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UGT1A3
Identifiers
Aliases	UGT1A3, UDPGT, UDPGT 1-3, UGT-1C, UGT1-03, UGT1.3, UGT1C, UGT1A3S, UDP glucuronosyltransferase family 1 member A3
External IDs	OMIM: 606428; MGI: 3576049; HomoloGene: 86211; GeneCards: UGT1A3; OMA:UGT1A3 - orthologs
Gene location (Human)
Chr.	Chromosome 2 (human)
End	233,773,300 bp
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)
End	88,146,719 bp
RNA expression pattern
	Top expressed in
	liver; ; right lobe of liver; ; muscle tissue; ; kidney; ; small intestine; ; duodenum; ; colon;
	Top expressed in
	right kidney; ; human kidney; ; granulocyte; ; renal cortex; ; liver; ; duodenum; ; lip; ; uterus; ; bone marrow; ; proximal tubule;
	More reference expression data
	n/a
Gene ontology
Molecular function	transferase activity; retinoic acid binding; hexosyltransferase activity; protein homodimerization activity; glycosyltransferase activity; glucuronosyltransferase activity; protein heterodimerization activity; enzyme binding; UDP-glycosyltransferase activity;
Cellular component	integral component of membrane; endoplasmic reticulum membrane; membrane; intracellular membrane-bounded organelle; endoplasmic reticulum;
Biological process	retinoic acid metabolic process; negative regulation of cellular glucuronidation; cellular glucuronidation; flavonoid glucuronidation; xenobiotic glucuronidation; negative regulation of glucuronosyltransferase activity; negative regulation of fatty acid metabolic process; metabolism;
	Sources:Amigo / QuickGO
Orthologs
	54659
	22236
	ENSG00000288702
	ENSMUSG00000090171
	P35503
	P70691
	NM_019093
	NM_013701
	NP_061966
	NP_038729
	Wikidata
View/Edit Human	View/Edit Mouse

UDP-glucuronosyltransferase 1-3 is an enzyme that in humans is encoded by the UGT1A3 gene.^[5]^[6]^[7]

This gene encodes a UDP-glucuronosyltransferase, an enzyme of the glucuronidation pathway that transforms small lipophilic molecules, such as steroids, bilirubin, hormones, and drugs, into water-soluble, excretable metabolites. This gene is part of a complex locus that encodes several UDP-glucuronosyltransferases. The locus includes thirteen unique alternate first exons followed by four common exons. Four of the alternate first exons are considered pseudogenes. Each of the remaining nine 5' exons may be spliced to the four common exons, resulting in nine proteins with different N-termini and identical C-termini. Each first exon encodes the substrate binding site, and is regulated by its own promoter. Substrates of this enzyme include estrone, 2-hydroxyestrone, and metabolites of benzo(a)pyrene.^[8]^[9]^[10]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000288702 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000090171 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Gene: UGT1A3 (ENSG00000243135) - Summary - Homo sapiens - Ensembl genome browser 89". may2017.archive.ensembl.org. Retrieved 2019-05-18.
^ "Gene: Ugt1a2 (ENSMUSG00000090171) - Summary - Mus musculus - Ensembl genome browser 89". may2017.archive.ensembl.org. Retrieved 2019-05-18.
^ Mackenzie PI, Owens IS, Burchell B, Bock KW, Bairoch A, Bélanger A, et al. (August 1997). "The UDP glycosyltransferase gene superfamily: recommended nomenclature update based on evolutionary divergence". Pharmacogenetics. 7 (4): 255–69. doi:10.1097/00008571-199708000-00001. PMID 9295054.
^ Ritter JK, Chen F, Sheen YY, Tran HM, Kimura S, Yeatman MT, Owens IS (February 1992). "A novel complex locus UGT1 encodes human bilirubin, phenol, and other UDP-glucuronosyltransferase isozymes with identical carboxyl termini". The Journal of Biological Chemistry. 267 (5): 3257–61. doi:10.1016/S0021-9258(19)50724-4. PMID 1339448.
^ Gong QH, Cho JW, Huang T, Potter C, Gholami N, Basu NK, Kubota S, Carvalho S, Pennington MW, Owens IS, Popescu NC (June 2001). "Thirteen UDPglucuronosyltransferase genes are encoded at the human UGT1 gene complex locus". Pharmacogenetics. 11 (4): 357–68. doi:10.1097/00008571-200106000-00011. PMID 11434514.
^ "UGT1A3 UDP glucuronosyltransferase family 1 member A3 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2019-05-18.

Tukey RH, Strassburg CP (2000). "Human UDP-glucuronosyltransferases: metabolism, expression, and disease". Annual Review of Pharmacology and Toxicology. 40: 581–616. doi:10.1146/annurev.pharmtox.40.1.581. PMID 10836148.
Tukey RH, Strassburg CP (March 2001). "Genetic multiplicity of the human UDP-glucuronosyltransferases and regulation in the gastrointestinal tract". Molecular Pharmacology. 59 (3): 405–14. doi:10.1124/mol.59.3.405. PMID 11179432. S2CID 21500183.
King CD, Rios GR, Green MD, Tephly TR (September 2000). "UDP-glucuronosyltransferases". Current Drug Metabolism. 1 (2): 143–61. doi:10.2174/1389200003339171. PMID 11465080.
Moghrabi N, Sutherland L, Wooster R, Povey S, Boxer M, Burchell B (May 1992). "Chromosomal assignment of human phenol and bilirubin UDP-glucuronosyltransferase genes (UGT1A-subfamily)". Annals of Human Genetics. 56 (2): 81–91. doi:10.1111/j.1469-1809.1992.tb01134.x. PMID 1503396. S2CID 40140345.
Mojarrabi B, Butler R, Mackenzie PI (August 1996). "cDNA cloning and characterization of the human UDP glucuronosyltransferase, UGT1A3". Biochemical and Biophysical Research Communications. 225 (3): 785–90. doi:10.1006/bbrc.1996.1251. PMID 8780690.
Strassburg CP, Manns MP, Tukey RH (July 1997). "Differential down-regulation of the UDP-glucuronosyltransferase 1A locus is an early event in human liver and biliary cancer". Cancer Research. 57 (14): 2979–85. PMID 9230212.
Strassburg CP, Oldhafer K, Manns MP, Tukey RH (August 1997). "Differential expression of the UGT1A locus in human liver, biliary, and gastric tissue: identification of UGT1A7 and UGT1A10 transcripts in extrahepatic tissue". Molecular Pharmacology. 52 (2): 212–20. doi:10.1124/mol.52.2.212. PMID 9271343. S2CID 37098463.
Strassburg CP, Manns MP, Tukey RH (April 1998). "Expression of the UDP-glucuronosyltransferase 1A locus in human colon. Identification and characterization of the novel extrahepatic UGT1A8". The Journal of Biological Chemistry. 273 (15): 8719–26. doi:10.1074/jbc.273.15.8719. PMID 9535849.
Green MD, King CD, Mojarrabi B, Mackenzie PI, Tephly TR (June 1998). "Glucuronidation of amines and other xenobiotics catalyzed by expressed human UDP-glucuronosyltransferase 1A3". Drug Metabolism and Disposition. 26 (6): 507–12. PMID 9616184.
Strassburg CP, Kneip S, Topp J, Obermayer-Straub P, Barut A, Tukey RH, Manns MP (November 2000). "Polymorphic gene regulation and interindividual variation of UDP-glucuronosyltransferase activity in human small intestine". The Journal of Biological Chemistry. 275 (46): 36164–71. doi:10.1074/jbc.M002180200. PMID 10748067.
Barbier O, Albert C, Martineau I, Vallée M, High K, Labrie F, Hum DW, Labrie C, Bélanger A (March 2001). "Glucuronidation of the nonsteroidal antiestrogen EM-652 (SCH 57068), by human and monkey steroid conjugating UDP-glucuronosyltransferase enzymes". Molecular Pharmacology. 59 (3): 636–45. doi:10.1124/mol.59.3.636. PMID 11179460. S2CID 38640331.
Turgeon D, Chouinard S, Belanger P, Picard S, Labbe JF, Borgeat P, Belanger A (June 2003). "Glucuronidation of arachidonic and linoleic acid metabolites by human UDP-glucuronosyltransferases". Journal of Lipid Research. 44 (6): 1182–91. doi:10.1194/jlr.M300010-JLR200. PMID 12639971.
Zhang JY, Zhan J, Cook CS, Ings RM, Breau AP (May 2003). "Involvement of human UGT2B7 and 2B15 in rofecoxib metabolism". Drug Metabolism and Disposition. 31 (5): 652–8. doi:10.1124/dmd.31.5.652. PMID 12695355. S2CID 23434477.