dynamics of the menstrual cycle. J Clin Endocrinol Metab. 2005 Aug;90(8):4866-72. Epub 2005 May 10. [PubMed Link Image]
  17. Archer JS, Love-Geffen TE, Herbst-Damm KL, Swinney DA, Chang JR: Effect of estradiol versus estradiol and testosterone on brain-activation patterns in postmenopausal women. Menopause. 2006 May-Jun;13(3):528-37. [PubMed Link Image]
  18. Anwar A, McTernan PG, Anderson LA, Askaa J, Moody CG, Barnett AH, Eggo MC, Kumar S: Site-specific regulation of oestrogen receptor-alpha and -beta by oestradiol in human adipose tissue. Diabetes Obes Metab. 2001 Oct;3(5):338-49. [PubMed Link Image]
  19. Tanko LB, Christiansen C: Effects of 17beta-oestradiol plus different doses of drospirenone on adipose tissue, adiponectin and atherogenic metabolites in postmenopausal women. J Intern Med. 2005 Dec;258(6):544-53. [PubMed Link Image]
  20. Sulcova J, Hampl R, Hill M, Starka L, Novacek A: Delayed effects of short-term transdermal application of 7-oxo-dehydroepiandrosterone on its metabolites, some hormonal steroids and relevant proteohormones in healthy male volunteers. Clin Chem Lab Med. 2005;43(2):221-7. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Estradiol 17-beta-dehydrogenase 2
  2. UDP-glucuronosyltransferase 2B28 precursor
  3. Estrogen receptor beta
  4. Estradiol 17-beta-dehydrogenase 8
  5. UDP-glucuronosyltransferase 2B4 precursor
  6. UDP-glucuronosyltransferase 1-4 precursor
  7. UDP-glucuronosyltransferase 2B15 precursor
  8. UDP-glucuronosyltransferase 2A1 precursor
  9. UDP-glucuronosyltransferase 1-1 precursor
  10. UDP-glucuronosyltransferase 1-9 precursor
  11. UDP-glucuronosyltransferase 1-3 precursor
  12. UDP-glucuronosyltransferase 2B17 precursor
  13. UDP-glucuronosyltransferase 1-6 precursor
  14. UDP-glucuronosyltransferase 1-5 precursor
  15. UDP-glucuronosyltransferase 2B11 precursor
  16. Dehydrogenase/reductase SDR family member 8 precursor
  17. Estradiol 17-beta-dehydrogenase 1
  18. 3-keto-steroid reductase
  19. Cytochrome P450 3A4
  20. Cytochrome P450 2C9
  21. Cytochrome P450 2C19
  22. Cytochrome P450 2E1
  23. Cytochrome P450 1B1
  24. Cytochrome P450 2F1
  25. Cytochrome P450 2B6
  26. Cytochrome P450 2A13
  27. Cytochrome P450 4B1
  28. Cytochrome P450 4Z1
  29. Cytochrome P450 1A2
  30. Cytochrome P450 19A1
  31. Cytochrome P450 2C8
  32. Cytochrome P450 2S1
  33. Cytochrome P450 2J2
  34. Cytochrome P450 2A7
  35. Cytochrome P450 2A6
  36. Sex hormone-binding globulin precursor
  37. Orphan nuclear receptor PXR
  38. Estrogen receptor
  39. Oxidoreductase
  40. UDP-glucuronosyltransferase 2A3 precursor
  41. Cytochrome P450, family 1, subfamily A, polypeptide 1
  42. Estradiol 17-beta-dehydrogenase 12
  43. UDP glycosyltransferase 1 family polypeptide A10 (HCG2039726, isoform CRA_f)
  44. UDP glycosyltransferase 1 family polypeptide A8 (HCG2039726, isoform CRA_e)
  45. UDP glycosyltransferase 1 family polypeptide A7
  46. cDNA FLJ76966, highly similar to Homo sapiens UDP glucuronosyltransferase 2 family, polypeptide B10 (UGT2B10), mRNA (UDP glucuronosyltransferase 2 family, polypeptide B10, isoform CRA_b)
  47. Cytochrome P450, family 3, subfamily A, polypeptide 7
  48. Cytochrome P450, family 2, subfamily D, polypeptide 6 (Cytochrome P450 2D6)
  49. Cytochrome P450, family 3, subfamily A, polypeptide 5 (Cytochrome P450, family 3, subfamily A, polypeptide 5, isoform CRA_a)
  50. Cytochrome P450, family 4, subfamily X, polypeptide 1 (Cytochrome P450, family 4, subfamily X, polypeptide 1, isoform CRA_b) (Cytochrome P450)
  51. Putative uncharacterized protein CYP3A43 (Cytochrome P450, family 3, subfamily A, polypeptide 43, isoform CRA_e)
  52. cDNA FLJ77672
  53. cDNA, FLJ93689, highly similar to Homo sapiens UDP glucuronosyltransferase 2 family, polypeptide B7 (UGT2B7), mRNA
  54. 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)
  55. cDNA, FLJ93938, Homo sapiens cytochrome P450, family 2, subfamily C, polypeptide 18(CYP2C18), mRNA (HCG39167, isoform CRA_b)
  56. cDNA FLJ45935 fis, clone PLACE7003985, highly similar to Estradiol 17-beta-dehydrogenase 1 (Hydroxysteroid (17-beta) dehydrogenase 1)
  57. cDNA, FLJ93594, Homo sapiens hydroxysteroid (17-beta) dehydrogenase 2 (HSD17B2),mRNA (Hydroxysteroid (17-beta) dehydrogenase 2)
Enzyme 1 [top]
Enzyme 1 ID 5685
Enzyme 1 Name Estradiol 17-beta-dehydrogenase 2
Enzyme 1 Synonyms
  1. 17-beta-HSD 2
  2. Microsomal 17-beta-hydroxysteroid dehydrogenase
  3. 20 alpha- hydroxysteroid dehydrogenase
  4. 20-alpha-HSD
  5. E2DH
Enzyme 1 Gene Name HSD17B2
Enzyme 1 Protein Sequence >Estradiol 17-beta-dehydrogenase 2
MSTFFSDTAWICLAVPTVLCGTVFCKYKKSSGQLWSWMVCLAGLCAVCLLILSPFWGLIL
FSVSCFLMYTYLSGQELLPVDQKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPG
AEELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAMLQDRGLWAVINNAGVLGFPTDGELL
LMTDYKQCMAVNFFGTVEVTKTFLPLLRKSKGRLVNVSSMGGGAPMERLASYGSSKAAVT
MFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSDKWEKLEKDILDHLPAEVQEDYGQDYI
LAQRNFLLLINSLASKDFSPVLRDIQHAILAKSPFAYYTPGKGAYLWICLAHYLPIGIYD
YFAKRHFGQDKPMPRALRMPNYKKKAT
Enzyme 1 Number of Residues 387
Enzyme 1 Molecular Weight 42786
Enzyme 1 Theoretical pI 8.62
Enzyme 1 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
Enzyme 1 General Function Lipid transport and metabolism
Enzyme 1 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 1 Pathways
  • Androgen and Estrogen Metabolism (map00150 Link Image)
Enzyme 1 Reactions
  • estradiol-17beta + NAD(P)+ = estrone + NAD(P)H + H+
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-20
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 306462 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P37059 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name DHB2_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 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 1 GenBank Gene ID L11708 Link Image
Enzyme 1 GeneCard ID HSD17B2 Link Image
Enzyme 1 GenAtlas ID HSD17B2 Link Image
Enzyme 1 HGNC ID HGNC:5211 Link Image
Enzyme 1 Chromosome Location 16
Enzyme 1 Locus 16q24.1-q24.2
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 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]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5687
Enzyme 2 Name UDP-glucuronosyltransferase 2B28 precursor
Enzyme 2 Synonyms
  1. UDPGT
Enzyme 2 Gene Name UGT2B28
Enzyme 2 Protein Sequence >UDP-glucuronosyltransferase 2B28 precursor
MALKWTSVLLLIHLGCYFSSGSCGKVLVWTGEYSHWMNMKTILKELVQRGHEVTVLASSA
SILFDPNDAFTLKLEVYPTSLTKTEFENIIMQQVKRWSDIQKDSFWLYFSQEQEILWEFH
DIFRNFCKDVVSNKKVMKKLQESRFDIIFADAFFPCGELLAALLNIPFVYSLCFTPGYTI
ERHSGGLIFPPSYIPVVMSKLSDQMTFMERVKNMIYVLYFDFWFQMCDMKKWDQFYSEVL
GRPTTLFETMGKADIWLMRNSWSFQFPHPFLPNIDFVGGLHCKPAKPLPKEMEEFVQSSG
ENGVVVFSLGSVISNMTAERANVIATALAKIPQKVLWRFDGNKPDALGLNTRLYKWIPQN
DLLGLPKTRAFITHGGANGIYEAIYHGIPMVGIPLFWDQPDNIAHMKAKGAAVRLDFHTM
SSTDLLNALKTVINDPSYKENVMKLSIIQHDQPVKPLHRAVFWIEFVMCHKGAKHLRVAA
RDLTWFQYHSLDVIGFLLACVATVIFVVTKFCLFCFWKFARKGKKGKRD
Enzyme 2 Number of Residues 529
Enzyme 2 Molecular Weight 60907
Enzyme 2 Theoretical pI 8.80
Enzyme 2 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 2 General Function Carbohydrate transport and metabolism
Enzyme 2 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 2 Pathways
Enzyme 2 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-24
Enzyme 2 Transmembrane Regions
  • 495-517
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 13603476 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q9BY64 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name UDB28_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 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 2 GenBank Gene ID AF177272 Link Image
Enzyme 2 GeneCard ID UGT2B28 Link Image
Enzyme 2 GenAtlas ID UGT2B28 Link Image
Enzyme 2 HGNC ID HGNC:13479 Link Image
Enzyme 2 Chromosome Location 4
Enzyme 2 Locus 4q13.2
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 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]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5688
Enzyme 3 Name Estrogen receptor beta
Enzyme 3 Synonyms
  1. ER-beta
Enzyme 3 Gene Name ESR2
Enzyme 3 Protein Sequence >Estrogen receptor beta
MDIKNSPSSLNSPSSYNCSQSILPLEHGSIYIPSSYVDSHHEYPAMTFYSPAVMNYSIPS
NVTNLEGGPGRQTTSPNVLWPTPGHLSPLVVHRQLSHLYAEPQKSPWCEARSLEHTLPVN
RETLKRKVSGNRCASPVTGPGSKRDAHFCAVCSDYASGYHYGVWSCEGCKAFFKRSIQGH
NDYICPATNQCTIDKNRRKSCQACRLRKCYEVGMVKCGSRRERCGYRLVRRQRSADEQLH
CAGKAKRSGGHAPRVRELLLDALSPEQLVLTLLEAEPPHVLISRPSAPFTEASMMMSLTK
LADKELVHMISWAKKIPGFVELSLFDQVRLLESCWMEVLMMGLMWRSIDHPGKLIFAPDL
VLDRDEGKCVEGILEIFDMLLATTSRFRELKLQHKEYLCVKAMILLNSSMYPLVTATQDA
DSSRKLAHLLNAVTDALVWVIAKSGISSQQQSMRLANLLMLLSHVRHASNKGMEHLLNMK
CKNVVPVYDLLLEMLNAHVLRGCKSSITGSECSPAEDSKSKEGSQNPQSQ
Enzyme 3 Number of Residues 530
Enzyme 3 Molecular Weight 59217
Enzyme 3 Theoretical pI 8.55
Enzyme 3 GO Classification
Function
  • DNA binding
  • binding
  • cation binding
  • ion binding
  • ligand-dependent nuclear receptor activity
  • nucleic acid binding
  • receptor activity
  • signal transducer activity
  • steroid binding
  • steroid hormone receptor activity
  • transcription factor activity
  • transition metal ion binding
  • zinc ion binding
Process
  • regulation of biological process
  • regulation of cellular metabolism
  • regulation of metabolism
  • regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • regulation of physiological process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Nuclear hormone receptor. Binds estrogens with an affinity similar to that of ESR1, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner. Isoform beta-cx lacks ligand binding ability and has no or only very low ere binding activity resulting in the loss of ligand-dependent transactivation ability. DNA- binding by ESR1 and ESR2 is rapidly lost at 37 degrees Celsius in the absence of ligand while in the presence of 17 beta-estradiol and 4-hydroxy-tamoxifen loss in DNA-binding at elevated temperature is more gradual
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 2911152 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q92731 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name ESR2_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1593 bp
ATGGATATAAAAAACTCACCATCTAGCCTTAATTCTCCTTCCTCCTACAACTGCAGTCAA
TCCATCTTACCCCTGGAGCACGGCTCCATATACATACCTTCCTCCTATGTAGACAGCCAC
CATGAATATCCAGCCATGACATTCTATAGCCCTGCTGTGATGAATTACAGCATTCCCAGC
AATGTCACTAACTTGGAAGGTGGGCCTGGTCGGCAGACCACAAGCCCAAATGTGTTGTGG
CCAACACCTGGGCACCTTTCTCCTTTAGTGGTCCATCGCCAGTTATCACATCTGTATGCG
GAACCTCAAAAGAGTCCCTGGTGTGAAGCAAGATCGCTAGAACACACCTTACCTGTAAAC
AGAGAGACACTGAAAAGGAAGGTTAGTGGGAACCGTTGCGCCAGCCCTGTTACTGGTCCA
GGTTCAAAGAGGGATGCTCACTTCTGCGCTGTCTGCAGCGATTACGCATCGGGATATCAC
TATGGAGTCTGGTCGTGTGAAGGATGTAAGGCCTTTTTTAAAAGAAGCATTCAAGGACAT
AATGATTATATTTGTCCAGCTACAAATCAGTGTACAATCGATAAAAACCGGCGCAAGAGC
TGCCAGGCCTGCCGACTTCGGAAGTGTTACGAAGTGGGAATGGTGAAGTGTGGCTCCCGG
AGAGAGAGATGTGGGTACCGCCTTGTGCGGAGACAGAGAAGTGCCGACGAGCAGCTGCAC
TGTGCCGGCAAGGCCAAGAGAAGTGGCGGCCACGCGCCCCGAGTGCGGGAGCTGCTGCTG
GACGCCCTGAGCCCCGAGCAGCTAGTGCTCACCCTCCTGGAGGCTGAGCCGCCCCATGTG
CTGATCAGCCGCCCCAGTGCGCCCTTCACCGAGGCCTCCATGATGATGTCCCTGACCAAG
TTGGCCGACAAGGAGTTGGTACACATGATCAGCTGGGCCAAGAAGATTCCCGGCTTTGTG
GAGCTCAGCCTGTTCGACCAAGTGCGGCTCTTGGAGAGCTGTTGGATGGAGGTGTTAATG
ATGGGGCTGATGTGGCGCTCAATTGACCACCCCGGCAAGCTCATCTTTGCTCCAGATCTT
GTTCTGGACAGGGATGAGGGGAAATGCGTAGAAGGAATTCTGGAAATCTTTGACATGCTC
CTGGCAACTACTTCAAGGTTTCGAGAGTTAAAACTCCAACACAAAGAATATCTCTGTGTC
AAGGCCATGATCCTGCTCAATTCCAGTATGTACCCTCTGGTCACAGCGACCCAGGATGCT
GACAGCAGCCGGAAGCTGGCTCACTTGCTGAACGCCGTGACCGATGCTTTGGTTTGGGTG
ATTGCCAAGAGCGGCATCTCCTCCCAGCAGCAATCCATGCGCCTGGCTAACCTCCTGATG
CTCCTGTCCCACGTCAGGCATGCGAGTAACAAGGGCATGGAACATCTGCTCAACATGAAG
TGCAAAAATGTGGTCCCAGTGTATGACCTGCTGCTGGAGATGCTGAATGCCCACGTGCTT
CGCGGGTGCAAGTCCTCCATCACGGGGTCCGAGTGCAGCCCGGCAGAGGACAGTAAAAGC
AAAGAGGGCTCCCAGAACCCACAGTCTCAGTGA
Enzyme 3 GenBank Gene ID AB006590 Link Image
Enzyme 3 GeneCard ID ESR2 Link Image
Enzyme 3 GenAtlas ID ESR2 Link Image
Enzyme 3 HGNC ID HGNC:3468 Link Image
Enzyme 3 Chromosome Location 14
Enzyme 3 Locus 14q23.2
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Ogawa S, Inoue S, Watanabe T, Hiroi H, Orimo A, Hosoi T, Ouchi Y, Muramatsu M: The complete primary structure of human estrogen receptor beta (hER beta) and its heterodimerization with ER alpha in vivo and in vitro. Biochem Biophys Res Commun. 1998 Feb 4;243(1):122-6. [PubMed Link Image]
  2. Moore JT, McKee DD, Slentz-Kesler K, Moore LB, Jones SA, Horne EL, Su JL, Kliewer SA, Lehmann JM, Willson TM: Cloning and characterization of human estrogen receptor beta isoforms. Biochem Biophys Res Commun. 1998 Jun 9;247(1):75-8. [PubMed Link Image]
  3. Mosselman S, Polman J, Dijkema R: ER beta: identification and characterization of a novel human estrogen receptor. FEBS Lett. 1996 Aug 19;392(1):49-53. [PubMed Link Image]
  4. Ogawa S, Inoue S, Watanabe T, Orimo A, Hosoi T, Ouchi Y, Muramatsu M: Molecular cloning and characterization of human estrogen receptor betacx: a potential inhibitor ofestrogen action in human. Nucleic Acids Res. 1998 Aug 1;26(15):3505-12. [PubMed Link Image]
  5. Lu B, Leygue E, Dotzlaw H, Murphy LJ, Murphy LC, Watson PH: Estrogen receptor-beta mRNA variants in human and murine tissues. Mol Cell Endocrinol. 1998 Mar 16;138(1-2):199-203. [PubMed Link Image]
  6. Li LC, Yeh CC, Nojima D, Dahiya R: Cloning and characterization of human estrogen receptor beta promoter. Biochem Biophys Res Commun. 2000 Aug 28;275(2):682-9. [PubMed Link Image]
  7. Chen H, Lin RJ, Schiltz RL, Chakravarti D, Nash A, Nagy L, Privalsky ML, Nakatani Y, Evans RM: Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell. 1997 Aug 8;90(3):569-80. [PubMed Link Image]
  8. Pace P, Taylor J, Suntharalingam S, Coombes RC, Ali S: Human estrogen receptor beta binds DNA in a manner similar to and dimerizes with estrogen receptor alpha. J Biol Chem. 1997 Oct 10;272(41):25832-8. [PubMed Link Image]
  9. Caira F, Antonson P, Pelto-Huikko M, Treuter E, Gustafsson JA: Cloning and characterization of RAP250, a novel nuclear receptor coactivator. J Biol Chem. 2000 Feb 25;275(8):5308-17. [PubMed Link Image]
  10. 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]
  11. 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]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5691
Enzyme 4 Name Estradiol 17-beta-dehydrogenase 8
Enzyme 4 Synonyms
  1. 17-beta-HSD 8
  2. 17- beta-hydroxysteroid dehydrogenase 8
  3. Protein Ke6
  4. Ke-6
Enzyme 4 Gene Name HSD17B8
Enzyme 4 Protein Sequence >Estradiol 17-beta-dehydrogenase 8
MASQLQNRLRSALALVTGAGSGIGRAVSVRLAGEGATVAACDLDRAAAQETVRLLGGPGS
KEGPPRGNHAAFQADVSEARAARCLLEQVQACFSRPPSVVVSCAGITQDEFLLHMSEDDW
DKVIAVNLKGTFLVTQAAAQALVSNGCRGSIINISSIVGKVGNVGQTNYAASKAGVIGLT
QTAARELGRHGIRCNSVLPGFIATPMTQKVPQKVVDKITEMIPMGHLGDPEDVADVVAFL
ASEDSGYITGTSVEVTGGLFM
Enzyme 4 Number of Residues 261
Enzyme 4 Molecular Weight 26974
Enzyme 4 Theoretical pI 6.50
Enzyme 4 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
Enzyme 4 General Function Lipid transport and metabolism
Enzyme 4 Specific Function Uses estradiol as its preferred substrate
Enzyme 4 Pathways
  • Androgen and Estrogen Metabolism (map00150 Link Image)
Enzyme 4 Reactions
  • estradiol-17beta + NAD(P)+ = estrone + NAD(P)H + H+
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 30583317 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q92506 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name DHB8_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >786 bp
ATGGCGTCTCAGCTCCAGAACCGACTCCGCTCCGCACTGGCCTTGGTCACAGGTGCGGGG
AGCGGCATCGGCCGAGCGGTCAGTGTACGCCTGGCCGGAGAGGGGGCCACCGTAGCTGCC
TGCGACCTGGACCGGGCAGCGGCACAGGAGACGGTGCGGCTGCTGGGCGGGCCAGGGAGC
AAGGAGGGGCCGCCCCGAGGGAACCATGCTGCCTTCCAGGCTGACGTGTCTGAGGCCAGG
GCCGCCAGGTGCCTGCTGGAACAAGTGCAGGCCTGCTTTTCTCGCCCACCATCTGTCGTT
GTGTCCTGTGCGGGCATCACCCAGGATGAGTTTCTGCTGCACATGTCTGAGGATGACTGG
GACAAAGTCATAGCTGTCAACCTCAAGGGCACCTTCCTAGTCACTCAGGCTGCAGCACAA
GCCCTGGTGTCCAATGGTTGTCGTGGTTCCATCATCAACATCAGTAGCATCGTAGGAAAG
GTGGGGAACGTGGGGCAGACAAACTATGCAGCATCCAAGGCTGGAGTGATTGGGCTGACC
CAGACCGCAGCCCGGGAGCTTGGACGACATGGGATCCGCTGTAACTCTGTCCTCCCAGGG
TTCATTGCAACACCCATGACACAGAAAGTGCCACAGAAAGTGGTGGACAAGATTACTGAA
ATGATCCCGATGGGACACTTGGGGGACCCTGAGGATGTGGCAGATGTGGTCGCATTCTTG
GCATCTGAAGATAGTGGATACATCACAGGGACCTCAGTGGAAGTCACTGGAGGTCTTTTC
ATGTAG
Enzyme 4 GenBank Gene ID BT007239 Link Image
Enzyme 4 GeneCard ID HSD17B8 Link Image
Enzyme 4 GenAtlas ID HSD17B8 Link Image
Enzyme 4 HGNC ID HGNC:3554 Link Image
Enzyme 4 Chromosome Location 6
Enzyme 4 Locus 6p21.3
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 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. 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]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5696
Enzyme 5 Name UDP-glucuronosyltransferase 2B4 precursor
Enzyme 5 Synonyms
  1. UDPGT
  2. Hyodeoxycholic acid
  3. HLUG25
  4. UDPGTh-1
Enzyme 5 Gene Name UGT2B4
Enzyme 5 Protein Sequence >UDP-glucuronosyltransferase 2B4 precursor
MSMKWTSALLLIQLSCYFSSGSCGKVLVWPTEFSHWMNIKTILDELVQRGHEVTVLASSA
SISFDPNSPSTLKFEVYPVSLTKTEFEDIIKQLVKRWAELPKDTFWSYFSQVQEIMWTFN
DILRKFCKDIVSNKKLMKKLQESRFDVVLADAVFPFGELLAELLKIPFVYSLRFSPGYAI
EKHSGGLLFPPSYVPVVMSELSDQMTFIERVKNMIYVLYFEFWFQIFDMKKWDQFYSEVL
GRPTTLSETMAKADIWLIRNYWDFQFPHPLLPNVEFVGGLHCKPAKPLPKEMEEFVQSSG
ENGVVVFSLGSMVSNTSEERANVIASALAKIPQKVLWRFDGNKPDTLGLNTRLYKWIPQN
DLLGHPKTRAFITHGGANGIYEAIYHGIPMVGVPLFADQPDNIAHMKAKGAAVSLDFHTM
SSTDLLNALKTVINDPLYKENAMKLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAA
HDLTWFQYHSLDVTGFLLACVATVIFIITKCLFCVWKFVRTGKKGKRD
Enzyme 5 Number of Residues 528
Enzyme 5 Molecular Weight 60513
Enzyme 5 Theoretical pI 8.75
Enzyme 5 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 5 General Function Carbohydrate transport and metabolism
Enzyme 5 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 5 Pathways
Enzyme 5 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-23
Enzyme 5 Transmembrane Regions
  • 493-509
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 37589 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P06133 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name UDB4_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 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 5 GenBank Gene ID Y00317 Link Image
Enzyme 5 GeneCard ID UGT2B4 Link Image
Enzyme 5 GenAtlas ID UGT2B4 Link Image
Enzyme 5 HGNC ID HGNC:12553 Link Image
Enzyme 5 Chromosome Location 4
Enzyme 5 Locus 4q13
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 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]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5719
Enzyme 6 Name UDP-glucuronosyltransferase 1-4 precursor
Enzyme 6 Synonyms
  1. UDP- glucuronosyltransferase 1A4
  2. UDPGT
  3. UGT1*4
  4. UGT1-04
  5. UGT1.4
  6. UGT- 1D
  7. UGT1D
  8. Bilirubin-specific UDPGT isozyme 2
  9. HUG-BR2
Enzyme 6 Gene Name UGT1A4
Enzyme 6 Protein Sequence >UDP-glucuronosyltransferase 1-4 precursor
MARGLQVPLPRLATGLLLLLSVQPWAESGKVLVVPTDGSPWLSMREALRELHARGHQAVV
LTPEVNMHIKEEKFFTLTAYAVPWTQKEFDRVTLGYTQGFFETEHLLKRYSRSMAIMNNV
SLALHRCCVELLHNEALIRHLNATSFDVVLTDPVNLCGAVLAKYLSIPAVFFWRYIPCDL
DFKGTQCPNPSSYIPKLLTTNSDHMTFLQRVKNMLYPLALSYICHTFSAPYASLASELFQ
REVSVVDLVSYASVWLFRGDFVMDYPRPIMPNMVFIGGINCANGKPLSQEFEAYINASGE
HGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQND
LLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMT
SEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAH
DLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 6 Number of Residues 534
Enzyme 6 Molecular Weight 60026
Enzyme 6 Theoretical pI 8.68
Enzyme 6 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 6 General Function Carbohydrate transport and metabolism
Enzyme 6 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 6 Pathways
Enzyme 6 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-28
Enzyme 6 Transmembrane Regions
  • 492-508
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 340137 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P22310 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name UD14_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >867 bp
ATGGCCAGAGGACTCCAGGTTCCCCTGCCGCGGCTGGCCACAGGACTGCTGCTCCTCCTC
AGTGTCCAGCCCTGGGCTGAGAGTGGAAAGGTGTTGGTGGTGCCCACTGATGGCAGCCCC
TGGCTCAGCATGCGGGAGGCCTTGCGGGAGCTCCATGCCAGAGGCCACCAGGCGGTGGTC
CTCACCCCAGAGGTGAATATGCACATCAAAGAAGAGAAATTTTTCACCCTGACAGCCTAT
GCTGTTCCATGGACCCAGAAGGAATTTGATCGCGTTACGCTGGGCTACACTCAAGGGTTC
TTTGAAACAGAACATCTTCTGAAGAGATATTCTAGAAGTATGGCAATTATGAACAATGTA
TCTTTGGCCCTTCATAGGTGTTGTGTGGAGCTACTGCATAATGAGGCCCTGATCAGGCAC
CTGAATGCTACTTCCTTTGATGTGGTTTTAACAGACCCCGTTAACCTCTGTGGGGCGGTG
CTGGCTAAGTACCTGTCGATTCCTGCTGTGTTTTTTTGGAGGTACATTCCATGTGACTTA
GACTTTAAGGGCACACAGTGTCCAAATCCTTCCTCCTATATTCCTAAGTTACTAACGACC
AATTCAGACCACATGACATTCCTGCAAAGGGTCAAGAACATGCTCTACCCTCTGGCCCTG
TCCTACATTTGCCATACTTTTTCTGCCCCTTATGCAAGTCTTGCCTCTGAGCTTTTTCAG
AGAGAGGTGTCAGTGGTGGATCTTGTCAGCTATGCATCCGTGTGGCTGTTCCGAGGGGAC
TTTGTGATGGACTACCCCAGGCCGATCATGCCCAACATGGTCTTCATTGGGGGCATCAAC
TGTGCCAACGGGAAGCCACTATCTCAG
Enzyme 6 GenBank Gene ID M84128 Link Image
Enzyme 6 GeneCard ID UGT1A4 Link Image
Enzyme 6 GenAtlas ID UGT1A4 Link Image
Enzyme 6 HGNC ID HGNC:12536 Link Image
Enzyme 6 Chromosome Location 2
Enzyme 6 Locus 2q37
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 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. 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]
  5. 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]
  6. 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]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5722
Enzyme 7 Name UDP-glucuronosyltransferase 2B15 precursor
Enzyme 7 Synonyms
  1. UDPGT
  2. UDPGTh-3
  3. HLUG4
Enzyme 7 Gene Name UGT2B15
Enzyme 7 Protein Sequence >UDP-glucuronosyltransferase 2B15 precursor
MSLKWTSVFLLIQLSCYFSSGSCGKVLVWPTEYSHWINMKTILEELVQRGHEVTVLTSSA
STLVNASKSSAIKLEVYPTSLTKNDLEDSLLKILDRWIYGVSKNTFWSYFSQLQELCWEY
YDYSNKLCKDAVLNKKLMMKLQESKFDVILADALNPCGELLAELFNIPFLYSLRFSVGYT
FEKNGGGFLFPPSYVPVVMSELSDQMIFMERIKNMIHMLYFDFWFQIYDLKKWDQFYSEV
LGRPTTLFETMGKAEMWLIRTYWDFEFPRPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSS
GENGIVVFSLGSMISNMSEESANMIASALAQIPQKVLWRFDGKKPNTLGSNTRLYKWLPQ
NDLLGHPKTKAFITHGGTNGIYEAIYHGIPMVGIPLFADQHDNIAHMKAKGAALSVDIRT
MSSRDLLNALKSVINDPVYKENVMKLSRIHHDQPMKPLDRAVFWIEFVMRHKGAKHLRVA
AHNLTWIQYHSLDVIAFLLACVATVIFIITKFCLFCFRKLAKKGKKKKRD
Enzyme 7 Number of Residues 530
Enzyme 7 Molecular Weight 60989
Enzyme 7 Theoretical pI 9.04
Enzyme 7 GO Classification Not Available
Enzyme 7 General Function Carbohydrate transport and metabolism
Enzyme 7 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 7 Pathways
Enzyme 7 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 7 Pfam Domain Function Not Available
Enzyme 7 Signals
  • 1-23
Enzyme 7 Transmembrane Regions
  • 495-515
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 23955933 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P54855 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name UDB15_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1593 bp
ATGTCTCTGAAATGGACGTCAGTCTTTCTGCTGATACAGCTCAGTTGTTACTTTAGCTCT
GGAAGCTGTGGAAAGGTGCTAGTGTGGCCCACAGAATACAGCCATTGGATAAATATGAAG
ACAATCCTGGAAGAGCTTGTTCAGAGGGGTCATGAGGTGACTGTGTTGACATCTTCGGCT
TCTACTCTTGTCAATGCCAGTAAATCATCTGCTATTAAATTAGAAGTTTATCCTACATCT
TTAACTAAAAATGATTTGGAAGATTCTCTTCTGAAAATTCTCGATAGATGGATATATGGT
GTTTCAAAAAATACATTTTGGTCATATTTTTCACAATTACAAGAATTGTGTTGGGAATAT
TATGACTACAGTAACAAGCTCTGTAAAGATGCAGTTTTGAATAAGAAACTTATGATGAAA
CTACAAGAGTCAAAGTTTGATGTCATTCTGGCAGATGCCCTTAATCCCTGTGGTGAGCTA
CTGGCTGAACTATTTAACATACCCTTTCTGTACAGTCTTCGATTCTCTGTTGGCTACACA
TTTGAGAAGAATGGTGGAGGATTTCTGTTCCCTCCTTCCTATGTACCTGTTGTTATGTCA
GAATTAAGTGATCAAATGATTTTCATGGAGAGGATAAAAAATATGATACATATGCTTTAT
TTTGACTTTTGGTTTCAAATTTATGATCTGAAGAAGTGGGACCAGTTTTATAGTGAAGTT
CTAGGAAGACCCACTACATTATTTGAGACAATGGGGAAAGCTGAAATGTGGCTCATTCGA
ACCTATTGGGATTTTGAATTTCCTCGCCCATTCTTACCAAATGTTGATTTTGTTGGAGGA
CTTCACTGTAAACCAGCCAAACCCCTGCCTAAGGAAATGGAAGAGTTTGTGCAGAGCTCT
GGAGAAAATGGTATTGTGGTGTTTTCTCTGGGGTCGATGATCAGTAACATGTCAGAAGAA
AGTGCCAACATGATTGCATCAGCCCTTGCCCAGATCCCACAAAAGGTTCTATGGAGATTT
GATGGCAAGAAGCCAAATACTTTAGGTTCCAATACTCGACTGTACAAGTGGTTACCCCAG
AATGACCTTCTTGGTCATCCCAAAACCAAAGCTTTTATAACTCATGGTGGAACCAATGGC
ATCTATGAGGCGATCTACCATGGGATCCCTATGGTGGGCATTCCCTTGTTTGCGGATCAA
CATGATAACATTGCTCACATGAAAGCCAAGGGAGCAGCCCTCAGTGTGGACATCAGGACC
ATGTCAAGTAGAGATTTGCTCAATGCATTGAAGTCAGTCATTAATGACCCTGTCTATAAA
GAGAATGTCATGAAATTATCAAGAATTCATCATGACCAACCAATGAAGCCCCTGGATCGA
GCAGTCTTCTGGATTGAGTTTGTCATGCGCCACAAAGGAGCCAAGCACCTTCGAGTCGCA
GCTCACAACCTCACCTGGATCCAGTACCACTCTTTGGATGTGATAGCATTCCTGCTGGCC
TGCGTGGCAACTGTGATATTTATCATCACAAAATTTTGCCTGTTTTGTTTCCGAAAGCTT
GCCAAAACAGGAAAGAAGAAGAAAAGAGATTAG
Enzyme 7 GenBank Gene ID AF548389 Link Image
Enzyme 7 GeneCard ID UGT2B15 Link Image
Enzyme 7 GenAtlas ID UGT2B15 Link Image
Enzyme 7 HGNC ID HGNC:12546 Link Image
Enzyme 7 Chromosome Location 4
Enzyme 7 Locus 4q13
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. 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]
  2. 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]
  3. 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]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5724
Enzyme 8 Name UDP-glucuronosyltransferase 2A1 precursor
Enzyme 8 Synonyms Not Available
Enzyme 8 Gene Name UGT2A1
Enzyme 8 Protein Sequence >UDP-glucuronosyltransferase 2A1 precursor
MLNNLLLFSLQISLIGTTLGGNVLIWPMEGSHWLNVKIIIDELIKKEHNVTVLVASGALF
ITPTSNPSLTFEIYKVPFGKERIEGVIKDFVSTWLENRPSPSTIWRFYQEMAKVIKDFHM
VSQEICDGVLKNQQLMAKLKKSKFEVLVSDPVFPCGDIVALKLGIPFMYSLRFSPASTVE
KHCGKVPYPPSYVPAVLSELTDQMSFTDRIRNFISYHLQDYMFETLWKSWDSYYSKALGR
PTTLCETMGKAEIWLIRTYWDFEFPRPYLPNFEFVGGLHCKPAKPLPKEMEEFIQSSGKN
GVVVFSLGSMVKNLTEEKANLIASALAQIPQKVLWRYKGKKPATLGNNTQLFDWIPQNDL
LGHPKTKAFITHGGTNGIYEAIYHGVPMVGVPMFADQPDNIAHMKAKGAAVEVNLNTMTS
VDLLSALRTVINEPSYKENAMRLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAHD
LTWFQYHSLDVIGFLLVCVTTAIFLVIQCCLFSCQKFGKIGKKKKRE
Enzyme 8 Number of Residues 527
Enzyme 8 Molecular Weight 59873
Enzyme 8 Theoretical pI 9.29
Enzyme 8 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 8 General Function Carbohydrate transport and metabolism
Enzyme 8 Specific Function UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform is active on odorants and seems to be involved in olfaction; it could help clear lipophilic odorant molecules from the sensory epithelium
Enzyme 8 Pathways
Enzyme 8 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-20
Enzyme 8 Transmembrane Regions
  • 491-507
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 4753766 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q9Y4X1 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name UDA1_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1584 bp
ATGTTAAACAACCTTCTGCTGTTCTCCCTTCAGATAAGTCTCATAGGAACCACTCTTGGT
GGGAATGTTTTGATTTGGCCAATGGAAGGTAGTCATTGGCTAAATGTTAAGATAATTATA
GATGAGCTCATTAAAAAGGAGCATAATGTGACTGTCCTAGTTGCCTCTGGTGCACTTTTC
ATCACACCAACCTCTAACCCATCTCTGACATTTGAAATATATAAGGTGCCCTTTGGCAAA
GAAAGAATAGAAGGAGTAATTAAGGACTTCGTTTCGACATGGCTGGAAAATAGACCATCT
CCTTCAACCATTTGGAGATTCTATCAGGAGATGGCCAAAGTAATCAAGGACTTCCACATG
GTGTCTCAGGAGATCTGTGATGGCGTTCTTAAAAACCAACAGCTGATGGCAAAGCTAAAG
AAAAGCAAGTTTGAAGTCCTGGTGTCTGATCCAGTATTTCCTTGTGGCGATATAGTAGCT
TTAAAACTTGGAATTCCATTTATGTACTCCTTGAGGTTTTCTCCAGCCTCAACAGTGGAA
AAGCACTGTGGGAAGGTACCATACCCTCCTTCCTATGTTCCTGCTGTTTTATCAGAACTC
ACCGACCAAATGTCTTTCACTGACAGAATAAGAAATTTCATCTCCTACCACCTACAGGAC
TACATGTTTGAAACTCTTTGGAAATCATGGGATTCATACTATAGTAAAGCTTTAGGAAGA
CCCACTACGTTATGTGAGACTATGGGGAAAGCTGAAATTTGGTTAATCCGAACATATTGG
GATTTTGAATTTCCTCGTCCATACTTACCTAATTTTGAGTTTGTTGGAGGATTGCACTGC
AAACCTGCCAAACCTTTACCTAAGGAAATGGAAGAATTTATCCAGAGCTCAGGTAAAAAT
GGTGTTGTGGTGTTTTCTCTGGGATCAATGGTCAAAAACCTTACAGAAGAAAAGGCCAAT
CTTATTGCCTCAGCCCTTGCCCAGATTCCACAGAAGGTTTTATGGAGATACAAAGGAAAG
AAACCAGCCACATTAGGAAACAATACTCAGCTCTTTGATTGGATACCCCAGAATGATCTT
CTTGGACATCCCAAAACCAAAGCTTTTATCACTCATGGTGGAACTAATGGGATCTACGAA
GCTATTTACCACGGAGTCCCTATGGTGGGAGTTCCCATGTTTGCTGATCAGCCTGATAAC
ATTGCTCACATGAAGGCCAAAGGAGCAGCTGTGGAAGTGAACCTAAACACAATGACAAGT
GTGGATTTGCTTAGCGCTTTGAGAACAGTCATTAATGAACCTTCTTATAAAGAGAATGCT
ATGAGGTTATCAAGAATTCACCATGATCAACCTGTAAAGCCCCTGGATCGAGCAGTCTTC
TGGATCGAGTTTGTCATGCGCCACAAAGGAGCCAAGCACCTTCGGGTTGCAGCCCATGAC
CTCACCTGGTTCCAGTACCACTCTTTGGATGTAATTGGGTTCTTGCTGGTCTGTGTGACA
ACGGCTATATTTTTGGTCATACAATGTTGTTTGTTTTCCTGTCAAAAATTTGGTAAGATA
GGAAAGAAGAAAAAAAGAGAATAG
Enzyme 8 GenBank Gene ID AJ006054 Link Image
Enzyme 8 GeneCard ID UGT2A1 Link Image
Enzyme 8 GenAtlas ID UGT2A1 Link Image
Enzyme 8 HGNC ID HGNC:12542 Link Image
Enzyme 8 Chromosome Location 4
Enzyme 8 Locus 4q13
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 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]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5725
Enzyme 9 Name UDP-glucuronosyltransferase 1-1 precursor
Enzyme 9 Synonyms
  1. UDP- glucuronosyltransferase 1A1
  2. UDPGT
  3. UGT1*1
  4. UGT1-01
  5. UGT1.1
  6. UGT- 1A
  7. UGT1A
  8. Bilirubin-specific UDPGT isozyme 1
  9. HUG-BR1
Enzyme 9 Gene Name UGT1A1
Enzyme 9 Protein Sequence >UDP-glucuronosyltransferase 1-1 precursor
MAVESQGGRPLVLGLLLCVLGPVVSHAGKILLIPVDGSHWLSMLGAIQQLQQRGHEIVVL
APDASLYIRDGAFYTLKTYPVPFQREDVKESFVSLGHNVFENDSFLQRVIKTYKKIKKDS
AMLLSGCSHLLHNKELMASLAESSFDVMLTDPFLPCSPIVAQYLSLPTVFFLHALPCSLE
FEATQCPNPFSYVPRPLSSHSDHMTFLQRVKNMLIAFSQNFLCDVVYSPYATLASEFLQR
EVTVQDLLSSASVWLFRSDFVKDYPRPIMPNMVFVGGINCLHQNPLSQEFEAYINASGEH
GIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDL
LGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTS
EDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHD
LTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 9 Number of Residues 533
Enzyme 9 Molecular Weight 59592
Enzyme 9 Theoretical pI 8.09
Enzyme 9 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 9 General Function Carbohydrate transport and metabolism
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
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-25
Enzyme 9 Transmembrane Regions
  • 491-507
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 184473 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P22309 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name UD11_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 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 9 GenBank Gene ID M57899 Link Image
Enzyme 9 GeneCard ID UGT1A1 Link Image
Enzyme 9 GenAtlas ID UGT1A1 Link Image
Enzyme 9 HGNC ID HGNC:12530 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. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. 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]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5726
Enzyme 10 Name UDP-glucuronosyltransferase 1-9 precursor
Enzyme 10 Synonyms
  1. UDP- glucuronosyltransferase 1A9
  2. UDPGT
  3. UGT1*9
  4. UGT1-9
  5. UGT1.9
  6. UGT- 1I
  7. UGT1I
  8. lugP4
Enzyme 10 Gene Name UGT1A9
Enzyme 10 Protein Sequence >UDP-glucuronosyltransferase 1-9 precursor
MACTGWTSPLPLCVCLLLTCGFAEAGKLLVVPMDGSHWFTMRSVVEKLILRGHEVVVVMP
EVSWQLGRSLNCTVKTYSTSYTLEDLDREFKAFAHAQWKAQVRSIYSLLMGSYNDIFDLF
FSNCRSLFKDKKLVEYLKESSFDAVFLDPFDNCGLIVAKYFSLPSVVFARGILCHYLEEG
AQCPAPLSYVPRILLGFSDAMTFKERVRNHIMHLEEHLLCHRFFKNALEIASEILQTPVT
EYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIV
VFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGH
PMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDL
ENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTW
YQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 10 Number of Residues 530
Enzyme 10 Molecular Weight 59942
Enzyme 10 Theoretical pI 7.96
Enzyme 10 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 10 General Function Carbohydrate transport and metabolism
Enzyme 10 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 10 Pathways
Enzyme 10 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • 1-25
Enzyme 10 Transmembrane Regions
  • 488-504
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 7690346 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID O60656 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name UD19_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1593 bp
ATGGCTTGCACAGGGTGGACCAGCCCCCTTCCTCTATGTGTGTGTCTGCTGCTGACCTGT
GGCTTTGCCGAGGCAGGGAAGCTAGTGGTAGTGCCCATGGATGGGAGCCACTGGTTCACC
ATGAGGTCGGTGGTGGAGAAACTCATTCTCAGGGGGCATGAGGTGGTTGTAGTCAGTGCC
AGAGGTGAGTTGGCAACTGGGAAGATCAATGAATTGCACAGTGAAGACTTATTCAACTTC
ATATACCTGGAGGATCTGGACCGGGAGTTCAAGGCTTTTGCCCATGCTCAATGGAAAGCA
CAAGTACGAAGTATATATTCTCTATTAATGGGTTCATACAATGACATTTTTGACTTATTT
TTTTCAAATTGCAGGAGTTTGTTTAAAGACAAAAAATTAGTAGAATACTTAAAGGAGAGT
TCTTTTGATGCAGTGTTTCTCGATCCTTTTGATAACTGTGGCTTAATTGTTGCCAAATAT
TTCTCCCTCCCCTCCGTGGTCTTCGCCAGGGGAATACTTTGCCACTATCTTGAAGAAGGT
GCACAGTGCCCTGCTCCTCTTTCCTATGTCCCCAGAATTCTCTTAGGGTTCTCAGATGAC
ATGACTTTCAAGGAGAGAGTACGGAACCACATCATGCACTTGGAGGAACATTTATTATGC
CACCGTTTTTTCAAAAATGCCCTAGAAATAGCCTCTGAAATTCTCCAAACACCTGTTACG
GAGTATGATCTCTACAGCCACACATCAATTTGGTTGTTGCGAACGGACTTTGTTTTGGAC
TATCCCAAACCCGTGATGCCCAACATGATCTTCATTGGTGGTATCAACTGCCATGAGAGG
AAAGCGTTGCCTATGGAATTTGAAGCCTACATTAATGCTTCTGGAGAACATGGAATTGTG
GGTTTCTCTTTGGGATCAATGGTCTCAGAAATTCCAGAGAAGAAAGCTATGGCAATTGCT
GATGCTTTGGGCAAAATCCCTCAGACAGTCCTGTGGCGGTACACTGGAACCCGACCATGC
AATCTTGCGAACAACACGATACTTGTTAAGTGGCTACCCCAAAACGATCTGCTTGGTCAC
CCGATGACCAGTGCCTTTATCACCCATGCTGGTTCCCATGGTGTTTATGAAAGCATATGC
AATGGCGTTCCCATGGTGATGATGCCCTTGTTTGGTGATCAGATGGACAATGCAAAGCGC
ATGGAGACTAAGGGAGCTGGAGTGACCATGAATGTTCTGGAAATGACTTCTGAAGAATTA
GAAAATGCTCTAAAAGCAGTCATCAATGACAAAAGTTACAAGGAGAACATCATGCGCCTC
TCCAGCCTTCACAAGGACCGCCCGGTGGAGCCGCTGGACCTGGCCGTGTTCTGGGTGGAG
TTTGTTATGAGGCACAAGGGCGCGACACACCTGCGCCCCGCAGCCCACGACCTCACCTGG
TACCAGTACCATTCCTTGGACGTGATTGGTTTCCTCTTGGCCGCCGTGCTGACAGTGGCC
TTCATCACCTGTAAATGTTGTGCTTATGGCTACCGGAAATGCTTGGGGAAAAAAGGGCGA
GTTAAGAAAGCCCACAAATCCAAGACCCATTGA
Enzyme 10 GenBank Gene ID S55985 Link Image
Enzyme 10 GeneCard ID UGT1A9 Link Image
Enzyme 10 GenAtlas ID UGT1A9 Link Image
Enzyme 10 HGNC ID HGNC:12541 Link Image
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus Not Available
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 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]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5728
Enzyme 11 Name UDP-glucuronosyltransferase 1-3 precursor
Enzyme 11 Synonyms
  1. UDP- glucuronosyltransferase 1A3
  2. UDPGT
  3. UGT1*3
  4. UGT1-03
  5. UGT1.3
  6. UGT- 1C
  7. UGT1C
Enzyme 11 Gene Name UGT1A3
Enzyme 11 Protein Sequence >UDP-glucuronosyltransferase 1-3 precursor
MATGLQVPLPWLATGLLLLLSVQPWAESGKVLVVPIDGSHWLSMREVLRELHARGHQAVV
LTPEVNMHIKEENFFTLTTYAISWTQDEFDRHVLGHTQLYFETEHFLKKFFRSMAMLNNM
SLVYHRSCVELLHNEALIRHLNATSFDVVLTDPVNLCAAVLAKYLSIPTVFFLRNIPCDL
DFKGTQCPNPSSYIPRLLTTNSDHMTFMQRVKNMLYPLALSYICHAFSAPYASLASELFQ
REVSVVDILSHASVWLFRGDFVMDYPRPIMPNMVFIGGINCANRKPLSQEFEAYINASGE
HGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQND
LLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMT
SEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAH
DLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 11 Number of Residues 534
Enzyme 11 Molecular Weight 60339
Enzyme 11 Theoretical pI 8.28
Enzyme 11 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 11 General Function Carbohydrate transport and metabolism
Enzyme 11 Specific Function UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds
Enzyme 11 Pathways
Enzyme 11 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • 1-28
Enzyme 11 Transmembrane Regions
  • 492-508
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 340135 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID P35503 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name UD13_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >867 bp
ATGGCCACAGGACTCCAGGTTCCCCTGCCGTGGCTGGCCACAGGACTGCTGCTTCTCCTC
AGTGTCCAGCCCTGGGCTGAGAGTGGAAAGGTGTTGGTGGTGCCCATTGATGGCAGCCAC
TGGCTCAGCATGCGGGAGGTCTTGCGGGAGCTCCATGCCAGAGGCCACCAGGCAGTGGTC
CTCACCCCAGAGGTGAATATGCACATCAAAGAAGAGAACTTTTTCACCCTGACAACCTAT
GCCATTTCGTGGACCCAGGATGAATTTGATCGCCATGTGCTGGGCCACACTCAACTGTAC
TTTGAAACAGAACATTTTCTGAAGAAATTTTTCAGAAGTATGGCAATGTTGAACAATATG
TCTTTGGTCTATCATAGGTCTTGTGTGGAGCTACTACATAATGAGGCCCTGATCAGGCAC
CTGAATGCTACTTCCTTTGATGTGGTTTTAACAGACCCCGTTAACCTCTGCGCGGCAGTG
CTGGCTAAGTACCTGTCGATTCCTACTGTGTTTTTTTTGAGGAACATTCCATGTGATTTA
GACTTTAAGGGCACACAGTGTCCAAACCCTTCCTCCTATATTCCTAGATTACTAACAACC
AATTCAGACCACATGACATTCATGCAAAGGGTCAAGAACATGCTCTACCCTCTGGCCCTG
TCCTACATTTGCCATGCTTTTTCTGCTCCTTATGCAAGCCTTGCCTCTGAGCTTTTTCAG
AGAGAGGTGTCAGTGGTGGATATTCTCAGTCATGCATCTGTGTGGCTGTTCCGAGGGGAC
TTTGTGATGGACTACCCCAGGCCAATCATGCCCAACATGGTCTTCATTGGGGGCATCAAC
TGTGCCAACAGGAAGCCACTATCTCAG
Enzyme 11 GenBank Gene ID M84127 Link Image
Enzyme 11 GeneCard ID UGT1A3 Link Image
Enzyme 11 GenAtlas ID UGT1A3 Link Image
Enzyme 11 HGNC ID HGNC:12535 Link Image
Enzyme 11 Chromosome Location 2
Enzyme 11 Locus 2q37
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 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 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5731
Enzyme 12 Name UDP-glucuronosyltransferase 2B17 precursor
Enzyme 12 Synonyms
  1. UDPGT
  2. C19- steroid-specific UDP-glucuronosyltransferase
Enzyme 12 Gene Name UGT2B17
Enzyme 12 Protein Sequence >UDP-glucuronosyltransferase 2B17 precursor
MSLKWMSVFLLMQLSCYFSSGSCGKVLVWPTEYSHWINMKTILEELVQRGHEVIVLTSSA
SILVNASKSSAIKLEVYPTSLTKNDLEDFFMKMFDRWTYSISKNTFWSYFSQLQELCWEY
SDYNIKLCEDAVLNKKLMRKLQESKFDVLLADAVNPCGELLAELLNIPFLYSLRFSVGYT
VEKNGGGFLFPPSYVPVVMSELSDQMIFMERIKNMIYMLYFDFWFQAYDLKKWDQFYSEV
LGRPTTLFETMGKAEMWLIRTYWDFEFPRPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSS
GENGIVVFSLGSMISNMSEESANMIASALAQIPQKVLWRFDGKKPNTLGSNTRLYKWLPQ
NDLLGHPKTKAFITHGGTNGIYEAIYHGIPMVGIPLFADQHDNIAHMKAKGAALSVDIRT
MSSRDLLNALKSVINDPIYKENIMKLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVA
AHNLTWIQYHSLDVIAFLLACVATMIFMITKCCLFCFRKLAKTGKKKKRD
Enzyme 12 Number of Residues 530
Enzyme 12 Molecular Weight 61096
Enzyme 12 Theoretical pI 8.73
Enzyme 12 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 12 General Function Carbohydrate transport and metabolism
Enzyme 12 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-3alpha,17beta-diol (3alpha-diol) > testosterone > androsterone (ADT)
Enzyme 12 Pathways
Enzyme 12 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • 1-23
Enzyme 12 Transmembrane Regions
  • 495-515
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 3287473 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID O75795 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name UDB17_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 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 12 GenBank Gene ID U59209 Link Image
Enzyme 12 GeneCard ID UGT2B17 Link Image
Enzyme 12 GenAtlas ID UGT2B17 Link Image
Enzyme 12 HGNC ID HGNC:12547 Link Image
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus Not Available
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 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]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5732
Enzyme 13 Name UDP-glucuronosyltransferase 1-6 precursor
Enzyme 13 Synonyms
  1. UDP- glucuronosyltransferase 1A6
  2. UDPGT
  3. UGT1*6
  4. UGT1-06
  5. UGT1.6
  6. UGT- 1F
  7. UGT1F
  8. Phenol-metabolizing UDP-glucuronosyltransferase
Enzyme 13 Gene Name UGT1A6
Enzyme 13 Protein Sequence >UDP-glucuronosyltransferase 1-6 precursor
MACLLRSFQRISAGVFFLALWGMVVGDKLLVVPQDGSHWLSMKDIVEVLSDRGHEIVVVV
PEVNLLLKESKYYTRKIYPVPYDQEELKNRYQSFGNNHFAERSFLTAPQTEYRNNMIVIG
LYFINCQSLLQDRDTLNFFKESKFDALFTDPALPCGVILAEYLGLPSVYLFRGFPCSLEH
TFSRSPDPVSYIPRCYTKFSDHMTFSQRVANFLVNLLEPYLFYCLFSKYEELASAVLKRD
VDIITLYQKVSVWLLRYDFVLEYPRPVMPNMVFIGGINCKKRKDLSQEFEAYINASGEHG
IVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLL
GHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSE
DLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDL
TWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 13 Number of Residues 532
Enzyme 13 Molecular Weight 60751
Enzyme 13 Theoretical pI 8.55
Enzyme 13 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 13 General Function Carbohydrate transport and metabolism
Enzyme 13 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 13 Pathways
Enzyme 13 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • 1-26
Enzyme 13 Transmembrane Regions
  • 490-506
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 340141 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID P19224 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name UD16_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >861 bp
ATGGCCTGCCTCCTTCGCTCATTTCAGAGAATTTCTGCAGGGGTTTTCTTCTTAGCACTT
TGGGGCATGGTTGTAGGTGACAAGCTGCTGGTGGTCCCTCAGGACGGAAGCCACTGGCTT
AGTATGAAGGATATAGTTGAGGTTCTCAGTGACCGGGGTCATGAGATTGTAGTGGTGGTG
CCTGAAGTTAATTTGCTTTTGAAAGAATCCAAATACTACACAAGAAAAATCTATCCAGTG
CCGTATGACCAAGAAGAGCTGAAGAACCGTTACCAATCATTTGGAAACAATCACTTTGCT
GAGCGATCATTCCTAACTGCTCCTCAGACAGAGTACAGGAATAACATGATTGTTATTGGC
CTGTACTTCATCAACTGCCAGAGCCTCCTGCAGGACAGGGACACCCTGAACTTCTTTAAG
GAGAGCAAGTTTGATGCTCTTTTCACAGACCCAGCCTTACCCTGTGGGGTGATCCTGGCT
GAGTATTTGGGCCTACCATCTGTGTACCTCTTCAGGGGTTTTCCGTGTTCCCTGGAGCAT
ACATTCAGCAGAAGCCCAGACCCTGTGTCCTACATTCCCAGGTGCTACACAAAGTTTTCA
GACCACATGACTTTTTCCCAACGAGTGGCCAACTTCCTTGTTAATTTGTTGGAGCCCTAT
CTATTTTATTGTCTGTTTTCAAAGTATGAAGAACTCGCATCAGCTGTCCTCAAGAGAGAT
GTGGATATAATCACCTTATATCAGAAGGTCTCTGTTTGGCTGTTAAGATATGACTTTGTG
CTTGAATATCCTAGGCCGGTCATGCCCAACATGGTCTTCATTGGAGGTATCAACTGTAAG
AAGAGGAAAGACTTGTCTCAG
Enzyme 13 GenBank Gene ID M84130 Link Image
Enzyme 13 GeneCard ID UGT1A6 Link Image
Enzyme 13 GenAtlas ID UGT1A6 Link Image
Enzyme 13 HGNC ID HGNC:12538 Link Image
Enzyme 13 Chromosome Location Not Available
Enzyme 13 Locus Not Available
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 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]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5733
Enzyme 14 Name UDP-glucuronosyltransferase 1-5 precursor
Enzyme 14 Synonyms
  1. UDP- glucuronosyltransferase 1A5
  2. UDPGT
  3. UGT1*5
  4. UGT1-05
  5. UGT1.5
  6. UGT- 1E
  7. UGT1E
Enzyme 14 Gene Name UGT1A5
Enzyme 14 Protein Sequence >UDP-glucuronosyltransferase 1-5 precursor
MATGLQVPLPQLATGLLLLLSVQPWAESGKVLVVPTDGSHWLSMREALRDLHARGHQVVV
LTLEVNMYIKEENFFTLTTYAISWTQDEFDRLLLGHTQSFFETEHLLMKFSRRMAIMNNM
SLIIHRSCVELLHNEALIRHLHATSFDVVLTDPFHLCAAVLAKYLSIPAVFFLRNIPCDL
DFKGTQCPNPSSYIPRLLTTNSDHMTFLQRVKNMLYPLALSYLCHAVSAPYASLASELFQ
REVSVVDLVSHASVWLFRGDFVMDYPRPIMPNMVFIGGINCANGKPLSQEFEAYINASGE
HGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQND
LLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMT
SEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAH
DLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 14 Number of Residues 534
Enzyme 14 Molecular Weight 60072
Enzyme 14 Theoretical pI 8.14
Enzyme 14 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 14 General Function Carbohydrate transport and metabolism
Enzyme 14 Specific Function UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds
Enzyme 14 Pathways
Enzyme 14 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • 1-28
Enzyme 14 Transmembrane Regions
  • 492-508
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 340139 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID P35504 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name UD15_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >867 bp
ATGGCCACAGGACTCCAGGTTCCCCTGCCGCAGCTGGCCACAGGACTGCTGCTTCTCCTC
AGTGTCCAGCCCTGGGCTGAGAGTGGGAAGGTGCTGGTGGTGCCCACTGATGGCAGCCAC
TGGCTCAGCATGCGGGAGGCCTTGCGGGACCTCCATGCGAGAGGCCACCAGGTGGTGGTC
CTCACCCTGGAGGTGAATATGTACATCAAAGAAGAGAACTTTTTCACCCTGACAACGTAT
GCCATTTCATGGACCCAGGACGAATTTGATCGCCTTTTGCTGGGTCACACTCAATCGTTC
TTTGAAACAGAACATCTTCTGATGAAATTTTCTAGAAGAATGGCAATTATGAACAATATG
TCTTTGATCATACATAGGTCTTGTGTGGAGCTACTGCATAATGAGGCCCTGATCAGGCAC
CTGCATGCTACTTCCTTTGATGTGGTTCTAACAGACCCCTTTCACCTCTGCGCGGCGGTG
CTGGCTAAGTACCTGTCGATTCCTGCTGTGTTTTTCTTGAGGAACATTCCATGTGATTTA
GACTTTAAGGGCACACAGTGTCCAAACCCTTCCTCCTATATTCCTAGATTACTAACGACC
AATTCAGACCACATGACATTCCTGCAAAGGGTCAAGAACATGCTCTACCCTCTGGCCCTG
TCCTACCTTTGCCATGCTGTTTCTGCTCCTTATGCAAGCCTTGCCTCTGAGCTTTTTCAG
AGAGAGGTGTCAGTGGTGGATCTTGTCAGCCATGCATCTGTGTGGCTGTTCCGAGGGGAC
TTTGTGATGGATTACCCCAGGCCGATCATGCCCAACATGGTCTTCATTGGGGGCATCAAC
TGTGCCAACGGGAAGCCACTATCTCAG
Enzyme 14 GenBank Gene ID M84129 Link Image
Enzyme 14 GeneCard ID UGT1A5 Link Image
Enzyme 14 GenAtlas ID UGT1A5 Link Image
Enzyme 14 HGNC ID HGNC:12537 Link Image
Enzyme 14 Chromosome Location 2
Enzyme 14 Locus 2q37
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 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 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5734
Enzyme 15 Name UDP-glucuronosyltransferase 2B11 precursor
Enzyme 15 Synonyms
  1. UDPGT
Enzyme 15 Gene Name UGT2B11
Enzyme 15 Protein Sequence >UDP-glucuronosyltransferase 2B11 precursor
MTLKWTSVLLLIHLSCYFSSGSCGKVLVWAAEYSHWMNMKTILKELVQRGHEVTVLASSA
SILFDPNDASTLKFEVYPTSLTKTEFENIIMQQVKRWSDIRKDSFWLYFSQEQEILWELY
DIFRNFCKDVVSNKKVMKKLQESRFDIVFADAVFPCGELLAALLNIRFVYSLRFTPGYTI
ERHSGGLIFPPSYIPIVMSKLSDQMTFMERVKNMIYVLYFDFWFQMSDMKKWDQFYSEVL
GRPTTLFETMGKADIWLMRNSWSFQFPHPFLPNVDFVGGFHCKPAKPLPKEMEEFVQSSG
ENGVVVFSLGSVISNMTAERANVIATALAKIPQKVLWRFDGNKPDALGLNTRLYKWIPQN
DLLGHPKTRAFITHGGANGIYEAIYHGIPMVGIPLFFDQPDNIAHMKAKGAAVRLDFNTM
SSTDLLNALKTVINDPLYKENIMKLSRIQHDQPVKPLDRAVFWIEFVMPHKGAKHLRVAA
HDLTWFQYHSLDVIGFLLACVATVIFIITKFCLFCFWKFARKGKKGKRD
Enzyme 15 Number of Residues 529
Enzyme 15 Molecular Weight 61039
Enzyme 15 Theoretical pI 9.29
Enzyme 15 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 15 General Function Carbohydrate transport and metabolism
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
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • 1-21
Enzyme 15 Transmembrane Regions
  • 493-513
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 3360273 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID O75310 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name UDB11_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 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 15 GenBank Gene ID AF016492 Link Image
Enzyme 15 GeneCard ID UGT2B11 Link Image
Enzyme 15 GenAtlas ID UGT2B11 Link Image
Enzyme 15 HGNC ID HGNC:12545 Link Image
Enzyme 15 Chromosome Location 4
Enzyme 15 Locus 4q13.2
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 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]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5818
Enzyme 16 Name Dehydrogenase/reductase SDR family member 8 precursor
Enzyme 16 Synonyms
  1. 17-beta-hydroxysteroid dehydrogenase 11
  2. 17-beta-HSD 11
  3. 17-beta- HSD XI
  4. 17betaHSDXI
  5. 17bHSD11
  6. 17betaHSD11
  7. Retinal short-chain dehydrogenase/reductase 2
  8. retSDR2
  9. Cutaneous T-cell lymphoma- associated antigen HD-CL-03
  10. CTCL tumor antigen HD-CL-03
Enzyme 16 Gene Name DHRS8
Enzyme 16 Protein Sequence >Dehydrogenase/reductase SDR family member 8 precursor
MKFLLDILLLLPLLIVCSLESFVKLFIPKRRKSVTGEIVLITGAGHGIGRLTAYEFAKLK
SKLVLWDINKHGLEETAAKCKGLGAKVHTFVVDCSNREDIYSSAKKVKAEIGDVSILVNN
AGVVYTSDLFATQDPQIEKTFEVNVLAHFWTTKAFLPAMTKNNHGHIVTVASAAGHVSVP
FLLAYCSSKFAAVGFHKTLTDELAALQITGVKTTCLCPNFVNTGFIKNPSTSLGPTLEPE
EVVNRLMHGILTEQKMIFIPSSIAFLTTLERILPERFLAVLKRKISVKFDAVIGYKMKAQ
Enzyme 16 Number of Residues 300
Enzyme 16 Molecular Weight 32964
Enzyme 16 Theoretical pI 9.70
Enzyme 16 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
Enzyme 16 General Function Lipid transport and metabolism
Enzyme 16 Specific Function Can convert androstan-3-alpha,17-beta-diol (3alpha-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 16 Pathways Not Available
Enzyme 16 Reactions Not Available
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • 1-19
Enzyme 16 Transmembrane Regions Not Available
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 6318544 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID Q8NBQ5 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name DHRS8_HUMAN Link Image
Enzyme 16 PDB ID 1YB1 Link Image
Enzyme 16 PDB File Show
Enzyme 16 3D Structure
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >903 bp
ATGAAATTTCTTCTGGACATCCTCCTGCTTCTCCCGTTACTGATCGTCTGCTCCCTAGAG
TCCTTCGTGAAGCTTTTTATTCCTAAGAGGAGAAAATCAGTCACCGGCGAAATCGTGCTG
ATTACAGGAGCTGGGCATGGAATTGGGAGACTGACTGCCTATGAATTTGCTAAACTTAAA
AGCAAGCTGGTTCTCTGGGATATAAATAAGCATGGACTGGAGGAAACAGCTGCCAAATGC
AAGGGACTGGGTGCCAAGGTTCATACCTTTGTGGTAGACTGCAGCAACCGAGAAGATATT
TACAGCTCTGCAAAGAAGGTGAAGGCAGAAATTGGAGATGTTAGTATTTTAGTAAATAAT
GCTGGTGTAGTCTATACATCAGATTTGTTTGCTACACAAGATCCTCAGATTGAAAAGACT
TTTGAAGTTAATGTACTTGCACATTTCTGGACTACAAAGGCATTTCTTCCTGCAATGACG
AAGAATAACCATGGCCATATTGTCACTGTGGCTTCGGCAGCTGGACATGTCTCGGTCCCC
TTCTTACTGGCTTACTGTTCAAGCAAGTTTGCTGCTGTTGGATTTCATAAAACTTTGACA
GATGAACTGGCTGCCTTACAAATAACTGGAGTCAAAACAACATGTCTGTGTCCTAATTTC
GTAAACACTGGCTTCATCAAAAATCCAAGTACAAGTTTGGGACCCACTCTGGAACCCGAG
GAAGTGGTAAACAGGCTGATGCATGGGATTCTGACTGAGCAGAAGATGATTTTTATTCCA
TCTTCTATAGCTTTTTTAACAACATTGGAAAGGATCCTTCCTGAGCGTTTCCTGGCAGTT
TTAAAACGAAAAATCAGTGTTAAGTTTGATGCAGTTATTGGATATAAAATGAAAGCGCAA
TAA
Enzyme 16 GenBank Gene ID AF126780 Link Image
Enzyme 16 GeneCard ID DHRS8 Link Image
Enzyme 16 GenAtlas ID DHRS8 Link Image
Enzyme 16 HGNC ID HGNC:22960 Link Image
Enzyme 16 Chromosome Location 4
Enzyme 16 Locus 4q22.1
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Haeseleer F, Palczewski K: Short-chain dehydrogenases/reductases in retina. Methods Enzymol. 2000;316:372-83. [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. 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]
  4. 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]
  5. 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 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 6128
Enzyme 17 Name Estradiol 17-beta-dehydrogenase 1
Enzyme 17 Synonyms
  1. 17-beta- hydroxysteroid dehydrogenase type 1
  2. 17-beta-HSD 1
  3. Placental 17- beta-hydroxysteroid dehydrogenase
  4. 20 alpha-hydroxysteroid dehydrogenase
  5. 20-alpha-HSD
  6. E2DH
Enzyme 17 Gene Name HSD17B1
Enzyme 17 Protein Sequence >Estradiol 17-beta-dehydrogenase 1
MARTVVLITGCSSGIGLHLAVRLASDPSQSFKVYATLRDLKTQGRLWEAARALACPPGSL
ETLQLDVRDSKSVAAARERVTEGRVDVLVCNAGLGLLGPLEALGEDAVASVLDVNVVGTV
RMLQAFLPDMKRRGSGRVLVTGSVGGLMGLPFNDVYCASKFALEGLCESLAVLLLPFGVH
LSLIECGPVHTAFMEKVLGSPEEVLDRTDIHTFHRFYQYLAHSKQVFREAAQNPEEVAEV
FLTALRAPKPTLRYFTTERFLPLLRMRLDDPSGSNYVTAMHREVFGDVPAKAEAGAEAGG
GAGPGAEDEAGRSAVGDPELGDPPAAPQ
Enzyme 17 Number of Residues 328
Enzyme 17 Molecular Weight 34980
Enzyme 17 Theoretical pI 5.42
Enzyme 17 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 17 General Function Lipid transport and metabolism
Enzyme 17 Specific Function Favors the reduction of estrogens and androgens. Also has 20-alpha-HSD activity. Uses preferentially NADH
Enzyme 17 Pathways
  • Androgen and Estrogen Metabolism (map00150 Link Image)
Enzyme 17 Reactions
  • estradiol-17beta + NAD(P)+ = estrone + NAD(P)H + H+
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • 1-30
Enzyme 17 Transmembrane Regions Not Available
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 23365 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID P14061 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name DHB1_HUMAN Link Image
Enzyme 17 PDB ID 1QYX Link Image
Enzyme 17 PDB File Show
Enzyme 17 3D Structure
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >987 bp
ATGGCCCGCACCGTGGTGCTCATCACCGGCTGTTCCTCGGGCATCGGCCTGCACTTGGCC
GTACGTCTGGCTTCAGATCCATCCCAGAGCTTCAAAGTGTATGCCACGTTGAGGGACCTG
AAAACACAGGGCCGGCTGTGGGAGGCGGCCCGGGCCCTGGCATGCCCTCCGGGATCCCTG
GAGACGTTGCAGCTGGACGTAAGGGACTCAAAATCCGTGGCCGCTGCCCGGGAACGCGTG
ACTGAGGGCCGCGTGGACGTGCTGGTGTGTAACGCAGGCCTGGGCCTGCTGGGGCCGCTG
GAGGCGCTGGGGGAGGACGCCGTGGCCTCTGTGCTGGACGTGAATGTAGTAGGGACTGTG
CGGATGCTGCAGGCCTTCCTGCCAGACATGAAGAGGCGCGGTTCGGGACGCGTGTTGGTG
ACCGGGAGCGTGGGAGGATTGATGGGGCTGCCTTTCAATGACGTTTATTGCGCCAGCAAG
TTCGCGCTCGAAGGCTTATGCGAGAGTCTGGCGGTTCTGCTGCTGCCCTTTGGGGTCCAC
TTGAGCCTGATCGAGTGCGGCCCAGTGCACACCGCCTTCATGGAGAAGGTGTTGGGCAGC
CCAGAGGAGGTGCTGGACCGCACGGACATCCACACCTTCCACCGCTTCTACCAATACCTC
GCCCACAGCAAGCAAGTCTTTCGCGAGGCGGCGCAGAACCCTGAGGAGGTGGCGGAGGTC
TTCCTCACCGCTTTGCGCGCCCCGAAGCCGACCCTGCGCTACTTCACCACCGAGCGCTTC
CTGCCCCTGCTGCGGATGCGCCTGGACGACCCCAGCGGCTCCAACTACGTCACCGCCATG
CACCGGGAAGTGTTCGGCGACGTTCCGGCAAAGGCCGAGGCTGGGGCCGAGGCTGGGGGC
GGGGCCGGGCCTGGGGCAGAGGACGAGGCCGGGCGCAGTGCGGTGGGGGACCCTGAGCTC
GGCGATCCTCCGGCCGCCCCGCAGTAA
Enzyme 17 GenBank Gene ID X13440 Link Image
Enzyme 17 GeneCard ID HSD17B1 Link Image
Enzyme 17 GenAtlas ID HSD17B1 Link Image
Enzyme 17 HGNC ID HGNC:5210 Link Image
Enzyme 17 Chromosome Location 17
Enzyme 17 Locus 17q11-q21
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 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. 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]
  7. 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]
  8. Galdes A, Auld DS, Vallee BL: Elucidation of the chemical nature of the steady-state intermediates in the mechanism of carboxypeptidase A. Biochemistry. 1986 Feb 11;25(3):646-51. [PubMed Link Image]
  9. 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]
  10. 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]
  11. 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]
  12. 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]
  13. 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]
  14. 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]
  15. 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 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 6129
Enzyme 18 Name 3-keto-steroid reductase
Enzyme 18 Synonyms
  1. Estradiol 17-beta- dehydrogenase 7
  2. 17-beta-HSD 7
  3. 17-beta-hydroxysteroid dehydrogenase 7
Enzyme 18 Gene Name HSD17B7
Enzyme 18 Protein Sequence >3-keto-steroid reductase
MRKVVLITGASSGIGLALCKRLLAEDDELHLCLACRNMSKAEAVCAALLASHPTAEVTIV
QVDVSNLQSVFRASKELKQRFQRLDCIYLNAGIMPNPQLNIKALFFGLFSRKVIHMFSTA
EGLLTQGDKITADGLQEVFETNVFGHFILIRELEPLLCHSDNPSQLIWTSSRSARKSNFS
LEDFQHSKGKEPYSSSKYATDLLSVALNRNFNQQGLYSNVACPGTALTNLTYGILPPFIW
TLLMPAILLLRFFANAFTLTPYNGTEALVWLFHQKPESLNPLIKYLSATTGFGRNYIMTQ
KMDLDEDTAEKFYQKLLELEKHIRVTIQKTDNQARLSGSCL
Enzyme 18 Number of Residues 341
Enzyme 18 Molecular Weight 38207
Enzyme 18 Theoretical pI 8.21
Enzyme 18 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
Enzyme 18 General Function Lipid transport and metabolism
Enzyme 18 Specific Function Responsible for the reduction of the keto group on the C-3 of sterols
Enzyme 18 Pathways
  • Androgen and Estrogen Metabolism (map00150 Link Image)
Enzyme 18 Reactions
  • 4alpha-methyl-5alpha-cholest-7-en-3beta-ol + NADP+ = 4alpha-methyl-5alpha-cholest-7-en-3-one + NADPH + H+
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • 1-19
Enzyme 18 Transmembrane Regions
  • 230-250
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 6721095 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID P56937 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name DHB7_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >1026 bp
ATGCGAAAGGTGGTTTTGATCACCGGGGCTAGCAGTGGCATTGGCCTGGCCCTCTGCAAG
CGGCTGCTGGCGGAAGATGATGAGCTTCATCTGTGTTTGGCGTGCAGGAACATGAGCAAG
GCAGAAGCTGTCTGTGCTGCTCTGCTGGCCTCTCACCCCACTGCTGAGGTCACCATTGTC
CAGGTGGATGTCAGCAACCTGCAGTCGGTCTTCCGGGCCTCCAAGGAACTTAAGCAAAGG
TTTCAGAGATTAGACTGTATATATCTAAATGCTGGGATCATGCCTAATCCACAACTAAAT
ATCAAAGCACTTTTCTTTGGCCTCTTTTCAAGAAAAGTGATTCATATGTTCTCCACAGCT
GAAGGCCTGCTGACCCAGGGTGATAAGATCACTGCTGATGGACTTCAGGAGGTGTTTGAG
ACCAATGTCTTTGGCCATTTTATCCTGATTCGGGAACTGGAGCCTCTCCTCTGTCACAGT
GACAATCCATCTCAGCTCATCTGGACATCATCTCGCAGTGCAAGGAAATCTAATTTCAGC
CTCGAGGACTTCCAGCACAGCAAAGGCAAGGAACCCTACAGCTCTTCCAAATATGCCACT
GACCTTTTGAGTGTGGCTTTGAACAGGAACTTCAACCAGCAGGGTCTCTATTCCAATGTG
GCCTGTCCAGGTACAGCATTGACCAATTTGACATATGGAATTCTGCCTCCGTTTATATGG
ACGCTGTTGATGCCGGCAATATTGCTACTTCGCTTTTTTGCAAATGCATTCACTTTGACA
CCATATAATGGAACAGAAGCTCTGGTATGGCTTTTCCACCAAAAGCCTGAATCTCTCAAT
CCTCTGATCAAATATCTGAGTGCCACCACTGGCTTTGGAAGAAATTATATTATGACCCAG
AAGATGGACCTAGATGAAGACACTGCTGAAAAATTTTATCAAAAGTTACTGGAACTGGAA
AAGCACATTAGGGTCACTATTCAAAAAACAGATAATCAGGCCAGGCTCAGTGGCTCATGC
CTATAA
Enzyme 18 GenBank Gene ID AF098786 Link Image
Enzyme 18 GeneCard ID HSD17B7 Link Image
Enzyme 18 GenAtlas ID HSD17B7 Link Image
Enzyme 18 HGNC ID HGNC:5215 Link Image
Enzyme 18 Chromosome Location 1
Enzyme 18 Locus 1q23
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 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. 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. 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]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 6306
Enzyme 19 Name Cytochrome P450 3A4
Enzyme 19 Synonyms
  1. Quinine 3-monooxygenase
  2. CYPIIIA4
  3. Nifedipine oxidase
  4. Taurochenodeoxycholate 6-alpha- hydroxylase
  5. NF-25
  6. P450-PCN1
Enzyme 19 Gene Name CYP3A4
Enzyme 19 Protein Sequence >Cytochrome P450 3A4
MALIPDLAMETWLLLAVSLVLLYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMF
DMECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISI
AEDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYS
MDVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICV
FPREVTNFLRKSVKRMKESRLEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSI
IFIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVLQMEYLDMVV
NETLRLFPIAMRLERVCKKDVEINGMFIPKGVVVMIPSYALHRDPKYWTEPEKFLPERFS
KKNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLG
GLLQPEKPVVLKVESRDGTVSGA
Enzyme 19 Number of Residues 503
Enzyme 19 Molecular Weight 57344
Enzyme 19 Theoretical pI 8.25
Enzyme 19 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 19 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 19 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 19 Pathways Not Available
Enzyme 19 Reactions
  • quinine + NADPH + H+ + O2 = 3-hydroxyquinine + NADP+ + H2O
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • 1-29
Enzyme 19 Transmembrane Regions Not Available
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 181374 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID P08684 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name CP3A4_HUMAN Link Image
Enzyme 19 PDB ID 1TQN Link Image
Enzyme 19 PDB File Show
Enzyme 19 3D Structure
Enzyme 19 Cellular Location Not Available
Enzyme 19 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 19 GenBank Gene ID M18907 Link Image
Enzyme 19 GeneCard ID CYP3A4 Link Image
Enzyme 19 GenAtlas ID CYP3A4 Link Image
Enzyme 19 HGNC ID HGNC:2637 Link Image
Enzyme 19 Chromosome Location 7
Enzyme 19 Locus 7q21.1
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. 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]
  2. 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]
  3. 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]
  4. 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]
  5. 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]
  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. 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]
  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. 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]
  10. 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]
  11. 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]
  12. 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]
  13. 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]
  14. 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]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 6324
Enzyme 20 Name Cytochrome P450 2C9
Enzyme 20 Synonyms
  1. (R-limonene 6-monooxygenase
  2. (S-limonene 6-monooxygenase
  3. (S- limonene 7-monooxygenase
  4. CYPIIC9
  5. P450 PB-1
  6. P450 MP-4/MP-8
  7. S- mephenytoin 4-hydroxylase
  8. P-450MP
Enzyme 20 Gene Name CYP2C9
Enzyme 20 Protein Sequence >Cytochrome P450 2C9
MDSLVVLVLCLSCLLLLSLWRQSSGRGKLPPGPTPLPVIGNILQIGIKDISKSLTNLSKV
YGPVFTLYFGLKPIVVLHGYEAVKEALIDLGEEFSGRGIFPLAERANRGFGIVFSNGKKW
KEIRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTKASPCDPTFILGCAPCNVICS
IIFHKRFDYKDQQFLNLMEKLNENIKILSSPWIQICNNFSPIIDYFPGTHNKLLKNVAFM
KSYILEKVKEHQESMDMNNPQDFIDCFLMKMEKEKHNQPSEFTIESLENTAVDLFGAGTE
TTSTTLRYALLLLLKHPEVTAKVQEEIERVIGRNRSPCMQDRSHMPYTDAVVHEVQRYID
LLPTSLPHAVTCDIKFRNYLIPKGTTILISLTSVLHDNKEFPNPEMFDPHHFLDEGGNFK
KSKYFMPFSAGKRICVGEALAGMELFLFLTSILQNFNLKSLVDPKNLDTTPVVNGFASVP
PFYQLCFIPV
Enzyme 20 Number of Residues 490
Enzyme 20 Molecular Weight 55629
Enzyme 20 Theoretical pI 7.99
Enzyme 20 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 20 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 20 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 20 Pathways
Enzyme 20 Reactions
  • (+)-(R)-limonene + NADPH + H+ + O2 = (+)-trans-carveol + NADP+ + H2O
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • 1-25
Enzyme 20 Transmembrane Regions Not Available
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 181366 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID P11712 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name CP2C9_HUMAN Link Image
Enzyme 20 PDB ID 1R9O Link Image
Enzyme 20 PDB File Show
Enzyme 20 3D Structure
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >1152 bp
AGAGGATTTGGAATTGTTTTCAGCAATGGAAAGAAATGGAAGGAGATCCGGCGTTTCTCC
CTCATGACGCTGCGGAATTTTGGGATGGGGAAGAGGAGCATTGAGGACCGTGTTCAAGAG
GAAGCCCGCTGCCTTGTGGAGGAGTTGAGAAAAACCAAGGCCTCACCCTGTGATCCCACT
TTCATCCTGGGCTGTGCTCCCTGCAATGTGATCTGCTCCATTATTTTCCATAAACGTTTT
GATTATAAAGATCAGCAATTTCTTAACTTAATGGAAAAGTTGAATGAAAACATCAAGATT
TTGAGCAGCCCCTGGATCCAGATCTGCAATAATTTTTCTCCTATCATTGATTACTTCCCG
GGAACTCACAACAAATTACTTAAAAACGTTGCTTTTATGAAAAGTTATATTTTGGAAAAA
GTAAAAGAACACCAAGAATCAATGGACATGAACAACCCTCAGGACTTTATTGATTGCTTC
CTGATGAAAATGGAGAAGGAAAAGCACAACCAACCATCAGAATTTACTATTGAAAGCTTG
GAAAACACTGCAGTTGACTTGTTTGGAGCTGGGACAGAGACGACAAGCACAACCCTGAGA
TATGCTCTCCTTCTCCTGCTGAAGCACCCAGAGGTCACAGCTAAAGTCCAGGAAGAGATT
GAACGTGTGATTGGCAGAAACCGGAGCCCCTGCATGCAAGACAGGAGCCACATGCCCTAC
ACAGATGCTGTGGTGCACGAGGTCCAGAGATGCATTGACCTTCTCCCCACCAGCCTGCCC
CATGCAGTGACCTGTGACATTAAATTCAGAAACTATCTCATTCCCAAGGGCACAACCATA
TTAATTTCCCTGACTTCTGTGCTACATGACAACAAAGAATTTCCCAACCCAGAGATGTTT
GACCCTCATCACTTTCTGGATGAAGGTGGCAATTTTAAGAAAAGTAAATACTTCATGCCT
TTCTCAGCAGGAAAACGGATTTGTGTGGGAGAAGCCCTGGCCGGCATGGAGCTGTTTTTA
TTCCTGACCTCCATTTTACAGAACTTTAACCTGAAATCTCTGGTTGACCCAAAGAACCTT
GACACCACTCCAGTTGTCAATGGATTTGCCTCTGTGCCGCCCTTCTACCAGCTGTGCTTC
ATTCCTGTCTGA
Enzyme 20 GenBank Gene ID M21940 Link Image
Enzyme 20 GeneCard ID CYP2C9 Link Image
Enzyme 20 GenAtlas ID CYP2C9 Link Image
Enzyme 20 HGNC ID HGNC:2623 Link Image
Enzyme 20 Chromosome Location 10
Enzyme 20 Locus 10q24
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 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]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 6326
Enzyme 21 Name Cytochrome P450 2C19
Enzyme 21 Synonyms
  1. (R-limonene 6-monooxygenase
  2. (S-limonene 6-monooxygenase
  3. (S- limonene 7-monooxygenase
  4. CYPIIC19
  5. P450-11A
  6. Mephenytoin 4- hydroxylase
  7. CYPIIC17
  8. P450-254C
Enzyme 21 Gene Name CYP2C19
Enzyme 21 Protein Sequence >Cytochrome P450 2C19
MDPFVVLVLCLSCLLLLSIWRQSSGRGKLPPGPTPLPVIGNILQIDIKDVSKSLTNLSKI
YGPVFTLYFGLERMVVLHGYEVVKEALIDLGEEFSGRGHFPLAERANRGFGIVFSNGKRW
KEIRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTKASPCDPTFILGCAPCNVICS
IIFQKRFDYKDQQFLNLMEKLNENIRIVSTPWIQICNNFPTIIDYFPGTHNKLLKNLAFM
ESDILEKVKEHQESMDINNPRDFIDCFLIKMEKEKQNQQSEFTIENLVITAADLLGAGTE
TTSTTLRYALLLLLKHPEVTAKVQEEIERVVGRNRSPCMQDRGHMPYTDAVVHEVQRYID
LIPTSLPHAVTCDVKFRNYLIPKGTTILTSLTSVLHDNKEFPNPEMFDPRHFLDEGGNFK
KSNYFMPFSAGKRICVGEGLARMELFLFLTFILQNFNLKSLIDPKDLDTTPVVNGFASVP
PFYQLCFIPV
Enzyme 21 Number of Residues 490
Enzyme 21 Molecular Weight 55932
Enzyme 21 Theoretical pI 7.42
Enzyme 21 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 21 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 21 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 21 Pathways
Enzyme 21 Reactions
  • (+)-(R)-limonene + NADPH + H+ + O2 = (+)-trans-carveol + NADP+ + H2O
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • 1-25
Enzyme 21 Transmembrane Regions Not Available
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 181344 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID P33261 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name CP2CJ_HUMAN Link Image
Enzyme 21 PDB ID 1R9O Link Image
Enzyme 21 PDB File Show
Enzyme 21 3D Structure
Enzyme 21 Cellular Location Not Available
Enzyme 21 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 21 GenBank Gene ID M61854 Link Image
Enzyme 21 GeneCard ID CYP2C19 Link Image
Enzyme 21 GenAtlas ID CYP2C19 Link Image
Enzyme 21 HGNC ID HGNC:2621 Link Image
Enzyme 21 Chromosome Location 10
Enzyme 21 Locus 10q24.1-q24.3
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 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. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 6840
Enzyme 22 Name Cytochrome P450 2E1
Enzyme 22 Synonyms
  1. CYPIIE1
  2. P450-J
Enzyme 22 Gene Name CYP2E1
Enzyme 22 Protein Sequence >Cytochrome P450 2E1
MSALGVTVALLVWAAFLLLVSMWRQVHSSWNLPPGPFPLPIIGNLFQLELKNIPKSFTRL
AQRFGPVFTLYVGSQRMVVMHGYKAVKEALLDYKDEFSGRGDLPAFHAHRDRGIIFNNGP
TWKDIRRFSLTTLRNYGMGKQGNESRIQREAHFLLEALRKTQGQPFDPTFLIGCAPCNVI
ADILFRKHFDYNDEKFLRLMYLFNENFHLLSTPWLQLYNNFPSFLHYLPGSHRKVIKNVA
EVKEYVSERVKEHHQSLDPNCPRDLTDCLLVEMEKEKHSAERLYTMDGITVTVADLFFAG
TETTSTTLRYGLLILMKYPEIEEKLHEEIDRVIGPSRIPAIKDRQEMPYMDAVVHEIQRF
ITLVPSNLPHEATRDTIFRGYLIPKGTVVVPTLDSVLYDNQEFPDPEKFKPEHFLNENGK
FKYSDYFKPFSTGKRVCAGEGLARMELFLLLCAILQHFNLKPLVDPKDIDLSPIHIGFGC
IPPRYKLCVIPRS
Enzyme 22 Number of Residues 493
Enzyme 22 Molecular Weight 56850
Enzyme 22 Theoretical pI 8.22
Enzyme 22 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 22 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 22 Specific Function Metabolizes several precarcinogens, drugs, and solvents to reactive metabolites
Enzyme 22 Pathways
Enzyme 22 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • 1-28
Enzyme 22 Transmembrane Regions Not Available
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 181360 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID P05181 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name CP2E1_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 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 22 GenBank Gene ID J02625 Link Image
Enzyme 22 GeneCard ID CYP2E1 Link Image
Enzyme 22 GenAtlas ID CYP2E1 Link Image
Enzyme 22 HGNC ID HGNC:2631 Link Image
Enzyme 22 Chromosome Location 10
Enzyme 22 Locus 10q24.3-qter
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 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. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 6843
Enzyme 23 Name Cytochrome P450 1B1
Enzyme 23 Synonyms
  1. CYPIB1
Enzyme 23 Gene Name CYP1B1
Enzyme 23 Protein Sequence >Cytochrome P450 1B1
MGTSLSPNDPWPLNPLSIQQTTLLLLLSVLATVHVGQRLLRQRRRQLRSAPPGPFAWPLI
GNAAAVGQAAHLSFARLARRYGDVFQIRLGSCPIVVLNGERAIHQALVQQGSAFADRPAF
ASFRVVSGGRSMAFGHYSEHWKVQRRAAHSMMRNFFTRQPRSRQVLEGHVLSEARELVAL
LVRGSADGAFLDPRPLTVVAVANVMSAVCFGCRYSHDDPEFRELLSHNEEFGRTVGAGSL
VDVMPWLQYFPNPVRTVFREFEQLNRNFSNFILDKFLRHCESLRPGAAPRDMMDAFILSA
EKKAAGDSHGGGARLDLENVPATITDIFGASQDTLSTALQWLLLLFTRYPDVQTRVQAEL
DQVVGRDRLPCMGDQPNLPYVLAFLYEAMRFSSFVPVTIPHATTANTSVLGYHIPKDTVV
FVNQWSVNHDPLKWPNPENFDPARFLDKDGLINKDLTSRVMIFSVGKRRCIGEELSKMQL
FLFISILAHQCDFRANPNEPAKMNFSYGLTIKPKSFKVNVTLRESMELLDSAVQNLQAKE
TCQ
Enzyme 23 Number of Residues 543
Enzyme 23 Molecular Weight 60847
Enzyme 23 Theoretical pI 9.23
Enzyme 23 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 23 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 23 Specific Function Participates in the metabolism of an as-yet-unknown biologically active molecule that is a participant in eye development
Enzyme 23 Pathways
Enzyme 23 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • 1-36
Enzyme 23 Transmembrane Regions Not Available
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 501031 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID Q16678 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name CP1B1_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 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 23 GenBank Gene ID U03688 Link Image
Enzyme 23 GeneCard ID CYP1B1 Link Image
Enzyme 23 GenAtlas ID CYP1B1 Link Image
Enzyme 23 HGNC ID HGNC:2597 Link Image
Enzyme 23 Chromosome Location 2
Enzyme 23 Locus 2p21
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 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. 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]
  4. 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]
  5. 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]
  6. 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]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 6847
Enzyme 24 Name Cytochrome P450 2F1
Enzyme 24 Synonyms
  1. CYPIIF1
Enzyme 24 Gene Name CYP2F1
Enzyme 24 Protein Sequence >Cytochrome P450 2F1
MDSISTAILLLLLALVCLLLTLSSRDKGKLPPGPRPLSILGNLLLLCSQDMLTSLTKLSK
EYGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSSGDR
WKVLRQFSIQILRNFGMGKRSIEERILEEGSFLLADVRKTEGEPFDPTFVLSRSVSNIIC
SVLFGSRFDYDDERLLTIIRLINDNFQIMSSPWGELYDILDPRFPSLLDWVPGPHQRIFQ
NFKCLRDLIAHSVHDHQASSPRDFIQCFLTKMAEEKEDPLSHFHMDTLLMTTHNLLFGGT
KTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFA
DIIPMNLPHRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSF
KKSPAFMPFSAGRRLCLGELLARMELFLYLTAILQSFSLQPLGAPEDIDLTPLSSGLGNL
PRPFQLCLRPR
Enzyme 24 Number of Residues 491
Enzyme 24 Molecular Weight 55500
Enzyme 24 Theoretical pI 7.40
Enzyme 24 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 24 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 24 Specific Function 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 24 Pathways
Enzyme 24 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • 1-24
Enzyme 24 Transmembrane Regions Not Available
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 181358 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID P24903 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name CP2F1_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >1476 bp
ATGGACAGCATAAGCACAGCCATCTTACTCCTGCTCCTGGCTCTCGTCTGTCTGCTCCTG
ACCCTAAGCTCAAGAGATAAGGGAAAGCTGCCTCCGGGACCCAGACCCCTCTCAATCCTG
GGAAACCTGCTGCTGCTTTGCTCCCAAGACATGCTGACTTCTCTCACTAAGCTGAGCAAG
GAGTATGGCTCCATGTACACAGTGCACCTGGGACCCAGGCGGGTGGTGGTCCTCAGCGGG
TACCAAGCTGTGAAGGAGGCCCTGGTGGACCAGGGAGAGGAGTTTAGTGGCCGCGGTGAC
TACCCTGCCTTTTTCAACTTTACCAAGGGCAATGGCATCGCCTTCTCCAGTGGGGATCGA
TGGAAGGTCCTGAGACAGTTCTCTATCCAGATTCTACGGAATTTCGGGATGGGGAAGAGA
AGCATTGAGGAGCGAATCCTAGAGGAGGGCAGCTTCCTGCTGGCGGACGTGCGGAAAACT
GAAGGCGAGCCCTTTGACCCCACGTTTGTGCTGAGTCGCTCAGTGTCCAACATTATCTGT
TCCGTGCTCTTCGGCAGCCGCTTCGACTATGATGATGAGCGTCTGCTCACCATTATCCGC
CTTATCAATGACAACTTCCAAATCATGAGCAGCCCCTGGGGCGAGTTGTACGACATCCTA
GACCCCAGATTCCCGAGCCTCCTGGACTGGGTGCCTGGGCCGCACCAACGCATCTTCCAG
AACTTCAAGTGCCTGAGAGACCTCATCGCCCACAGCGTCCACGACCACCAGGCCTCGTCT
CCCCGGGACTTCATCCAGTGCTTCCTCACCAAGATGGCAGAGGAGAAGGAGGACCCACTG
AGCCACTTCCACATGGATACCCTGCTGATGACCACACATAACCTGCTCTTTGGCGGCACC
AAGACGGTGAGCACCACGCTGCACCACGCCTTCCTGGCACTCATGAAGTACCCAAAAGTT
CAAGCCCGCGTGCAGGAGGAGATCGACCTCGTGGTGGGACGCGCGCGGCTGCCGGCGCTG
AAGGACCGCGCGGCCATGCCTTACACAGACGCGGTGATCCACGAGGTGCAGCGCTTTGCA
GACATCATCCCCATGAACTTGCCGCACCGCGTCACTAGGGACACGGCCTTTCGCGGCTTC
CTGATACCCAAGGGCACCGATGTCATCACCCTCCTTAACACCGTCCACTACGACCCCAGC
CAGTTCCTGACGCCCCAGGAGTTCAACCCCGAGCATTTTTTGGATGCCAATCAGTCCTTC
AAGAAGAGTCCAGCCTTCATGCCCTTCTCAGCTGGGCGCCGTCTGTGCCTGGGAGAGCTG
CTGGCGCGCATGGAGCTCTTTCTGTACCTCACCGCCATCCTGCAGAGCTTTTCGCTGCAG
CCGCTGGGTGCGCCCGAGGACATCGACCTGACCCCACTCAGCTCAGGTCTTGGCAATTTG
CCGCGGCCTTTCCAGCTGTGCCTGCGCCCGCGCTAA
Enzyme 24 GenBank Gene ID J02906 Link Image
Enzyme 24 GeneCard ID CYP2F1 Link Image
Enzyme 24 GenAtlas ID CYP2F1 Link Image
Enzyme 24 HGNC ID HGNC:2632 Link Image
Enzyme 24 Chromosome Location 19
Enzyme 24 Locus 19q13.2
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 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]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 6849
Enzyme 25 Name Cytochrome P450 2B6
Enzyme 25 Synonyms
  1. CYPIIB6
  2. P450 IIB1
Enzyme 25 Gene Name CYP2B6
Enzyme 25 Protein Sequence >Cytochrome P450 2B6
MELSVLLFLALLTGLLLLLVQRHPNTHDRLPPGPRPLPLLGNLLQMDRRGLLKSFLRFRE
KYGDVFTVHLGPRPVVMLCGVEAIREALVDKAEAFSGRGKIAMVDPFFRGYGVIFANGNR
WKVLRRFSVTTMRDFGMGKRSVEERIQEEAQCLIEELRKSKGALMDPTFLFQSITANIIC
SIVFGKRFHYQDQEFLKMLNLFYQTFSLISSVFGQLFELFSGFLKYFPGAHRQVYKNLQE
INAYIGHSVEKHRETLDPSAPKDLIDTYLLHMEKEKSNAHSEFSHQNLNLNTLSLFFAGT
ETTSTTLRYGFLLMLKYPHVAERVYREIEQVIGPHRPPELHDRAKMPYTEAVIYEIQRFS
DLLPMGVPHIVTQHTSFRGYIIPKDTEVFLILSTALHDPHYFEKPDAFNPDHFLDANGAL
KKTEAFIPFSLGKRICLGEGIARAELFLFFTTILQNFSMASPVAPEDIDLTPQECGVGKI
PPTYQIRFLPR
Enzyme 25 Number of Residues 491
Enzyme 25 Molecular Weight 56279
Enzyme 25 Theoretical pI 8.44
Enzyme 25 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 25 General Function Secondary metabolites biosynthesis, transport and catabolism
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
Enzyme 25 Pathways
Enzyme 25 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • 1-21
Enzyme 25 Transmembrane Regions Not Available
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 181296 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID P20813 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name CP2B6_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 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 25 GenBank Gene ID M29874 Link Image
Enzyme 25 GeneCard ID CYP2B6 Link Image
Enzyme 25 GenAtlas ID CYP2B6 Link Image
Enzyme 25 HGNC ID HGNC:2615 Link Image
Enzyme 25 Chromosome Location 19
Enzyme 25 Locus 19q13.2
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 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. 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]
  3. Thum T, Borlak J: Gene expression in distinct regions of the heart. Lancet. 2000 Mar 18;355(9208):979-83. [PubMed Link Image]
  4. 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]
  5. 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]
  6. 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]
  7. 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 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 6852
Enzyme 26 Name Cytochrome P450 2A13
Enzyme 26 Synonyms
  1. CYPIIA13
Enzyme 26 Gene Name CYP2A13
Enzyme 26 Protein Sequence >Cytochrome P450 2A13
MLASGLLLVTLLACLTVMVLMSVWRQRKSRGKLPPGPTPLPFIGNYLQLNTEQMYNSLMK
ISERYGPVFTIHLGPRRVVVLCGHDAVKEALVDQAEEFSGRGEQATFDWLFKGYGVAFSN
GERAKQLRRFSIATLRGFGVGKRGIEERIQEEAGFLIDALRGTHGANIDPTFFLSRTVSN
VISSIVFGDRFDYEDKEFLSLLRMMLGSFQFTATSTGQLYEMFSSVMKHLPGPQQQAFKE
LQGLEDFIAKKVEHNQRTLDPNSPRDFIDSFLIRMQEEEKNPNTEFYLKNLVMTTLNLFF
AGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGKNRQPKFEDRAKMPYTEAVIHEIQ
RFGDMLPMGLAHRVNKDTKFRDFFLPKGTEVFPMLGSVLRDPRFFSNPRDFNPQHFLDKK
GQFKKSDAFVPFSIGKRYCFGEGLARMELFLFFTTIMQNFRFKSPQSPKDIDVSPKHVGF
ATIPRNYTMSFLPR
Enzyme 26 Number of Residues 494
Enzyme 26 Molecular Weight 56688
Enzyme 26 Theoretical pI 9.78
Enzyme 26 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 26 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 26 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
Enzyme 26 Pathways
Enzyme 26 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • 1-22
Enzyme 26 Transmembrane Regions Not Available
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 1777437 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID Q16696 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name CP2AD_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >1485 bp
ATGCTGGCCTCAGGGCTGCTTCTGGTGACCTTGCTGGCCTGCCTGACTGTGATGGTCTTG
ATGTCAGTCTGGCGGCAGAGGAAGAGCAGGGGGAAGCTGCCTCCGGGACCCACCCCATTG
CCCTTCATTGGAAACTACCTCCAGCTGAACACAGAGCAGATGTACAACTCCCTCATGAAG
ATCAGTGAGCGCTATGGCCCTGTGTTCACCATTCACTTGGGGCCCCGGCGGGTCGTGGTG
CTGTGCGGACATGATGCCGTCAAGGAGGCTCTGGTGGACCAGGCTGAGGAGTTCAGCGGG
CGAGGCGAGCAGGCCACCTTCGACTGGCTCTTCAAAGGCTATGGCGTGGCGTTCAGCAAC
GGGGAGCGCGCCAAGCAGCTCCGGCGCTTCTCCATCGCCACCCTAAGGGGTTTTGGCGTG
GGCAAGCGCGGCATCGAGGAACGCATCCAGGAGGAGGCGGGCTTCCTCATCGACGCCCTC
CGGGGCACGCACGGCGCCAATATCGATCCCACCTTCTTCCTGAGCCGCACAGTCTCCAAT
GTCATCAGCTCCATTGTCTTTGGGGACCGCTTTGACTATGAGGACAAAGAGTTCCTGTCA
CTGTTGCGCATGATGCTGGGAAGGTTCCAGTTCACGGGAACCTCCACGGGGCAGCTCTAT
GAGATGTTCTCTTCGGTGATGAAACACCTGCCAGGACCACAGCAACAGGCCTTTAAGGAG
CTGCAAGGGCTGGAGGACTTCATCGCCAAGAAGGTGGAGCACAACCAGCGCACGCTGGAT
CCCAATTCCCCACGGGACTTCATCGACTCCTTTCTCATCCGCATGCAGGAGGAGGAGAAG
AACCCCAACACAGAGTTCTACTTGAAGAACCTGGTGATGACCACCCTGAACCTCTTCTTT
GCGGGCACTGAGACCGTGAGCACCACCCTGCGCTACGGTTTCCTGCTGCTCATGAAGCAC
CCAGAGGTGGAGGCCAAGGTCCATGAGGAGATTGACAGAGTGATCGGCAAGAACCGGCAG
CCCAAGTTTGAGGACCGGGCCAAGATGCCCTACACAGAGGCAGTGATCCACGAGATCCAA
AGATTTGGAGACATGCTCCCCATGGGTTTGGCCCACAGGGTCAACAAGGACACCAAGTTT
CGGGATTTCTTCCTCCCTAAGGGCACTGAAGTGTTCCCTATGCTGGGCTCCGAGCTGAGA
GACCCCAGGTTCTTCTCCAACCCCCAGGACTGCAGTCCCCAGCACTTCCTGGATGAGAAG
GGGCAGTTTAAGAAGAGTGATGCTTTTGTGCCCTTTTCCATCGGAAAGCGGTACTGTTTT
GGAGAAGGCCTGGCCAGAATGGAGCTCTTTCTCTTCTTCACCACCATCATGCAGAACTTT
CGCTTCAAGTCCCCTCAGTCGCCTAAGGATATCGACGTGTCCCCCAAACACGTGGGCTTT
GCCACGATCCCACGAAACTACACCATGAGCTTCCTGCCCCGCTGA
Enzyme 26 GenBank Gene ID U22028 Link Image
Enzyme 26 GeneCard ID CYP2A13 Link Image
Enzyme 26 GenAtlas ID CYP2A13 Link Image
Enzyme 26 HGNC ID HGNC:2608 Link Image
Enzyme 26 Chromosome Location 19
Enzyme 26 Locus 19q13.2
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 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. 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]
  4. 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 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 6854
Enzyme 27 Name Cytochrome P450 4B1
Enzyme 27 Synonyms
  1. CYPIVB1
  2. P450-HP
Enzyme 27 Gene Name CYP4B1
Enzyme 27 Protein Sequence >Cytochrome P450 4B1
MVPSFLSLSFSSLGLWASGLILVLGFLKLIHLLLRRQTLAKAMDKFPGPPTHWLFGHALE
IQETGSLDKVVSWAHQFPYAHPLWFGQFIGFLNIYEPDYAKAVYSRGDPKAPDVYDFFLQ
WIGRGLLVLEGPKWLQHRKLLTPGFHYDVLKPYVAVFTESTRIMLDKWEEKAREGKSFDI
FCDVGHMALNTLMKCTFGRGDTGLGHRDSSYYLAVSDLTLLMQQRLVSFQYHNDFIYWLT
PHGRRFLRACQVAHDHTDQVIRERKAALQDEKVRKKIQNRRHLDFLDILLGARDEDDIKL
SDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDL
GKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRSLPAGSLISMHIYALHRNSAVWP
DPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDP
SRLPIKMPQLVLRSKNGFHLHLKPLGPGSGK
Enzyme 27 Number of Residues 511
Enzyme 27 Molecular Weight 58992
Enzyme 27 Theoretical pI 8.39
Enzyme 27 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 27 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 27 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 27 Pathways
Enzyme 27 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • 1-40
Enzyme 27 Transmembrane Regions Not Available
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 180969 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID P13584 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name CP4B1_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >1536 bp
ATGGTGCCCAGCTTCCTCTCCCTGAGCTTCTCCTCCTTGGGCCTGTGGGCTTCTGGGCTG
ATCTTGGTCTTAGGCTTTCTCAAGCTCATCCACCTGCTGCTGCGGAGGCGAACGTTGGCT
AAGGCTATGGACAAATTCCCAGGGCCTCCCACCCACTGGCTTTTTGGACATGCCCTCGAG
ATCCAGGAGACGGGGAGCCTGGACAAAGTGGTGTCCTGGGCCCACCAGTTCCCGTATGCC
CACCCACTCTGGTTCGGACAGTTCATTGGCTTCCTGAACATCTATGAGCCTGACTATGCC
AAAGCTGTGTACAGCCGTGGGGACCCTAAGGCCCCTGATGTGTATGACTTCTTCCTCCAG
TGGATTGGGAGAGGCCTGCTGGTTCTTGAGGGGCCCAAGTGGTTGCAGCACCGCAAGCTG
CTCACACCTGGCTTTCATTATGATGTGCTGAAGCCCTATGTGGCCGTGTTCACTGAGTCT
ACACGTATCATGCTGGACAAGTGGGAAGAGAAAGCTCGGGAGGGTAAGTCCTTTGACATC
TTCTGCGATGTGGGTCACATGGCGCTGAACACACTCATGAAGTGCACCTTTGGAAGAGGA
GACACCGGCCTGGGCCACAGGGACAGCAGCTACTACCTTGCAGTCAGCGATCTCACTCTG
TTGATGCAGCAGCGCCTTGTGTCCTTCCAGTACCATAATGACTTCATCTACTGGCTCACC
CCACATGGCCGCCGCTTCCTGCGGGCCTGCCAGGTGGCCCATGACCATACAGACCAGGTC
ATCAGGGAGCGGAAGGCAGCCCTGCAGGATGAGAAGGTGCGGAAGAAGATCCAGAACCGG
AGGCACCTGGACTTCCTGGACATTCTCCTGGGTGCCCGGGATGAAGATGACATCAAACTG
TCAGATGCAGACCTCCGGGCTGAAGTGGACACATTCATGTTTGAAGGCCATGACACCACC
ACCAGTGGTATCTCCTGGTTTCTCTACTGCATGGCCCTGTACCCTGAGCACCAGCATCGT
TGTAGAGAGGAGGTCCGCGAGATCCTAGGGGACCAGGACTTCTTCCAGTGGGATGATCTG
GGCAAAATGACTTATCTGACCATGTGCATCAAGGAGAGCTTCCGCCTCTACCCACCTGTG
CCCCAGGTGTACCGCCAGCTCAGCAAGCCTGTCACCTTTGTGGATGGCCGGTCTCTACCT
GCAGGAAGCCTGATCTCTATGCATATCTATGCCCTCCATAGGAACAGTGCTGTATGGCCC
GACCCTGAGGTCTTTGACTCTCTGCGCTTTTCCACTGAGAATGCATCCAAACGCCATCCC
TTTGCCTTTATGCCCTTCTCTGCTGGGCCCAGGAACTGCATTGGGCAGCAGTTTGCCATG
AGTGAGATGAAGGTGGTCACAGCCATGTGCTTGCTCCGCTTTGAGTTCTCTCTGGACCCC
TCACGGCTGCCCATCAAGATGCCCCAGCTTGTCCTGCGCTCCAAGAATGGCTTTCACCTC
CACCTGAAGCCACTGGGCCCTGGGTCTGGGAAGTAG
Enzyme 27 GenBank Gene ID J02871 Link Image
Enzyme 27 GeneCard ID CYP4B1 Link Image
Enzyme 27 GenAtlas ID CYP4B1 Link Image
Enzyme 27 HGNC ID HGNC:2644 Link Image
Enzyme 27 Chromosome Location 1
Enzyme 27 Locus 1p34-p12
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 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]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 6855
Enzyme 28 Name Cytochrome P450 4Z1
Enzyme 28 Synonyms
  1. CYPIVZ1
Enzyme 28 Gene Name CYP4Z1
Enzyme 28 Protein Sequence >Cytochrome P450 4Z1
MEPSWLQELMAHPFLLLILLCMSLLLFQVIRLYQRRRWMIRALHLFPAPPAHWFYGHKEF
YPVKEFEVYHKLMEKYPCAVPLWVGPFTMFFSVHDPDYAKILLKRQDPKSAVSHKILESW
VGRGLVTLDGSKWKKHRQIVKPGFNISILKIFITMMSESVRMMLNKWEEHIAQNSRLELF
QHVSLMTLDSIMKCAFSHQGSIQLDSTLDSYLKAVFNLSKISNQRMNNFLHHNDLVFKFS
SQGQIFSKFNQELHQFTEKVIQDRKESLKDKLKQDTTQKRRWDFLDILLSAKSENTKDFS
EADLQAEVKTFMFAGHDTTSSAISWILYCLAKYPEHQQRCRDEIRELLGDGSSITWEHLS
QMPYTTMCIKECLRLYAPVVNISRLLDKPITFPDGRSLPAGITVFINIWALHHNPYFWED
PQVFNPLRFSRENSEKIHPYAFIPFSAGLRNCIGQHFAIIECKVAVALTLLRFKLAPDHS
RPPQPVRQVVLKSKNGIHVFAKKVC
Enzyme 28 Number of Residues 505
Enzyme 28 Molecular Weight 59087
Enzyme 28 Theoretical pI 9.63
Enzyme 28 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 28 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 28 Specific Function RH + reduced flavoprotein + O(2) = ROH + oxidized flavoprotein + H(2)O
Enzyme 28 Pathways
Enzyme 28 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • 1-23
Enzyme 28 Transmembrane Regions
  • 139-156
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 29690384 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID Q86W10 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name CP4Z1_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >1518 bp
ATGGAGCCCTCCTGGCTTCAGGAACTCATGGCTCACCCCTTCTTGCTGCTGATCCTCCTC
TGCATGTCTCTGCTGCTGTTTCAGGTAATCAGGTTGTACCAGAGGAGGAGATGGATGATC
AGAGCCCTGCACCTGTTTCCTGCACCCCCTGCCCACTGGTTCTATGGCCACAAGGAGTTT
TACCCAGTAAAGGAGTTTGAGGTGTATCATAAGCTGATGGAAAAATACCCATGTGCTGTT
CCCTTGTGGGTTGGACCCTTTACGATGTTCTTCAGTGTCCATGACCCAGACTATGCCAAG
ATTCTCCTGAAAAGACAAGATCCCAAAAGTGCTGTTAGCCACAAAATCCTTGAATCCTGG
GTTGGTCGAGGACTTGTGACCCTGGATGGTTCTAAATGGAAAAAGCACCGCCAGATTGTG
AAACCTGGCTTCAACATCAGCATTCTGAAAATATTCATCACCATGATGTCTGAGAGTGTT
CGGATGATGCTGAACAAATGGGAGGAACACATTGCCCAAAACTCACGTCTGGAGCTCTTT
CAACATGTCTCCCTGATGACCCTGGACAGCATCATGAAGTGTGCCTTCAGCCACCAGGGC
AGCATCCAGTTGGACAGTACCCTGGACTCATACCTGAAAGCAGTGTTCAACCTTAGCAAA
ATCTCCAACCAGCGCATGAACAATTTTCTACATCACAACGACCTGGTTTTCAAATTCAGC
TCTCAAGGCCAAATCTTTTCTAAATTTAACCAAGAACTTCATCAGTTCACAGAGAAAGTA
ATCCAGGACCGGAAGGAGTCTCTTAAGGATAAGCTAAAACAAGATACTACTCAGAAAAGG
CGCTGGGATTTTCTGGACATACTTTTGAGTGCCAAAAGCGAAAACACCAAAGATTTCTCT
GAAGCAGATCTCCAGGCTGAAGTGAAAACGTTCATGTTTGCAGGACATGACACCACATCC
AGTGCTATCTCCTGGATCCTTTACTGCTTGGCAAAGTACCCTGAGCATCAGCAGAGATGC
CGAGATGAAATCAGGGAACTCCTAGGGGATGGGTCTTCTATTACCTGGGAACACCTGAGC
CAGATGCCTTACACCACGATGTGCATCAAGGAATGCCTCCGCCTCTACGCACCGGTAGTA
AACATATCCCGGTTACTCGACAAACCCATCACCTTTCCAGATGGACGCTCCTTACCTGCA
GGAATAACTGTGTTTATCAATATTTGGGCTCTTCACCACAACCCCTATTTCTGGGAAGAC
CCTCAGGTCTTTAACCCCTTGAGATTCTCCAGGGAAAATTCTGAAAAAATACATCCCTAT
GCCTTCATACCATTCTCAGCTGGATTAAGGAACTGCATTGGGCAGCATTTTGCCATAATT
GAGTGTAAAGTGGCAGTGGCATTAACTCTGCTCCGCTTCAAGCTGGCTCCAGACCACTCA
AGGCCTCCCCAGCCTGTTCGTCAAGTTGTCCTCAAGTCCAAGAATGGAATCCATGTGTTT
GCAAAAAAAGTTTGCTAA
Enzyme 28 GenBank Gene ID AY262056 Link Image
Enzyme 28 GeneCard ID CYP4Z1 Link Image
Enzyme 28 GenAtlas ID CYP4Z1 Link Image
Enzyme 28 HGNC ID HGNC:20583 Link Image
Enzyme 28 Chromosome Location 1
Enzyme 28 Locus 1p33
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 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]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 6856
Enzyme 29 Name Cytochrome P450 1A2
Enzyme 29 Synonyms
  1. CYPIA2
  2. P450-P3
  3. P(3450
  4. P450 4
Enzyme 29 Gene Name CYP1A2
Enzyme 29 Protein Sequence >Cytochrome P450 1A2
MALSQSVPFSATELLLASAIFCLVFWVLKGLRPRVPKGLKSPPEPWGWPLLGHVLTLGKN
PHLALSRMSQRYGDVLQIRIGSTPVLVLSRLDTIRQALVRQGDDFKGRPDLYTSTLITDG
QSLTFSTDSGPVWAARRRLAQNALNTFSIASDPASSSSCYLEEHVSKEAKALISRLQELM
AGPGHFDPYNQVVVSVANVIGAMCFGQHFPESSDEMLSLVKNTHEFVETASSGNPLDFFP
ILRYLPNPALQRFKAFNQRFLWFLQKTVQEHYQDFDKNSVRDITGALFKHSKKGPRASGN
LIPQEKIVNLVNDIFGAGFDTVTTAISWSLMYLVTKPEIQRKIQKELDTVIGRERRPRLS
DRPQLPYLEAFILETFRHSSFLPFTIPHSTTRDTTLNGFYIPKKCCVFVNQWQVNHDPEL
WEDPSEFRPERFLTADGTAINKPLSEKMMLFGMGKRRCIGEVLAKWEIFLFLAILLQQLE
FSVPPGVKVDLTPIYGLTMKHARCEHVQARRFSIN
Enzyme 29 Number of Residues 515
Enzyme 29 Molecular Weight 58295
Enzyme 29 Theoretical pI 9.43
Enzyme 29 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 29 General Function Secondary metabolites biosynthesis, transport and catabolism
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. 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
Enzyme 29 Pathways
Enzyme 29 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • 1-30
Enzyme 29 Transmembrane Regions Not Available
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 30339 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID P05177 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name CP1A2_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 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 29 GenBank Gene ID Z00036 Link Image
Enzyme 29 GeneCard ID CYP1A2 Link Image
Enzyme 29 GenAtlas ID CYP1A2 Link Image
Enzyme 29 HGNC ID HGNC:2596 Link Image
Enzyme 29 Chromosome Location 15
Enzyme 29 Locus 15q24
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 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. 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]
  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. 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]
  9. Chevalier D, Cauffiez C, Allorge D, Lo-Guidice JM, Lhermitte M, Lafitte JJ, Broly F: Five novel natural allelic variants-951A&gt;C, 1042G&gt;A (D348N), 1156A&gt;T (I386F), 1217G&gt;A (C406Y) and 1291C&gt;T (C431Y)-of the human CYP1A2 gene in a French Caucasian population. Hum Mutat. 2001 Apr;17(4):355-6. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 6857
Enzyme 30 Name Cytochrome P450 19A1
Enzyme 30 Synonyms
  1. Aromatase
  2. CYPXIX
  3. Estrogen synthetase
  4. P-450AROM
Enzyme 30 Gene Name CYP19A1
Enzyme 30 Protein Sequence >Cytochrome P450 19A1
MVLEMLNPIHYNITSIVPEAMPAATMPVLLLTGLFLLVWNYEGTSSIPGPGYCMGIGPLI
SHGRFLWMGIGSACNYYNRVYGEFMRVWISGEETLIISKSSSMFHIMKHNHYSSRFGSKL
GLQCIGMHEKGIIFNNNPELWKTTRPFFMKALSGPGLVRMVTVCAESLKTHLDRLEEVTN
ESGYVDVLTLLRRVMLDTSNTLFLRIPLDESAIVVKIQGYFDAWQALLIKPDIFFKISWL
YKKYEKSVKDLKDAIEVLIAEKRRRISTEEKLEECMDFATELILAEKRGDLTRENVNQCI
LEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKIDDIQKLKVMENFI
YESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHRLEFFPKPNEFTLENFAK
NVPYRYFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQCVESIQKIHDLSLH
PDETKNMLEMIFTPRNSDRCLEH
Enzyme 30 Number of Residues 503
Enzyme 30 Molecular Weight 57884
Enzyme 30 Theoretical pI 7.56
Enzyme 30 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 30 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 30 Specific Function Catalyzes the formation of aromatic C18 estrogens from C19 androgens
Enzyme 30 Pathways
Enzyme 30 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • None
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 179002 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID P11511 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name CP19A_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 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
CCAGATGAGACTAAAAACATGCTGGAAATGATCTTTACCCCAAGAAGCTCAGACAGGTGT
CTGGAACACTAG
Enzyme 30 GenBank Gene ID M22246 Link Image
Enzyme 30 GeneCard ID CYP19A1 Link Image
Enzyme 30 GenAtlas ID CYP19A1 Link Image
Enzyme 30 HGNC ID HGNC:2594 Link Image
Enzyme 30 Chromosome Location 15
Enzyme 30 Locus 15q21.1
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 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. 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]
  9. 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]
  10. 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]
  11. 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]
  12. 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]
  13. 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]
  14. 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]
  15. 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]
  16. 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]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 6858
Enzyme 31 Name Cytochrome P450 2C8
Enzyme 31 Synonyms
  1. CYPIIC8
  2. P450 form 1
  3. P450 MP- 12/MP-20
  4. P450 IIC2
  5. S-mephenytoin 4-hydroxylase
Enzyme 31 Gene Name CYP2C8
Enzyme 31 Protein Sequence >Cytochrome P450 2C8
MEPFVVLVLCLSFMLLFSLWRQSCRRRKLPPGPTPLPIIGNMLQIDVKDICKSFTNFSKV
YGPVFTVYFGMNPIVVFHGYEAVKEALIDNGEEFSGRGNSPISQRITKGLGIISSNGKRW
KEIRRFSLTTLRNFGMGKRSIEDRVQEEAHCLVEELRKTKASPCDPTFILGCAPCNVICS
VVFQKRFDYKDQNFLTLMKRFNENFRILNSPWIQVCNNFPLLIDCFPGTHNKVLKNVALT
RSYIREKVKEHQASLDVNNPRDFIDCFLIKMEQEKDNQKSEFNIENLVGTVADLFVAGTE
TTSTTLRYGLLLLLKHPEVTAKVQEEIDHVIGRHRSPCMQDRSHMPYTDAVVHEIQRYSD
LVPTGVPHAVTTDTKFRNYLIPKGTTIMALLTSVLHDDKEFPNPNIFDPGHFLDKNGNFK
KSDYFMPFSAGKRICAGEGLARMELFLFLTTILQNFNLKSVDDLKNLNTTAVTKGIVSLP
PSYQICFIPV
Enzyme 31 Number of Residues 490
Enzyme 31 Molecular Weight 55825
Enzyme 31 Theoretical pI 8.62
Enzyme 31 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 31 General Function Secondary metabolites biosynthesis, transport and catabolism
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. 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 31 Pathways
Enzyme 31 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • 1-26
Enzyme 31 Transmembrane Regions
  • 60-82
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 181326 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID P10632 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name CP2C8_HUMAN Link Image
Enzyme 31 PDB ID 1PQ2 Link Image
Enzyme 31 PDB File Show
Enzyme 31 3D Structure
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >1473 bp
ATGGAACCTTTTGTGGTCCTGGTGCTGTGTCTCTCTTTTATGCTTCTCTTTTCACTCTGG
AGACAGAGCTGTAGGAGAAGGAAGCTCCCTCCTGGCCCCACTCCTCTTCCTATTATTGGA
AATATGCTACAGATAGATGTTAAGGACATCTGCAAATCTTTCACCAATTTCTCAAAAGTC
TATGGTCCTGTGTTCACCGTGTATTTTGGCATGAATCCCATAGTGGTGTTTCATGGATAT
GAGGCAGTGAAGGAAGCCCTGATTGATAATGGAGAGGAGTTTTCTGGAAGAGGCAATTCC
CCAATATCTCAAAGAATTACTAAAGGACTTGGAATCATTTCCAGCAATGGAAAGAGATGG
AAGGAGATCCGGCGTTTCTCCCTCACAAACTTGCGGAATTTTGGGATGGGGAAGAGGAGC
ATTGAGGACCGTGTTCAAGAGGAAGCTCACTGCCTTGTGGAGGAGTTGAGAAAAACCAAG
GCTTCACCCTGTGATCCCACTTTCATCCTGGGCTGTGCTCCCTGCAATGTGATCTGCTCC
GTTGTTTTCCAGAAACGATTTGATTATAAAGATCAGAATTTTCTCACCCTGATGAAAAGA
TTCAATGAAAACTTCAGGATTCTGAACTCCCCATGGATCCAGGTCTGCAATAATTTCCCT
CTACTCATTGATTGTTTCCCAGGAACTCACAACAAAGTGCTTAAAAATGTTGCTCTTACA
CGAAGTTACATTAGGGAGAAAGTAAAAGAACACCAAGCATCACTGGATGTTAACAATCCT
CGGGACTTTATGGATTGCTTCCTGATCAAAATGGAGCAGGAAAAGGACAACCAAAAGTCA
GAATTCAATATTGAAAACTTGGTTGGCACTGTAGCTGATCTATTTGTTGCTGGAACAGAG
ACAACAAGCACCACTCTGAGATATGGACTCCTGCTCCTGCTGAAGCACCCAGAGGTCACA
GCTAAAGTCCAGGAAGAGATTGATCATGTAATTGGCAGACACAGGAGCCCCTGCATGCAG
GATAGGAGCCACATGCCTTACACTGATGCTGTAGTGCACGAGATCCAGAGATACAGTGAC
CTTGTCCCCACCGGTGTGCCCCATGCAGTGACCACTGATACTAAGTTCAGAAACTACCTC
ATCCCCAAGGGCACAACCATAATGGCATTACTGACTTCCGTGCTACATGATGACAAAGAA
TTTCCTAATCCAAATATCTTTGACCCTGGCCACTTTCTAGATAAGAATGGCAACTTTAAG
AAAAGTGACTACTTCATGCCTTTCTCAGCAGGAAAACGAATTTGTGCAGGAGAAGGACTT
GCCCGCATGGAGCTATTTTTATTTCTAACCACAATTTTACAGAACTTTAACCTGAAATCT
GTTGATGATTTAAAGAACCTCAATACTACTGCAGTTACCAAAGGGATTGTTTCTCTGCCA
CCCTCATACCAGATCTGCTTCATCCCTGTCTGA
Enzyme 31 GenBank Gene ID M17397 Link Image
Enzyme 31 GeneCard ID CYP2C8 Link Image
Enzyme 31 GenAtlas ID CYP2C8 Link Image
Enzyme 31 HGNC ID HGNC:2622 Link Image
Enzyme 31 Chromosome Location 10
Enzyme 31 Locus 10q23.33
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 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. 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]
  5. 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]
  6. 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]
  7. 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]
  8. Kolyada AY: Sequence of a human liver cytochrome P-450 cDNA clone. Nucleic Acids Res. 1990 Sep 25;18(18):5550. [PubMed Link Image]
  9. 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]
  10. 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]
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 6859
Enzyme 32 Name Cytochrome P450 2S1
Enzyme 32 Synonyms
  1. CYPIIS1
Enzyme 32 Gene Name CYP2S1
Enzyme 32 Protein Sequence >Cytochrome P450 2S1
MEATGTWALLLALALLLLLTLALSGTRARGHLPPGPTPLPLLGNLLQLRPGALYSGLMRL
SKKYGPVFTIYLGPWRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFSN
GERWRQLRKFTMLALRDLGMGKREGEELIQAEARCLVETFQGTEGRPFDPSLLLAQATSN
VVCSLLFGLRFSYEDKEFQAVVRAAGGTLLGVSSQGGQTYEMFSWFLRPLPGPHKQLLHH
VSTLAAFTVRQVQQHQGNLDASGPARDLVDAFLLKMAQEEQNPGTEFTNKNMLMTVIYLL
FAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEA
QRLLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDA
DGRFRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSLESPCPPDTLSLKPTVSG
LFNIPPAFQLQVRPTDLHSTTQTR
Enzyme 32 Number of Residues 504
Enzyme 32 Molecular Weight 55818
Enzyme 32 Theoretical pI 8.84
Enzyme 32 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 32 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 32 Specific Function Has a potential importance for extrahepatic xenobiotic metabolism
Enzyme 32 Pathways
Enzyme 32 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • 1-28
Enzyme 32 Transmembrane Regions
  • 297-319
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 13161184 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID Q96SQ9 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name CP2S1_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 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 32 GenBank Gene ID AF335278 Link Image
Enzyme 32 GeneCard ID CYP2S1 Link Image
Enzyme 32 GenAtlas ID CYP2S1 Link Image
Enzyme 32 HGNC ID HGNC:15654 Link Image
Enzyme 32 Chromosome Location 19
Enzyme 32 Locus 19q13.1
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 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]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 6861
Enzyme 33 Name Cytochrome P450 2J2
Enzyme 33 Synonyms
  1. CYPIIJ2
  2. Arachidonic acid epoxygenase
Enzyme 33 Gene Name CYP2J2
Enzyme 33 Protein Sequence >Cytochrome P450 2J2
MLAAMGSLAAALWAVVHPRTLLLGTVAFLLAADFLKRRRPKNYPPGPWRLPFLGNFFLVD
FEQSHLEVQLFVKKYGNLFSLELGDISAVLITGLPLIKEALIHMDQNFGNRPVTPMREHI
FKKNGLIMSSGQAWKEQRRFTLTALRNFGLGKKSLEERIQEEAQHLTEAIKEENGQPFDP
HFKINNAVSNIICSITFGERFEYQDSWFQQLLKLLDEVTYLEASKTCQLYNVFPWIMKFL
PGPHQTLFSNWKKLKLFVSHMIDKHRKDWNPAETRDFIDAYLKEMSKHTGNPTSSFHEEN
LICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQGQQPSTAARESMP
YTNAVIHEVQRMGNIIPLNVPREVTVDTTLAGYHLPKGTMILTNLTALHRDPTEWATPDT
FNPDHFLENGQFKKREAFMPFSIGKRACLGEQLARTELFIFFTSLMQKFTFRPPNNEKLS
LKFRMGITISPVSHRLCAVPQV
Enzyme 33 Number of Residues 502
Enzyme 33 Molecular Weight 57611
Enzyme 33 Theoretical pI 8.87
Enzyme 33 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 33 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 33 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 33 Pathways
Enzyme 33 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • 1-32
Enzyme 33 Transmembrane Regions
  • 75-97
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 18254513 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID P51589 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name CP2J2_HUMAN Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 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 33 GenBank Gene ID U37143 Link Image
Enzyme 33 GeneCard ID CYP2J2 Link Image
Enzyme 33 GenAtlas ID CYP2J2 Link Image
Enzyme 33 HGNC ID HGNC:2634 Link Image
Enzyme 33 Chromosome Location 1
Enzyme 33 Locus 1p31.3-p31.2
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 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]
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 6862
Enzyme 34 Name Cytochrome P450 2A7
Enzyme 34 Synonyms
  1. CYPIIA7
  2. P450-IIA4
Enzyme 34 Gene Name CYP2A7
Enzyme 34 Protein Sequence >Cytochrome P450 2A7
MLASGLLLVALLACLTVMVLMSVWQQRKSRGKLPPGPTPLPFIGNYLQLNTEHICDSIMK
FSECYGPVFTIHLGPRRVVVLCGHDAVREALVDQAEEFSGRGEQATFDWVFKGYGVAFSN
GERAKQLLRFAIATLRDFGVGKRGIEERIQEESGFLIEAIRSSHGANIDPTFFLSRTVSN
VISSIVFGDRFDYEDKEFLSLLSMMLGIFQFTSTSTGQLYEMFSSVMKHLPGPQQQAFKL
LQGLEDFIAKKVEHNQRTLDPNSPQDFIDSFLIHMQEEEKNPNTEFYLKNLMMSTLNLFI
AGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGKNRQPKFEDRTKMPYMEAVIHEIQ
RFGDVIPMSLARRVKKDTKFRDFFLPKGTEVFPMLGSVLRDPSFFSNPQDFNPQHFLDDK
GQFKKSDAFVPFSIGKRYCFGEGLARMELFLFFTTVMQNFRLKSSQSPKDIDVSSKHVGF
ATIPRNYTMSFLPR
Enzyme 34 Number of Residues 494
Enzyme 34 Molecular Weight 56409
Enzyme 34 Theoretical pI 7.96
Enzyme 34 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 34 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 34 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 34 Pathways
Enzyme 34 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • 1-31
Enzyme 34 Transmembrane Regions Not Available
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein 181270 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID P20853 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name CP2A7_HUMAN Link Image
Enzyme 34 PDB ID Not Available
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >1485 bp
ATGCTGGCCTCAGGGCTGCTTCTGGTGGCCTTGCTGGCCTGCCTGACTGTGATGGTCTTG
ATGTCTGTCTGGCAGCAGAGGAAGAGCAGGGGGAAGCTGCCTCCGGGACCCACCCCACTG
CCCTTCATTGGAAACTACCTCCAGCTGAACACAGAGCACATATGTGACTCCATCATGAAG
TTCAGTGAGTGCTATGGCCCCGTGTTCACCATTCACTTGGGGCCCCGGCGGGTCGTGGTG
CTGTGTGGACATGATGCCGTCAGGGAGGCTCTGGTGGACCAGGCTGAGGAGTTCAGCGGG
CGAGGCGAGCAAGCCACCTTCGACTGGGTCTTCAAAGGCTATGGCGTGGCGTTCAGCAAC
GGGGAGCGCGCCAAGCAGCTCCTGCGCTTTGCCATCGCCACCCTGAGGGACTTCGGGGTG
GGCAAGCGAGGCATCGAGGAGCGCATCCAGGAGGAGTCGGGCTTCCTCATCGAGGCCATC
CGGAGCAGCCACGGCGCCAATATCGATCCCACCTTCTTCCTGAGCCGCACAGTCTCCAAT
GTCATCAGCTCCATTGTCTTTGGGGACCGCTTTGACTATGAGGACAAAGAGTTCCTGTCA
CTGCTGAGCATGATGCTAGGAATCTTCCAGTTCACGTCAACCTCCACGGGGCAGCTCTAT
GAGATGTTCTCTTCGGTGATGAAACACCTGCCAGGACCACAGCAACAGGCCTTTAAGTTG
CTGCAAGGGCTGGAGGACTTCATAGCCAAGAAGGTGGAGCACAACCAGCGCACGCTGGAT
CCCAATTCCCCACAGGACTTCATCGACTCCTTTCTCATCCACATGCAGGAGGAGGAGAAG
AACCCCAACACGGAGTTCTACTTGAAGAACCTGATGATGAGCACGTTGAACCTCTTCATT
GCAGGCACGGAGACCGTCAGCACCACCCTGCGCTATGGCTTCTTGCTGCTCATGAAGCAC
CCAGAGGTGGAGGCCAAGGTCCATGAGGAGATTGACAGAGTGATCGGCAAGAACCGGCAG
CCCAAGTTTGAGGACCGGACCAAGATGCCCTACATGGAGGCAGTGATCCACGAGATCCAA
AGATTTGGAGACGTGATCCCCATGAGTTTGGCCCGCAGAGTCAAAAAGGACACCAAGTTT
CGGGATTTTTTCCTCCCTAAGGGCACCGAAGTGTTCCCTATGCTGGGCTCCGTGCTGAGA
GACCCCAGTTTCTTCTCCAACCCCCAGGACTTCAATCCCCAGCACTTCCTGGATGACAAG
GGGCAGTTTAAGAAGAGTGATGCTTTTGTGCCCTTTTCCATCGGAAAGCGGTACTGTTTC
GGAGAAGGCCTGGCCAGAATGGAGCTCTTTCTCTTCTTCACCACCGTCATGCAGAACTTC
CGCCTCAAGTCCTCCCAGTCACCTAAGGACATTGACGTGTCCTCCAAACACGTGGGCTTT
GCCACGATCCCACGAAACTACACCATGAGCTTCCTGCCCCGCTGA
Enzyme 34 GenBank Gene ID M33317 Link Image
Enzyme 34 GeneCard ID CYP2A7 Link Image
Enzyme 34 GenAtlas ID CYP2A7 Link Image
Enzyme 34 HGNC ID HGNC:2611 Link Image
Enzyme 34 Chromosome Location 19
Enzyme 34 Locus 19q13.2
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 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]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 6863
Enzyme 35 Name Cytochrome P450 2A6
Enzyme 35 Synonyms
  1. CYPIIA6
  2. Coumarin 7-hydroxylase
  3. P450 IIA3
  4. CYP2A3
  5. P450(I
Enzyme 35 Gene Name CYP2A6
Enzyme 35 Protein Sequence >Cytochrome P450 2A6
MLASGMLLVALLVCLTVMVLMSVWQQRKSKGKLPPGPTPLPFIGNYLQLNTEQMYNSLMK
ISERYGPVFTIHLGPRRVVVLCGHDAVREALVDQAEEFSGRGEQATFDWVFKGYGVVFSN
GERAKQLRRFSIATLRDFGVGKRGIEERIQEEAGFLIDAHRGTGGANIDPTFFLSRTVSN
VISSIVFGDRFDYKDKEFLSLLRMMLGIFQFTSTSTGQLYEMFSSVMKHLPGPQQQAFQL
LQGLEDFIAKKVEHNQRTLDPNSPRDFIDSFLIRMQEEEKNPNTEFYLKNLVMTTLNLFI
GGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGKNRQPKFEDRAKMPYMEAVIHEIQ
RFGDVIPMSLARRVKKDTKFRDFFLPKGTEVYPMLGSVLRDPSFFSNPQDFNPQHFLNEK
GQFKKSDAFVPFSIGKRNCFGEGLARMELFLFFTTVMQNFRLKSSQSPKDIDVSPKHVGF
ATIPRNYTMSFLPR
Enzyme 35 Number of Residues 494
Enzyme 35 Molecular Weight 56542
Enzyme 35 Theoretical pI 9.69
Enzyme 35 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 35 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 35 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
Enzyme 35 Pathways
Enzyme 35 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • 1-25
Enzyme 35 Transmembrane Regions Not Available
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 29547 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID P11509 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name CP2A6_HUMAN Link Image
Enzyme 35 PDB ID Not Available
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >1470 bp
ATGCTTCTGGTGGCCTTGCTGGTCTGCCTGACTGTAATGGTCTTGATGTCTGTTTGGCAG
CAGAGGAAGAACAAGGGGAAGCTGCCTCCGGGACCCACCCCATTGCCCTTCATTGGAAAC
TACCTGCAGCTGAACACAGAGCAGATGTACAACTCCCTCATGAAGATCAGTGAGCGCTAT
GGCCCCGTGTTCACCATTCACTTGGGGCCCCGGCGGGTCGTGGTGCTGTGTGGACATGAT
GCCGTCAGGGAGGCTCTGGTGGACCAGGCTGAGGAGTTCAGCGGGCGAGGCGAGCAAGCC
ACCTTCGACTGGGTCTTCAAAGGCTATGGCGTGGTATTCAGCAACGGGGAGCGCGCCAAG
CAGCTCCGGCGCTTCTCCATCGCCACCCTGCGGGACTTCGGGGTGGGCAAGCGAGGCATC
GAGGAGCGCATCCAGGAGGAGGCGGGCTTCCTCATCGACGCCCTCCGGGGCACTGGCGGC
GCCAATATCGATCCCACCTTCTTCCTGAGCCGCACAGTCTCCAATGTCATCAGCTCCATT
GTCTTTGGGGACCGCTTTGACTATAAGGACAAAGAGTTCCTGTCACTGTTGCGCATGATG
CTAGGAATCTTCCAGTTCACGTCAACCTCCACGGGGCAGCTCTATGAGATGTTCTCTTCG
GTGATGAAACACCTGCCAGGACCACAGCAACAGGCCTTTCAGTTGCTGCAAGGGCTGGAG
GACTTCATAGCCAAGAAGGTGGAGCACAAACAGCGCACGCTGGATCCCAATTCCCCACGG
GACTTCATTGACTCCTTTCTCATCCGCATGCAGGAGGAGGAGAAGAACCCCAACACGGAG
TTCTACTTGAAAAACCTGGTGATGACCACGTTGAACCTCTTCATTGGGGGCACCGAGACC
GTCAGCACCACCCTGCGCTATGGCTTCTTGCTGCTCATGAAGCACCCAGAGGTGGAGGCC
CAGGTCCATGAGGAGATTGACAGAGTGATCGGCAAGAACCGGCAGCCCAAGTTTGAGGAC
CGGGCCAAGATGCCCTACATGGAGGCAGTGATCCACGAGATCCAAAGATTTGGAGACGTG
ATCCCCATGAGTTTGGCCCGCAGAGTCAAAAAGGACACCAAGTTTCGGGATTTCTTCCTC
CCTAAGGGCACCGAAGTGTACCCTATGCTGGGCTCTGTGCTGAGAGACCCCAGTTTCTTC
TCCAACCCCCAGGACTTCAATCCCCAGCACTTCCTGAATGAGAAGGGGCAGTTTAAGAAG
AGTGATGCTTTTGTGCCCTTTTCCATCGGAAAGCGGAACTGTTTCGGAGAAGGCCTGGCC
AGAATGGAGCTCTTTCTCTTCTTCACCACCGTCATGCAGAACTTCCGCCTCAAGTCCTCC
CAGTCACCTAAGGACATTGACGTGTCCCCCAAACACGTGGGCTTTGCCACGATCCCACGA
AACTACACCATGAGCTTCCTGCCCCGCTGA
Enzyme 35 GenBank Gene ID X13897 Link Image
Enzyme 35 GeneCard ID CYP2A6 Link Image
Enzyme 35 GenAtlas ID CYP2A6 Link Image
Enzyme 35 HGNC ID HGNC:2610 Link Image
Enzyme 35 Chromosome Location 19
Enzyme 35 Locus 19q13.2
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 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, 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]
  3. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 6946
Enzyme 36 Name Sex hormone-binding globulin precursor
Enzyme 36 Synonyms
  1. SHBG
  2. Sex steroid-binding protein
  3. SBP
  4. Testis-specific androgen-binding protein
  5. ABP
  6. Testosterone-estrogen-binding globulin
  7. Testosterone-estradiol- binding globulin
  8. TeBG
Enzyme 36 Gene Name SHBG
Enzyme 36 Protein Sequence >Sex hormone-binding globulin precursor
MESRGPLATSRLLLLLLLLLLRHTRQGWALRPVLPTQSAHDPPAVHLSNGPGQEPIAVMT
FDLTKITKTSSSFEVRTWDPEGVIFYGDTNPKDDWFMLGLRDGRPEIQLHNHWAQLTVGA
GPRLDDGRWHQVEVKMEGDSVLLEVDGEEVLRLRQVSGPLTSKRHPIMRIALGGLLFPAS
NLRLPLVPALDGCLRRDSWLDKQAEISASAPTSLRSCDVESNPGIFLPPGTQAEFNLRDI
PQPHAEPWAFSLDLGLKQAAGSGHLLALGTPENPSWLSLHLQDQKVVLSSGSGPGLDLPL
VLGLPLQLKLSMSRVVLSQGSKMKALALPPLGLAPLLNLWAKPQGRLFLGALPGEDSSTS
FCLNGLWAQGQRLDVDQALNRSHEIWTHSCPQSPGNGTDASH
Enzyme 36 Number of Residues 402
Enzyme 36 Molecular Weight 43780
Enzyme 36 Theoretical pI 6.70
Enzyme 36 GO Classification Not Available
Enzyme 36 General Function Not Available
Enzyme 36 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 36 Pathways Not Available
Enzyme 36 Reactions Not Available
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • 1-29
Enzyme 36 Transmembrane Regions Not Available
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 296673 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID P04278 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name SHBG_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 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 36 GenBank Gene ID X16349 Link Image
Enzyme 36 GeneCard ID SHBG Link Image
Enzyme 36 GenAtlas ID SHBG Link Image
Enzyme 36 HGNC ID HGNC:10839 Link Image
Enzyme 36 Chromosome Location 17
Enzyme 36 Locus 17p13-p12
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 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. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. 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 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 7527
Enzyme 37 Name Orphan nuclear receptor PXR
Enzyme 37 Synonyms
  1. Pregnane X receptor
  2. Orphan nuclear receptor PAR1
  3. Steroid and xenobiotic receptor
  4. SXR
Enzyme 37 Gene Name NR1I2
Enzyme 37 Protein Sequence >Orphan nuclear receptor PXR
MEVRPKESWNHADFVHCEDTESVPGKPSVNADEEVGGPQICRVCGDKATGYHFNVMTCEG
CKGFFRRAMKRNARLRCPFRKGACEITRKTRRQCQACRLRKCLESGMKKEMIMSDEAVEE
RRALIKRKKSERTGTQPLGVQGLTEEQRMMIRELMDAQMKTFDTTFSHFKNFRLPGVLSS
GCELPESLQAPSREEAAKWSQVRKDLCSLKVSLQLRGEDGSVWNYKPPADSGGKEIFSLL
PHMADMSTYMFKGIISFAKVISYFRDLPIEDQISLLKGAAFELCQLRFNTVFNAETGTWE
CGRLSYCLEDTAGGFQQLLLEPMLKFHYMLKKLQLHEEEYVLMQAISLFSPDRPGVLQHR
VVDQLQEQFAITLKSYIECNRPQPAHRFLFLKIMAMLTELRSINAQHTQRLLRIQDIHPF
ATPLMQELFGITGS
Enzyme 37 Number of Residues 434
Enzyme 37 Molecular Weight 49762
Enzyme 37 Theoretical pI 8.44
Enzyme 37 GO Classification
Function
  • DNA binding
  • binding
  • ligand-dependent nuclear receptor activity
  • nucleic acid binding
  • receptor activity
  • signal transducer activity
  • steroid hormone receptor activity
  • transcription factor activity
Process
  • regulation of biological process
  • regulation of cellular metabolism
  • regulation of metabolism
  • regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • regulation of physiological process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 37 General Function Not Available
Enzyme 37 Specific Function Orphan receptor; its natural ligand is probably pregnane. Binds to a response element in the CYP3A4 and ABCB1/MDR1 genes promoter. Activates its expression in response to a wide variety of endobiotics and xenobiotics
Enzyme 37 Pathways Not Available
Enzyme 37 Reactions Not Available
Enzyme 37 Pfam Domain Function
Enzyme 37 Signals
  • None
Enzyme 37 Transmembrane Regions
  • None
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein 3511138 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID O75469 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name PXR_HUMAN Link Image
Enzyme 37 PDB ID Not Available
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence >1305 bp
CTGGAGGTGAGACCCAAAGAAAGCTGGAACCATGCTGACTTTGTACACTGTGAGGACACA
GAGTCTGTTCCTGGAAAGCCCAGTGTCAACGCAGATGAGGAAGTCGGAGGTCCCCAAATC
TGCCGTGTATGTGGGGACAAGGCCACTGGCTATCACTTCAATGTCATGACATGTGAAGGA
TGCAAGGGCTTTTTCAGGAGGGCCATGAAACGCAACGCCCGGCTGAGGTGCCCCTTCCGG
AAGGGCGCCTGCGAGATCACCCGGAAGACCCGGCGACAGTGCCAGGCCTGCCGCCTGCGC
AAGTGCCTGGAGAGCGGCATGAAGAAGGAGATGATCATGTCCGACGAGGCCGTGGAGGAG
AGGCGGGCCTTGATCAAGCGGAAGAAAAGTGAACGGACAGGGACTCAGCCACTGGGAGTG
CAGGGGCTGACAGAGGAGCAGCGGATGATGATCAGGGAGCTGATGGACGCTCAGATGAAA
ACCTTTGACACTACCTTCTCCCATTTCAAGAATTTCCGGCTGCCAGGGGTGCTTAGCAGT
GGCTGCGAGTTGCCAGAGTCTCTGCAGGCCCCATCGAGGGAAGAAGCTGCCAAGTGGAGC
CAGGTCCGGAAAGATCTGTGCTCTTTGAAGGTCTCTCTGCAGCTGCGGGGGGAGGATGGC
AGTGTCTGGAACTACAAACCCCCAGCCGACAGTGGCGGGAAAGAGATCTTCTCCCTGCTG
CCCCACATGGCTGACATGTCAACCTACATGTTCAAAGGCATCATCAGCTTTGCCAAAGTC
ATCTCCTACTTCAGGGACTTGCCCATCGAGGACCAGATCTCCCTGCTGAAGGGGGCCGCT
TTCGAGCTGTGTCAACTGAGATTCAACACAGTGTTCAACGCGGAGACTGGAACCTGGGAG
TGTGGCCGGCTGTCCTACTGCTTGGAAGACACTGCAGGTGGCTTCCAGCAACTTCTACTG
GAGCCCATGCTGAAATTCCACTACATGCTGAAGAAGCTGCAGCTGCATGAGGAGGAGTAT
GTGCTGATGCAGGCCATCTCCCTCTTCTCCCCAGACCGCCCAGGTGTGCTGCAGCACCGC
GTGGTGGACCAGCTGCAGGAGCAATTCGCCATTACTCTGAAGTCCTACATTGAATGCAAT
CGGCCCCAGCCTGCTCATAGGTTCTTGTTCCTGAAGATCATGGCTATGCTCACCGAGCTC
CGCAGCATCAATGCTCAGCACACCCAGCGGCTGCTGCGCATCCAGGACATACACCCCTTT
GCTACGCCCCTCATGCAGGAGTTGTTCGGCATCACAGGTAGCTGA
Enzyme 37 GenBank Gene ID AF061056 Link Image
Enzyme 37 GeneCard ID NR1I2 Link Image
Enzyme 37 GenAtlas ID NR1I2 Link Image
Enzyme 37 HGNC ID HGNC:7968 Link Image
Enzyme 37 Chromosome Location 3
Enzyme 37 Locus 3q12-q13.3
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References
  1. Lehmann JM, McKee DD, Watson MA, Willson TM, Moore JT, Kliewer SA: The human orphan nuclear receptor PXR is activated by compounds that regulate CYP3A4 gene expression and cause drug interactions. J Clin Invest. 1998 Sep 1;102(5):1016-23. [PubMed Link Image]
  2. Bertilsson G, Heidrich J, Svensson K, Asman M, Jendeberg L, Sydow-Backman M, Ohlsson R, Postlind H, Blomquist P, Berkenstam A: Identification of a human nuclear receptor defines a new signaling pathway for CYP3A induction. Proc Natl Acad Sci U S A. 1998 Oct 13;95(21):12208-13. [PubMed Link Image]
  3. Zhang J, Kuehl P, Green ED, Touchman JW, Watkins PB, Daly A, Hall SD, Maurel P, Relling M, Brimer C, Yasuda K, Wrighton SA, Hancock M, Kim RB, Strom S, Thummel K, Russell CG, Hudson JR Jr, Schuetz EG, Boguski MS: The human pregnane X receptor: genomic structure and identification and functional characterization of natural allelic variants. Pharmacogenetics. 2001 Oct;11(7):555-72. [PubMed Link Image]
  4. Blumberg B, Sabbagh W Jr, Juguilon H, Bolado J Jr, van Meter CM, Ong ES, Evans RM: SXR, a novel steroid and xenobiotic-sensing nuclear receptor. Genes Dev. 1998 Oct 15;12(20):3195-205. [PubMed Link Image]
  5. Kawana K, Ikuta T, Kobayashi Y, Gotoh O, Takeda K, Kawajiri K: Molecular mechanism of nuclear translocation of an orphan nuclear receptor, SXR. Mol Pharmacol. 2003 Mar;63(3):524-31. [PubMed Link Image]
  6. Watkins RE, Wisely GB, Moore LB, Collins JL, Lambert MH, Williams SP, Willson TM, Kliewer SA, Redinbo MR: The human nuclear xenobiotic receptor PXR: structural determinants of directed promiscuity. Science. 2001 Jun 22;292(5525):2329-33. Epub 2001 Jun 14. [PubMed Link Image]
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 7559
Enzyme 38 Name Estrogen receptor
Enzyme 38 Synonyms
  1. ER
  2. Estradiol receptor
  3. ER-alpha
Enzyme 38 Gene Name ESR1
Enzyme 38 Protein Sequence >Estrogen receptor
MTMTLHTKASGMALLHQIQGNELEPLNRPQLKIPLERPLGEVYLDSSKPAVYNYPEGAAY
EFNAAAAANAQVYGQTGLPYGPGSEAAAFGSNGLGGFPPLNSVSPSPLMLLHPPPQLSPF
LQPHGQQVPYYLENEPSGYTVREAGPPAFYRPNSDNRRQGGRERLASTNDKGSMAMESAK
ETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQAC
RLRKCYEVGMMKGGIRKDRRGGRMLKHKRQRDDGEGRGEVGSAGDMRAANLWPSPLMIKR
SKKNSLALSLTADQMVSALLDAEPPILYSEYDPTRPFSEASMMGLLTNLADRELVHMINW
AKRVPGFVDLTLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEG
MVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLD
KITDTLIHLMAKAGLTLQQQHQRLAQLLLILSHIRHMSNKGMEHLYSMKCKNVVPLYDLL
LEMLDAHRLHAPTSRGGASVEETDQSHLATAGSTSSHSLQKYYITGEAEGFPATV
Enzyme 38 Number of Residues 595
Enzyme 38 Molecular Weight 66217
Enzyme 38 Theoretical pI 8.14
Enzyme 38 GO Classification
Function
  • DNA binding
  • binding
  • cation binding
  • ion binding
  • ligand-dependent nuclear receptor activity
  • nucleic acid binding
  • receptor activity
  • signal transducer activity
  • steroid binding
  • steroid hormone receptor activity
  • transcription factor activity
  • transition metal ion binding
  • zinc ion binding
Process
  • regulation of biological process
  • regulation of cellular metabolism
  • regulation of metabolism
  • regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • regulation of physiological process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 38 General Function Not Available
Enzyme 38 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
Enzyme 38 Pathways Not Available
Enzyme 38 Reactions Not Available
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • None
Enzyme 38 Transmembrane Regions
  • None
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein 31620888 Link Image
Enzyme 38 UniProtKB/Swiss-Prot ID P03372 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name ESR1_HUMAN Link Image
Enzyme 38 PDB ID Not Available
Enzyme 38 Cellular Location Not Available
Enzyme 38 Gene Sequence >63 bp
ATGCGCTGCGTCGCCTCTAACCTCGGGCTGTGCTCTTTTTCCAGGTGGCCCGCCGGTTTC
TGA
Enzyme 38 GenBank Gene ID X03635 Link Image
Enzyme 38 GeneCard ID ESR1 Link Image
Enzyme 38 GenAtlas ID ESR1 Link Image
Enzyme 38 HGNC ID HGNC:3467 Link Image
Enzyme 38 Chromosome Location 6
Enzyme 38 Locus 6q25.1
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 General References
  1. 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]
  2. 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]
  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. 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]
  6. 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]
  7. 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]
  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. 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]
  12. 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]
  13. 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]
  14. 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]
  15. 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]
  16. 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]
  17. 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]
  18. 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]
  19. 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]
  20. 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]
  21. 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]
  22. 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]
  23. 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]
  24. 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]
  25. 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]
  26. 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]
Enzyme 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 8369
Enzyme 39 Name Oxidoreductase
Enzyme 39 Synonyms
  1. Hydroxysteroid
  2. 17-betadehydrogenase 6
  3. 3- hydroxysteroid epimerase
Enzyme 39 Gene Name HSD17B6
Enzyme 39 Protein Sequence >Oxidoreductase
MWLYLAAFVGLYYLLHWYRERQVVSHLQDKYVFITGCDSGFGNLLARQLDARGLRVLAAC
LTEKGAEQLRGQTSDRLETVTLDVTKMESIAAATQWVKEHVGDRGLWGLVNNAGILTPIT
LCEWLNTEDSMNMLKVNLIGVIQVTLSMLPLVRRARGRIVNVSSILGRVAFFVGGYCVSK
YGVEAFSDILRREIQHFGVKISIVEPGYFRTGMTNMTQSLERMKQSWKEAPKHIKETYGQ
QYFDALYNIMKEGLLNCSTNLNLVTDCMEHALTSVHPRTRYSAGWDAKFFFIPLSYLPTS
LADYILTRSWPKPAQAV
Enzyme 39 Number of Residues 317
Enzyme 39 Molecular Weight 35966
Enzyme 39 Theoretical pI 8.91
Enzyme 39 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
Enzyme 39 General Function Lipid transport and metabolism
Enzyme 39 Specific Function Not Available
Enzyme 39 Pathways Not Available
Enzyme 39 Reactions Not Available
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • 1-25
Enzyme 39 Transmembrane Regions Not Available
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein 2338748 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID O14756 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name O14756_HUMAN Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence >954 bp
ATGTGGCTCTACCTGGCAGCCTTCGTGGGCCTGTACTACCTTCTGCACTGGTACCGGGAG
AGGCAGGTGGTGAGCCACCTCCAAGACAAGTATGTCTTTATCACGGGCTGTGACTCGGGC
TTTGGGAACCTACTGGCCAGACAGCTGGATGCACGAGGCTTGAGAGTGCTGGCTGCGTGT
CTGACGGAGAAGGGGGCCGAGCAGCTGAGGGGCCAGACGTCTGACAGGCTGGAGACGGTG
ACCCTGGATGTTACCAAGATGGAGAGCATCGCTGCAGCTACTCAGTGGGTGAAGGAGCAT
GTGGGGGACAGAGGACTCTGGGGACTGGTGAACAATGCAGGCATTCTTACACCAATTACC
TTATGTGAGTGGCTGAACACTGAGGACTCTATGAATATGCTCAAAGTGAACCTCATTGGT
GTGATCCAGGTGACCTTGAGCATGCTTCCTTTGGTGAGGAGAGCACGGGGAAGAATTGTC
AATGTCTCCAGCATTCTGGGAAGAGTTGCTTTCTTTGTAGGAGGCTACTGTGTCTCCAAG
TATGGAGTGGAAGCCTTTTCAGATATTCTGAGGCGTGAGATTCAACATTTTGGGGTGAAA
ATCAGCATAGTTGAACCTGGCTACTTCAGAACGGGAATGACAAACATGACACAGTCCTTA
GAGCGAATGAAGCAAAGTTGGAAAGAAGCCCCCAAGCATATTAAGGAGACCTATGGACAG
CAGTATTTTGATGCCCTTTACAATATCATGAAGGAAGGGCTGTTGAATTGTAGCACAAAC
CTGAACCTGGTCACTGACTGCATGGAACATGCTCTGACATCGGTGCATCCGCGAACTCGA
TATTCAGCTGGCTGGGATGCTAAATTTTTCTTCATCCCTCTATCTTATTTACCTACATCA
CTGGCAGACTACATTTTGACTAGATCTTGGCCCAAACCAGCCCAGGCAGTCTAA
Enzyme 39 GenBank Gene ID AF016509 Link Image
Enzyme 39 GeneCard ID HSD17B6 Link Image
Enzyme 39 GenAtlas ID HSD17B6 Link Image
Enzyme 39 HGNC ID HGNC:23316 Link Image
Enzyme 39 Chromosome Location 12
Enzyme 39 Locus 12q13
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 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. 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]
  3. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
  4. Huang XF, Luu-The V: Molecular characterization of a first human 3(alpha--&gt;beta)-hydroxysteroid epimerase. J Biol Chem. 2000 Sep 22;275(38):29452-7. [PubMed Link Image]
Enzyme 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 12970
Enzyme 40 Name UDP-glucuronosyltransferase 2A3 precursor
Enzyme 40 Synonyms Not Available
Enzyme 40 Gene Name UGT2A3
Enzyme 40 Protein Sequence >UDP-glucuronosyltransferase 2A3 precursor
MRSDKSALVFLLLQLFCVGCGFCGKVLVWPCDMSHWLNVKVILEELIVRGHEVTVLTHSK
PSLIDYRKPSALKFEVVHMPQDRTEENEIFVDLALNVLPGLSTWQSVIKLNDFFVEIRGT
LKMMCESFIYNQTLMKKLQETNYDVMLIDPVIPCGDLMAELLAVPFVLTLRISVGGNMER
SCGKLPAPLSYVPVPMTGLTDRMTFLERVKNSMLSVLFHFWIQDYDYHFWEEFYSKALGR
PTTLCETVGKAEIWLIRTYWDFEFPQPYQPNFEFVGGLHCKPAKALPKEMENFVQSSGED
GIVVFSLGSLFQNVTEEKANIIASALAQIPQKVLWRYKGKKPSTLGANTRLYDWIPQNDL
LGHPKTKAFITHGGMNGIYEAIYHGVPMVGVPIFGDQLDNIAHMKAKGAAVEINFKTMTS
EDLLRALRTVITDSSYKENAMRLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRSAAHD
LTWFQHYSIDVIGFLLTCVATAIFLFTKCFLFSCQKFNKTRKIEKRE
Enzyme 40 Number of Residues 527
Enzyme 40 Molecular Weight 60285
Enzyme 40 Theoretical pI 8.04
Enzyme 40 GO Classification
Function
  • binding
  • catalytic activity
  • ion binding
  • metal ion binding
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • cation transport
  • cellular physiological process
  • ion transport
  • metabolism
  • metal ion transport
  • physiological process
  • transport
Component
Enzyme 40 General Function Carbohydrate transport and metabolism
Enzyme 40 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 40 Pathways
Enzyme 40 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside [RN:R01383] ALL_REAC R01383 > R02358 R02389 R02478 R02502 R02902 R03091 R04352 R04353 R04354 R04683 R07106
Enzyme 40 Pfam Domain Function
Enzyme 40 Signals
  • 1-23
Enzyme 40 Transmembrane Regions
  • 492-512
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein 44889644 Link Image
Enzyme 40 UniProtKB/Swiss-Prot ID Q6UWM9 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name UD2A3_HUMAN Link Image
Enzyme 40 PDB ID Not Available
Enzyme 40 Cellular Location Not Available
Enzyme 40 Gene Sequence Not Available
Enzyme 40 GenBank Gene ID AY542891 Link Image
Enzyme 40 GeneCard ID Q6UWM9 Link Image
Enzyme 40 GenAtlas ID UGT2A3 Link Image
Enzyme 40 HGNC ID HGNC:28528 Link Image
Enzyme 40 Chromosome Location Not Available
Enzyme 40 Locus Not Available
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 General References
  1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 13116
Enzyme 41 Name Cytochrome P450, family 1, subfamily A, polypeptide 1
Enzyme 41 Synonyms
  1. Cytochrome P450, family 1, subfamily A, polypeptide 1, isoform CRA_a
Enzyme 41 Gene Name CYP1A1
Enzyme 41 Protein Sequence >Cytochrome P450, family 1, subfamily A, polypeptide 1
MLFPISMSATEFLLASVIFCLVFWVIRASRPQVPKGLKNPPGPWGWPLIGHMLTLGKNPH
LALSRMSQQYGDVLQIRIGSTPVVVLSGLDTIRQALVRQGDDFKGRPDLYTFTLISNGQS
MSFSPDSGPVWAARRRLAQNGLKSFSIASDPASSTSCYLEEHVSKEAEVLISTLQELMAG
PGHFNPYRYVVVSVTNVICAICFGRRYDHNHQELLSLVNLNNNFGEVVGSGNPADFIPIL
RYLPNPSLNAFKDLNEKFYSFMQKMVKEHYKTFEKGHIRDITDSLIEHCQEKQLDENANV
QLSDEKIINIVLDLFGAGFDTVTTAISWSLMYLVMNPRVQRKIQEELDTVIGRSRRPRLS
DRSHLPYMEAFILETFRHSSFVPFTIPHSTTRDTSLKGFYIPKGRCVFVNQWQINHDQKL
WVNPSEFLPERFLTPDGAIDKVLSEKVIIFGMGKRKCIGETIARWEVFLFLAILLQRVEF
SVPLGVKVDMTPIYGLTMKHACCEHFQMQLRS
Enzyme 41 Number of Residues 512
Enzyme 41 Molecular Weight 58166
Enzyme 41 Theoretical pI 8.47
Enzyme 41 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 41 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 41 Specific Function Not Available
Enzyme 41 Pathways Not Available
Enzyme 41 Reactions Not Available
Enzyme 41 Pfam Domain Function
Enzyme 41 Signals
  • None
Enzyme 41 Transmembrane Regions
  • None
Enzyme 41 Essentiality Not Available
Enzyme 41 GenBank ID Protein 117606758 Link Image
Enzyme 41 UniProtKB/Swiss-Prot ID A0N0X8 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name A0N0X8_HUMAN Link Image
Enzyme 41 PDB ID Not Available
Enzyme 41 Cellular Location Not Available
Enzyme 41 Gene Sequence Not Available
Enzyme 41 GenBank Gene ID EF094025 Link Image
Enzyme 41 GeneCard ID A0N0X8 Link Image
Enzyme 41 GenAtlas ID Not Available
Enzyme 41 HGNC ID Not Available
Enzyme 41 Chromosome Location Not Available
Enzyme 41 Locus Not Available
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 General References Not Available
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 14588
Enzyme 42 Name Estradiol 17-beta-dehydrogenase 12
Enzyme 42 Synonyms
  1. 17-beta-HSD 12
  2. 17- beta-hydroxysteroid dehydrogenase 12
  3. 3-ketoacyl-CoA reductase
  4. KAR
Enzyme 42 Gene Name HSD17B12
Enzyme 42 Protein Sequence >Estradiol 17-beta-dehydrogenase 12
MESALPAAGFLYWVGAGTVAYLALRISYSLFTALRVWGVGNEAGVGPGLGEWAVVTGSTD
GIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDFASEDIYDKIKT
GLAGLEIGILVNNVGMSYEYPEYFLDVPDLDNVIKKMININILSVCKMTQLVLPGMVERS
KGAILNISSGSGMLPVPLLTIYSATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLA
KIRKPTLDKPSPETFVKSAIKTVGLQSRTNGYLIHALMGSIISNLPSWIYLKIVMNMNKS
TRAHYLKKTKKN
Enzyme 42 Number of Residues 312
Enzyme 42 Molecular Weight 34325
Enzyme 42 Theoretical pI 9.79
Enzyme 42 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
Enzyme 42 General Function Not Available
Enzyme 42 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 42 Pathways
  • Androgen and Estrogen Metabolism (map00150 Link Image)
Enzyme 42 Reactions
  • estradiol-17beta + NAD(P)+ = estrone + NAD(P)H + H+ [RN:R02352 R02353] ALL_REAC R02352 R02353
  • (other) R04681 R04682
Enzyme 42 Pfam Domain Function
Enzyme 42 Signals
  • 1-29
Enzyme 42 Transmembrane Regions
  • 4-24 182-202 271-291
Enzyme 42 Essentiality Not Available
Enzyme 42 GenBank ID Protein 5531815 Link Image
Enzyme 42 UniProtKB/Swiss-Prot ID Q53GQ0 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name DHB12_HUMAN Link Image
Enzyme 42 PDB ID Not Available
Enzyme 42 Cellular Location Not Available
Enzyme 42 Gene Sequence >939 bp
ATGGAGAGCGCTCTCCCCGCCGCCGGCTTCCTGTACTGGGTCGGCGCGGGCACCGTGGCC
TACCTAGCCCTGCGTATTTCGTACTCGCTCTTCACGGCCCTCCGGGTCTGGGGAGTGGGG
AATGAGGCGGGGGTCGGCCCGGGGCTCGGAGAGTGGGCAGTTGTCACAGGTAGTACTGAT
GGAATTGGAAAATCATATGCAGAAGAGTTAGCAAAGCATGGAATGAAGGTTGTCCTTATC
AGCAGATCAAAGGATAAACTTGACCAGGTTTCCAGTGAAATAAAAGAAAAATTCAAAGTG
GAGACAAGAACCATTGCTGTTGACTTTGCATCAGAAGATATTTATGATAAAATTAAAACA
GGCTTGGCTGGTCTTGAAATCGGCATCTTAGTGAACAACGTGGGAATGTCGTATGAGTAT
CCTGAATACTTTTTGGATGTTCCTGACTTGGACAATGTGATCAAGAAAATGATAAATATT
AATATTCTTTCTGTTTGTAAGATGACACAATTGGTACTGCCTGGCATGGTGGAAAGATCC
AAAGGGGCTATTCTGAACATTTCATCTGGCAGTGGCATGCTCCCTGTCCCACTCTTGACC
ATCTATTCTGCAACCAAGACTTTTGTAGATTTCTTCTCTCAGTGCCTCCATGAGGAGTAT
AGGAGCAAGGGCGTCTTTGTGCAGAGTGTCCTGCCATACTTCGTAGCTACAAAACTGGCT
AAAATCCGGAAGCCAACTTTGGATAAGCCCTCTCCGGAGACGTTTGTGAAGTCTGCAATT
AAAACAGTCGGCCTGCAATCCCGAACCAATGGATACCTGATCCATGCTCTTATGGGCTCG
ATAATCTCAAACCTGCCTTCTTGGATTTATTTGAAAATAGTCATGAATATGAACAAGTCT
ACACGGGCTCACTATCTGAAGAAAACCAAGAAGAACTAA
Enzyme 42 GenBank Gene ID AF078850 Link Image
Enzyme 42 GeneCard ID Q53GQ0 Link Image
Enzyme 42 GenAtlas ID HSD17B12 Link Image
Enzyme 42 HGNC ID HGNC:18646 Link Image
Enzyme 42 Chromosome Location 11
Enzyme 42 Locus 11p11.2
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 General References Not Available
Enzyme 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 15056
Enzyme 43 Name UDP glycosyltransferase 1 family polypeptide A10 (HCG2039726, isoform CRA_f)
Enzyme 43 Synonyms Not Available
Enzyme 43 Gene Name UGT1A10
Enzyme 43 Protein Sequence >UDP glycosyltransferase 1 family polypeptide A10 (HCG2039726, isoform CRA_f)
MARAGWTSPVPLCVCLLLTCGFAEAGKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMP
EVSWQLERSLNCTVKTYSTSYTLEDQNREFMVFAHAQWKAQAQSIFSLLMSSSSGFLDLF
FSHCRSLFNDRKLVEYLKESSFDAVFLDPFDTCGLIVAKYFSLPSVVFTRGIFCHHLEEG
AQCPAPLSYVPNDLLGFSDAMTFKERVWNHIVHLEDHLFCQYLFRNALEIASEILQTPVT
AYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIV
VFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGH
PMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDL
ENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTW
YQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 43 Number of Residues 530
Enzyme 43 Molecular Weight 59810
Enzyme 43 Theoretical pI 7.31
Enzyme 43 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 43 General Function Carbohydrate transport and metabolism
Enzyme 43 Specific Function Not Available
Enzyme 43 Pathways Not Available
Enzyme 43 Reactions Not Available
Enzyme 43 Pfam Domain Function
Enzyme 43 Signals
  • None
Enzyme 43 Transmembrane Regions
  • None
Enzyme 43 Essentiality Not Available
Enzyme 43 GenBank ID Protein 40849852 Link Image
Enzyme 43 UniProtKB/Swiss-Prot ID Q5DT02 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name Q5DT02_HUMAN Link Image
Enzyme 43 PDB ID Not Available
Enzyme 43 Cellular Location Not Available
Enzyme 43 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 43 GenBank Gene ID AY435137 Link Image
Enzyme 43 GeneCard ID Q5DT02 Link Image
Enzyme 43 GenAtlas ID UGT1A10 Link Image
Enzyme 43 HGNC ID HGNC:12531 Link Image
Enzyme 43 Chromosome Location Not Available
Enzyme 43 Locus Not Available
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 General References Not Available
Enzyme 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 15057
Enzyme 44 Name UDP glycosyltransferase 1 family polypeptide A8 (HCG2039726, isoform CRA_e)
Enzyme 44 Synonyms Not Available
Enzyme 44 Gene Name UGT1A8
Enzyme 44 Protein Sequence >UDP glycosyltransferase 1 family polypeptide A8 (HCG2039726, isoform CRA_e)
MARTGWTSPIPLCVSLLLTCGFAEAGKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMP
EVSWQLGKSLNCTVKTYSTSYTLEDLDREFMDFADAQWKAQVRSLFSLFLSSSNGFFNLF
FSHCRSLFNDRKLVEYLKESSFDAVFLDPFDACGLIVAKYFSLPSVVFARGIACHYLEEG
AQCPAPLSYVPRILLGFSDAMTFKERVRNHIMHLEEHLFCQYFSKNALEIASEILQTPVT
AYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIV
VFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGH
PMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDL
ENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTW
YQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 44 Number of Residues 530
Enzyme 44 Molecular Weight 59742
Enzyme 44 Theoretical pI 7.73
Enzyme 44 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 44 General Function Carbohydrate transport and metabolism
Enzyme 44 Specific Function Not Available
Enzyme 44 Pathways Not Available
Enzyme 44 Reactions Not Available
Enzyme 44 Pfam Domain Function
Enzyme 44 Signals
  • None
Enzyme 44 Transmembrane Regions
  • None
Enzyme 44 Essentiality Not Available
Enzyme 44 GenBank ID Protein 40849864 Link Image
Enzyme 44 UniProtKB/Swiss-Prot ID Q5DSZ6 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name Q5DSZ6_HUMAN Link Image
Enzyme 44 PDB ID Not Available
Enzyme 44 Cellular Location Not Available
Enzyme 44 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 44 GenBank Gene ID AY435143 Link Image
Enzyme 44 GeneCard ID Q5DSZ6 Link Image
Enzyme 44 GenAtlas ID UGT1A8 Link Image
Enzyme 44 HGNC ID HGNC:12540 Link Image
Enzyme 44 Chromosome Location Not Available
Enzyme 44 Locus Not Available
Enzyme 44 SNPs SNPJam Report Link Image
Enzyme 44 General References Not Available
Enzyme 44 Metabolite References Not Available
Enzyme 45 [top]
Enzyme 45 ID 15058
Enzyme 45 Name UDP glycosyltransferase 1 family polypeptide A7
Enzyme 45 Synonyms Not Available
Enzyme 45 Gene Name UGT1A7
Enzyme 45 Protein Sequence >UDP glycosyltransferase 1 family polypeptide A7
MARAGWTGLLPLYVCLLLTCGFAKAGKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMP
EVSWQLGRSLNCTVKTYSTSYTLEDQDREFMVFADARWTAPLRSAFSLLTSSSNGIFDLF
FSNCRSLFNDRKLVEYLKESCFDAVFLDPFDACGLIVAKYFSLPSVVFARGIFCHYLEEG
AQCPAPLSYVPRLLLGFSDAMTFKERVWNHIMHLEEHLFCPYFFKNVLEIASEILQTPVT
AYDLYSHTSIWLLRTDFVLEYPKPVMPNMIFIGGINCHQGKPVPMEFEAYINASGEHGIV
VFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGH
PMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDL
ENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTW
YQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 45 Number of Residues 530
Enzyme 45 Molecular Weight 59819
Enzyme 45 Theoretical pI 7.85
Enzyme 45 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 45 General Function Carbohydrate transport and metabolism
Enzyme 45 Specific Function Not Available
Enzyme 45 Pathways Not Available
Enzyme 45 Reactions Not Available
Enzyme 45 Pfam Domain Function
Enzyme 45 Signals
  • None
Enzyme 45 Transmembrane Regions
  • None
Enzyme 45 Essentiality Not Available
Enzyme 45 GenBank ID Protein 40849862 Link Image
Enzyme 45 UniProtKB/Swiss-Prot ID Q5DSZ7 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name Q5DSZ7_HUMAN Link Image
Enzyme 45 PDB ID Not Available
Enzyme 45 Cellular Location Not Available
Enzyme 45 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 45 GenBank Gene ID AY435142 Link Image
Enzyme 45 GeneCard ID Q5DSZ7 Link Image
Enzyme 45 GenAtlas ID UGT1A7 Link Image
Enzyme 45 HGNC ID HGNC:12539 Link Image
Enzyme 45 Chromosome Location Not Available
Enzyme 45 Locus Not Available
Enzyme 45 SNPs SNPJam Report Link Image
Enzyme 45 General References Not Available
Enzyme 45 Metabolite References Not Available
Enzyme 46 [top]
Enzyme 46 ID 15059
Enzyme 46 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 46 Synonyms Not Available
Enzyme 46 Gene Name UGT2B10
Enzyme 46 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 46 Number of Residues 528
Enzyme 46 Molecular Weight 60775
Enzyme 46 Theoretical pI 9.40
Enzyme 46 GO Classification Not Available
Enzyme 46 General Function Carbohydrate transport and metabolism
Enzyme 46 Specific Function Not Available
Enzyme 46 Pathways Not Available
Enzyme 46 Reactions Not Available
Enzyme 46 Pfam Domain Function Not Available
Enzyme 46 Signals
  • None
Enzyme 46 Transmembrane Regions
  • None
Enzyme 46 Essentiality Not Available
Enzyme 46 GenBank ID Protein 158258913 Link Image
Enzyme 46 UniProtKB/Swiss-Prot ID A8K9M3 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name A8K9M3_HUMAN Link Image
Enzyme 46 PDB ID Not Available
Enzyme 46 Cellular Location Not Available
Enzyme 46 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 46 GenBank Gene ID AK292738 Link Image
Enzyme 46 GeneCard ID A8K9M3 Link Image
Enzyme 46 GenAtlas ID Not Available
Enzyme 46 HGNC ID Not Available
Enzyme 46 Chromosome Location Not Available
Enzyme 46 Locus Not Available
Enzyme 46 SNPs SNPJam Report Link Image
Enzyme 46 General References Not Available
Enzyme 46 Metabolite References Not Available
Enzyme 47 [top]
Enzyme 47 ID 15174
Enzyme 47 Name Cytochrome P450, family 3, subfamily A, polypeptide 7
Enzyme 47 Synonyms Not Available
Enzyme 47 Gene Name CYP3A7
Enzyme 47 Protein Sequence >Cytochrome P450, family 3, subfamily A, polypeptide 7
MDLIPNLAVETWLLLAVSLILLYLYGTRTHGLFKKLGIPGPTPLPFLGNALSFRKGYWTF
DMECYKKYRKVWGIYDCQQPMLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKNAISI
AEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKHVFGAYS
MDVITSTSFGVSIDSLNNPQDPFVENTKKLLRFNPLDPFVLSIKVFPFLTPILEALNITV
FPRKVISFLTKSVKQIKEGRLKETQKHRVDFLQLMIDSQNSKDSETHKALSDLELMAQSI
IFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVV
NETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFS
KKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKPCKETQIPLKLRFG
GLLLTEKPIVLKAESRDETVSGA
Enzyme 47 Number of Residues 503
Enzyme 47 Molecular Weight 57471
Enzyme 47 Theoretical pI 9.52
Enzyme 47 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 47 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 47 Specific Function Not Available
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 Not Available
Enzyme 47 UniProtKB/Swiss-Prot ID A4D288 Link Image
Enzyme 47 UniProtKB/Swiss-Prot Entry Name A4D288_HUMAN Link Image
Enzyme 47 PDB ID Not Available
Enzyme 47 Cellular Location Not Available
Enzyme 47 Gene Sequence Not Available
Enzyme 47 GenBank Gene ID CH236956 Link Image
Enzyme 47 GeneCard ID A4D288 Link Image
Enzyme 47 GenAtlas ID Not Available
Enzyme 47 HGNC ID Not Available
Enzyme 47 Chromosome Location Not Available
Enzyme 47 Locus Not Available
Enzyme 47 SNPs SNPJam Report Link Image
Enzyme 47 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 47 Metabolite References Not Available
Enzyme 48 [top]
Enzyme 48 ID 15175
Enzyme 48 Name Cytochrome P450, family 2, subfamily D, polypeptide 6 (Cytochrome P450 2D6)
Enzyme 48 Synonyms Not Available
Enzyme 48 Gene Name CYP2D6
Enzyme 48 Protein Sequence >Cytochrome P450, family 2, subfamily D, polypeptide 6 (Cytochrome P450 2D6)
MGLEALVPLAVIVAIFLLLVDLMHRRQRWAARYPPGPLPLPGLGNLLHVDFQNTPYCFDQ
LRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGPRSQGVF
LARYGPAWREQRRFSVSTLRNLGLGKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDK
AVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVLNAVPVLLHIPALAGKV
LRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAEMEKAKGNPESSFNDENLCIVVA
DLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVI
HEVQRFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHF
LDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVPTGQPRPSHHGV
FAFLVTPSPYELCAVPR
Enzyme 48 Number of Residues 497
Enzyme 48 Molecular Weight 55731
Enzyme 48 Theoretical pI 7.09
Enzyme 48 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 48 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 48 Specific Function Not Available
Enzyme 48 Pathways Not Available
Enzyme 48 Reactions Not Available
Enzyme 48 Pfam Domain Function
Enzyme 48 Signals
  • None
Enzyme 48 Transmembrane Regions
  • None
Enzyme 48 Essentiality Not Available
Enzyme 48 GenBank ID Protein 45768272 Link Image
Enzyme 48 UniProtKB/Swiss-Prot ID Q6NWU0 Link Image
Enzyme 48 UniProtKB/Swiss-Prot Entry Name Q6NWU0_HUMAN Link Image
Enzyme 48 PDB ID Not Available
Enzyme 48 Cellular Location Not Available
Enzyme 48 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 48 GenBank Gene ID BC067432 Link Image
Enzyme 48 GeneCard ID Q6NWU0 Link Image
Enzyme 48 GenAtlas ID CYP2D6 Link Image
Enzyme 48 HGNC ID HGNC:2625 Link Image
Enzyme 48 Chromosome Location 22
Enzyme 48 Locus 22q13.1
Enzyme 48 SNPs SNPJam Report Link Image
Enzyme 48 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 48 Metabolite References Not Available
Enzyme 49 [top]
Enzyme 49 ID 15176
Enzyme 49 Name Cytochrome P450, family 3, subfamily A, polypeptide 5 (Cytochrome P450, family 3, subfamily A, polypeptide 5, isoform CRA_a)
Enzyme 49 Synonyms Not Available
Enzyme 49 Gene Name CYP3A5
Enzyme 49 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 49 Number of Residues 502
Enzyme 49 Molecular Weight 57109
Enzyme 49 Theoretical pI 9.09
Enzyme