UGT1A3
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| UGT1A3 |
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| Identifiers |
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Aliases |
UGT1A3, UDPGT, UDPGT 1-3, UGT-1C, UGT1-03, UGT1.3, UGT1C, UGT1A3S, UDP glucuronosyltransferase family 1 member A3 |
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External IDs |
MGI: 3576049 HomoloGene: 86211 GeneCards: UGT1A3 |
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| Gene location (Human) |
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 |
Chr. |
Chromosome 2 (human)[1] |
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Band |
2q37.1 |
Start |
233,729,108 bp[1] |
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End |
233,773,299 bp[1] |
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| Gene location (Mouse) |
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 |
Chr. |
Chromosome 1 (mouse)[2] |
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|
Band |
1|1 D |
Start |
88,200,601 bp[2] |
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End |
88,218,997 bp[2] |
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| Gene ontology |
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Molecular function |
• transferase activity • retinoic acid binding • transferase activity, transferring hexosyl groups • protein homodimerization activity • transferase activity, transferring glycosyl groups • glucuronosyltransferase activity • protein heterodimerization activity • enzyme binding • UDP-glycosyltransferase activity
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Cellular component |
• integral component of membrane • endoplasmic reticulum membrane • membrane • intracellular membrane-bounded organelle • endoplasmic reticulum
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Biological process |
• retinoic acid metabolic process • negative regulation of cellular glucuronidation • cellular glucuronidation • flavonoid glucuronidation • xenobiotic glucuronidation • drug metabolic process • negative regulation of glucuronosyltransferase activity • negative regulation of fatty acid metabolic process • metabolism
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Sources:Amigo / QuickGO
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| Orthologs |
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Species |
Human |
Mouse |
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Entrez |
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Ensembl |
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UniProt |
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RefSeq (mRNA) |
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RefSeq (protein) |
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Location (UCSC) |
Chr 2: 233.73 – 233.77 Mb |
Chr 1: 88.2 – 88.22 Mb |
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PubMed search |
[3] |
[4] |
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| Wikidata |
View/Edit Human |
View/Edit Mouse |
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UDP-glucuronosyltransferase 1-3 is an enzyme that in humans is encoded by the UGT1A3 gene.[5][6][7][8]
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 alpha-pyrene.[8]
References[edit]
^ abc GRCh38: Ensembl release 89: ENSG00000243135 - Ensembl, May 2017
^ abc GRCm38: Ensembl release 89: ENSMUSG00000090171 - Ensembl, May 2017
^ "Human PubMed Reference:"..mw-parser-output cite.citation{font-style:inherit}.mw-parser-output q{quotes:"""""""'""'"}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/6/65/Lock-green.svg/9px-Lock-green.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-limited a,.mw-parser-output .cs1-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/d/d6/Lock-gray-alt-2.svg/9px-Lock-gray-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Lock-red-alt-2.svg/9px-Lock-red-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{font-size:100%}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}
^ "Mouse PubMed Reference:".
^ Mackenzie PI, Owens IS, Burchell B, Bock KW, Bairoch A, Belanger A, Fournel-Gigleux S, Green M, Hum DW, Iyanagi T, Lancet D, Louisot P, Magdalou J, Chowdhury JR, Ritter JK, Schachter H, Tephly TR, Tipton KF, Nebert DW (Oct 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 (Mar 1992). "A novel complex locus UGT1 encodes human bilirubin, phenol, and other UDP-glucuronosyltransferase isozymes with identical carboxyl termini". J Biol Chem. 267 (5): 3257–61. PMID 1339448.
^ Gong QH, Cho JW, Huang T, Potter C, Gholami N, Basu NK, Kubota S, Carvalho S, Pennington MW, Owens IS, Popescu NC (Jul 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.
^ ab "Entrez Gene: UGT1A3 UDP glucuronosyltransferase 1 family, polypeptide A3".
Further reading[edit]
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Tukey RH, Strassburg CP (2000). "Human UDP-glucuronosyltransferases: metabolism, expression, and disease". Annu. Rev. Pharmacol. Toxicol. 40: 581–616. doi:10.1146/annurev.pharmtox.40.1.581. PMID 10836148.
Tukey RH, Strassburg CP (2001). "Genetic multiplicity of the human UDP-glucuronosyltransferases and regulation in the gastrointestinal tract". Mol. Pharmacol. 59 (3): 405–14. PMID 11179432.
King CD, Rios GR, Green MD, Tephly TR (2001). "UDP-glucuronosyltransferases". Curr. Drug Metab. 1 (2): 143–61. doi:10.2174/1389200003339171. PMID 11465080.
Moghrabi N, Sutherland L, Wooster R, et al. (1992). "Chromosomal assignment of human phenol and bilirubin UDP-glucuronosyltransferase genes (UGT1A-subfamily)". Ann. Hum. Genet. 56 (Pt 2): 81–91. doi:10.1111/j.1469-1809.1992.tb01134.x. PMID 1503396.
Mojarrabi B, Butler R, Mackenzie PI (1996). "cDNA cloning and characterization of the human UDP glucuronosyltransferase, UGT1A3". Biochem. Biophys. Res. Commun. 225 (3): 785–90. doi:10.1006/bbrc.1996.1251. PMID 8780690.
Strassburg CP, Manns MP, Tukey RH (1997). "Differential down-regulation of the UDP-glucuronosyltransferase 1A locus is an early event in human liver and biliary cancer". Cancer Res. 57 (14): 2979–85. PMID 9230212.
Strassburg CP, Oldhafer K, Manns MP, Tukey RH (1997). "Differential expression of the UGT1A locus in human liver, biliary, and gastric tissue: identification of UGT1A7 and UGT1A10 transcripts in extrahepatic tissue". Mol. Pharmacol. 52 (2): 212–20. PMID 9271343.
Strassburg CP, Manns MP, Tukey RH (1998). "Expression of the UDP-glucuronosyltransferase 1A locus in human colon. Identification and characterization of the novel extrahepatic UGT1A8". J. Biol. Chem. 273 (15): 8719–26. doi:10.1074/jbc.273.15.8719. PMID 9535849.
Green MD, King CD, Mojarrabi B, et al. (1998). "Glucuronidation of amines and other xenobiotics catalyzed by expressed human UDP-glucuronosyltransferase 1A3". Drug Metab. Dispos. 26 (6): 507–12. PMID 9616184.
Strassburg CP, Kneip S, Topp J, et al. (2000). "Polymorphic gene regulation and interindividual variation of UDP-glucuronosyltransferase activity in human small intestine". J. Biol. Chem. 275 (46): 36164–71. doi:10.1074/jbc.M002180200. PMID 10748067.
Barbier O, Albert C, Martineau I, et al. (2001). "Glucuronidation of the nonsteroidal antiestrogen EM-652 (SCH 57068), by human and monkey steroid conjugating UDP-glucuronosyltransferase enzymes". Mol. Pharmacol. 59 (3): 636–45. PMID 11179460.
Turgeon D, Chouinard S, Belanger P, et al. (2004). "Glucuronidation of arachidonic and linoleic acid metabolites by human UDP-glucuronosyltransferases". J. Lipid Res. 44 (6): 1182–91. doi:10.1194/jlr.M300010-JLR200. PMID 12639971.
Zhang JY, Zhan J, Cook CS, et al. (2003). "Involvement of human UGT2B7 and 2B15 in rofecoxib metabolism". Drug Metab. Dispos. 31 (5): 652–8. doi:10.1124/dmd.31.5.652. PMID 12695355.
Transferases: glycosyltransferases (EC 2.4)
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2.4.1: Hexosyl- transferases
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Glucosyl- |
Phosphorylase
- Glycogen synthase
- Debranching enzyme
- Branching enzyme
- 1,3-Beta-glucan synthase
- Ceramide glucosyltransferase
- N-glycosyltransferase
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Galactosyl- |
- Lactose synthase
- B-N-acetylglucosaminyl-glycopeptide b-1,4-galactosyltransferase
Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase (C1GALT1)
|
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Glucuronosyl- |
- UGT1A1
- UGT1A3
- UGT1A4
- UGT1A5
- UGT1A6
- UGT1A7
- UGT1A8
- UGT1A9
- UGT1A10
- UGT2A1
- UGT2A2
- UGT2A3
- UGT2B4
- UGT2B7
- UGT2B10
- UGT2B11
- UGT2B15
- UGT2B17
- UGT2B28
Hyaluronan synthase: HAS1
- HAS2
- HAS3
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Fucosyl- |
- POFUT1
- POFUT2
- FUT1
- FUT2
- FUT3
- FUT4
- FUT5
- FUT6
- FUT7
- FUT8
- FUT9
- FUT10
- FUT11
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Mannosyl- |
Dolichyl-phosphate-mannose-protein mannosyltransferase
- DPM1
- DPM3
- ALG1
- ALG2
- ALG3
- ALG6
- ALG8
- ALG9
- ALG12
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2.4.2: Pentosyl- transferases
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Ribose |
ADP-ribosyltransferase |
NAD+:diphthamide ADP-ribosyltransferase
NAD(P)+:arginine ADP-ribosyltransferase
- Pertussis toxin
- Cholera toxin
- Poly ADP ribose polymerase
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Phosphoribosyltransferase |
- Adenine phosphoribosyltransferase
- Hypoxanthine-guanine phosphoribosyltransferase
- Uracil phosphoribosyltransferase
- Amidophosphoribosyltransferase
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Other |
Purine nucleoside phosphorylase: Thymidine phosphorylase
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Other |
Xylosyltransferase
Arabinosyltransferase
- Indolylacetylinositol arabinosyltransferase
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2.4.99: Sialyl transferases
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- Beta-galactoside alpha-2,6-sialyltransferase
- Monosialoganglioside sialyltransferase
- ST8SIA4
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