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Identification
HMDB Protein ID HMDBP12662
Secondary Accession Numbers None
Name UDP-glucuronosyltransferase 2A2
Synonyms
  1. UDPGT 2A2
Gene Name UGT2A2
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile (PubMed:19858781, PubMed:18719240, PubMed:23756265, PubMed:23288867). Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds (PubMed:19858781, PubMed:23756265). Catalyzes the glucuronidation of endogenous estrogen hormone estradiol (PubMed:18719240, PubMed:23288867). Contributes to bile acid (BA) detoxification by catalyzing the glucuronidation of BA substrates, which are natural detergents for dietary lipids absorption (PubMed:23756265). Shows a potential role in detoxification of toxic waste compounds in the amniotic fluid before birth, and air-born chemical after birth (PubMed:19858781).
Pathways
  • Ascorbate and aldarate metabolism
  • Bile secretion
  • Biosynthesis of cofactors
  • Chemical carcinogenesis - DNA adducts
  • Chemical carcinogenesis - receptor activation
  • Drug metabolism - cytochrome P450
  • Drug metabolism - other enzymes
  • Metabolism of xenobiotics by cytochrome P450
  • Pentose and glucuronate interconversions
  • Porphyrin and chlorophyll metabolism
  • Retinol metabolism
  • Steroid hormone biosynthesis
Reactions Not Available
GO Classification
Biological Process
cellular glucuronidation
bile acid metabolic process
Cellular Component
endoplasmic reticulum membrane
integral to membrane
Molecular Function
glucuronosyltransferase activity
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 536
Molecular Weight 60771.605
Theoretical pI 8.796
Pfam Domain Function
Signals Not Available
Transmembrane Regions
  • 16-36;501-521;
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P0DTE5
UniProtKB/Swiss-Prot Entry Name UD2A2_HUMAN
PDB IDs Not Available
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed:15815621 ]
  2. Sneitz N, Court MH, Zhang X, Laajanen K, Yee KK, Dalton P, Ding X, Finel M: Human UDP-glucuronosyltransferase UGT2A2: cDNA construction, expression, and functional characterization in comparison with UGT2A1 and UGT2A3. Pharmacogenet Genomics. 2009 Dec;19(12):923-34. doi: 10.1097/FPC.0b013e3283330767. [PubMed:19858781 ]
  3. Itaaho K, Mackenzie PI, Ikushiro S, Miners JO, Finel M: The configuration of the 17-hydroxy group variably influences the glucuronidation of beta-estradiol and epiestradiol by human UDP-glucuronosyltransferases. Drug Metab Dispos. 2008 Nov;36(11):2307-15. doi: 10.1124/dmd.108.022731. Epub 2008 Aug 21. [PubMed:18719240 ]
  4. Perreault M, Gauthier-Landry L, Trottier J, Verreault M, Caron P, Finel M, Barbier O: The Human UDP-glucuronosyltransferase UGT2A1 and UGT2A2 enzymes are highly active in bile acid glucuronidation. Drug Metab Dispos. 2013 Sep;41(9):1616-20. doi: 10.1124/dmd.113.052613. Epub 2013 Jun 11. [PubMed:23756265 ]
  5. Sneitz N, Vahermo M, Mosorin J, Laakkonen L, Poirier D, Finel M: Regiospecificity and stereospecificity of human UDP-glucuronosyltransferases in the glucuronidation of estriol, 16-epiestriol, 17-epiestriol, and 13-epiestradiol. Drug Metab Dispos. 2013 Mar;41(3):582-91. doi: 10.1124/dmd.112.049072. Epub 2013 Jan 3. [PubMed:23288867 ]