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Human Metabolome Database Version 2.5

 

Showing metabocard for Androsterone (HMDB00031)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-04-08 15:33:08
Accession Number HMDB00031
Secondary Accession Numbers Not Available
Common Name Androsterone
Description Androsterone is an inactive breakdown metabolite of testosterone, the product of a reaction mediated by the enzyme oxidative 17beta-hydroxysteroid dehydrogenase (EC 1.1.1.51, 17beta-HSD). Androsterone is also can be metabolized from other adrenal androgens such as dehydroepiandrosterone, dihydrotestosterone or androstenedione, and is considered an inactive end product; however, it can be a physiological effector in its own right. Androsterone might be converted back to dihydrotestosterone. Humans (and other primates) are unique among mammals in having high levels of circulating androsterone glucuronide, a process that is the major role uridine-diphospho-glucuronosyltransferase (EC 2.4.1.17, UGT) enzymes for glucuronidation of steroid metabolism in humans. Conjugation of androsterone is a pathway found in all vertebrates and is widely recognized that the liver is a major site of glucuronidation; however it is now clear that extrahepatic tissues are also involved in the conjugation of compounds to which these tissues are exposed. High levels of androsterone glucuronide found in the human prostate, breast cyst fluid and ovary follicular fluid suggest that glucuronidation of 5alpha-reduced C19 steroids occurs in these tissues as well. In doping control, the ratio of androsterone/etiocholanone provides valuable information that allows the assignment of a urine specimen to a particular person or the identification of urine samples with identical steroid profiles; this is particularly important to detect attempts of urine manipulation including urine alteration and substitution. (PMID: 9188497, 17017935, 14643063, 12943709, 9699884, 17260133)
Synonyms
  1. (3R,5S,8R,9S,10S,13S,14S)-3-hydroxy-10,13-dimethyl-1,2,3,4,5,6,7,8,9,11,12,14,15,16-tetradecahydrocyclopenta[a]phenanthren-17-one
  2. (3alpha,5alpha)-3-hydroxy-Androstan-17-one
  3. 3-Epihydroxyetioallocholan-17-one
  4. 3-Hydroxyandrostan-17-one
  5. 3-alpha-Hydroxy-17-androstanone
  6. 3-alpha-Hydroxy-5-alpha-androstan-17-one
  7. 3-alpha-Hydroxy-5-alpha-androstane-17-one
  8. 3-alpha-Hydroxyetioallocholan-17-one
  9. 3-alpha-hydroxy-5alpha-Androstan-17-one
  10. 3-hydroxy-(3-alpha,5-alpha)-Androstan-17-one
  11. 3a-Hydroxyetioallocholan-17-one
  12. 3alpha-Hydroxy-17-androstanone
  13. 3alpha-Hydroxy-5alpha-androstan-17-one
  14. 3alpha-Hydroxyetioallocholan-17-one
  15. 5-alpha-Androstan-3-alpha-ol-17-one
  16. 5-alpha-Androstane-3alpha-ol-17-one
  17. 5-alpha-Androsterone
  18. 5a-Androstan-3a-ol-17-one
  19. 5a-Androstane-3a-ol-17-one
  20. 5a-Androsterone
  21. 5alpha-Androstane-3alpha-ol-17-one
  22. 5alpha-Androsterone
  23. Androkinine
  24. Androstanon-3-alpha-ol-17-one
  25. Androsterone
  26. Androtine
  27. Atromide ICI
  28. cis-Androsterone
Chemical IUPAC Name (3R,5S,8R,9S,10S,13S,14S)-3-hydroxy-10,13-dimethyl-1,2,3,4,5,6,7,8,9,11,12,14,15,16-tetradecahydrocyclopenta[a]phenanthren-17-one
Chemical Formula C19H30O2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Cholesterols and derivatives
Class
  • Steroids and Steroid Derivatives
Sub Class
  • Ketosteroids
Family
  • Mammalian Metabolite
Species
  • ketone
  • secondary alcohol
Biofunction
  • Hormones, Membrane component
Application
Source
  • Endogenous
Average Molecular Weight 290.440
Monoisotopic Molecular Weight 290.224579
Isomeric SMILES C[C@]12CCC(O)C[C@@H]1CC[C@@H]1[C@@H]2CC[C@@]2(C)[C@H]1CCC2=O
Canonical SMILES CC12CCC(O)CC1CCC1C2CCC2(C)C1CCC2=O
KEGG Compound ID C00523 Link Image
BioCyc ID ANDROSTERONE Link Image
BiGG ID 35244 Link Image
Wikipedia Link Androsterone Link Image
NuGOwiki Link HMDB00031 Link Image
Metagene Link HMDB00031 Link Image
METLIN ID 2797 Link Image
PubChem Compound 5879 Link Image
PubChem Substance 7885731 Link Image
ChEBI ID 16032 Link Image
CAS Registry Number 53-41-8
InChI Identifier InChI=1/C19H30O2/c1-18-9-7-13(20)11-12(18)3-4-14-15-5-6-17(21)19(15,2)10-8-16(14)18/h12-16,20H,3-11H2,1-2H3/t12-,13-,14-,15-,16-,18-,19-/m0/s1
Synthesis Reference Marker, Russell E. Androsterone. Journal of the American Chemical Society (1935), 57 1755-6.
Melting Point (Experimental) 185 oC
Experimental Water Solubility 0.012 mg/mL at 23 oC [YALKOWSKY,SH & DANNENFELSER,RM (1992)] Source: PhysProp
Predicted Water Solubility 6.34e-03 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity 3.69 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity 3.71 [Predicted by ALOGPS]; 4.3 [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 Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Membrane (Predicted from LogP)
  • Cytoplasm
  • endoplasmic reticulum
  • Extracellular
Biofluid Location
  • Blood
  • N/A
  • Urine
Tissue Location
Tissue References
Intestine
Most Tissues
Primarily Liver
Prostate
Testes
Concentrations (Normal)
Biofluid Blood
Value 0.00065 (0.00053-0.00088) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Kancheva L, Hill M, Vcelakova H, Vrbikova J, Pelikanova T, Starka L: The identification and simultaneous quantification of neuroactive androstane steroids and their polar conjugates in the serum of adult men, using gas chromatography-mass spectrometry. Steroids. 2007 Oct;72(11-12):792-801. Epub 2007 Jul 10. [PubMed Link Image]
Biofluid Blood
Value 0.12 +/- 0.014 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Kim YS, Zhang H, Kim HY: Profiling neurosteroids in cerebrospinal fluids and plasma by gas chromatography/electron capture negative chemical ionization mass spectrometry. Anal Biochem. 2000 Jan 15;277(2):187-95. [PubMed Link Image]
Biofluid N/A
Value 0.041 +/-0.017 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal Prostate tissue
Comments Not Available
References
  • Hammond GL: Endogenous steroid levels in the human prostate from birth to old age: a comparison of normal and diseased tissues. J Endocrinol. 1978 Jul;78(1):7-19. [PubMed Link Image]
Biofluid Urine
Value 0.66 umol/mmol creatinine
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Teller WM, Homoki J, Wudy S, Schlickenrieder JH: Adrenarche is dissociated from gonadarche--studies in patients with Turner's syndrome. Acta Endocrinol Suppl (Copenh). 1986;279:232-40. [PubMed Link Image]
Biofluid Urine
Value 6.69 +/- 1.65 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Schonberger W, Benes P, Morsches B, Zabel B, Scheidt E: [Improvement in the longitudinal growth in Ullrich-Turner syndrome with oxandrolone. Function of urinary excretion of steroid hormones] Dtsch Med Wochenschr. 1982 Jul 2;107(26):1008-11. [PubMed Link Image]
Biofluid Urine
Value 0.36 (0.11-0.67) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Gilad S, Chayen R, Tordjman K, Kisch E, Stern N: Assessment of 5 alpha-reductase activity in hirsute women: comparison of serum androstanediol glucuronide with urinary androsterone and aetiocholanolone excretion. Clin Endocrinol (Oxf). 1994 Apr;40(4):459-64. [PubMed Link Image]
Biofluid Urine
Value 0.27 (0.23-0.33) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Shamim W, Yousufuddin M, Bakhai A, Coats AJ, Honour JW: Gender differences in the urinary excretion rates of cortisol and androgen metabolites. Ann Clin Biochem. 2000 Nov;37 ( Pt 6):770-4. [PubMed Link Image]
Biofluid Urine
Value 0.16 (0.11-0.18) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Shamim W, Yousufuddin M, Bakhai A, Coats AJ, Honour JW: Gender differences in the urinary excretion rates of cortisol and androgen metabolites. Ann Clin Biochem. 2000 Nov;37 ( Pt 6):770-4. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid N/A
Value 0.014 +/- 0.001 uM
Age Adult:>18 yrs old
Sex Both
Condition Benign prostatic hyperplasia
Comments Tissue Source: prostate tissue
References
  • Hammond GL: Endogenous steroid levels in the human prostate from birth to old age: a comparison of normal and diseased tissues. J Endocrinol. 1978 Jul;78(1):7-19. [PubMed Link Image]
Biofluid Urine
Value 0.77 +/- 0.08 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Comments Not Available
References
  • Gilad S, Chayen R, Tordjman K, Kisch E, Stern N: Assessment of 5 alpha-reductase activity in hirsute women: comparison of serum androstanediol glucuronide with urinary androsterone and aetiocholanolone excretion. Clin Endocrinol (Oxf). 1994 Apr;40(4):459-64. [PubMed Link Image]
Biofluid Urine
Value 0.000092 +/- 0.000082 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
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 prostatic hyperplasia
  • Hammond GL: Endogenous steroid levels in the human prostate from birth to old age: a comparison of normal and diseased tissues. J Endocrinol. 1978 Jul;78(1):7-19. [PubMed Link Image]
OMIM ID
  • 600082 Link Image (Benign prostatic hyperplasia)
Pathways Not Available
General References
  1. Muller L, Phillipou G: Quantification of 5 alpha- and 5 beta-androstanediols in urine by gas chromatography-mass spectrometry. Clin Chem. 1987 Feb;33(2 Pt 1):256-60. [PubMed Link Image]
  2. Schonberger W, Benes P, Morsches B, Zabel B, Scheidt E: [Improvement in the longitudinal growth in Ullrich-Turner syndrome with oxandrolone. Function of urinary excretion of steroid hormones] Dtsch Med Wochenschr. 1982 Jul 2;107(26):1008-11. [PubMed Link Image]
  3. Kim YS, Zhang H, Kim HY: Profiling neurosteroids in cerebrospinal fluids and plasma by gas chromatography/electron capture negative chemical ionization mass spectrometry. Anal Biochem. 2000 Jan 15;277(2):187-95. [PubMed Link Image]
  4. Labows JN, Preti G, Hoelzle E, Leyden J, Kligman A: Steroid analysis of human apocrine secretion. Steroids. 1979 Sep;34(3):249-58. [PubMed Link Image]
  5. Raju U, Kadner S, Levitz M, Kaganowicz A, Blaustein A: Glucosiduronidation and esterification of androsterone by human breast tumors in vitro. Steroids. 1981 Apr;37(4):399-407. [PubMed Link Image]
  6. Kaminski RM, Marini H, Kim WJ, Rogawski MA: Anticonvulsant activity of androsterone and etiocholanolone. Epilepsia. 2005 Jun;46(6):819-27. [PubMed Link Image]
  7. Grosse J, Anielski P, Hemmersbach P, Lund H, Mueller RK, Rautenberg C, Thieme D: Formation of 19-norsteroids by in situ demethylation of endogenous steroids in stored urine samples. Steroids. 2005 Jul;70(8):499-506. Epub 2005 Mar 29. [PubMed Link Image]
  8. Toth I, Faredin I: Steroids excreted by human skin. II. C19-steroid sulphates in human axillary sweat. Acta Med Hung. 1985;42(1-2):21-8. [PubMed Link Image]
  9. Teller WM, Homoki J, Wudy S, Schlickenrieder JH: Adrenarche is dissociated from gonadarche--studies in patients with Turner's syndrome. Acta Endocrinol Suppl (Copenh). 1986;279:232-40. [PubMed Link Image]
  10. Mitamura K, Setaka M, Shimada K, Honma S, Namiki M, Koh E, Mizokami A: Determination of sulfates of androsterone and epiandrosterone in human serum using isotope diluted liquid chromatography-electrospray ionization-mass spectrometry. Biomed Chromatogr. 2005 Dec;19(10):796-801. [PubMed Link Image]
  11. Tchedam Ngatcha B, Luu-The V, Labrie F, Poirier D: Androsterone 3alpha-ether-3beta-substituted and androsterone 3beta-substituted derivatives as inhibitors of type 3 17beta-hydroxysteroid dehydrogenase: chemical synthesis and structure-activity relationship. J Med Chem. 2005 Aug 11;48(16):5257-68. [PubMed Link Image]
  12. Hammond GL: Endogenous steroid levels in the human prostate from birth to old age: a comparison of normal and diseased tissues. J Endocrinol. 1978 Jul;78(1):7-19. [PubMed Link Image]
  13. Wikipedia Link Image
Metabolic Enzymes
  1. Aldo-keto reductase family 1 member C4
  2. Bile salt sulfotransferase
  3. Aldo-keto reductase family 1 member C3
  4. Aldo-keto reductase family 1 member C1
  5. Aldo-keto reductase family 1 member C2
  6. UDP-glucuronosyltransferase 2B28 precursor
  7. UDP-glucuronosyltransferase 2B4 precursor
  8. UDP-glucuronosyltransferase 1-4 precursor
  9. UDP-glucuronosyltransferase 2B7 precursor
  10. UDP-glucuronosyltransferase 2B15 precursor
  11. UDP-glucuronosyltransferase 2A1 precursor
  12. UDP-glucuronosyltransferase 1-1 precursor
  13. UDP-glucuronosyltransferase 1-9 precursor
  14. UDP-glucuronosyltransferase 1-3 precursor
  15. UDP-glucuronosyltransferase 2B17 precursor
  16. UDP-glucuronosyltransferase 1-6 precursor
  17. UDP-glucuronosyltransferase 1-5 precursor
  18. UDP-glucuronosyltransferase 2B11 precursor
  19. Androgen receptor
  20. Dehydrogenase/reductase SDR family member 9 precursor
  21. Sterol/retinol dehydrogenase
  22. UDP-glucuronosyltransferase 2A3 precursor
  23. UDP glycosyltransferase 1 family polypeptide A10 (HCG2039726, isoform CRA_f)
  24. UDP glycosyltransferase 1 family polypeptide A8 (HCG2039726, isoform CRA_e)
  25. UDP glycosyltransferase 1 family polypeptide A7
  26. cDNA FLJ76966, highly similar to Homo sapiens UDP glucuronosyltransferase 2 family, polypeptide B10 (UGT2B10), mRNA (UDP glucuronosyltransferase 2 family, polypeptide B10, isoform CRA_b)
  27. cDNA, FLJ93689, highly similar to Homo sapiens UDP glucuronosyltransferase 2 family, polypeptide B7 (UGT2B7), mRNA
Enzyme 1 [top]
Enzyme 1 ID 5303
Enzyme 1 Name Aldo-keto reductase family 1 member C4
Enzyme 1 Synonyms
  1. Chlordecone reductase
  2. CDR
  3. 3-alpha-hydroxysteroid dehydrogenase type I
  4. 3-alpha-HSD1
  5. Dihydrodiol dehydrogenase 4
  6. DD4
  7. HAKRA
Enzyme 1 Gene Name AKR1C4
Enzyme 1 Protein Sequence >Aldo-keto reductase family 1 member C4
MDPKYQRVELNDGHFMPVLGFGTYAPPEVPRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQ
VGLAIRSKIADGSVKREDIFYTSKLWCTFFQPQMVQPALESSLKKLQLDYVDLYLLHFPM
ALKPGETPLPKDENGKVIFDTVDLSATWEVMEKCKDAGLAKSIGVSNFNCRQLEMILNKP
GLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRHKLWVDPNSPVLLEDPV
LCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLN
RNYRYVVMDFLMDHPDYPFSDEY
Enzyme 1 Number of Residues 323
Enzyme 1 Molecular Weight 37095
Enzyme 1 Theoretical pI 7.19
Enzyme 1 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
Component
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Catalyzes the transformation of the potent androgen dihydrotestosterone (DHT) into the less active form, 5-alpha- androstan-3alpha,17beta-diol (3-alpha-diol). Also has some 20- alpha-hydroxysteroid dehydrogenase activity. The biotransformation of the pesticide chlordecone (kepone) to its corresponding alcohol leads to increased biliary excretion of the pesticide and concomitant reduction of its neurotoxicity since bile is the major excretory route
Enzyme 1 Pathways
Enzyme 1 Reactions
  • chlordecone alcohol + NADP+ = chlordecone + NADPH + H+
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 4261710 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P17516 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name AK1C4_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >972 bp
ATGGATCCCAAATATCAGCGTGTAGAGCTAAATGATGGTCATTTCATGCCCGTATTGGGA
TTTGGCACCTATGCACCTCCAGAGGTTCCGAGGAACAGAGCTGTAGAGGTCACCAAATTA
GCAATAGAAGCTGGCTTCCGCCATATTGATTCTGCTTATTTATACAATAATGAGGAGCAG
GTTGGACTGGCCATCCGAAGCAAGATTGCAGATGGCAGTGTGAAGAGAGAAGACATATTC
TACACTTCAAAGCTTTGGTGCACTTTCTTTCAACCACAGATGGTCCAACCAGCCTTGGAA
AGCTCACTGAAAAAACTTCAACTGGACTATGTTGACCTCTATCTTCTTCATTTCCCAATG
GCTCTCAAGCCAGGTGAGACGCCACTACCAAAAGATGAAAATGGAAAAGTAATATTCGAC
ACAGTGGATCTCTCTGCCACATGGGAGGTCATGGAGAAGTGTAAGGATGCAGGATTGGCC
AAGTCCATCGGGGTGTCAAACTTCAACTGCAGGCAGCTGGAGATGATCCTCAACAAGCCA
GGACTCAAGTACAAGCCTGTCTGCAACCAGGTAGAATGTCATCCTTACCTCAACCAGAGC
AAACTGCTGGATTTCTGCAAGTCAAAAGACATTGTTCTGGTTGCCCACAGTGCTCTGGGA
ACCCAACGACATAAACTATGGGTGGACCCAAACTCCCCAGTTCTTTTGGAGGACCCAGTT
CTTTGTGCCTTAGCAAAGAAACACAAACGAACCCCAGCCCTGATTGCCCTGCGCTACCAG
CTGCAGCGTGGGGTTGTGGTCCTGGCCAAGAGCTACAATGAGCAGCGGATCAGAGAGAAC
ATCCAGGTTTTTGAATTCCAGTTGACATCAGAGGATATGAAAGTTCTAGATGGTCTAAAC
AGAAATTATCGATATGTTGTCATGGATTTTCTTATGGACCATCCTGATTATCCATTTTCA
GATGAATATTAG
Enzyme 1 GenBank Gene ID S68287 Link Image
Enzyme 1 GeneCard ID AKR1C4 Link Image
Enzyme 1 GenAtlas ID AKR1C4 Link Image
Enzyme 1 HGNC ID HGNC:387 Link Image
Enzyme 1 Chromosome Location 10
Enzyme 1 Locus 10p15-p14
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Qin KN, New MI, Cheng KC: Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase. J Steroid Biochem Mol Biol. 1993 Dec;46(6):673-9. [PubMed Link Image]
  2. Khanna M, Qin KN, Wang RW, Cheng KC: Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases. J Biol Chem. 1995 Aug 25;270(34):20162-8. [PubMed Link Image]
  3. Khanna M, Qin KN, Cheng KC: Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning of multiple cDNAs encoding structurally related proteins in humans. J Steroid Biochem Mol Biol. 1995 Jun;53(1-6):41-6. [PubMed Link Image]
  4. Kume T, Iwasa H, Shiraishi H, Yokoi T, Nagashima K, Otsuka M, Terada T, Takagi T, Hara A, Kamataki T: Characterization of a novel variant (S145C/L311V) of 3alpha-hydroxysteroid/dihydrodiol dehydrogenase in human liver. Pharmacogenetics. 1999 Dec;9(6):763-71. [PubMed Link Image]
  5. Nishizawa M, Nakajima T, Yasuda K, Kanzaki H, Sasaguri Y, Watanabe K, Ito S: Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes. Genes Cells. 2000 Feb;5(2):111-25. [PubMed Link Image]
  6. Dufort I, Labrie F, Luu-The V: Human types 1 and 3 3 alpha-hydroxysteroid dehydrogenases: differential lability and tissue distribution. J Clin Endocrinol Metab. 2001 Feb;86(2):841-6. [PubMed Link Image]
  7. Winters CJ, Molowa DT, Guzelian PS: Isolation and characterization of cloned cDNAs encoding human liver chlordecone reductase. Biochemistry. 1990 Jan 30;29(4):1080-7. [PubMed Link Image]
  8. Deyashiki Y, Ogasawara A, Nakayama T, Nakanishi M, Miyabe Y, Sato K, Hara A: Molecular cloning of two human liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder. Biochem J. 1994 Apr 15;299 ( Pt 2):545-52. [PubMed Link Image]
  9. Binstock JM, Iyer RB, Hamby CV, Fried VA, Schwartz IS, Weinstein BI, Southren AL: Human hepatic 3 alpha-hydroxysteroid dehydrogenase: possible identity with human hepatic chlordecone reductase. Biochem Biophys Res Commun. 1992 Sep 16;187(2):760-6. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5583
Enzyme 2 Name Bile salt sulfotransferase
Enzyme 2 Synonyms
  1. Hydroxysteroid Sulfotransferase
  2. HST
  3. Dehydroepiandrosterone sulfotransferase
  4. DHEA-ST
  5. ST2
  6. ST2A3
Enzyme 2 Gene Name SULT2A1
Enzyme 2 Protein Sequence >Bile salt sulfotransferase
MSDDFLWFEGIAFPTMGFRSETLRKVRDEFVIRDEDVIILTYPKSGTNWLAEILCLMHSK
GDAKWIQSVPIWERSPWVESEIGYTALSETESPRLFSSHLPIQLFPKSFFSSKAKVIYLM
RNPRDVLVSGYFFWKNMKFIKKPKSWEEYFEWFCQGTVLYGSWFDHIHGWMPMREEKNFL
LLSYEELKQDTGRTIEKICQFLGKTLEPEELNLILKNSSFQSMKENKMSNYSLLSVDYVV
DKAQLLRKGVSGDWKNHFTVAQAEDFDKLFQEKMADLPRELFPWE
Enzyme 2 Number of Residues 285
Enzyme 2 Molecular Weight 33780
Enzyme 2 Theoretical pI 5.76
Enzyme 2 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
Component
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Catalyzes the sulfation of steroids and bile acids in the liver and adrenal glands
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions
  • 3'-phosphoadenylyl sulfate + taurolithocholate = adenosine 3',5'-bisphosphate + taurolithocholate sulfate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 306702 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q06520 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name ST2A1_HUMAN Link Image
Enzyme 2 PDB ID 1OV4 Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >858 bp
ATGTCGGACGATTTCTTATGGTTTGAAGGCATAGCTTTCCCTACTATGGGTTTCAGATCC
GAAACCTTAAGAAAAGTACGTGATGAGTTCGTGATAAGGGATGAAGATGTAATAATATTG
ACTTACCCCAAATCAGGAACAAACTGGTTGGCTGAGATTCTCTGCCTGATGCACTCCAAG
GGGGATGCCAAGTGGATCCAATCTGTGCCCATCTGGGAGCGATCACCCTGGGTAGAGAGT
GAGATTGGGTATACAGCACTCAGTGAAAGCGAGAGTCCACGTTTATTCTCCTCCCACCTC
CCCATCCAGTTATTCCCCAAGTCTTTCTTCAGTTCCAAGGCCAAGGTGATTTATCTCATG
AGAAATCCCAGAGATGTTTTGGTGTCTGGTTATTTTTTCTGGAAAAACATGAAGTTTATT
AAGAAACCAAAGTCATGGGAAGAATATTTTGAATGGTTTTGTCAAGGAACTGTGCTATAT
GGGTCATGGTTTGACCACATTCATGGCTGGATGCCCATGAGAGAGGAGAAAAACTTCCTG
TTACTGAGTTATGAGGAGCTGAAACAGGACACAGGAAGAACCATAGAGAAGATCTGTCAA
TTCCTGGGAAAGACGTTAGAACCCGAAGAACTGAACTTAATTCTCAAGAACAGCTCCTTT
CAGAGCATGAAAGAAAACAAGATGTCCAATTATTCCCTCCTGAGTGTTGATTATGTAGTG
GACAAAGCACAACTTCTGAGAAAAGGTGTATCTGGGGACTGGAAAAATCACTTCACAGTG
GCCCAAGCTGAAGACTTTGATAAATTGTTCCAAGAGAAGATGGCAGATCTTCCTCGAGAG
CTGTTCCCATGGGAATAA
Enzyme 2 GenBank Gene ID L20000 Link Image
Enzyme 2 GeneCard ID SULT2A1 Link Image
Enzyme 2 GenAtlas ID SULT2A1 Link Image
Enzyme 2 HGNC ID HGNC:11458 Link Image
Enzyme 2 Chromosome Location 19
Enzyme 2 Locus 19q13.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Comer KA, Falany JL, Falany CN: Cloning and expression of human liver dehydroepiandrosterone sulphotransferase. Biochem J. 1993 Jan 1;289 ( Pt 1):233-40. [PubMed Link Image]
  2. Otterness DM, Wieben ED, Wood TC, Watson WG, Madden BJ, McCormick DJ, Weinshilboum RM: Human liver dehydroepiandrosterone sulfotransferase: molecular cloning and expression of cDNA. Mol Pharmacol. 1992 May;41(5):865-72. [PubMed Link Image]
  3. Forbes KJ, Hagen M, Glatt H, Hume R, Coughtrie MW: Human fetal adrenal hydroxysteroid sulphotransferase: cDNA cloning, stable expression in V79 cells and functional characterisation of the expressed enzyme. Mol Cell Endocrinol. 1995 Jul;112(1):53-60. [PubMed Link Image]
  4. Luu-The V, Dufort I, Paquet N, Reimnitz G, Labrie F: Structural characterization and expression of the human dehydroepiandrosterone sulfotransferase gene. DNA Cell Biol. 1995 Jun;14(6):511-8. [PubMed Link Image]
  5. Otterness DM, Her C, Aksoy S, Kimura S, Wieben ED, Weinshilboum RM: Human dehydroepiandrosterone sulfotransferase gene: molecular cloning and structural characterization. DNA Cell Biol. 1995 Apr;14(4):331-41. [PubMed Link Image]
  6. Kong AN, Yang L, Ma M, Tao D, Bjornsson TD: Molecular cloning of the alcohol/hydroxysteroid form (hSTa) of sulfotransferase from human liver. Biochem Biophys Res Commun. 1992 Aug 31;187(1):448-54. [PubMed Link Image]
Enzyme 2 Metabolite References
  1. Chang HJ, Shi R, Rehse P, Lin SX: Identifying androsterone (ADT) as a cognate substrate for human dehydroepiandrosterone sulfotransferase (DHEA-ST) important for steroid homeostasis: structure of the enzyme-ADT complex. J Biol Chem. 2004 Jan 23;279(4):2689-96. Epub 2003 Oct 21. [PubMed Link Image]
Enzyme 3 [top]
Enzyme 3 ID 5596
Enzyme 3 Name Aldo-keto reductase family 1 member C3
Enzyme 3 Synonyms
  1. Trans-1,2- dihydrobenzene-1,2-diol dehydrogenase
  2. 3-alpha- hydroxysteroid dehydrogenase type 2
  3. 3-alpha-HSD type 2
  4. 3-alpha-HSD type II, brain
  5. Prostaglandin F synthase
  6. PGFS
  7. Estradiol 17-beta-dehydrogenase
  8. 17-beta-hydroxysteroid dehydrogenase type 5
  9. 17-beta-HSD 5
  10. Chlordecone reductase homolog HAKRb
  11. HA1753
  12. Dihydrodiol dehydrogenase type I
  13. Dihydrodiol dehydrogenase 3
  14. DD3
  15. DD-3
Enzyme 3 Gene Name AKR1C3
Enzyme 3 Protein Sequence >Aldo-keto reductase family 1 member C3
MDSKQQCVKLNDGHFMPVLGFGTYAPPEVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQ
VGLAIRSKIADGSVKREDIFYTSKLWSTFHRPELVRPALENSLKKAQLDYVDLYLIHSPM
SLKPGEELSPTDENGKVIFDIVDLCTTWEAMEKCKDAGLAKSIGVSNFNRRQLEMILNKP
GLKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRDKRWVDPNSPVLLEDPV
LCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLD
RNLHYFNSDSFASHPNYPYSDEY
Enzyme 3 Number of Residues 323
Enzyme 3 Molecular Weight 36845
Enzyme 3 Theoretical pI 8.06
Enzyme 3 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
Component
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Catalyzes the conversion of aldehydes and ketones to alcohols. Catalyzes the reduction of prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ) and the oxidation of 9alpha,11beta- PGF2 to PGD2. Functions as a bi-directional 3alpha-, 17beta- and 20alpha HSD. Can interconvert active androgens, estrogens and progestins with their cognate inactive metabolites. Preferentially transforms androstenedione (4-dione) to testosterone
Enzyme 3 Pathways
Enzyme 3 Reactions
  • trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 4261711 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P42330 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name AK1C3_HUMAN Link Image
Enzyme 3 PDB ID 1XF0 Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >972 bp
ATGGATTCCAAACAGCAGTGTGTAAAGCTAAATGATGGCCACTTCATGCCTGTATTGGGA
TTTGGCACCTATGCACCTCCAGAGGTTCCGAGAAGTAAAGCTTTGGAGGTCACAAAATTA
GCAATAGAAGCTGGGTTCCGCCATATAGATTCTGCTCATTTATACAATAATGAGGAGCAG
GTTGGACTGGCCATCCGAAGCAAGATTGCAGATGGCAGTGTTGAGAGAGAAGACATATTC
TACACTTCAAAGCTTTGGTCCACTTTTCATCGACCAGAGTTGGTCCGACCAGCCTTGGAA
AACTCACTGAAGAAAGCTCAATTGGACTATGTTGACCTCTATCTTATTCATTCTCCAATG
TCTCTAAAGCCAGGTGAGGAACTTTCACCAACAGATGAAAATGGAAAAGTAATATTTGAC
ATAGTGGATCTCTGTACCACCTGGGAGGCCATGGAGAAGTGTAAGGATGCAGGATTGGCC
AAGTCCATTGGGGTATCAAACTTCAACCGCAGGCAGCTGGAGATCATCCTCAACAAGCCA
GGACTCAAGTACAAGCCTGTCTGCAACCAGGTAGAATGTCATCCGTATTTCAACCGGAGT
AAATTGCTAGATTTCTGCAAGTCGAAAGATATTGTTCTGGTTGCCTATAGTGCTCTGGGA
TCTCAACGAGACAAACGATGGGTGGACCCGAACTCCCCGGTCCTCTTGGAGGACCCAGTC
CTTTGTGCCTTGGCAAAAAAGCACAAGCGAACCCCAGCCCTGATTGCCCTGCGCTACCAG
CTGCAGCGTGGGGTTGTGGTCCTGGCCAAGAGCTACAATGAGCAGCGCATCAGACAGAAC
GTGCAGGTTTTTGAGTTCCAGTTGACTGCAGAGGACATGAAAGCCATAGATGGCCTAGAC
AGAAATCTCCACTATTTTAACAGTGATAGTTTTGCTAGCCACCCTAATTATCCATATTCA
GATGAATATTAA
Enzyme 3 GenBank Gene ID S68288 Link Image
Enzyme 3 GeneCard ID AKR1C3 Link Image
Enzyme 3 GenAtlas ID AKR1C3 Link Image
Enzyme 3 HGNC ID HGNC:386 Link Image
Enzyme 3 Chromosome Location 10
Enzyme 3 Locus 10p15-p14
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Qin KN, New MI, Cheng KC: Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase. J Steroid Biochem Mol Biol. 1993 Dec;46(6):673-9. [PubMed Link Image]
  2. Khanna M, Qin KN, Wang RW, Cheng KC: Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases. J Biol Chem. 1995 Aug 25;270(34):20162-8. [PubMed Link Image]
  3. Khanna M, Qin KN, Cheng KC: Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning of multiple cDNAs encoding structurally related proteins in humans. J Steroid Biochem Mol Biol. 1995 Jun;53(1-6):41-6. [PubMed Link Image]
  4. Lin HK, Jez JM, Schlegel BP, Peehl DM, Pachter JA, Penning TM: Expression and characterization of recombinant type 2 3 alpha-hydroxysteroid dehydrogenase (HSD) from human prostate: demonstration of bifunctional 3 alpha/17 beta-HSD activity and cellular distribution. Mol Endocrinol. 1997 Dec;11(13):1971-84. [PubMed Link Image]
  5. Suzuki-Yamamoto T, Nishizawa M, Fukui M, Okuda-Ashitaka E, Nakajima T, Ito S, Watanabe K: cDNA cloning, expression and characterization of human prostaglandin F synthase. FEBS Lett. 1999 Dec 3;462(3):335-40. [PubMed Link Image]
  6. Griffin LD, Mellon SH: Selective serotonin reuptake inhibitors directly alter activity of neurosteroidogenic enzymes. Proc Natl Acad Sci U S A. 1999 Nov 9;96(23):13512-7. [PubMed Link Image]
  7. Nishizawa M, Nakajima T, Yasuda K, Kanzaki H, Sasaguri Y, Watanabe K, Ito S: Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes. Genes Cells. 2000 Feb;5(2):111-25. [PubMed Link Image]
  8. Penning TM, Burczynski ME, Jez JM, Lin HK, Ma H, Moore M, Ratnam K, Palackal N: Structure-function aspects and inhibitor design of type 5 17beta-hydroxysteroid dehydrogenase (AKR1C3). Mol Cell Endocrinol. 2001 Jan 22;171(1-2):137-49. [PubMed Link Image]
  9. Nagase T, Miyajima N, Tanaka A, Sazuka T, Seki N, Sato S, Tabata S, Ishikawa K, Kawarabayasi Y, Kotani H, et al.: Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1995;2(1):37-43. [PubMed Link Image]
  10. Dufort I, Rheault P, Huang XF, Soucy P, Luu-The V: Characteristics of a highly labile human type 5 17beta-hydroxysteroid dehydrogenase. Endocrinology. 1999 Feb;140(2):568-74. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5623
Enzyme 4 Name Aldo-keto reductase family 1 member C1
Enzyme 4 Synonyms
  1. 20-alpha- hydroxysteroid dehydrogenase
  2. 20-alpha-HSD
  3. Trans- 1,2-dihydrobenzene-1,2-diol dehydrogenase
  4. High- affinity hepatic bile acid-binding protein
  5. HBAB
  6. Chlordecone reductase homolog HAKRC
  7. Dihydrodiol dehydrogenase 1/2
  8. DD1/DD2
Enzyme 4 Gene Name AKR1C1
Enzyme 4 Protein Sequence >Aldo-keto reductase family 1 member C1
MDSKYQCVKLNDGHFMPVLGFGTYAPAEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQ
VGLAIRSKIADGSVKREDIFYTSKLWCNSHRPELVRPALERSLKNLQLDYVDLYLIHFPV
SVKPGEEVIPKDENGKILFDTVDLCATWEAVEKCKDAGLAKSIGVSNFNRRQLEMILNKP
GLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLEDPV
LCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLN
RNVRYLTLDIFAGPPNYPFSDEY
Enzyme 4 Number of Residues 323
Enzyme 4 Molecular Weight 36789
Enzyme 4 Theoretical pI 7.99
Enzyme 4 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
Component
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function Converts progesterone to its inactive form, 20alpha- dihydroxyprogesterone (20alpha-OHP). In the liver and intestine, may have a role in the transport of bile. May have a role in monitoring the intrahepatic bile acid concentration. May play a role in myelin formation
Enzyme 4 Pathways
Enzyme 4 Reactions
  • trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + 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 181549 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q04828 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name AK1C1_HUMAN Link Image
Enzyme 4 PDB ID 1MRQ Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >972 bp
ATGGATTCGAAATATCAGTGTGTGAAGCTGAATGATGGTCACTTCATGCCTGTCCTGGGA
TTTGGCACCTATGCGCCTGCAGAGGTTCCTAAAAGTAAAGCTTTAGAGGCCACCAAATTG
GCAATTGAAGCTGGCTTCCGCCATATTGATTCTGCTCATTTATACAATAATGAGGAGCAG
GTTGGACTGGCCATCCGAAGCAAGATTGCAGATGGCAGTGTGAAGAGAGAAGACATATTC
TACACTTCAAAGCTTTGGTGCAATTCCCATCGACCAGAGTTGGTCCGACCAGCCTTGGAA
AGGTCACTGAAAAATCTTCAATTGGATTATGTTGACCTCTACCTTATTCATTTTCCAGTG
TCTGTAAAGCCAGGTGAGGAAGTGATCCCAAAAGATGAAAATGGAAAAATACTATTTGAC
ACAGTGGATCTCTGTGCCACGTGGGAGGCCGTGGAGAAGTGTAAAGATGCAGGATTGGCC
AAGTCCATCGGGGTGTCCAACTTCAACCGCAGGCAGCTGGAGATGATCCTCAACAAGCCA
GGGCTCAAGTACAAGCCTGTCTGCAACCAGGTGGAATGTCATCCTTACTTCAACCAGAGA
AAACTGCTGGATTTCTGCAAGTCAAAAGACATTGTTCTGGTTGCCTATAGTGCTCTGGGA
TCCCACCGAGAAGAACCATGGGTGGACCCGAACTCCCCGGTGCTCTTGGAGGACCCAGTC
CTTTGTGCCTTGGCAAAAAAGCACAAGCGAACCCCAGCCCTGATTGCCCTGCGCTACCAG
CTACAGCGTGGGGTTGTGGTCCTGGCCAAGAGCTACAATGAGCAGCGCATCAGACAGAAC
GTGCAGGTGTTTGAATTCCAGTTGACTTCAGAGGAGATGAAAGCCATAGATGGCCTAAAC
AGAAATGTGCGATATTTGACCCTTGATATTTTTGCTGGCCCCCCTAATTATCCATTTTCT
GATGAATATTAA
Enzyme 4 GenBank Gene ID M86609 Link Image
Enzyme 4 GeneCard ID AKR1C1 Link Image
Enzyme 4 GenAtlas ID AKR1C1 Link Image
Enzyme 4 HGNC ID HGNC:384 Link Image
Enzyme 4 Chromosome Location 10
Enzyme 4 Locus 10p15-p14
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Stolz A, Hammond L, Lou H, Takikawa H, Ronk M, Shively JE: cDNA cloning and expression of the human hepatic bile acid-binding protein. A member of the monomeric reductase gene family. J Biol Chem. 1993 May 15;268(14):10448-57. [PubMed Link Image]
  2. Lou H, Hammond L, Sharma V, Sparkes RS, Lusis AJ, Stolz A: Genomic organization and chromosomal localization of a novel human hepatic dihydrodiol dehydrogenase with high affinity bile acid binding. J Biol Chem. 1994 Mar 18;269(11):8416-22. [PubMed Link Image]
  3. Khanna M, Qin KN, Cheng KC: Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning of multiple cDNAs encoding structurally related proteins in humans. J Steroid Biochem Mol Biol. 1995 Jun;53(1-6):41-6. [PubMed Link Image]
  4. Nishizawa M, Nakajima T, Yasuda K, Kanzaki H, Sasaguri Y, Watanabe K, Ito S: Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes. Genes Cells. 2000 Feb;5(2):111-25. [PubMed Link Image]
  5. Zhang Y, Dufort I, Rheault P, Luu-The V: Characterization of a human 20alpha-hydroxysteroid dehydrogenase. J Mol Endocrinol. 2000 Oct;25(2):221-8. [PubMed Link Image]
  6. Qin KN, New MI, Cheng KC: Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase. J Steroid Biochem Mol Biol. 1993 Dec;46(6):673-9. [PubMed Link Image]
  7. Deyashiki Y, Ogasawara A, Nakayama T, Nakanishi M, Miyabe Y, Sato K, Hara A: Molecular cloning of two human liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder. Biochem J. 1994 Apr 15;299 ( Pt 2):545-52. [PubMed Link Image]
  8. Couture JF, Legrand P, Cantin L, Luu-The V, Labrie F, Breton R: Human 20alpha-hydroxysteroid dehydrogenase: crystallographic and site-directed mutagenesis studies lead to the identification of an alternative binding site for C21-steroids. J Mol Biol. 2003 Aug 15;331(3):593-604. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5624
Enzyme 5 Name Aldo-keto reductase family 1 member C2
Enzyme 5 Synonyms
  1. Trans-1,2- dihydrobenzene-1,2-diol dehydrogenase
  2. Type III 3- alpha-hydroxysteroid dehydrogenase
  3. 3-alpha-HSD3
  4. Chlordecone reductase homolog HAKRD
  5. Dihydrodiol dehydrogenase/bile acid-binding protein
  6. DD/BABP
  7. Dihydrodiol dehydrogenase 2
  8. DD2
Enzyme 5 Gene Name AKR1C2
Enzyme 5 Protein Sequence >Aldo-keto reductase family 1 member C2
MDSKYQCVKLNDGHFMPVLGFGTYAPAEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQ
VGLAIRSKIADGSVKREDIFYTSKLWSNSHRPELVRPALERSLKNLQLDYVDLYLIHFPV
SVKPGEEVIPKDENGKILFDTVDLCATWEAMEKCKDAGLAKSIGVSNFNHRLLEMILNKP
GLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLEDPV
LCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLN
RNVRYLTLDIFAGPPNYPFSDEY
Enzyme 5 Number of Residues 323
Enzyme 5 Molecular Weight 36736
Enzyme 5 Theoretical pI 7.55
Enzyme 5 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
Component
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function Works in concert with the 5alpha/5beta-steroid reductases to convert steroid hormones into the 3alpha/5alpha and 3alpha/5beta-tetrahydrosteroids. Catalyzes the inactivation of the most potent androgen 5-alpha-dihydrotestosterone (5alpha-DHT) to 5-alpha-androstane-3alpha,17beta-diol (3-alpha-diol)
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions
  • trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 531160 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P52895 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name AK1C2_HUMAN Link Image
Enzyme 5 PDB ID 1IHI Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >972 bp
ATGGATTCGAAATACCAGTGTGTGAAGCTGAATGATGGTCACTTCATGCCTGTCCTGGGA
TTTGGCACCTATGCGCCTGCAGAGGTTCCTAAAAGTAAAGCTCTAGAGGCCGTCAAATTG
GCAATAGAAGCCGGGTTCCACCATATTGATTCTGCACATGTTTACAATAATGAGGAGCAG
GTTGGACTGGCCATCCGAAGCAAGATTGCAGATGGCAGTGTGAAGAGAGAAGACATATTC
TACACTTCAAAGCTTTGGAGCAATTCCCATCGACCAGAGTTGGTCCGACCAGCCTTGGAA
AGGTCACTGAAAAATCTTCAATTGGACTATGTTGACCTCTATCTTATTCATTTTCCAGTG
TCTGTAAAGCCAGGTGAGGAAGTGATCCCAAAAGATGAAAATGGAAAAATACTATTTGAC
ACAGTGGATCTCTGTGCCACGTGGGAGGCCATGGAGAAGTGTAAAGATGCAGGATTGGCC
AAGTCCATCGGGGTGTCCAACTTCAACCACAGGCTGCTGGAGATGATCCTCAACAAGCCA
GGGCTCAAGTACAAGCCTGTCTGCAACCAGGTGGAATGTCATCCTTACTTCAACCAGAGA
AAACTGCTGGATTTCTGCAAGTCAAAAGACATTGTTCTGGTTGCCTATAGTGCTCTGGGA
TCCCATCGAGAAGAACCATGGGTGGACCCGAACTCCCCGGTGCTCTTGGAGGACCCAGTC
CTTTGTGCCTTGGCAAAAAAGCACAAGCGAACCCCAGCCCTGATTGCCCTGCGCTACCAG
CTGCAGCGTGGGGTTGTGGTCCTGGCCAAGAGCTACAATGAGCAGCGCATCAGACAGAAC
GTGCAGGTGTTTGAATTCCAGTTGACTTCAGAGGAGATGAAAGCCATAGATGGCCTAAAC
AGAAATGTGCGATATTTGACCCTTGATATTTTTGCTGGCCCCCCTAATTATCCATTTTCT
GATGAATATTAA
Enzyme 5 GenBank Gene ID U05598 Link Image
Enzyme 5 GeneCard ID AKR1C2 Link Image
Enzyme 5 GenAtlas ID AKR1C2 Link Image
Enzyme 5 HGNC ID HGNC:385 Link Image
Enzyme 5 Chromosome Location 10
Enzyme 5 Locus 10p15-p14
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Ciaccio PJ, Tew KD: cDNA and deduced amino acid sequences of a human colon dihydrodiol dehydrogenase. Biochim Biophys Acta. 1994 Jun 28;1186(1-2):129-32. [PubMed Link Image]
  2. Qin KN, New MI, Cheng KC: Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase. J Steroid Biochem Mol Biol. 1993 Dec;46(6):673-9. [PubMed Link Image]
  3. Qin KN, Khanna M, Cheng KC: Structure of a gene coding for human dihydrodiol dehydrogenase/bile acid-binding protein. Gene. 1994 Nov 18;149(2):357-61. [PubMed Link Image]
  4. Shiraishi H, Ishikura S, Matsuura K, Deyashiki Y, Ninomiya M, Sakai S, Hara A: Sequence of the cDNA of a human dihydrodiol dehydrogenase isoform (AKR1C2) and tissue distribution of its mRNA. Biochem J. 1998 Sep 1;334 ( Pt 2):399-405. [PubMed Link Image]
  5. Nishizawa M, Nakajima T, Yasuda K, Kanzaki H, Sasaguri Y, Watanabe K, Ito S: Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes. Genes Cells. 2000 Feb;5(2):111-25. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5687
Enzyme 6 Name UDP-glucuronosyltransferase 2B28 precursor
Enzyme 6 Synonyms
  1. UDPGT
Enzyme 6 Gene Name UGT2B28
Enzyme 6 Protein Sequence >UDP-glucuronosyltransferase 2B28 precursor
MALKWTSVLLLIHLGCYFSSGSCGKVLVWTGEYSHWMNMKTILKELVQRGHEVTVLASSA
SILFDPNDAFTLKLEVYPTSLTKTEFENIIMQQVKRWSDIQKDSFWLYFSQEQEILWEFH
DIFRNFCKDVVSNKKVMKKLQESRFDIIFADAFFPCGELLAALLNIPFVYSLCFTPGYTI
ERHSGGLIFPPSYIPVVMSKLSDQMTFMERVKNMIYVLYFDFWFQMCDMKKWDQFYSEVL
GRPTTLFETMGKADIWLMRNSWSFQFPHPFLPNIDFVGGLHCKPAKPLPKEMEEFVQSSG
ENGVVVFSLGSVISNMTAERANVIATALAKIPQKVLWRFDGNKPDALGLNTRLYKWIPQN
DLLGLPKTRAFITHGGANGIYEAIYHGIPMVGIPLFWDQPDNIAHMKAKGAAVRLDFHTM
SSTDLLNALKTVINDPSYKENVMKLSIIQHDQPVKPLHRAVFWIEFVMCHKGAKHLRVAA
RDLTWFQYHSLDVIGFLLACVATVIFVVTKFCLFCFWKFARKGKKGKRD
Enzyme 6 Number of Residues 529
Enzyme 6 Molecular Weight 60907
Enzyme 6 Theoretical pI 8.80
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 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 6 Pathways
Enzyme 6 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-24
Enzyme 6 Transmembrane Regions
  • 495-517
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 13603476 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q9BY64 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name UDB28_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 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 6 GenBank Gene ID AF177272 Link Image
Enzyme 6 GeneCard ID UGT2B28 Link Image
Enzyme 6 GenAtlas ID UGT2B28 Link Image
Enzyme 6 HGNC ID HGNC:13479 Link Image
Enzyme 6 Chromosome Location 4
Enzyme 6 Locus 4q13.2
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 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 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5696
Enzyme 7 Name UDP-glucuronosyltransferase 2B4 precursor
Enzyme 7 Synonyms
  1. UDPGT
  2. Hyodeoxycholic acid
  3. HLUG25
  4. UDPGTh-1
Enzyme 7 Gene Name UGT2B4
Enzyme 7 Protein Sequence >UDP-glucuronosyltransferase 2B4 precursor
MSMKWTSALLLIQLSCYFSSGSCGKVLVWPTEFSHWMNIKTILDELVQRGHEVTVLASSA
SISFDPNSPSTLKFEVYPVSLTKTEFEDIIKQLVKRWAELPKDTFWSYFSQVQEIMWTFN
DILRKFCKDIVSNKKLMKKLQESRFDVVLADAVFPFGELLAELLKIPFVYSLRFSPGYAI
EKHSGGLLFPPSYVPVVMSELSDQMTFIERVKNMIYVLYFEFWFQIFDMKKWDQFYSEVL
GRPTTLSETMAKADIWLIRNYWDFQFPHPLLPNVEFVGGLHCKPAKPLPKEMEEFVQSSG
ENGVVVFSLGSMVSNTSEERANVIASALAKIPQKVLWRFDGNKPDTLGLNTRLYKWIPQN
DLLGHPKTRAFITHGGANGIYEAIYHGIPMVGVPLFADQPDNIAHMKAKGAAVSLDFHTM
SSTDLLNALKTVINDPLYKENAMKLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAA
HDLTWFQYHSLDVTGFLLACVATVIFIITKCLFCVWKFVRTGKKGKRD
Enzyme 7 Number of Residues 528
Enzyme 7 Molecular Weight 60513
Enzyme 7 Theoretical pI 8.75
Enzyme 7 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
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 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 7 Pathways
Enzyme 7 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-23
Enzyme 7 Transmembrane Regions
  • 493-509
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 37589 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P06133 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name UDB4_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 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 7 GenBank Gene ID Y00317 Link Image
Enzyme 7 GeneCard ID UGT2B4 Link Image
Enzyme 7 GenAtlas ID UGT2B4 Link Image
Enzyme 7 HGNC ID HGNC:12553 Link Image
Enzyme 7 Chromosome Location 4
Enzyme 7 Locus 4q13
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 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 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5719
Enzyme 8 Name UDP-glucuronosyltransferase 1-4 precursor
Enzyme 8 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 8 Gene Name UGT1A4
Enzyme 8 Protein Sequence >UDP-glucuronosyltransferase 1-4 precursor
MARGLQVPLPRLATGLLLLLSVQPWAESGKVLVVPTDGSPWLSMREALRELHARGHQAVV
LTPEVNMHIKEEKFFTLTAYAVPWTQKEFDRVTLGYTQGFFETEHLLKRYSRSMAIMNNV
SLALHRCCVELLHNEALIRHLNATSFDVVLTDPVNLCGAVLAKYLSIPAVFFWRYIPCDL
DFKGTQCPNPSSYIPKLLTTNSDHMTFLQRVKNMLYPLALSYICHTFSAPYASLASELFQ
REVSVVDLVSYASVWLFRGDFVMDYPRPIMPNMVFIGGINCANGKPLSQEFEAYINASGE
HGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQND
LLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMT
SEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAH
DLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 8 Number of Residues 534
Enzyme 8 Molecular Weight 60026
Enzyme 8 Theoretical pI 8.68
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 glucuronidates bilirubin IX- alpha to form both the IX-alpha-C8 and IX-alpha-C12 monoconjugates and diconjugate
Enzyme 8 Pathways
Enzyme 8 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-28
Enzyme 8 Transmembrane Regions
  • 492-508
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 340137 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P22310 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name UD14_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >867 bp
ATGGCCAGAGGACTCCAGGTTCCCCTGCCGCGGCTGGCCACAGGACTGCTGCTCCTCCTC
AGTGTCCAGCCCTGGGCTGAGAGTGGAAAGGTGTTGGTGGTGCCCACTGATGGCAGCCCC
TGGCTCAGCATGCGGGAGGCCTTGCGGGAGCTCCATGCCAGAGGCCACCAGGCGGTGGTC
CTCACCCCAGAGGTGAATATGCACATCAAAGAAGAGAAATTTTTCACCCTGACAGCCTAT
GCTGTTCCATGGACCCAGAAGGAATTTGATCGCGTTACGCTGGGCTACACTCAAGGGTTC
TTTGAAACAGAACATCTTCTGAAGAGATATTCTAGAAGTATGGCAATTATGAACAATGTA
TCTTTGGCCCTTCATAGGTGTTGTGTGGAGCTACTGCATAATGAGGCCCTGATCAGGCAC
CTGAATGCTACTTCCTTTGATGTGGTTTTAACAGACCCCGTTAACCTCTGTGGGGCGGTG
CTGGCTAAGTACCTGTCGATTCCTGCTGTGTTTTTTTGGAGGTACATTCCATGTGACTTA
GACTTTAAGGGCACACAGTGTCCAAATCCTTCCTCCTATATTCCTAAGTTACTAACGACC
AATTCAGACCACATGACATTCCTGCAAAGGGTCAAGAACATGCTCTACCCTCTGGCCCTG
TCCTACATTTGCCATACTTTTTCTGCCCCTTATGCAAGTCTTGCCTCTGAGCTTTTTCAG
AGAGAGGTGTCAGTGGTGGATCTTGTCAGCTATGCATCCGTGTGGCTGTTCCGAGGGGAC
TTTGTGATGGACTACCCCAGGCCGATCATGCCCAACATGGTCTTCATTGGGGGCATCAAC
TGTGCCAACGGGAAGCCACTATCTCAG
Enzyme 8 GenBank Gene ID M84128 Link Image
Enzyme 8 GeneCard ID UGT1A4 Link Image
Enzyme 8 GenAtlas ID UGT1A4 Link Image
Enzyme 8 HGNC ID HGNC:12536 Link Image
Enzyme 8 Chromosome Location 2
Enzyme 8 Locus 2q37
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 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 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5721
Enzyme 9 Name UDP-glucuronosyltransferase 2B7 precursor
Enzyme 9 Synonyms
  1. UDPGT
  2. 3,4- catechol estrogen specific
  3. UDPGTh-2
Enzyme 9 Gene Name UGT2B7
Enzyme 9 Protein Sequence >UDP-glucuronosyltransferase 2B7 precursor
MSVKWTSVILLIQLSFCFSSGNCGKVLVWAAEYSHWMNIKTILDELIQRGHEVTVLASSA
SILFDPNNSSALKIEIYPTSLTKTELENFIMQQIKRWSDLPKDTFWLYFSQVQEIMSIFG
DITRKFCKDVVSNKKFMKKVQESRFDVIFADAIFPCSELLAELFNIPFVYSLSFSPGYTF
EKHSGGFIFPPSYVPVVMSELTDQMTFMERVKNMIYVLYFDFWFEIFDMKKWDQFYSEVL
GRPTTLSETMGKADVWLIRNSWNFQFPHPLLPNVDFVGGLHCKPAKPLPKEMEDFVQSSG
ENGVVVFSLGSMVSNMTEERANVIASALAQIPQKVLWRFDGNKPDTLGLNTRLYKWIPQN
DLLGHPKTRAFITHGGANGIYEAIYHGIPMVGIPLFADQPDNIAHMKARGAAVRVDFNTM
SSTDLLNALKRVINDPSYKENVMKLSRIQHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAA
HDLTWFQYHSLDVIGFLLVCVATVIFIVTKCCLFCFWKFARKAKKGKND
Enzyme 9 Number of Residues 529
Enzyme 9 Molecular Weight 60695
Enzyme 9 Theoretical pI 8.45
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 Its unique specificity for 3,4-catechol estrogens and estriol suggests it may play an important role in regulating the level and activity of these potent and active estrogen metabolites
Enzyme 9 Pathways
Enzyme 9 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-23
Enzyme 9 Transmembrane Regions
  • 493-509
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 340080 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P16662 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name UDB7_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1590 bp
ATGTCTGTGAAATGGACTTCAGTAATTTTGCTAATACAACTGAGCTTTTGCTTTAGCTCT
GGGAATTGTGGAAAGGTGCTGGTGTGGGCAGCAGAATACAGCCATTGGATGAATATAAAG
ACAATCCTGGATGAGCTTATTCAGAGAGGTCATGAGGTGACTGTACTGGCATCTTCAGCT
TCCATTCTTTTTGATCCCAACAACTCATCCGCTCTTAAAATTGAAATTTATCCCACATCT
TTAACTAAAACTGAGTTGGAGAATTTCATCATGCAACAGATTAAGAGATGGTCAGACCTT
CCAAAAGATACATTTTGGTTATATTTTTCACAAGTACAGGAAATCATGTCAATATTTGGT
GACATAACTAGAAAGTTCTGTAAAGATGTAGTTTCAAATAAGAAATTTATGAAAAAAGTA
CAAGAGTCAAGATTTGACGTCATTTTTGCAGATGCTATTTTTCCCTGTAGTGAGCTGCTG
GCTGAGCTATTTAACATACCCTTTGTGTACAGTCTCAGCTTCTCTCCTGGCTACACTTTT
GAAAAGCATAGTGGAGGATTTATTTTCCCTCCTTCCTACGTACCTGTTGTTATGTCAGAA
TTAACTGATCAAATGACTTTCATGGAGAGGGTAAAAAATATGATCTATGTGCTTTACTTT
GACTTTTGGTTCGAAATATTTGACATGAAGAAGTGGGATCAGTTTTATAGTGAAGTTCTA
GGAAGACCCACTACGTTATCTGAGACAATGGGGAAAGCTGACGTATGGCTTATTCGAAAC
TCCTGGAATTTTCAGTTTCCTCATCCACTCTTACCAAATGTTGATTTTGTTGGAGGACTC
CACTGCAAACCTGCCAAACCCCTGCCTAAGGAAATGGAAGACTTTGTACAGAGCTCTGGA
GAAAATGGTGTTGTGGTGTTTTCTCTGGGGTCAATGGTCAGTAACATGACAGAAGAAAGG
GCCAACGTAATTGCATCAGCCCTGGCCCAGATCCCACAAAAGGTTCTGTGGAGATTTGAT
GGGAATAAACCAGATACCTTAGGTCTCAATACTCGGCTGTATAAGTGGATACCCCAGAAT
GACCTTCTAGGTCATCCAAAGACCAGAGCTTTTATAACTCATGGTGGAGCCAATGGCATC
TACGAGGCAATCTACCATGGGATCCCTATGGTGGGGATTCCATTGTTTGCCGATCAACCT
GATAACATTGCTCACATGAAGGCCAGGGGAGCAGCTGTTAGAGTGGACTTCAACACAATG
TCGAGTACAGACTTGCTGAATGCATTGAAGAGAGTAATTAATGATCCTTCATATAAAGAG
AATGTTATGAAATTATCAAGAATTCAACATGATCAACCAGTGAAGCCCCTGGATCGAGCA
GTCTTCTGGATTGAATTTGTCATGCGCCACAAAGGAGCTAAACACCTTCGGGTTGCAGCC
CACGACCTCACCTGGTTCCAGTACCACTCTTTGGATGTGATTGGGTTCCTGCTGGTCTGT
GTGGCAACTGTGATATTTATCGTCACAAAATGTTGTCTGTTTTGTTTCTGGAAGTTTGCT
AGAAAAGCAAAGAAGGGAAAAAATGATTAG
Enzyme 9 GenBank Gene ID J05428 Link Image
Enzyme 9 GeneCard ID UGT2B7 Link Image
Enzyme 9 GenAtlas ID UGT2B7 Link Image
Enzyme 9 HGNC ID HGNC:12554 Link Image
Enzyme 9 Chromosome Location 4
Enzyme 9 Locus 4q13
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Ritter JK, Sheen YY, Owens IS: Cloning and expression of human liver UDP-glucuronosyltransferase in COS-1 cells. 3,4-catechol estrogens and estriol as primary substrates. J Biol Chem. 1990 May 15;265(14):7900-6. [PubMed Link Image]
  2. Bhasker CR, McKinnon W, Stone A, Lo AC, Kubota T, Ishizaki T, Miners JO: Genetic polymorphism of UDP-glucuronosyltransferase 2B7 (UGT2B7) at amino acid 268: ethnic diversity of alleles and potential clinical significance. Pharmacogenetics. 2000 Nov;10(8):679-85. [PubMed Link Image]
Enzyme 9 Metabolite References
  1. Coffman BL, King CD, Rios GR, Tephly TR: The glucuronidation of opioids, other xenobiotics, and androgens by human UGT2B7Y(268) and UGT2B7H(268). Drug Metab Dispos. 1998 Jan;26(1):73-7. [PubMed Link Image]
Enzyme 10 [top]
Enzyme 10 ID 5722
Enzyme 10 Name UDP-glucuronosyltransferase 2B15 precursor
Enzyme 10 Synonyms
  1. UDPGT
  2. UDPGTh-3
  3. HLUG4
Enzyme 10 Gene Name UGT2B15
Enzyme 10 Protein Sequence >UDP-glucuronosyltransferase 2B15 precursor
MSLKWTSVFLLIQLSCYFSSGSCGKVLVWPTEYSHWINMKTILEELVQRGHEVTVLTSSA
STLVNASKSSAIKLEVYPTSLTKNDLEDSLLKILDRWIYGVSKNTFWSYFSQLQELCWEY
YDYSNKLCKDAVLNKKLMMKLQESKFDVILADALNPCGELLAELFNIPFLYSLRFSVGYT
FEKNGGGFLFPPSYVPVVMSELSDQMIFMERIKNMIHMLYFDFWFQIYDLKKWDQFYSEV
LGRPTTLFETMGKAEMWLIRTYWDFEFPRPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSS
GENGIVVFSLGSMISNMSEESANMIASALAQIPQKVLWRFDGKKPNTLGSNTRLYKWLPQ
NDLLGHPKTKAFITHGGTNGIYEAIYHGIPMVGIPLFADQHDNIAHMKAKGAALSVDIRT
MSSRDLLNALKSVINDPVYKENVMKLSRIHHDQPMKPLDRAVFWIEFVMRHKGAKHLRVA
AHNLTWIQYHSLDVIAFLLACVATVIFIITKFCLFCFRKLAKKGKKKKRD
Enzyme 10 Number of Residues 530
Enzyme 10 Molecular Weight 60989
Enzyme 10 Theoretical pI 9.04
Enzyme 10 GO Classification Not Available
Enzyme 10 General Function Carbohydrate transport and metabolism
Enzyme 10 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 10 Pathways
Enzyme 10 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 10 Pfam Domain Function Not Available
Enzyme 10 Signals
  • 1-23
Enzyme 10 Transmembrane Regions
  • 495-515
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 23955933 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P54855 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name UDB15_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 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 10 GenBank Gene ID AF548389 Link Image
Enzyme 10 GeneCard ID UGT2B15 Link Image
Enzyme 10 GenAtlas ID UGT2B15 Link Image
Enzyme 10 HGNC ID HGNC:12546 Link Image
Enzyme 10 Chromosome Location 4
Enzyme 10 Locus 4q13
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 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 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5724
Enzyme 11 Name UDP-glucuronosyltransferase 2A1 precursor
Enzyme 11 Synonyms Not Available
Enzyme 11 Gene Name UGT2A1
Enzyme 11 Protein Sequence >UDP-glucuronosyltransferase 2A1 precursor
MLNNLLLFSLQISLIGTTLGGNVLIWPMEGSHWLNVKIIIDELIKKEHNVTVLVASGALF
ITPTSNPSLTFEIYKVPFGKERIEGVIKDFVSTWLENRPSPSTIWRFYQEMAKVIKDFHM
VSQEICDGVLKNQQLMAKLKKSKFEVLVSDPVFPCGDIVALKLGIPFMYSLRFSPASTVE
KHCGKVPYPPSYVPAVLSELTDQMSFTDRIRNFISYHLQDYMFETLWKSWDSYYSKALGR
PTTLCETMGKAEIWLIRTYWDFEFPRPYLPNFEFVGGLHCKPAKPLPKEMEEFIQSSGKN
GVVVFSLGSMVKNLTEEKANLIASALAQIPQKVLWRYKGKKPATLGNNTQLFDWIPQNDL
LGHPKTKAFITHGGTNGIYEAIYHGVPMVGVPMFADQPDNIAHMKAKGAAVEVNLNTMTS
VDLLSALRTVINEPSYKENAMRLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAHD
LTWFQYHSLDVIGFLLVCVTTAIFLVIQCCLFSCQKFGKIGKKKKRE
Enzyme 11 Number of Residues 527
Enzyme 11 Molecular Weight 59873
Enzyme 11 Theoretical pI 9.29
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. 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 11 Pathways
Enzyme 11 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • 1-20
Enzyme 11 Transmembrane Regions
  • 491-507
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 4753766 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q9Y4X1 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name UDA1_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 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 11 GenBank Gene ID AJ006054 Link Image
Enzyme 11 GeneCard ID UGT2A1 Link Image
Enzyme 11 GenAtlas ID UGT2A1 Link Image
Enzyme 11 HGNC ID HGNC:12542 Link Image
Enzyme 11 Chromosome Location 4
Enzyme 11 Locus 4q13
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 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 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5725
Enzyme 12 Name UDP-glucuronosyltransferase 1-1 precursor
Enzyme 12 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 12 Gene Name UGT1A1
Enzyme 12 Protein Sequence >UDP-glucuronosyltransferase 1-1 precursor
MAVESQGGRPLVLGLLLCVLGPVVSHAGKILLIPVDGSHWLSMLGAIQQLQQRGHEIVVL
APDASLYIRDGAFYTLKTYPVPFQREDVKESFVSLGHNVFENDSFLQRVIKTYKKIKKDS
AMLLSGCSHLLHNKELMASLAESSFDVMLTDPFLPCSPIVAQYLSLPTVFFLHALPCSLE
FEATQCPNPFSYVPRPLSSHSDHMTFLQRVKNMLIAFSQNFLCDVVYSPYATLASEFLQR
EVTVQDLLSSASVWLFRSDFVKDYPRPIMPNMVFVGGINCLHQNPLSQEFEAYINASGEH
GIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDL
LGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTS
EDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHD
LTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 12 Number of Residues 533
Enzyme 12 Molecular Weight 59592
Enzyme 12 Theoretical pI 8.09
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. This isoform glucuronidates bilirubin IX- alpha to form both the IX-alpha-C8 and IX-alpha-C12 monoconjugates and diconjugate
Enzyme 12 Pathways
Enzyme 12 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • 1-25
Enzyme 12 Transmembrane Regions
  • 491-507
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 184473 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID P22309 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name UD11_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 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 12 GenBank Gene ID M57899 Link Image
Enzyme 12 GeneCard ID UGT1A1 Link Image
Enzyme 12 GenAtlas ID UGT1A1 Link Image
Enzyme 12 HGNC ID HGNC:12530 Link Image
Enzyme 12 Chromosome Location 2
Enzyme 12 Locus 2q37
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 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 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5726
Enzyme 13 Name UDP-glucuronosyltransferase 1-9 precursor
Enzyme 13 Synonyms
  1. UDP- glucuronosyltransferase 1A9
  2. UDPGT
  3. UGT1*9
  4. UGT1-9
  5. UGT1.9
  6. UGT- 1I
  7. UGT1I
  8. lugP4
Enzyme 13 Gene Name UGT1A9
Enzyme 13 Protein Sequence >UDP-glucuronosyltransferase 1-9 precursor
MACTGWTSPLPLCVCLLLTCGFAEAGKLLVVPMDGSHWFTMRSVVEKLILRGHEVVVVMP
EVSWQLGRSLNCTVKTYSTSYTLEDLDREFKAFAHAQWKAQVRSIYSLLMGSYNDIFDLF
FSNCRSLFKDKKLVEYLKESSFDAVFLDPFDNCGLIVAKYFSLPSVVFARGILCHYLEEG
AQCPAPLSYVPRILLGFSDAMTFKERVRNHIMHLEEHLLCHRFFKNALEIASEILQTPVT
EYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIV
VFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGH
PMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDL
ENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTW
YQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 13 Number of Residues 530
Enzyme 13 Molecular Weight 59942
Enzyme 13 Theoretical pI 7.96
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
  • 1-25
Enzyme 13 Transmembrane Regions
  • 488-504
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 7690346 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID O60656 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name UD19_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 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 13 GenBank Gene ID S55985 Link Image
Enzyme 13 GeneCard ID UGT1A9 Link Image
Enzyme 13 GenAtlas ID UGT1A9 Link Image
Enzyme 13 HGNC ID HGNC:12541 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. 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 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5728
Enzyme 14 Name UDP-glucuronosyltransferase 1-3 precursor
Enzyme 14 Synonyms
  1. UDP- glucuronosyltransferase 1A3
  2. UDPGT
  3. UGT1*3
  4. UGT1-03
  5. UGT1.3
  6. UGT- 1C
  7. UGT1C
Enzyme 14 Gene Name UGT1A3
Enzyme 14 Protein Sequence >UDP-glucuronosyltransferase 1-3 precursor
MATGLQVPLPWLATGLLLLLSVQPWAESGKVLVVPIDGSHWLSMREVLRELHARGHQAVV
LTPEVNMHIKEENFFTLTTYAISWTQDEFDRHVLGHTQLYFETEHFLKKFFRSMAMLNNM
SLVYHRSCVELLHNEALIRHLNATSFDVVLTDPVNLCAAVLAKYLSIPTVFFLRNIPCDL
DFKGTQCPNPSSYIPRLLTTNSDHMTFMQRVKNMLYPLALSYICHAFSAPYASLASELFQ
REVSVVDILSHASVWLFRGDFVMDYPRPIMPNMVFIGGINCANRKPLSQEFEAYINASGE
HGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQND
LLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMT
SEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAH
DLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 14 Number of Residues 534
Enzyme 14 Molecular Weight 60339
Enzyme 14 Theoretical pI 8.28
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 340135 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID P35503 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name UD13_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >867 bp
ATGGCCACAGGACTCCAGGTTCCCCTGCCGTGGCTGGCCACAGGACTGCTGCTTCTCCTC
AGTGTCCAGCCCTGGGCTGAGAGTGGAAAGGTGTTGGTGGTGCCCATTGATGGCAGCCAC
TGGCTCAGCATGCGGGAGGTCTTGCGGGAGCTCCATGCCAGAGGCCACCAGGCAGTGGTC
CTCACCCCAGAGGTGAATATGCACATCAAAGAAGAGAACTTTTTCACCCTGACAACCTAT
GCCATTTCGTGGACCCAGGATGAATTTGATCGCCATGTGCTGGGCCACACTCAACTGTAC
TTTGAAACAGAACATTTTCTGAAGAAATTTTTCAGAAGTATGGCAATGTTGAACAATATG
TCTTTGGTCTATCATAGGTCTTGTGTGGAGCTACTACATAATGAGGCCCTGATCAGGCAC
CTGAATGCTACTTCCTTTGATGTGGTTTTAACAGACCCCGTTAACCTCTGCGCGGCAGTG
CTGGCTAAGTACCTGTCGATTCCTACTGTGTTTTTTTTGAGGAACATTCCATGTGATTTA
GACTTTAAGGGCACACAGTGTCCAAACCCTTCCTCCTATATTCCTAGATTACTAACAACC
AATTCAGACCACATGACATTCATGCAAAGGGTCAAGAACATGCTCTACCCTCTGGCCCTG
TCCTACATTTGCCATGCTTTTTCTGCTCCTTATGCAAGCCTTGCCTCTGAGCTTTTTCAG
AGAGAGGTGTCAGTGGTGGATATTCTCAGTCATGCATCTGTGTGGCTGTTCCGAGGGGAC
TTTGTGATGGACTACCCCAGGCCAATCATGCCCAACATGGTCTTCATTGGGGGCATCAAC
TGTGCCAACAGGAAGCCACTATCTCAG
Enzyme 14 GenBank Gene ID M84127 Link Image
Enzyme 14 GeneCard ID UGT1A3 Link Image
Enzyme 14 GenAtlas ID UGT1A3 Link Image
Enzyme 14 HGNC ID HGNC:12535 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 5731
Enzyme 15 Name UDP-glucuronosyltransferase 2B17 precursor
Enzyme 15 Synonyms
  1. UDPGT
  2. C19- steroid-specific UDP-glucuronosyltransferase
Enzyme 15 Gene Name UGT2B17
Enzyme 15 Protein Sequence >UDP-glucuronosyltransferase 2B17 precursor
MSLKWMSVFLLMQLSCYFSSGSCGKVLVWPTEYSHWINMKTILEELVQRGHEVIVLTSSA
SILVNASKSSAIKLEVYPTSLTKNDLEDFFMKMFDRWTYSISKNTFWSYFSQLQELCWEY
SDYNIKLCEDAVLNKKLMRKLQESKFDVLLADAVNPCGELLAELLNIPFLYSLRFSVGYT
VEKNGGGFLFPPSYVPVVMSELSDQMIFMERIKNMIYMLYFDFWFQAYDLKKWDQFYSEV
LGRPTTLFETMGKAEMWLIRTYWDFEFPRPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSS
GENGIVVFSLGSMISNMSEESANMIASALAQIPQKVLWRFDGKKPNTLGSNTRLYKWLPQ
NDLLGHPKTKAFITHGGTNGIYEAIYHGIPMVGIPLFADQHDNIAHMKAKGAALSVDIRT
MSSRDLLNALKSVINDPIYKENIMKLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVA
AHNLTWIQYHSLDVIAFLLACVATMIFMITKCCLFCFRKLAKTGKKKKRD
Enzyme 15 Number of Residues 530
Enzyme 15 Molecular Weight 61096
Enzyme 15 Theoretical pI 8.73
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. The major substrates of this isozyme are eugenol > 4-methylumbelliferone > dihydrotestosterone (DHT) > androstane-3alpha,17beta-diol (3alpha-diol) > testosterone > androsterone (ADT)
Enzyme 15 Pathways
Enzyme 15 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • 1-23
Enzyme 15 Transmembrane Regions
  • 495-515
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 3287473 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID O75795 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name UDB17_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 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 15 GenBank Gene ID U59209 Link Image
Enzyme 15 GeneCard ID UGT2B17 Link Image
Enzyme 15 GenAtlas ID UGT2B17 Link Image
Enzyme 15 HGNC ID HGNC:12547 Link Image
Enzyme 15 Chromosome Location Not Available
Enzyme 15 Locus Not Available
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 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 15 Metabolite References
  1. 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 16 [top]
Enzyme 16 ID 5732
Enzyme 16 Name UDP-glucuronosyltransferase 1-6 precursor
Enzyme 16 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 16 Gene Name UGT1A6
Enzyme 16 Protein Sequence >UDP-glucuronosyltransferase 1-6 precursor
MACLLRSFQRISAGVFFLALWGMVVGDKLLVVPQDGSHWLSMKDIVEVLSDRGHEIVVVV
PEVNLLLKESKYYTRKIYPVPYDQEELKNRYQSFGNNHFAERSFLTAPQTEYRNNMIVIG
LYFINCQSLLQDRDTLNFFKESKFDALFTDPALPCGVILAEYLGLPSVYLFRGFPCSLEH
TFSRSPDPVSYIPRCYTKFSDHMTFSQRVANFLVNLLEPYLFYCLFSKYEELASAVLKRD
VDIITLYQKVSVWLLRYDFVLEYPRPVMPNMVFIGGINCKKRKDLSQEFEAYINASGEHG
IVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLL
GHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSE
DLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDL
TWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 16 Number of Residues 532
Enzyme 16 Molecular Weight 60751
Enzyme 16 Theoretical pI 8.55
Enzyme 16 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 16 General Function Carbohydrate transport and metabolism
Enzyme 16 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 16 Pathways
Enzyme 16 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • 1-26
Enzyme 16 Transmembrane Regions
  • 490-506
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 340141 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID P19224 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name UD16_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >861 bp
ATGGCCTGCCTCCTTCGCTCATTTCAGAGAATTTCTGCAGGGGTTTTCTTCTTAGCACTT
TGGGGCATGGTTGTAGGTGACAAGCTGCTGGTGGTCCCTCAGGACGGAAGCCACTGGCTT
AGTATGAAGGATATAGTTGAGGTTCTCAGTGACCGGGGTCATGAGATTGTAGTGGTGGTG
CCTGAAGTTAATTTGCTTTTGAAAGAATCCAAATACTACACAAGAAAAATCTATCCAGTG
CCGTATGACCAAGAAGAGCTGAAGAACCGTTACCAATCATTTGGAAACAATCACTTTGCT
GAGCGATCATTCCTAACTGCTCCTCAGACAGAGTACAGGAATAACATGATTGTTATTGGC
CTGTACTTCATCAACTGCCAGAGCCTCCTGCAGGACAGGGACACCCTGAACTTCTTTAAG
GAGAGCAAGTTTGATGCTCTTTTCACAGACCCAGCCTTACCCTGTGGGGTGATCCTGGCT
GAGTATTTGGGCCTACCATCTGTGTACCTCTTCAGGGGTTTTCCGTGTTCCCTGGAGCAT
ACATTCAGCAGAAGCCCAGACCCTGTGTCCTACATTCCCAGGTGCTACACAAAGTTTTCA
GACCACATGACTTTTTCCCAACGAGTGGCCAACTTCCTTGTTAATTTGTTGGAGCCCTAT
CTATTTTATTGTCTGTTTTCAAAGTATGAAGAACTCGCATCAGCTGTCCTCAAGAGAGAT
GTGGATATAATCACCTTATATCAGAAGGTCTCTGTTTGGCTGTTAAGATATGACTTTGTG
CTTGAATATCCTAGGCCGGTCATGCCCAACATGGTCTTCATTGGAGGTATCAACTGTAAG
AAGAGGAAAGACTTGTCTCAG
Enzyme 16 GenBank Gene ID M84130 Link Image
Enzyme 16 GeneCard ID UGT1A6 Link Image
Enzyme 16 GenAtlas ID UGT1A6 Link Image
Enzyme 16 HGNC ID HGNC:12538 Link Image
Enzyme 16 Chromosome Location Not Available
Enzyme 16 Locus Not Available
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 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 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 5733
Enzyme 17 Name UDP-glucuronosyltransferase 1-5 precursor
Enzyme 17 Synonyms
  1. UDP- glucuronosyltransferase 1A5
  2. UDPGT
  3. UGT1*5
  4. UGT1-05
  5. UGT1.5
  6. UGT- 1E
  7. UGT1E
Enzyme 17 Gene Name UGT1A5
Enzyme 17 Protein Sequence >UDP-glucuronosyltransferase 1-5 precursor
MATGLQVPLPQLATGLLLLLSVQPWAESGKVLVVPTDGSHWLSMREALRDLHARGHQVVV
LTLEVNMYIKEENFFTLTTYAISWTQDEFDRLLLGHTQSFFETEHLLMKFSRRMAIMNNM
SLIIHRSCVELLHNEALIRHLHATSFDVVLTDPFHLCAAVLAKYLSIPAVFFLRNIPCDL
DFKGTQCPNPSSYIPRLLTTNSDHMTFLQRVKNMLYPLALSYLCHAVSAPYASLASELFQ
REVSVVDLVSHASVWLFRGDFVMDYPRPIMPNMVFIGGINCANGKPLSQEFEAYINASGE
HGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQND
LLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMT
SEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAH
DLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 17 Number of Residues 534
Enzyme 17 Molecular Weight 60072
Enzyme 17 Theoretical pI 8.14
Enzyme 17 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 17 General Function Carbohydrate transport and metabolism
Enzyme 17 Specific Function UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds
Enzyme 17 Pathways
Enzyme 17 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • 1-28
Enzyme 17 Transmembrane Regions
  • 492-508
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 340139 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID P35504 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name UD15_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >867 bp
ATGGCCACAGGACTCCAGGTTCCCCTGCCGCAGCTGGCCACAGGACTGCTGCTTCTCCTC
AGTGTCCAGCCCTGGGCTGAGAGTGGGAAGGTGCTGGTGGTGCCCACTGATGGCAGCCAC
TGGCTCAGCATGCGGGAGGCCTTGCGGGACCTCCATGCGAGAGGCCACCAGGTGGTGGTC
CTCACCCTGGAGGTGAATATGTACATCAAAGAAGAGAACTTTTTCACCCTGACAACGTAT
GCCATTTCATGGACCCAGGACGAATTTGATCGCCTTTTGCTGGGTCACACTCAATCGTTC
TTTGAAACAGAACATCTTCTGATGAAATTTTCTAGAAGAATGGCAATTATGAACAATATG
TCTTTGATCATACATAGGTCTTGTGTGGAGCTACTGCATAATGAGGCCCTGATCAGGCAC
CTGCATGCTACTTCCTTTGATGTGGTTCTAACAGACCCCTTTCACCTCTGCGCGGCGGTG
CTGGCTAAGTACCTGTCGATTCCTGCTGTGTTTTTCTTGAGGAACATTCCATGTGATTTA
GACTTTAAGGGCACACAGTGTCCAAACCCTTCCTCCTATATTCCTAGATTACTAACGACC
AATTCAGACCACATGACATTCCTGCAAAGGGTCAAGAACATGCTCTACCCTCTGGCCCTG
TCCTACCTTTGCCATGCTGTTTCTGCTCCTTATGCAAGCCTTGCCTCTGAGCTTTTTCAG
AGAGAGGTGTCAGTGGTGGATCTTGTCAGCCATGCATCTGTGTGGCTGTTCCGAGGGGAC
TTTGTGATGGATTACCCCAGGCCGATCATGCCCAACATGGTCTTCATTGGGGGCATCAAC
TGTGCCAACGGGAAGCCACTATCTCAG
Enzyme 17 GenBank Gene ID M84129 Link Image
Enzyme 17 GeneCard ID UGT1A5 Link Image
Enzyme 17 GenAtlas ID UGT1A5 Link Image
Enzyme 17 HGNC ID HGNC:12537 Link Image
Enzyme 17 Chromosome Location 2
Enzyme 17 Locus 2q37
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Ritter JK, Chen F, Sheen YY, Tran HM, Kimura S, Yeatman MT, Owens IS: A novel complex locus UGT1 encodes human bilirubin, phenol, and other UDP-glucuronosyltransferase isozymes with identical carboxyl termini. J Biol Chem. 1992 Feb 15;267(5):3257-61. [PubMed Link Image]
  2. 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 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 5734
Enzyme 18 Name UDP-glucuronosyltransferase 2B11 precursor
Enzyme 18 Synonyms
  1. UDPGT
Enzyme 18 Gene Name UGT2B11
Enzyme 18 Protein Sequence >UDP-glucuronosyltransferase 2B11 precursor
MTLKWTSVLLLIHLSCYFSSGSCGKVLVWAAEYSHWMNMKTILKELVQRGHEVTVLASSA
SILFDPNDASTLKFEVYPTSLTKTEFENIIMQQVKRWSDIRKDSFWLYFSQEQEILWELY
DIFRNFCKDVVSNKKVMKKLQESRFDIVFADAVFPCGELLAALLNIRFVYSLRFTPGYTI
ERHSGGLIFPPSYIPIVMSKLSDQMTFMERVKNMIYVLYFDFWFQMSDMKKWDQFYSEVL
GRPTTLFETMGKADIWLMRNSWSFQFPHPFLPNVDFVGGFHCKPAKPLPKEMEEFVQSSG
ENGVVVFSLGSVISNMTAERANVIATALAKIPQKVLWRFDGNKPDALGLNTRLYKWIPQN
DLLGHPKTRAFITHGGANGIYEAIYHGIPMVGIPLFFDQPDNIAHMKAKGAAVRLDFNTM
SSTDLLNALKTVINDPLYKENIMKLSRIQHDQPVKPLDRAVFWIEFVMPHKGAKHLRVAA
HDLTWFQYHSLDVIGFLLACVATVIFIITKFCLFCFWKFARKGKKGKRD
Enzyme 18 Number of Residues 529
Enzyme 18 Molecular Weight 61039
Enzyme 18 Theoretical pI 9.29
Enzyme 18 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 18 General Function Carbohydrate transport and metabolism
Enzyme 18 Specific Function UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds
Enzyme 18 Pathways
Enzyme 18 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • 1-21
Enzyme 18 Transmembrane Regions
  • 493-513
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 3360273 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID O75310 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name UDB11_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 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 18 GenBank Gene ID AF016492 Link Image
Enzyme 18 GeneCard ID UGT2B11 Link Image
Enzyme 18 GenAtlas ID UGT2B11 Link Image
Enzyme 18 HGNC ID HGNC:12545 Link Image
Enzyme 18 Chromosome Location 4
Enzyme 18 Locus 4q13.2
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 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 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 6947
Enzyme 19 Name Androgen receptor
Enzyme 19 Synonyms
  1. Dihydrotestosterone receptor
Enzyme 19 Gene Name AR
Enzyme 19 Protein Sequence >Androgen receptor
MEVQLGLGRVYPRPPSKTYRGAFQNLFQSVREVIQNPGPRHPEAASAAPPGASLLLLQQQ
QQQQQQQQQQQQQQQQQQETSPRQQQQQQGEDGSPQAHRRGPTGYLVLDEEQQPSQPQSA
LECHPERGCVPEPGAAVAASKGLPQQLPAPPDEDDSAAPSTLSLLGPTFPGLSSCSADLK
DILSEASTMQLLQQQQQEAVSEGSSSGRAREASGAPTSSKDNYLGGTSTISDNAKELCKA
VSVSMGLGVEALEHLSPGEQLRGDCMYAPLLGVPPAVRPTPCAPLAECKGSLLDDSAGKS
TEDTAEYSPFKGGYTKGLEGESLGCSGSAAAGSSGTLELPSTLSLYKSGALDEAAAYQSR
DYYNFPLALAGPPPPPPPPHPHARIKLENPLDYGSAWAAAAAQCRYGDLASLHGAGAAGP
GSGSPSAAASSSWHTLFTAEEGQLYGPCGGGGGGGGGGGGGGGGGGGGGGGGEAGAVAPY
GYTRPPQGLAGQESDFTAPDVWYPGGMVSRVPYPSPTCVKSEMGPWMDSYSGPYGDMRLE
TARDHVLPIDYYFPPQKTCLICGDEASGCHYGALTCGSCKVFFKRAAEGKQKYLCASRND
CTIDKFRRKNCPSCRLRKCYEAGMTLGARKLKKLGNLKLQEEGEASSTTSPTEETTQKLT
VSHIEGYECQPIFLNVLEAIEPGVVCAGHDNNQPDSFAALLSSLNELGERQLVHVVKWAK
ALPGFRNLHVDDQMAVIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRM
YSQCVRMRHLSQEFGWLQITPQEFLCMKALLLFSIIPVDGLKNQKFFDELRMNYIKELDR
IIACKRKNPTSCSRRFYQLTKLLDSVQPIARELHQFTFDLLIKSHMVSVDFPEMMAEIIS
VQVPKILSGKVKPIYFHTQ
Enzyme 19 Number of Residues 919
Enzyme 19 Molecular Weight 98990
Enzyme 19 Theoretical pI 6.38
Enzyme 19 GO Classification
Function
  • DNA binding
  • androgen receptor activity
  • binding
  • ligand-dependent nuclear receptor activity
  • nucleic acid binding
  • receptor activity
  • signal transducer activity
  • steroid binding
  • 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 19 General Function Not Available
Enzyme 19 Specific Function The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Activated, but not phosphorylated, by HIPK3
Enzyme 19 Pathways Not Available
Enzyme 19 Reactions Not Available
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 178628 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID P10275 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name ANDR_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >2760 bp
ATGGAAGTGCAGTTAGGGCTGGGAAGGGTCTACCCTCGGCCGCCGTCCAAGACCTACCGA
GGAGCTTTCCAGAATCTGTTCCAGAGCGTGCGCGAAGTGATCCAGAACCCGGGCCCCAGG
CACCCAGAGGCCGCGAGCGCAGCACCTCCCGGCGCCAGTTTGCTGCTGCTGCAGCAGCAG
CAGCAGCAGCAGCAGCAGCAGCAGCAGCAGCAGCAGCAGCAGCAGCAGCAGCAAGAGACT
AGCCCCAGGCAGCAGCAGCAGCAGCAGGGTGAGGATGGTTCTCCCCAAGCCCATCGTAGA
GGCCCCACAGGCTACCTGGTCCTGGATGAGGAACAGCAACCTTCACAGCCGCAGTCGGCC
CTGGAGTGCCACCCCGAGAGAGGTTGCGTCCCAGAGCCTGGAGCCGCCGTGGCCGCCAGC
AAGGGGCTGCCGCAGCAGCTGCCAGCACCTCCGGACGAGGATGACTCAGCTGCCCCATCC
ACGTTGTCCCTGCTGGGCCCCACTTTCCCCGGCTTAAGCAGCTGCTCCGCTGACCTTAAA
GACATCCTGAGCGAGGCCAGCACCATGCAACTCCTTCAGCAACAGCAGCAGGAAGCAGTA
TCCGAAGGCAGCAGCAGCGGGAGAGCGAGGGAGGCCTCGGGGGCTCCCACTTCCTCCAAG
GACAATTACTTAGGGGGCACTTCGACCATTTCTGACAACGCCAAGGAGTTGTGTAAGGCA
GTGTCGGTGTCCATGGGCCTGGGTGTGGAGGCGTTGGAGCATCTGAGTCCAGGGGAACAG
CTTCGGGGGGATTGCATGTACGCCCCACTTTTGGGAGTTCCACCCGCTGTGCGTCCCACT
CCTTGTGCCCCATTGGCCGAATGCAAAGGTTCTCTGCTAGACGACAGCGCAGGCAAGAGC
ACTGAAGATACTGCTGAGTATTCCCCTTTCAAGGGAGGTTACACCAAAGGGCTAGAAGGC
GAGAGCCTAGGCTGCTCTGGCAGCGCTGCAGCAGGGAGCTCCGGGACACTTGAACTGCCG
TCTACCCTGTCTCTCTACAAGTCCGGAGCACTGGACGAGGCAGCTGCGTACCAGAGTCGC
GACTACTACAACTTTCCACTGGCTCTGGCCGGACCGCCGCCCCCTCCGCCGCCTCCCCAT
CCCCACGCTCGCATCAAGCTGGAGAACCCGCTGGACTACGGCAGCGCCTGGGCGGCTGCG
GCGGCGCAGTGCCGCTATGGGGACCTGGCGAGCCTGCATGGCGCGGGTGCAGCGGGACCC
GGTTCTGGGTCACCCTCAGCCGCCGCTTCCTCATCCTGGCACACTCTCTTCACAGCCGAA
GAAGGCCAGTTGTATGGACCGTGTGGTGGTGGTGGGGGTGGTGGCGGCGGCGGCGGCGGC
GGCGGCGGCGGCGGCGGCGGCGGCGGCGGCGGCGGCGAGGCGGGAGCTGTAGCCCCCTAC
GGCTACACTCGGCCCCCTCAGGGGCTGGCGGGCCAGGAAAGCGACTTCACCGCACCTGAT
GTGTGGTACCCTGGCGGCATGGTGAGCAGAGTGCCCTATCCCAGTCCCACTTGTGTCAAA
AGCGAAATGGGCCCCTGGATGGATAGCTACTCCGGACCTTACGGGGACATGCGTTTGGAG
ACTGCCAGGGACCATGTTTTGCCCATTGACTATTACTTTCCACCCCAGAAGACCTGCCTG
ATCTGTGGAGATGAAGCTTCTGGGTGTCACTATGGAGCTCTCACATGTGGAAGCTGCAAG
GTCTTCTTCAAAAGAGCCGCTGAAGGGAAACAGAAGTACCTGTGCGCCAGCAGAAATGAT
TGCACTATTGATAAATTCCGAAGGAAAAATTGTCCATCTTGTCGTCTTCGGAAATGTTAT
GAAGCAGGGATGACTCTGGGAGCCCGGAAGCTGAAGAAACTTGGTAATCTGAAACTACAG
GAGGAAGGAGAGGCTTCCAGCACCACCAGCCCCACTGAGGAGACAACCCAGAAGCTGACA
GTGTCACACATTGAAGGCTATGAATGTCAGCCCATCTTTCTGAATGTCCTGGAAGCCATT
GAGCCAGGTGTAGTGTGTGCTGGACACGACAACAACCAGCCCGACTCCTTTGCAGCCTTG
CTCTCTAGCCTCAATGAACTGGGAGAGAGACAGCTTGTACACGTGGTCAAGTGGGCCAAG
GCCTTGCCTGGCTTCCGCAACTTACACGTGGACGACCAGATGGCTGTCATTCAGTACTCC
TGGATGGGGCTCATGGTGTTTGCCATGGGCTGGCGATCCTTCACCAATGTCAACTCCAGG
ATGCTCTACTTCGCCCCTGATCTGGTTTTCAATGAGTACCGCATGCACAAGTCCCGGATG
TACAGCCAGTGTGTCCGAATGAGGCACCTCTCTCAAGAGTTTGGATGGCTCCAAATCACC
CCCCAGGAATTCCTGTGCATGAAAGCACTGCTACTCTTCAGCATTATTCCAGTGGATGGG
CTGAAAAATCAAAAATTCTTTGATGAACTTCGAATGAACTACATCAAGGAACTCGATCGT
ATCATTGCATGCAAAAGAAAAAATCCCACATCCTGCTCAAGACGCTTCTACCAGCTCACC
AAGCTCCTGGACTCCGTGCAGCCTATTGCGAGAGAGCTGCATCAGTTCACTTTTGACCTG
CTAATCAAGTCACACATGGTGAGCGTGGACTTTCCGGAAATGATGGCAGAGATCATCTCT
GTGCAAGTGCCCAAGATCCTTTCTGGGAAAGTCAAGCCCATCTATTTCCACACCCAGTGA
Enzyme 19 GenBank Gene ID M20132 Link Image
Enzyme 19 GeneCard ID AR Link Image
Enzyme 19 GenAtlas ID AR Link Image
Enzyme 19 HGNC ID HGNC:644 Link Image
Enzyme 19 Chromosome Location X
Enzyme 19 Locus Xq11.2-q12
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Lubahn DB, Joseph DR, Sar M, Tan J, Higgs HN, Larson RE, French FS, Wilson EM: The human androgen receptor: complementary deoxyribonucleic acid cloning, sequence analysis and gene expression in prostate. Mol Endocrinol. 1988 Dec;2(12):1265-75. [PubMed Link Image]
  2. Lubahn DB, Brown TR, Simental JA, Higgs HN, Migeon CJ, Wilson EM, French FS: Sequence of the intron/exon junctions of the coding region of the human androgen receptor gene and identification of a point mutation in a family with complete androgen insensitivity. Proc Natl Acad Sci U S A. 1989 Dec;86(23):9534-8. [PubMed Link Image]
  3. Govindan MV: Specific region in hormone binding domain is essential for hormone binding and trans-activation by human androgen receptor. Mol Endocrinol. 1990 Mar;4(3):417-27. [PubMed Link Image]
  4. Chang CS, Kokontis J, Liao ST: Structural analysis of complementary DNA and amino acid sequences of human and rat androgen receptors. Proc Natl Acad Sci U S A. 1988 Oct;85(19):7211-5. [PubMed Link Image]
  5. Rao MA, Cheng H, Quayle AN, Nishitani H, Nelson CC, Rennie PS: RanBPM, a nuclear protein that interacts with and regulates transcriptional activity of androgen receptor and glucocorticoid receptor. J Biol Chem. 2002 Dec 13;277(50):48020-7. Epub 2002 Oct 1. [PubMed Link Image]
  6. Tilley WD, Marcelli M, Wilson JD, McPhaul MJ: Characterization and expression of a cDNA encoding the human androgen receptor. Proc Natl Acad Sci U S A. 1989 Jan;86(1):327-31. [PubMed Link Image]
  7. Marcelli M, Tilley WD, Wilson CM, Griffin JE, Wilson JD, McPhaul MJ: Definition of the human androgen receptor gene structure permits the identification of mutations that cause androgen resistance: premature termination of the receptor protein at amino acid residue 588 causes complete androgen resistance. Mol Endocrinol. 1990 Aug;4(8):1105-16. [PubMed Link Image]
  8. Faber PW, Kuiper GG, van Rooij HC, van der Korput JA, Brinkmann AO, Trapman J: The N-terminal domain of the human androgen receptor is encoded by one, large exon. Mol Cell Endocrinol. 1989 Feb;61(2):257-62. [PubMed Link Image]
  9. Chang CS, Kokontis J, Liao ST: Molecular cloning of human and rat complementary DNA encoding androgen receptors. Science. 1988 Apr 15;240(4850):324-6. [PubMed Link Image]
  10. Trapman J, Klaassen P, Kuiper GG, van der Korput JA, Faber PW, van Rooij HC, Geurts van Kessel A, Voorhorst MM, Mulder E, Brinkmann AO: Cloning, structure and expression of a cDNA encoding the human androgen receptor. Biochem Biophys Res Commun. 1988 May 31;153(1):241-8. [PubMed Link Image]
  11. Kuiper GG, Faber PW, van Rooij HC, van der Korput JA, Ris-Stalpers C, Klaassen P, Trapman J, Brinkmann AO: Structural organization of the human androgen receptor gene. J Mol Endocrinol. 1989 May;2(3):R1-4. [PubMed Link Image]
  12. Lubahn DB, Joseph DR, Sullivan PM, Willard HF, French FS, Wilson EM: Cloning of human androgen receptor complementary DNA and localization to the X chromosome. Science. 1988 Apr 15;240(4850):327-30. [PubMed Link Image]
  13. Ris-Stalpers C, Trifiro MA, Kuiper GG, Jenster G, Romalo G, Sai T, van Rooij HC, Kaufman M, Rosenfield RL, Liao S, et al.: Substitution of aspartic acid-686 by histidine or asparagine in the human androgen receptor leads to a functionally inactive protein with altered hormone-binding characteristics. Mol Endocrinol. 1991 Oct;5(10):1562-9. [PubMed Link Image]
  14. Sleddens HF, Oostra BA, Brinkmann AO, Trapman J: Trinucleotide repeat polymorphism in the androgen receptor gene (AR). Nucleic Acids Res. 1992 Mar 25;20(6):1427. [PubMed Link Image]
  15. Giovannucci E, Stampfer MJ, Krithivas K, Brown M, Dahl D, Brufsky A, Talcott J, Hennekens CH, Kantoff PW: The CAG repeat within the androgen receptor gene and its relationship to prostate cancer. Proc Natl Acad Sci U S A. 1997 Apr 1;94(7):3320-3. [PubMed Link Image]
  16. Waragai M, Lammers CH, Takeuchi S, Imafuku I, Udagawa Y, Kanazawa I, Kawabata M, Mouradian MM, Okazawa H: PQBP-1, a novel polyglutamine tract-binding protein, inhibits transcription activation by Brn-2 and affects cell survival. Hum Mol Genet. 1999 Jun;8(6):977-87. [PubMed Link Image]
  17. Hsiao PW, Lin DL, Nakao R, Chang C: The linkage of Kennedy's neuron disease to ARA24, the first identified androgen receptor polyglutamine region-associated coactivator. J Biol Chem. 1999 Jul 16;274(29):20229-34. [PubMed Link Image]
  18. Oettgen P, Finger E, Sun Z, Akbarali Y, Thamrongsak U, Boltax J, Grall F, Dube A, Weiss A, Brown L, Quinn G, Kas K, Endress G, Kunsch C, Libermann TA: PDEF, a novel prostate epithelium-specific ets transcription factor, interacts with the androgen receptor and activates prostate-specific antigen gene expression. J Biol Chem. 2000 Jan 14;275(2):1216-25. [PubMed Link Image]
  19. Sharma M, Zarnegar M, Li X, Lim B, Sun Z: Androgen receptor interacts with a novel MYST protein, HBO1. J Biol Chem. 2000 Nov 10;275(45):35200-8. [PubMed Link Image]
  20. Wong CW, McNally C, Nickbarg E, Komm BS, Cheskis BJ: Estrogen receptor-interacting protein that modulates its nongenomic activity-crosstalk with Src/Erk phosphorylation cascade. Proc Natl Acad Sci U S A. 2002 Nov 12;99(23):14783-8. Epub 2002 Nov 1. [PubMed Link Image]
  21. Niki T, Takahashi-Niki K, Taira T, Iguchi-Ariga SM, Ariga H: DJBP: a novel DJ-1-binding protein, negatively regulates the androgen receptor by recruiting histone deacetylase complex, and DJ-1 antagonizes this inhibition by abrogation of this complex. Mol Cancer Res. 2003 Feb;1(4):247-61. [PubMed Link Image]
  22. Matias PM, Donner P, Coelho R, Thomaz M, Peixoto C, Macedo S, Otto N, Joschko S, Scholz P, Wegg A, Basler S, Schafer M, Egner U, Carrondo MA: Structural evidence for ligand specificity in the binding domain of the human androgen receptor. Implications for pathogenic gene mutations. J Biol Chem. 2000 Aug 25;275(34):26164-71. [PubMed Link Image]
  23. Matias PM, Carrondo MA, Coelho R, Thomaz M, Zhao XY, Wegg A, Crusius K, Egner U, Donner P: Structural basis for the glucocorticoid response in a mutant human androgen receptor (AR(ccr)) derived from an androgen-independent prostate cancer. J Med Chem. 2002 Mar 28;45(7):1439-46. [PubMed Link Image]
  24. Pinsky L, Trifiro M, Kaufman M, Beitel LK, Mhatre A, Kazemi-Esfarjani P, Sabbaghian N, Lumbroso R, Alvarado C, Vasiliou M, et al.: Androgen resistance due to mutation of the androgen receptor. Clin Invest Med. 1992 Oct;15(5):456-72. [PubMed Link Image]
  25. Brown TR, Scherer PA, Chang YT, Migeon CJ, Ghirri P, Murono K, Zhou Z: Molecular genetics of human androgen insensitivity. Eur J Pediatr. 1993;152 Suppl 2:S62-9. [PubMed Link Image]
  26. Sultan C, Lumbroso S, Poujol N, Belon C, Boudon C, Lobaccaro JM: Mutations of androgen receptor gene in androgen insensitivity syndromes. J Steroid Biochem Mol Biol. 1993 Nov;46(5):519-30. [PubMed Link Image]
  27. Patterson MN, Hughes IA, Gottlieb B, Pinsky L: The androgen receptor gene mutations database. Nucleic Acids Res. 1994 Sep;22(17):3560-2. [PubMed Link Image]
  28. Brinkmann AO, Jenster G, Ris-Stalpers C, van der Korput JA, Bruggenwirth HT, Boehmer AL, Trapman J: Androgen receptor mutations. J Steroid Biochem Mol Biol. 1995 Jun;53(1-6):443-8. [PubMed Link Image]
  29. Gottlieb B, Trifiro M, Lumbroso R, Pinsky L: The androgen receptor gene mutations database. Nucleic Acids Res. 1997 Jan 1;25(1):158-62. [PubMed Link Image]
  30. Veldscholte J, Ris-Stalpers C, Kuiper GG, Jenster G, Berrevoets C, Claassen E, van Rooij HC, Trapman J, Brinkmann AO, Mulder E: A mutation in the ligand binding domain of the androgen receptor of human LNCaP cells affects steroid binding characteristics and response to anti-androgens. Biochem Biophys Res Commun. 1990 Dec 14;173(2):534-40. [PubMed Link Image]
  31. Brown TR, Lubahn DB, Wilson EM, French FS, Migeon CJ, Corden JL: Functional characterization of naturally occurring mutant androgen receptors from subjects with complete androgen insensitivity. Mol Endocrinol. 1990 Dec;4(12):1759-72. [PubMed Link Image]
  32. Marcelli M, Tilley WD, Zoppi S, Griffin JE, Wilson JD, McPhaul MJ: Androgen resistance associated with a mutation of the androgen receptor at amino acid 772 (Arg----Cys) results from a combination of decreased messenger ribonucleic acid levels and impairment of receptor function. J Clin Endocrinol Metab. 1991 Aug;73(2):318-25. [PubMed Link Image]
  33. Marcelli M, Zoppi S, Grino PB, Griffin JE, Wilson JD, McPhaul MJ: A mutation in the DNA-binding domain of the androgen receptor gene causes complete testicular feminization in a patient with receptor-positive androgen resistance. J Clin Invest. 1991 Mar;87(3):1123-6. [PubMed Link Image]
  34. McPhaul MJ, Marcelli M, Tilley WD, Griffin JE, Isidro-Gutierrez RF, Wilson JD: Molecular basis of androgen resistance in a family with a qualitative abnormality of the androgen receptor and responsive to high-dose androgen therapy. J Clin Invest. 1991 Apr;87(4):1413-21. [PubMed Link Image]
  35. La Spada AR, Wilson EM, Lubahn DB, Harding AE, Fischbeck KH: Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy. Nature. 1991 Jul 4;352(6330):77-9. [PubMed Link Image]
  36. Prior L, Bordet S, Trifiro MA, Mhatre A, Kaufman M, Pinsky L, Wrogeman K, Belsham DD, Pereira F, Greenberg C, et al.: Replacement of arginine 773 by cysteine or histidine in the human androgen receptor causes complete androgen insensitivity with different receptor phenotypes. Am J Hum Genet. 1992 Jul;51(1):143-55. [PubMed Link Image]
  37. Saunders PT, Padayachi T, Tincello DG, Shalet SM, Wu FC: Point mutations detected in the androgen receptor gene of three men with partial androgen insensitivity syndrome. Clin Endocrinol (Oxf). 1992 Sep;37(3):214-20. [PubMed Link Image]
  38. Sweet CR, Behzadian MA, McDonough PG: A unique point mutation in the androgen receptor gene in a family with complete androgen insensitivity syndrome. Fertil Steril. 1992 Oct;58(4):703-7. [PubMed Link Image]
  39. Jakubiczka S, Werder EA, Wieacker P: Point mutation in the steroid-binding domain of the androgen receptor gene in a family with complete androgen insensitivity syndrome (CAIS). Hum Genet. 1992 Nov;90(3):311-2. [PubMed Link Image]
  40. Batch JA, Williams DM, Davies HR, Brown BD, Evans BA, Hughes IA, Patterson MN: Androgen receptor gene mutations identified by SSCP in fourteen subjects with androgen insensitivity syndrome. Hum Mol Genet. 1992 Oct;1(7):497-503. [PubMed Link Image]
  41. Nakao R, Haji M, Yanase T, Ogo A, Takayanagi R, Katsube T, Fukumaki Y, Nawata H: A single amino acid substitution (Met786----Val) in the steroid-binding domain of human androgen receptor leads to complete androgen insensitivity syndrome. J Clin Endocrinol Metab. 1992 May;74(5):1152-7. [PubMed Link Image]
  42. Wilson CM, Griffin JE, Wilson JD, Marcelli M, Zoppi S, McPhaul MJ: Immunoreactive androgen receptor expression in subjects with androgen resistance. J Clin Endocrinol Metab. 1992 Dec;75(6):1474-8. [PubMed Link Image]
  43. McPhaul MJ, Marcelli M, Zoppi S, Wilson CM, Griffin JE, Wilson JD: Mutations in the ligand-binding domain of the androgen receptor gene cluster in two regions of the gene. J Clin Invest. 1992 Nov;90(5):2097-101. [PubMed Link Image]
  44. Veldscholte J, Berrevoets CA, Ris-Stalpers C, Kuiper GG, Jenster G, Trapman J, Brinkmann AO, Mulder E: The androgen receptor in LNCaP cells contains a mutation in the ligand binding domain which affects steroid binding characteristics and response to antiandrogens. J Steroid Biochem Mol Biol. 1992 Mar;41(3-8):665-9. [PubMed Link Image]
  45. Zoppi S, Marcelli M, Deslypere JP, Griffin JE, Wilson JD, McPhaul MJ: Amino acid substitutions in the DNA-binding domain of the human androgen receptor are a frequent cause of receptor-binding positive androgen resistance. Mol Endocrinol. 1992 Mar;6(3):409-15. [PubMed Link Image]
  46. De Bellis A, Quigley CA, Cariello NF, el-Awady MK, Sar M, Lane MV, Wilson EM, French FS: Single base mutations in the human androgen receptor gene causing complete androgen insensitivity: rapid detection by a modified denaturing gradient gel electrophoresis technique. Mol Endocrinol. 1992 Nov;6(11):1909-20. [PubMed Link Image]
  47. Wooster R, Mangion J, Eeles R, Smith S, Dowsett M, Averill D, Barrett-Lee P, Easton DF, Ponder BA, Stratton MR: A germline mutation in the androgen receptor gene in two brothers with breast cancer and Reifenstein syndrome. Nat Genet. 1992 Oct;2(2):132-4. [PubMed Link Image]
  48. Newmark JR, Hardy DO, Tonb DC, Carter BS, Epstein JI, Isaacs WB, Brown TR, Barrack ER: Androgen receptor gene mutations in human prostate cancer. Proc Natl Acad Sci U S A. 1992 Jul 15;89(14):6319-23. [PubMed Link Image]
  49. Macke JP, Hu N, Hu S, Bailey M, King VL, Brown T, Hamer D, Nathans J: Sequence variation in the androgen receptor gene is not a common determinant of male sexual orientation. Am J Hum Genet. 1993 Oct;53(4):844-52. [PubMed Link Image]
  50. Lumbroso S, Lobaccaro JM, Belon C, Martin D, Chaussain JL, Sultan C: A new mutation within the deoxyribonucleic acid-binding domain of the androgen receptor gene in a family with complete androgen insensitivity syndrome. Fertil Steril. 1993 Nov;60(5):814-9. [PubMed Link Image]
  51. Lobaccaro JM, Lumbroso S, Ktari R, Dumas R, Sultan C: An exonic point mutation creates a MaeIII site in the androgen receptor gene of a family with complete androgen insensitivity syndrome. Hum Mol Genet. 1993 Jul;2(7):1041-3. [PubMed Link Image]
  52. Lobaccaro JM, Lumbroso S, Belon C, Galtier-Dereure F, Bringer J, Lesimple T, Namer M, Cutuli BF, Pujol H, Sultan C: Androgen receptor gene mutation in male breast cancer. Hum Mol Genet. 1993 Nov;2(11):1799-802. [PubMed Link Image]
  53. Adeyemo O, Kallio PJ, Palvimo JJ, Kontula K, Janne OA: A single-base substitution in exon 6 of the androgen receptor gene causing complete androgen insensitivity: the mutated receptor fails to transactivate but binds to DNA in vitro. Hum Mol Genet. 1993 Nov;2(11):1809-12. [PubMed Link Image]
  54. Nakao R, Yanase T, Sakai Y, Haji M, Nawata H: A single amino acid substitution (gly743 --> val) in the steroid-binding domain of the human androgen receptor leads to Reifenstein syndrome. J Clin Endocrinol Metab. 1993 Jul;77(1):103-7. [PubMed Link Image]
  55. Hiort O, Huang Q, Sinnecker GH, Sadeghi-Nejad A, Kruse K, Wolfe HJ, Yandell DW: Single strand conformation polymorphism analysis of androgen receptor gene mutations in patients with androgen insensitivity syndromes: application for diagnosis, genetic counseling, and therapy. J Clin Endocrinol Metab. 1993 Jul;77(1):262-6. [PubMed Link Image]
  56. Batch JA, Evans BA, Hughes IA, Patterson MN: Mutations of the androgen receptor gene identified in perineal hypospadias. J Med Genet. 1993 Mar;30(3):198-201. [PubMed Link Image]
  57. Lobaccaro JM, Lumbroso S, Berta P, Chaussain JL, Sultan C: Complete androgen insensitivity syndrome associated with a de novo mutation of the androgen receptor gene detected by single strand conformation polymorphism. J Steroid Biochem Mol Biol. 1993 Mar;44(3):211-6. [PubMed Link Image]
  58. Suzuki H, Sato N, Watabe Y, Masai M, Seino S, Shimazaki J: Androgen receptor gene mutations in human prostate cancer. J Steroid Biochem Mol Biol. 1993 Dec;46(6):759-65. [PubMed Link Image]
  59. Kazemi-Esfarjani P, Beitel LK, Trifiro M, Kaufman M, Rennie P, Sheppard P, Matusik R, Pinsky L: Substitution of valine-865 by methionine or leucine in the human androgen receptor causes complete or partial androgen insensitivity, respectively with distinct androgen receptor phenotypes. Mol Endocrinol. 1993 Jan;7(1):37-46. [PubMed Link Image]
  60. Mowszowicz I, Lee HJ, Chen HT, Mestayer C, Portois MC, Cabrol S, Mauvais-Jarvis P, Chang C: A point mutation in the second zinc finger of the DNA-binding domain of the androgen receptor gene causes complete androgen insensitivity in two siblings with receptor-positive androgen resistance. Mol Endocrinol. 1993 Jul;7(7):861-9. [PubMed Link Image]
  61. Culig Z, Hobisch A, Cronauer MV, Cato AC, Hittmair A, Radmayr C, Eberle J, Bartsch G, Klocker H: Mutant androgen receptor detected in an advanced-stage prostatic carcinoma is activated by adrenal androgens and progesterone. Mol Endocrinol. 1993 Dec;7(12):1541-50. [PubMed Link Image]
  62. Castagnaro M, Yandell DW, Dockhorn-Dworniczak B, Wolfe HJ, Poremba C: [Androgen receptor gene mutations and p53 gene analysis in advanced prostate cancer] Verh Dtsch Ges Pathol. 1993;77:119-23. [PubMed Link Image]
  63. Schoenberg MP, Hakimi JM, Wang S, Bova GS, Epstein JI, Fischbeck KH, Isaacs WB, Walsh PC, Barrack ER: Microsatellite mutation (CAG24-->18) in the androgen receptor gene in human prostate cancer. Biochem Biophys Res Commun. 1994 Jan 14;198(1):74-80. [PubMed Link Image]
  64. Gaddipati JP, McLeod DG, Heidenberg HB, Sesterhenn IA, Finger MJ, Moul JW, Srivastava S: Frequent detection of codon 877 mutation in the androgen receptor gene in advanced prostate cancers. Cancer Res. 1994 Jun 1;54(11):2861-4. [PubMed Link Image]
  65. Lobaccaro JM, Belon C, Lumbroso S, Olewniczack G, Carre-Pigeon F, Job JC, Chaussain JL, Toublanc JE, Sultan C: Molecular prenatal diagnosis of partial androgen insensitivity syndrome based on the Hind III polymorphism of the androgen receptor gene. Clin Endocrinol (Oxf). 1994 Mar;40(3):297-302. [PubMed Link Image]
  66. Lumbroso S, Lobaccaro JM, Belon C, Amram S, Bachelard B, Garandeau P, Sultan C: Molecular prenatal exclusion of familial partial androgen insensitivity (Reifenstein syndrome) Eur J Endocrinol. 1994 Apr;130(4):327-32. [PubMed Link Image]
  67. Imasaki K, Hasegawa T, Okabe T, Sakai Y, Haji M, Takayanagi R, Nawata H: Single amino acid substitution (840Arg-->His) in the hormone-binding domain of the androgen receptor leads to incomplete androgen insensitivity syndrome associated with a thermolabile androgen receptor. Eur J Endocrinol. 1994 Jun;130(6):569-74. [PubMed Link Image]
  68. Hiort O, Klauber G, Cendron M, Sinnecker GH, Keim L, Schwinger E, Wolfe HJ, Yandell DW: Molecular characterization of the androgen receptor gene in boys with hypospadias. Eur J Pediatr. 1994 May;153(5):317-21. [PubMed Link Image]
  69. Beitel LK, Prior L, Vasiliou DM, Gottlieb B, Kaufman M, Lumbroso R, Alvarado C, McGillivray B, Trifiro M, Pinsky L: Complete androgen insensitivity due to mutations in the probable alpha-helical segments of the DNA-binding domain in the human androgen receptor. Hum Mol Genet. 1994 Jan;3(1):21-7. [PubMed Link Image]
  70. Hiort O, Wodtke A, Struve D, Zollner A, Sinnecker GH: Detection of point mutations in the androgen receptor gene using non-isotopic single strand conformation polymorphism analysis. German Collaborative Intersex Study Group. Hum Mol Genet. 1994 Jul;3(7):1163-6. [PubMed Link Image]
  71. Baldazzi L, Baroncini C, Pirazzoli P, Balsamo A, Capelli M, Marchetti G, Bernardi F, Cacciari E: Two mutations causing complete androgen insensitivity: a frame-shift in the steroid binding domain and a Cys-->Phe substitution in the second zinc finger of the androgen receptor. Hum Mol Genet. 1994 Jul;3(7):1169-70. [PubMed Link Image]
  72. De Bellis A, Quigley CA, Marschke KB, el-Awady MK, Lane MV, Smith EP, Sar M, Wilson EM, French FS: Characterization of mutant androgen receptors causing partial androgen insensitivity syndrome. J Clin Endocrinol Metab. 1994 Mar;78(3):513-22. [PubMed Link Image]
  73. Tsukada T, Inoue M, Tachibana S, Nakai Y, Takebe H: An androgen receptor mutation causing androgen resistance in undervirilized male syndrome. J Clin Endocrinol Metab. 1994 Oct;79(4):1202-7. [PubMed Link Image]
  74. Beitel LK, Kazemi-Esfarjani P, Kaufman M, Lumbroso R, DiGeorge AM, Killinger DW, Trifiro MA, Pinsky L: Substitution of arginine-839 by cysteine or histidine in the androgen receptor causes different receptor phenotypes in cultured cells and coordinate degrees of clinical androgen resistance. J Clin Invest. 1994 Aug;94(2):546-54. [PubMed Link Image]
  75. Marcelli M, Zoppi S, Wilson CM, Griffin JE, McPhaul MJ: Amino acid substitutions in the hormone-binding domain of the human androgen receptor alter the stability of the hormone receptor complex. J Clin Invest. 1994 Oct;94(4):1642-50. [PubMed Link Image]
  76. Yong EL, Ng SC, Roy AC, Yun G, Ratnam SS: Pregnancy after hormonal correction of severe spermatogenic defect due to mutation in androgen receptor gene. Lancet. 1994 Sep 17;344(8925):826-7. [PubMed Link Image]
  77. Ris-Stalpers C, Hoogenboezem T, Sleddens HF, Verleun-Mooijman MC, Degenhart HJ, Drop SL, Halley DJ, Oosterwijk JC, Hodgins MB, Trapman J, et al.: A practical approach to the detection of androgen receptor gene mutations and pedigree analysis in families with x-linked androgen insensitivity. Pediatr Res. 1994 Aug;36(2):227-34. [PubMed Link Image]
  78. Imai A, Ohno T, Iida K, Ohsuye K, Okano Y, Tamaya T: A frame-shift mutation of the androgen receptor gene in a patient with receptor-negative complete testicular feminization: comparison with a single base substitution in a receptor-reduced incomplete form. Ann Clin Biochem. 1995 Sep;32 ( Pt 5):482-6. [PubMed Link Image]
  79. Takahashi H, Furusato M, Allsbrook WC Jr, Nishii H, Wakui S, Barrett JC, Boyd J: Prevalence of androgen receptor gene mutations in latent prostatic carcinomas from Japanese men. Cancer Res. 1995 Apr 15;55(8):1621-4. [PubMed Link Image]
  80. Davies HR, Hughes IA, Patterson MN: Genetic counselling in complete androgen insensitivity syndrome: trinucleotide repeat polymorphisms, single-strand conformation polymorphism and direct detection of two novel mutations in the androgen receptor gene. Clin Endocrinol (Oxf). 1995 Jul;43(1):69-77. [PubMed Link Image]
  81. Quigley CA, De Bellis A, Marschke KB, el-Awady MK, Wilson EM, French FS: Androgen receptor defects: historical, clinical, and molecular perspectives. Endocr Rev. 1995 Jun;16(3):271-321. [PubMed Link Image]
  82. Shkolny DL, Brown TR, Punnett HH, Kaufman M, Trifiro MA, Pinsky L: Characterization of alternative amino acid substitutions at arginine 830 of the androgen receptor that cause complete androgen insensitivity in three families. Hum Mol Genet. 1995 Apr;4(4):515-21. [PubMed Link Image]
  83. Belsham DD, Pereira F, Greenberg CR, Liao S, Wrogemann K: Leu-676-Pro mutation of the androgen receptor causes complete androgen insensitivity syndrome in a large Hutterite kindred. Hum Mutat. 1995;5(1):28-33. [PubMed Link Image]
  84. Murono K, Mendonca BB, Arnhold IJ, Rigon AC, Migeon CJ, Brown TR: Human androgen insensitivity due to point mutations encoding amino acid substitutions in the androgen receptor steroid-binding domain. Hum Mutat. 1995;6(2):152-62. [PubMed Link Image]
  85. Peterziel H, Culig Z, Stober J, Hobisch A, Radmayr C, Bartsch G, Klocker H, Cato AC: Mutant androgen receptors in prostatic tumors distinguish between amino-acid-sequence requirements for transactivation and ligand binding. Int J Cancer. 1995 Nov 15;63(4):544-50. [PubMed Link Image]
  86. Allera A, Herbst MA, Griffin JE, Wilson JD, Schweikert HU, McPhaul MJ: Mutations of the androgen receptor coding sequence are infrequent in patients with isolated hypospadias. J Clin Endocrinol Metab. 1995 Sep;80(9):2697-9. [PubMed Link Image]
  87. Elo JP, Kvist L, Leinonen K, Isomaa V, Henttu P, Lukkarinen O, Vihko P: Mutated human androgen receptor gene detected in a prostatic cancer patient is also activated by estradiol. J Clin Endocrinol Metab. 1995 Dec;80(12):3494-500. [PubMed Link Image]
  88. Gast A, Neuschmid-Kaspar F, Klocker H, Cato AC: A single amino acid exchange abolishes dimerization of the androgen receptor and causes Reifenstein syndrome. Mol Cell Endocrinol. 1995 Apr 28;111(1):93-8. [PubMed Link Image]
  89. Taplin ME, Bubley GJ, Shuster TD, Frantz ME, Spooner AE, Ogata GK, Keer HN, Balk SP: Mutation of the androgen-receptor gene in metastatic androgen-independent prostate cancer. N Engl J Med. 1995 May 25;332(21):1393-8. [PubMed Link Image]
  90. Hiort O, Sinnecker GH, Holterhus PM, Nitsche EM, Kruse K: The clinical and molecular spectrum of androgen insensitivity syndromes. Am J Med Genet. 1996 May 3;63(1):218-22. [PubMed Link Image]
  91. Tilley WD, Buchanan G, Hickey TE, Bentel JM: Mutations in the androgen receptor gene are associated with progression of human prostate cancer to androgen independence. Clin Cancer Res. 1996 Feb;2(2):277-85. [PubMed Link Image]
  92. Weidemann W, Linck B, Haupt H, Mentrup B, Romalo G, Stockklauser K, Brinkmann AO, Schweikert HU, Spindler KD: Clinical and biochemical investigations and molecular analysis of subjects with mutations in the androgen receptor gene. Clin Endocrinol (Oxf). 1996 Dec;45(6):733-9. [PubMed Link Image]
  93. Malmgren H, Gustavsson J, Tuvemo T, Dahl N: Rapid detection of a mutation hot-spot in the human androgen receptor. Clin Genet. 1996 Oct;50(4):202-5. [PubMed Link Image]
  94. Bevan CL, Brown BB, Davies HR, Evans BA, Hughes IA, Patterson MN: Functional analysis of six androgen receptor mutations identified in patients with partial androgen insensitivity syndrome. Hum Mol Genet. 1996 Feb;5(2):265-73. [PubMed Link Image]
  95. Choong CS, Sturm MJ, Strophair JA, McCulloch RK, Tilley WD, Leedman PJ, Hurley DM: Partial androgen insensitivity caused by an androgen receptor mutation at amino acid 907 (Gly-->Arg) that results in decreased ligand binding affinity and reduced androgen receptor messenger ribonucleic acid levels. J Clin Endocrinol Metab. 1996 Jan;81(1):236-43. [PubMed Link Image]
  96. Lumbroso S, Lobaccaro JM, Georget V, Leger J, Poujol N, Terouanne B, Evain-Brion D, Czernichow P, Sultan C: A novel substitution (Leu707Arg) in exon 4 of the androgen receptor gene causes complete androgen resistance. J Clin Endocrinol Metab. 1996 May;81(5):1984-8. [PubMed Link Image]
  97. Rodien P, Mebarki F, Mowszowicz I, Chaussain JL, Young J, Morel Y, Schaison G: Different phenotypes in a family with androgen insensitivity caused by the same M780I point mutation in the androgen receptor gene. J Clin Endocrinol Metab. 1996 Aug;81(8):2994-8. [PubMed Link Image]
  98. Choong CS, Quigley CA, French FS, Wilson EM: A novel missense mutation in the amino-terminal domain of the human androgen receptor gene in a family with partial androgen insensitivity syndrome causes reduced efficiency of protein translation. J Clin Invest. 1996 Sep 15;98(6):1423-31. [PubMed Link Image]
  99. Bruggenwirth HT, Boehmer AL, Verleun-Mooijman MC, Hoogenboezem T, Kleijer WJ, Otten BJ, Trapman J, Brinkmann AO: Molecular basis of androgen insensitivity. J Steroid Biochem Mol Biol. 1996 Aug;58(5-6):569-75. [PubMed Link Image]
  100. Sutherland RW, Wiener JS, Hicks JP, Marcelli M, Gonzales ET Jr, Roth DR, Lamb DJ: Androgen receptor gene mutations are rarely associated with isolated penile hypospadias. J Urol. 1996 Aug;156(2 Pt 2):828-31. [PubMed Link Image]
  101. Lobaccaro JM, Poujol N, Chiche L, Lumbroso S, Brown TR, Sultan C: Molecular modeling and in vitro investigations of the human androgen receptor DNA-binding domain: application for the study of two mutations. Mol Cell Endocrinol. 1996 Feb 5;116(2):137-47. [PubMed Link Image]
  102. Imasaki K, Okabe T, Murakami H, Tanaka Y, Haji M, Takayanagi R, Nawata H: Androgen insensitivity syndrome due to new mutations in the DNA-binding domain of the androgen receptor. Mol Cell Endocrinol. 1996 Jun 18;120(1):15-24. [PubMed Link Image]
  103. Evans BA, Harper ME, Daniells CE, Watts CE, Matenhelia S, Green J, Griffiths K: Low incidence of androgen receptor gene mutations in human prostatic tumors using single strand conformation polymorphism analysis. Prostate. 1996 Mar;28(3):162-71. [PubMed Link Image]
  104. Suzuki H, Akakura K, Komiya A, Aida S, Akimoto S, Shimazaki J: Codon 877 mutation in the androgen receptor gene in advanced prostate cancer: relation to antiandrogen withdrawal syndrome. Prostate. 1996 Sep;29(3):153-8. [PubMed Link Image]
  105. Boehmer AL, Brinkmann AO, Niermeijer MF, Bakker L, Halley DJ, Drop SL: Germ-line and somatic mosaicism in the androgen insensitivity syndrome: implications for genetic counseling. Am J Hum Genet. 1997 Apr;60(4):1003-6. [PubMed Link Image]
  106. Koivisto P, Kononen J, Palmberg C, Tammela T, Hyytinen E, Isola J, Trapman J, Cleutjens K, Noordzij A, Visakorpi T, Kallioniemi OP: Androgen receptor gene amplification: a possible molecular mechanism for androgen deprivation therapy failure in prostate cancer. Cancer Res. 1997 Jan 15;57(2):314-9. [PubMed Link Image]
  107. Tincello DG, Saunders PT, Hodgins MB, Simpson NB, Edwards CR, Hargreaves TB, Wu FC: Correlation of clinical, endocrine and molecular abnormalities with in vivo responses to high-dose testosterone in patients with partial androgen insensitivity syndrome. Clin Endocrinol (Oxf). 1997 Apr;46(4):497-506. [PubMed Link Image]
  108. Essawi M, Gad YZ, el-Rouby O, Temtamy SA, Sabour YA, el-Awady MK: Molecular analysis of androgen resistance syndromes in Egyptian patients. Dis Markers. 1997 Apr;13(2):99-105. [PubMed Link Image]
  109. Sinnecker GH, Hiort O, Nitsche EM, Holterhus PM, Kruse K: Functional assessment and clinical classification of androgen sensitivity in patients with mutations of the androgen receptor gene. German Collaborative Intersex Study Group. Eur J Pediatr. 1997 Jan;156(1):7-14. [PubMed Link Image]
  110. Jakubiczka S, Nedel S, Werder EA, Schleiermacher E, Theile U, Wolff G, Wieacker P: Mutations of the androgen receptor gene in patients with complete androgen insensitivity. Hum Mutat. 1997;9(1):57-61. [PubMed Link Image]
  111. Watanabe M, Ushijima T, Shiraishi T, Yatani R, Shimazaki J, Kotake T, Sugimura T, Nagao M: Genetic alterations of androgen receptor gene in Japanese human prostate cancer. Jpn J Clin Oncol. 1997 Dec;27(6):389-93. [PubMed Link Image]
  112. Wang C, Uchida T: [Androgen receptor gene mutations in prostate cancer] Nippon Hinyokika Gakkai Zasshi. 1997 May;88(5):550-6. [PubMed Link Image]
  113. Komori S, Sakata K, Tanaka H, Shima H, Koyama K: DNA analysis of the androgen receptor gene in two cases with complete androgen insensitivity syndrome. J Obstet Gynaecol Res. 1997 Jun;23(3):277-81. [PubMed Link Image]
  114. Albers N, Ulrichs C, Gluer S, Hiort O, Sinnecker GH, Mildenberger H, Brodehl J: Etiologic classification of severe hypospadias: implications for prognosis and management. J Pediatr. 1997 Sep;131(3):386-92. [PubMed Link Image]
  115. Ko TM, Yang YS, Wu MY, Kao CH, Hsu PM, Chuang SM, Lee TY: Complete androgen insensitivity syndrome. Molecular characterization in two Chinese women. J Reprod Med. 1997 Jul;42(7):424-8. [PubMed Link Image]
  116. Bevan CL, Hughes IA, Patterson MN: Wide variation in androgen receptor dysfunction in complete androgen insensitivity syndrome. J Steroid Biochem Mol Biol. 1997 Apr;61(1-2):19-26. [PubMed Link Image]
  117. Radmayr C, Culig Z, Glatzl J, Neuschmid-Kaspar F, Bartsch G, Klocker H: Androgen receptor point mutations as the underlying molecular defect in 2 patients with androgen insensitivity syndrome. J Urol. 1997 Oct;158(4):1553-6. [PubMed Link Image]
  118. Komori S, Kasumi H, Sakata K, Tanaka H, Hamada K, Koyama K: Molecular analysis of the androgen receptor gene in 4 patients with complete androgen insensitivity. Arch Gynecol Obstet. 1998;261(2):95-100. [PubMed Link Image]
  119. Cabral DF, Maciel-Guerra AT, Hackel C: Mutations of androgen receptor gene in Brazilian patients with male pseudohermaphroditism. Braz J Med Biol Res. 1998 Jun;31(6):775-8. [PubMed Link Image]
  120. Wang Q, Ghadessy FJ, Yong EL: Analysis of the transactivation domain of the androgen receptor in patients with male infertility. Clin Genet. 1998 Sep;54(3):185-92. [PubMed Link Image]
  121. Tanaka H, Komori S, Sakata K, Shima H, Koyama K: One additional mutation at exon A amplifies thermolability of androgen receptor in a case with complete androgen insensitivity syndrome. Gynecol Endocrinol. 1998 Apr;12(2):75-82. [PubMed Link Image]
  122. Lundberg Giwercman Y, Nikoshkov A, Lindsten K, Bystrom B, Pousette A, Chibalin AV, Arvidsson S, Tiulpakov A, Semitcheva TV, Peterkova V, Hagenfeldt K, Ritzen EM, Wedell A: Functional characterisation of mutations in the ligand-binding domain of the androgen receptor gene in patients with androgen insensitivity syndrome. Hum Genet. 1998 Oct;103(4):529-31. [PubMed Link Image]
  123. Dork T, Schnieders F, Jakubiczka S, Wieacker P, Schroeder-Kurth T, Schmidtke J: A new missense substitution at a mutational hot spot of the androgen receptor in siblings with complete androgen insensitivity syndrome. Hum Mutat. 1998;11(4):337-9. [PubMed Link Image]
  124. Nordenskjold A, Soderhall S: An androgen receptor gene mutation (A645D) in a boy with a normal phenotype. Hum Mutat. 1998;11(4):339. [PubMed Link Image]
  125. Weidemann W, Peters B, Romalo G, Spindler KD, Schweikert HU: Response to androgen treatment in a patient with partial androgen insensitivity and a mutation in the deoxyribonucleic acid-binding domain of the androgen receptor. J Clin Endocrinol Metab. 1998 Apr;83(4):1173-6. [PubMed Link Image]
  126. Georget V, Terouanne B, Lumbroso S, Nicolas JC, Sultan C: Trafficking of androgen receptor mutants fused to green fluorescent protein: a new investigation of partial androgen insensitivity syndrome. J Clin Endocrinol Metab. 1998 Oct;83(10):3597-603. [PubMed Link Image]
  127. Wang Q, Ghadessy FJ, Trounson A, de Kretser D, McLachlan R, Ng SC, Yong EL: Azoospermia associated with a mutation in the ligand-binding domain of an androgen receptor displaying normal ligand binding, but defective trans-activation. J Clin Endocrinol Metab. 1998 Dec;83(12):4303-9. [PubMed Link Image]
  128. Hiort O, Sinnecker GH, Holterhus PM, Nitsche EM, Kruse K: Inherited and de novo androgen receptor gene mutations: investigation of single-case families. J Pediatr. 1998 Jun;132(6):939-43. [PubMed Link Image]
  129. Yong EL, Tut TG, Ghadessy FJ, Prins G, Ratnam SS: Partial androgen insensitivity and correlations with the predicted three dimensional structure of the androgen receptor ligand-binding domain. Mol Cell Endocrinol. 1998 Feb;137(1):41-50. [PubMed Link Image]
  130. Knoke I, Jakubiczka S, Lehnert H, Wieacker P: A new point mutation of the androgen receptor gene in a patient with partial androgen resistance and severe oligozoospermia. Andrologia. 1999 Jul;31(4):199-201. [PubMed Link Image]
  131. Taplin ME, Bubley GJ, Ko YJ, Small EJ, Upton M, Rajeshkumar B, Balk SP: Selection for androgen receptor mutations in prostate cancers treated with androgen antagonist. Cancer Res. 1999 Jun 1;59(11):2511-5. [PubMed Link Image]
  132. Melo KF, Latronico AC, Costa EM, Billerbeck AE, Mendonca BB, Arnhold IJ: A novel point mutation (R840S) in the androgen receptor in a Brazilian family with partial androgen insensitivity syndrome. Hum Mutat. 1999 Oct;14(4):353. [PubMed Link Image]
  133. Gottlieb B, Vasiliou DM, Lumbroso R, Beitel LK, Pinsky L, Trifiro MA: Analysis of exon 1 mutations in the androgen receptor gene. Hum Mutat. 1999;14(6):527-39. [PubMed Link Image]
  134. Chen CP, Chern SR, Wang TY, Wang W, Wang KL, Jeng CJ: Androgen receptor gene mutations in 46,XY females with germ cell tumours. Hum Reprod. 1999 Mar;14(3):664-70. [PubMed Link Image]
  135. Kanayama H, Naroda T, Inoue Y, Kurokawa Y, Kagawa S: A case of complete testicular feminization: laparoscopic orchiectomy and analysis of androgen receptor gene mutation. Int J Urol. 1999 Jun;6(6):327-30. [PubMed Link Image]
  136. Shkolny DL, Beitel LK, Ginsberg J, Pekeles G, Arbour L, Pinsky L, Trifiro MA: Discordant measures of androgen-binding kinetics in two mutant androgen receptors causing mild or partial androgen insensitivity, respectively. J Clin Endocrinol Metab. 1999 Feb;84(2):805-10. [PubMed Link Image]
  137. Wallen MJ, Linja M, Kaartinen K, Schleutker J, Visakorpi T: Androgen receptor gene mutations in hormone-refractory prostate cancer. J Pathol. 1999 Dec;189(4):559-63. [PubMed Link Image]
  138. Zhao XY, Boyle B, Krishnan AV, Navone NM, Peehl DM, Feldman D: Two mutations identified in the androgen receptor of the new human prostate cancer cell line MDA PCa 2a. J Urol. 1999 Dec;162(6):2192-9. [PubMed Link Image]
  139. Ong YC, Wong HB, Adaikan G, Yong EL: Directed pharmacological therapy of ambiguous genitalia due to an androgen receptor gene mutation. Lancet. 1999 Oct 23;354(9188):1444-5. [PubMed Link Image]
  140. Peters I, Weidemann W, Romalo G, Knorr D, Schweikert HU, Spindler KD: An androgen receptor mutation in the direct vicinity of the proposed C-terminal alpha-helix of the ligand binding domain containing the AF-2 transcriptional activating function core is associated with complete androgen insensitivity. Mol Cell Endocrinol. 1999 Feb 25;148(1-2):47-53. [PubMed Link Image]
  141. Nazareth LV, Stenoien DL, Bingman WE 3rd, James AJ, Wu C, Zhang Y, Edwards DP, Mancini M, Marcelli M, Lamb DJ, Weigel NL: A C619Y mutation in the human androgen receptor causes inactivation and mislocalization of the receptor with concomitant sequestration of SRC-1 (steroid receptor coactivator 1) Mol Endocrinol. 1999 Dec;13(12):2065-75. [PubMed Link Image]
  142. Holterhus PM, Wiebel J, Sinnecker GH, Bruggenwirth HT, Sippell WG, Brinkmann AO, Kruse K, Hiort O: Clinical and molecular spectrum of somatic mosaicism in androgen insensitivity syndrome. Pediatr Res. 1999 Dec;46(6):684-90. [PubMed Link Image]
  143. Yaegashi N, Uehara S, Senoo M, Sato J, Fujiwara J, Funato T, Sasaki T, Yajima A: Point mutations in the steroid-binding domain of the androgen receptor gene of five Japanese patients with androgen insensitivity syndrome. Tohoku J Exp Med. 1999 Mar;187(3):263-72. [PubMed Link Image]
  144. Nordenskjold A, Friedman E, Tapper-Persson M, Soderhall C, Leviav A, Svensson J, Anvret M: Screening for mutations in candidate genes for hypospadias. Urol Res. 1999;27(1):49-55. [PubMed Link Image]
  145. Marcelli M, Ittmann M, Mariani S, Sutherland R, Nigam R, Murthy L, Zhao Y, DiConcini D, Puxeddu E, Esen A, Eastham J, Weigel NL, Lamb DJ: Androgen receptor mutations in prostate cancer. Cancer Res. 2000 Feb 15;60(4):944-9. [PubMed Link Image]
  146. Ahmed SF, Cheng A, Dovey L, Hawkins JR, Martin H, Rowland J, Shimura N, Tait AD, Hughes IA: Phenotypic features, androgen receptor binding, and mutational analysis in 278 clinical cases reported as androgen insensitivity syndrome. J Clin Endocrinol Metab. 2000 Feb;85(2):658-65. [PubMed Link Image]
  147. Chavez B, Mendez JP, Ulloa-Aguirre A, Larrea F, Vilchis F: Eight novel mutations of the androgen receptor gene in patients with androgen insensitivity syndrome. J Hum Genet. 2001;46(10):560-5. [PubMed Link Image]
  148. Sills ES, Sholes TE, Perloe M, Kaplan CR, Davis JG, Tucker MJ: Characterization of a novel receptor mutation A-->T at exon 4 in complete androgen insensitivity syndrome and a carrier sibling via bidirectional polymorphism sequence analysis. Int J Mol Med. 2002 Jan;9(1):45-8. [PubMed Link Image]
Enzyme 19 Metabolite References
  1. Peterziel H, Culig Z, Stober J, Hobisch A, Radmayr C, Bartsch G, Klocker H, Cato AC: Mutant androgen receptors in prostatic tumors distinguish between amino-acid-sequence requirements for transactivation and ligand binding. Int J Cancer. 1995 Nov 15;63(4):544-50. [PubMed Link Image]
Enzyme 20 [top]
Enzyme 20 ID 8106
Enzyme 20 Name Dehydrogenase/reductase SDR family member 9 precursor
Enzyme 20 Synonyms
  1. 3- alpha hydroxysteroid dehydrogenase
  2. 3alpha-HSD
  3. RDH-E2
  4. Short-chain dehydrogenase/reductase retSDR8
  5. NADP-dependent retinol dehydrogenase/reductase
  6. RDHL
Enzyme 20 Gene Name DHRS9
Enzyme 20 Protein Sequence >Dehydrogenase/reductase SDR family member 9 precursor
MLFWVLGLLILCGFLWTRKGKLKIEDITDKYIFITGCDSGFGNLAARTFDKKGFHVIAAC
LTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKGLWGLINNAGVPGVLA
PTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAIVGGGYTPSK
YAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLAIWEQLSPDIKQQYGE
GYIEKSLDKLKGNKSYVNMDLSPVVECMDHALTSLFPKTHYAAGKDAKIFWIPLSHMPAA
LQDFLLLKQKAELANPKAV
Enzyme 20 Number of Residues 319
Enzyme 20 Molecular Weight 35227
Enzyme 20 Theoretical pI 8.89
Enzyme 20 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
Enzyme 20 General Function Lipid transport and metabolism
Enzyme 20 Specific Function 3-alpha-hydroxysteroid dehydrogenase that converts 3- alpha-tetrahydroprogesterone (allopregnanolone) to dihydroxyprogesterone and 3-alpha-androstanediol to dihydroxyprogesterone. May play a role in the biosynthesis of retinoic acid from retinaldehyde, but seems to have low activity with retinoids. Can utilize both NADH and NADPH
Enzyme 20 Pathways Not Available
Enzyme 20 Reactions Not Available
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • 1-17
Enzyme 20 Transmembrane Regions Not Available
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 13649974 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q9BPW9 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name DHRS9_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >960 bp
ATGCTCTTTTGGGTGCTAGGCCTCCTAATCCTCTGTGGTTTTCTGTGGACTCGTAAAGGA
AAACTAAAGATTGAAGACATCACTGATAAGTACATTTTTATCACTGGATGTGACTCGGGC
TTTGGAAACTTGGCAGCCAGAACTTTTGATAAAAAGGGATTTCATGTAATCGCTGCCTGT
CTGACTGAATCAGGATCAACAGCTTTAAAGGCAGAAACCTCAGAGAGACTTCGTACTGTG
CTTCTGGATGTGACCGACCCAGAGAATGTCAAGAGGACTGCCCAGTGGGTGAAGAACCAA
GTTGGGGAGAAAGGTCTCTGGGGTCTGATCAATAATGCTGGTGTTCCCGGCGTGCTGGCT
CCCACTGACTGGCTGACACTAGAGGACTACAGAGAACCTATTGAAGTGAACCTGTTTGGA
CTCATCAGTGTGACACTAAATATGCTTCCTTTGGTCAAGAAAGCTCAAGGGAGAGTTATT
AATGTCTCCAGTGTTGGAGGTCGCCTTGCAATCGTTGGAGGGGGCTATACTCCATCCAAA
TATGCAGTGGAAGGTTTCAATGACAGCTTAAGACGGGACATGAAAGCTTTTGGTGTGCAC
GTCTCATGCATTGAACCAGGATTGTTCAAAACAAACTTGGCAGATCCAGTAAAGGTAATT
GAAAAAAAACTCGCCATTTGGGAGCAGCTGTCTCCAGACATCAAACAACAATATGGAGAA
GGTTACATTGAAAAAAGTCTAGACAAACTGAAAGGCAATAAATCCTATGTGAACATGGAC
CTCTCTCCGGTGGTAGAGTGCATGGACCACGCTCTAACAAGTCTCTTCCCTAAGACTCAT
TATGCCGCTGGAAAAGATGCCAAAATTTTCTGGATACCTCTGTCTCACATGCCAGCAGCT
TTGCAAGACTTTTTATTGTTGAAACAGAAAGCAGAGCTGGCTAATCCCAAGGCAGTGTGA
Enzyme 20 GenBank Gene ID AF343729 Link Image
Enzyme 20 GeneCard ID DHRS9 Link Image
Enzyme 20 GenAtlas ID DHRS9 Link Image
Enzyme 20 HGNC ID HGNC:16888 Link Image
Enzyme 20 Chromosome Location 2
Enzyme 20 Locus 2q31.1
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Chetyrkin SV, Belyaeva OV, Gough WH, Kedishvili NY: Characterization of a novel type of human microsomal 3alpha -hydroxysteroid dehydrogenase: unique tissue distribution and catalytic properties. J Biol Chem. 2001 Jun 22;276(25):22278-86. Epub 2001 Apr 9. [PubMed Link Image]
  2. Soref CM, Di YP, Hayden L, Zhao YH, Satre MA, Wu R: Characterization of a novel airway epithelial cell-specific short chain alcohol dehydrogenase/reductase gene whose expression is up-regulated by retinoids and is involved in the metabolism of retinol. J Biol Chem. 2001 Jun 29;276(26):24194-202. Epub 2001 Apr 13. [PubMed Link Image]
  3. Markova NG, Pinkas-Sarafova A, Karaman-Jurukovska N, Jurukovski V, Simon M: Expression pattern and biochemical characteristics of a major epidermal retinol dehydrogenase. Mol Genet Metab. 2003 Feb;78(2):119-35. [PubMed Link Image]
  4. 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]
  5. Haeseleer F, Palczewski K: Short-chain dehydrogenases/reductases in retina. Methods Enzymol. 2000;316:372-83. [PubMed Link Image]
Enzyme 20 Metabolite References
  1. Klein J, Thomas H, Post K, Worner W, Oesch F: Dihydrodiol dehydrogenase activities of rabbit liver are associated with hydroxysteroid dehydrogenases and aldo-keto reductases. Eur J Biochem. 1992 May 1;205(3):1155-62. [PubMed Link Image]
Enzyme 21 [top]
Enzyme 21 ID 8526
Enzyme 21 Name Sterol/retinol dehydrogenase
Enzyme 21 Synonyms Not Available
Enzyme 21 Gene Name Not Available
Enzyme 21 Protein Sequence >Sterol/retinol dehydrogenase
MWLYLAVFVGLYYLLHWYRERQVLSHLRDKYVFITGCDSGFGKLLARQLDARGLRVLAAC
LTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKECVRDKGLWGLVNNAGISLPTA
PNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRKARGRVVNVSSVMGRVSLFGGGYCISK
YGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKERFLKSFLEIWDRSSPEVKEAYGE
KFVADYKKSAEQMEQKCTQDLSLVTNCMEHALIACHPRTRYSAGWDAKLLYLPMSYMPTF
LVDAIMYWVSPSPAKAL
Enzyme 21 Number of Residues 317
Enzyme 21 Molecular Weight 35646
Enzyme 21 Theoretical pI 8.77
Enzyme 21 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
Enzyme 21 General Function Lipid transport and metabolism
Enzyme 21 Specific Function Not Available
Enzyme 21 Pathways Not Available
Enzyme 21 Reactions Not Available
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 3372592 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID O75452 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name O75452_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >954 bp
ATGTGGCTCTACCTGGCGGTTTTCGTGGGCCTGTACTACCTTCTGCACTGGTACCGGGAG
AGGCAGGTGCTGAGCCACCTGAGAGATAAGTATGTGTTCATCACGGGCTGTGACTCTGGC
TTCGGGAAACTGCTGGCCAGACAGCTGGATGCACGAGGCTTGCGGGTGCTGGCTGCATGT
CTGACGGAGAAAGGAGCCGAGCAGCTGAGGGGCCAGACTTCAGACAGGCTGGAGACGGTG
ACCCTGGATGTTACCAAGACAGAGAGCGTTGCTGCAGCCGCCCAGTGGGTGAAGGAGTGC
GTGAGAGACAAAGGACTCTGGGGCCTGGTGAATAATGCTGGCATCTCCTTGCCCACGGCT
CCCAATGAGTTGCTCACCAAGCAGGACTTCGTGACCATACTGGACGTGAACTTGTTGGGG
GTGATTGATGTGACTCTGAGCCTGCTGCCCTTAGTGAGGAAGGCCAGGGGCCGTGTGGTC
AACGTCTCCAGTGTCATGGGCCGGGTGTCACTTTTTGGTGGAGGCTACTGCATCTCCAAG
TATGGCGTGGAAGCCTTCTCTGACTCCCTCAGGAGGGAACTCTCCTACTTTGGGGTGAAG
GTGGCTATGATTGAACCTGGCTATTTCAAGACTGCTGTGACCAGTAAGGAGAGATTCTTA
AAGAGCTTCCTGGAGATTTGGGACCGGTCCAGTCCAGAGGTCAAGGAGGCCTATGGCGAG
AAGTTTGTTGCAGACTATAAGAAATCAGCTGAACAAATGGAGCAGAAGTGCACACAGGAT
CTGTCGTTGGTGACCAACTGCATGGAGCATGCGCTGATTGCCTGCCACCCCCGTACTCGC
TACTCAGCTGGCTGGGATGCCAAGCTTCTCTACCTCCCCATGAGCTACATGCCCACCTTC
CTGGTGGATGCCATTATGTACTGGGTCTCTCCAAGCCCGGCCAAGGCTCTATGA
Enzyme 21 GenBank Gene ID AF057034 Link Image
Enzyme 21 GeneCard ID Not Available
Enzyme 21 GenAtlas ID Not Available
Enzyme 21 HGNC ID HGNC:29674 Link Image
Enzyme 21 Chromosome Location Not Available
Enzyme 21 Locus Not Available
Enzyme 21 SNPs Not Available
Enzyme 21 General References
  1. Gough WH, VanOoteghem S, Sint T, Kedishvili NY: cDNA cloning and characterization of a new human microsomal NAD+-dependent dehydrogenase that oxidizes all-trans-retinol and 3alpha-hydroxysteroids. J Biol Chem. 1998 Jul 31;273(31):19778-85. [PubMed Link Image]
Enzyme 21 Metabolite References
  1. Karlsson T, Vahlquist A, Kedishvili N, Torma H: 13-cis-retinoic acid competitively inhibits 3 alpha-hydroxysteroid oxidation by retinol dehydrogenase RoDH-4: a mechanism for its anti-androgenic effects in sebaceous glands? Biochem Biophys Res Commun. 2003 Mar 28;303(1):273-8. [PubMed Link Image]
Enzyme 22 [top]
Enzyme 22 ID 12970
Enzyme 22 Name UDP-glucuronosyltransferase 2A3 precursor
Enzyme 22 Synonyms Not Available
Enzyme 22 Gene Name UGT2A3
Enzyme 22 Protein Sequence >UDP-glucuronosyltransferase 2A3 precursor
MRSDKSALVFLLLQLFCVGCGFCGKVLVWPCDMSHWLNVKVILEELIVRGHEVTVLTHSK
PSLIDYRKPSALKFEVVHMPQDRTEENEIFVDLALNVLPGLSTWQSVIKLNDFFVEIRGT
LKMMCESFIYNQTLMKKLQETNYDVMLIDPVIPCGDLMAELLAVPFVLTLRISVGGNMER
SCGKLPAPLSYVPVPMTGLTDRMTFLERVKNSMLSVLFHFWIQDYDYHFWEEFYSKALGR
PTTLCETVGKAEIWLIRTYWDFEFPQPYQPNFEFVGGLHCKPAKALPKEMENFVQSSGED
GIVVFSLGSLFQNVTEEKANIIASALAQIPQKVLWRYKGKKPSTLGANTRLYDWIPQNDL
LGHPKTKAFITHGGMNGIYEAIYHGVPMVGVPIFGDQLDNIAHMKAKGAAVEINFKTMTS
EDLLRALRTVITDSSYKENAMRLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRSAAHD
LTWFQHYSIDVIGFLLTCVATAIFLFTKCFLFSCQKFNKTRKIEKRE
Enzyme 22 Number of Residues 527
Enzyme 22 Molecular Weight 60285
Enzyme 22 Theoretical pI 8.04
Enzyme 22 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 22 General Function Carbohydrate transport and metabolism
Enzyme 22 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 22 Pathways
Enzyme 22 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 22 Pfam Domain Function
Enzyme 22 Signals
  • 1-23
Enzyme 22 Transmembrane Regions
  • 492-512
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 44889644 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID Q6UWM9 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name UD2A3_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence Not Available
Enzyme 22 GenBank Gene ID AY542891 Link Image
Enzyme 22 GeneCard ID Q6UWM9 Link Image
Enzyme 22 GenAtlas ID UGT2A3 Link Image
Enzyme 22 HGNC ID HGNC:28528 Link Image
Enzyme 22 Chromosome Location Not Available
Enzyme 22 Locus Not Available
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 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 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 15056
Enzyme 23 Name UDP glycosyltransferase 1 family polypeptide A10 (HCG2039726, isoform CRA_f)
Enzyme 23 Synonyms Not Available
Enzyme 23 Gene Name UGT1A10
Enzyme 23 Protein Sequence >UDP glycosyltransferase 1 family polypeptide A10 (HCG2039726, isoform CRA_f)
MARAGWTSPVPLCVCLLLTCGFAEAGKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMP
EVSWQLERSLNCTVKTYSTSYTLEDQNREFMVFAHAQWKAQAQSIFSLLMSSSSGFLDLF
FSHCRSLFNDRKLVEYLKESSFDAVFLDPFDTCGLIVAKYFSLPSVVFTRGIFCHHLEEG
AQCPAPLSYVPNDLLGFSDAMTFKERVWNHIVHLEDHLFCQYLFRNALEIASEILQTPVT
AYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIV
VFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGH
PMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDL
ENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTW
YQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 23 Number of Residues 530
Enzyme 23 Molecular Weight 59810
Enzyme 23 Theoretical pI 7.31
Enzyme 23 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 23 General Function Carbohydrate transport and metabolism
Enzyme 23 Specific Function Not Available
Enzyme 23 Pathways Not Available
Enzyme 23 Reactions Not Available
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • None
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 40849852 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID Q5DT02 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name Q5DT02_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 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 23 GenBank Gene ID AY435137 Link Image
Enzyme 23 GeneCard ID Q5DT02 Link Image
Enzyme 23 GenAtlas ID UGT1A10 Link Image
Enzyme 23 HGNC ID HGNC:12531 Link Image
Enzyme 23 Chromosome Location Not Available
Enzyme 23 Locus Not Available
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References Not Available
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 15057
Enzyme 24 Name UDP glycosyltransferase 1 family polypeptide A8 (HCG2039726, isoform CRA_e)
Enzyme 24 Synonyms Not Available
Enzyme 24 Gene Name UGT1A8
Enzyme 24 Protein Sequence >UDP glycosyltransferase 1 family polypeptide A8 (HCG2039726, isoform CRA_e)
MARTGWTSPIPLCVSLLLTCGFAEAGKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMP
EVSWQLGKSLNCTVKTYSTSYTLEDLDREFMDFADAQWKAQVRSLFSLFLSSSNGFFNLF
FSHCRSLFNDRKLVEYLKESSFDAVFLDPFDACGLIVAKYFSLPSVVFARGIACHYLEEG
AQCPAPLSYVPRILLGFSDAMTFKERVRNHIMHLEEHLFCQYFSKNALEIASEILQTPVT
AYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIV
VFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGH
PMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDL
ENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTW
YQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 24 Number of Residues 530
Enzyme 24 Molecular Weight 59742
Enzyme 24 Theoretical pI 7.73
Enzyme 24 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 24 General Function Carbohydrate transport and metabolism
Enzyme 24 Specific Function Not Available
Enzyme 24 Pathways Not Available
Enzyme 24 Reactions Not Available
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 40849864 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID Q5DSZ6 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name Q5DSZ6_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 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 24 GenBank Gene ID AY435143 Link Image
Enzyme 24 GeneCard ID Q5DSZ6 Link Image
Enzyme 24 GenAtlas ID UGT1A8 Link Image
Enzyme 24 HGNC ID HGNC:12540 Link Image
Enzyme 24 Chromosome Location Not Available
Enzyme 24 Locus Not Available
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References Not Available
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 15058
Enzyme 25 Name UDP glycosyltransferase 1 family polypeptide A7
Enzyme 25 Synonyms Not Available
Enzyme 25 Gene Name UGT1A7
Enzyme 25 Protein Sequence >UDP glycosyltransferase 1 family polypeptide A7
MARAGWTGLLPLYVCLLLTCGFAKAGKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMP
EVSWQLGRSLNCTVKTYSTSYTLEDQDREFMVFADARWTAPLRSAFSLLTSSSNGIFDLF
FSNCRSLFNDRKLVEYLKESCFDAVFLDPFDACGLIVAKYFSLPSVVFARGIFCHYLEEG
AQCPAPLSYVPRLLLGFSDAMTFKERVWNHIMHLEEHLFCPYFFKNVLEIASEILQTPVT
AYDLYSHTSIWLLRTDFVLEYPKPVMPNMIFIGGINCHQGKPVPMEFEAYINASGEHGIV
VFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGH
PMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDL
ENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTW
YQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 25 Number of Residues 530
Enzyme 25 Molecular Weight 59819
Enzyme 25 Theoretical pI 7.85
Enzyme 25 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 25 General Function Carbohydrate transport and metabolism
Enzyme 25 Specific Function Not Available
Enzyme 25 Pathways Not Available
Enzyme 25 Reactions Not Available
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 40849862 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID Q5DSZ7 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name Q5DSZ7_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 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 25 GenBank Gene ID AY435142 Link Image
Enzyme 25 GeneCard ID Q5DSZ7 Link Image
Enzyme 25 GenAtlas ID UGT1A7 Link Image
Enzyme 25 HGNC ID HGNC:12539 Link Image
Enzyme 25 Chromosome Location Not Available
Enzyme 25 Locus Not Available
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References Not Available
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 15059
Enzyme 26 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 26 Synonyms Not Available
Enzyme 26 Gene Name UGT2B10
Enzyme 26 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 26 Number of Residues 528
Enzyme 26 Molecular Weight 60775
Enzyme 26 Theoretical pI 9.40
Enzyme 26 GO Classification Not Available
Enzyme 26 General Function Carbohydrate transport and metabolism
Enzyme 26 Specific Function Not Available
Enzyme 26 Pathways Not Available
Enzyme 26 Reactions Not Available
Enzyme 26 Pfam Domain Function Not Available
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 158258913 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID A8K9M3 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name A8K9M3_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 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 26 GenBank Gene ID AK292738 Link Image
Enzyme 26 GeneCard ID A8K9M3 Link Image
Enzyme 26 GenAtlas ID Not Available
Enzyme 26 HGNC ID Not Available
Enzyme 26 Chromosome Location Not Available
Enzyme 26 Locus Not Available
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References Not Available
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 16420
Enzyme 27 Name cDNA, FLJ93689, highly similar to Homo sapiens UDP glucuronosyltransferase 2 family, polypeptide B7 (UGT2B7), mRNA
Enzyme 27 Synonyms Not Available
Enzyme 27 Gene Name Not Available
Enzyme 27 Protein Sequence >cDNA, FLJ93689, highly similar to Homo sapiens UDP glucuronosyltransferase 2 family, polypeptide B7 (UGT2B7), mRNA
MSVKWTSVILLIQLSFCFSSGNCGKVLVWAAEYSHWMNIKTILDELIQRGHEVTVLASSA
SILFDPNNSSALKIEIYPTSLTKTELENFIMQQIKRWSDLPKDTFWLYFSQVQEIMSIFG
DITRKFCKDVVSNKKFMKKVQESRFDVIFADAIFPCSELLAELFNIPFVYSLSFSPGYTF
EKHSGGFIFPPSYVPVVMSELTDQMTFMERVKNMIYVLYFDFWFEIFDMKKWDQFYSEVL
GRPTTLSETMGKADVWLIRNSWNFQFPYPLLPNVDFVGGLHCKPAKPLPKEMEDFVQSSG
ENGVVVFSLGSMVSNMTEERANVIASALAQIPQKVLWRFDGNKPDTLGLNTRLYKWIPQN
DLLGHPKTRAFITHGGANGIYEAIYHGIPMVGIPLFADQPDNIAHMKARGAAVRVDFNTM
SSTDLLNALKRVINDPSYKENVMKLSRIQHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAA
HDLTWFQYHSLDVIGFLLVCVATVIFIVTKCCLFCFWKFARKAKKGKND
Enzyme 27 Number of Residues 529
Enzyme 27 Molecular Weight 60721
Enzyme 27 Theoretical pI 8.45
Enzyme 27 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 27 General Function Carbohydrate transport and metabolism
Enzyme 27 Specific Function Not Available
Enzyme 27 Pathways Not Available
Enzyme 27 Reactions Not Available
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein Not Available
Enzyme 27 UniProtKB/Swiss-Prot ID B2R810 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name B2R810_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence Not Available
Enzyme 27 GenBank Gene ID AK313190 Link Image
Enzyme 27 GeneCard ID B2R810 Link Image
Enzyme 27 GenAtlas ID Not Available
Enzyme 27 HGNC ID Not Available
Enzyme 27 Chromosome Location Not Available
Enzyme 27 Locus Not Available
Enzyme 27 SNPs Not Available
Enzyme 27 General References Not Available
Enzyme 27 Metabolite References Not Available