UGT2A1

UDP glucuronosyltransferase 2 family, polypeptide B1, also known as UGT2B1, is an enzyme that in humans is encoded by the UGT2B1 gene.[5][6]

UGT2A1
Identifiers
Aliases	UGT2A1, UDPGT2A1, UDP glucuronosyltransferase family 2 member A1 complex locus
External IDs	OMIM: 604716 MGI: 2149905 HomoloGene: 136808 GeneCards: UGT2A1
Gene location (Human) Chr. Chromosome 4 (human)[1] Band 4q13.3 Start 69,588,417 bp[1] End 69,653,249 bp[1]
Gene location (Mouse) Chr. Chromosome 5 (mouse)[2] Band 5|5 E1 Start 87,459,490 bp[2] End 87,490,871 bp[2]
Gene ontology Molecular function • transferase activity, transferring glycosyl groups • transferase activity • glucuronosyltransferase activity • transferase activity, transferring hexosyl groups • UDP-glycosyltransferase activity Cellular component • integral component of membrane • intracellular membrane-bounded organelle • membrane Biological process • sensory perception of smell • detection of chemical stimulus • cellular glucuronidation • response to stimulus • metabolism Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	10941	94215
Ensembl	ENSG00000173610	ENSMUSG00000106677
UniProt	Q9Y4X1	Q80X89
RefSeq (mRNA)	NM_001252274 NM_001252275 NM_001301239 NM_006798	NM_053184
RefSeq (protein)	NP_001099147 NP_001288162 NP_001239203 NP_001239204 NP_001288168 NP_006789	NP_444414
Location (UCSC)	Chr 4: 69.59 – 69.65 Mb	Chr 5: 87.46 – 87.49 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

The olfactory neuroepithelium, which lines the posterior nasal cavity, is exposed to a wide range of odorants and airborne toxic compounds. Odorants, which are mostly small lipophilic molecules, enter the mucus flow and reach the odorant receptors on sensory neurons. Odorant sensing is generally a transient process, requiring an effective signal termination, which could be provided by biotransformation of the odorant in the epithelial supporting cells. Xenobiotic-metabolizing enzymes in the olfactory epithelium have been suggested to catalyze inactivation and facilitate elimination of odorants.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000173610 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000106677 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Jedlitschky G, Cassidy AJ, Sales M, Pratt N, Burchell B (June 1999). "Cloning and characterization of a novel human olfactory UDP-glucuronosyltransferase". Biochem. J. 340 (3): 837–43. doi:10.1042/0264-6021:3400837. PMC 1220318. PMID 10359671.
6. "Entrez Gene: UGT2B1 UDP glucuronosyltransferase 2 family, polypeptide B1".

Further reading

• Iida A, Saito S, Sekine A, et al. (2002). "Catalog of 86 single-nucleotide polymorphisms (SNPs) in three uridine diphosphate glycosyltransferase genes: UGT2A1, UGT2B15, and UGT8". J. Hum. Genet. 47 (10): 505–10. doi:10.1007/s100380200075. PMID 12376738.
• Tukey RH, Strassburg CP (2001). "Genetic multiplicity of the human UDP-glucuronosyltransferases and regulation in the gastrointestinal tract". Mol. Pharmacol. 59 (3): 405–14. doi:10.1124/mol.59.3.405. PMID 11179432.
• 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.
• Heydel J, Leclerc S, Bernard P, et al. (2001). "Rat olfactory bulb and epithelium UDP-glucuronosyltransferase 2A1 (UGT2A1) expression: in situ mRNA localization and quantitative analysis". Brain Res. Mol. Brain Res. 90 (1): 83–92. doi:10.1016/S0169-328X(01)00080-8. PMID 11376859.
• Saito A, Kawamoto M, Kamatani N (2009). "Association study between single-nucleotide polymorphisms in 199 drug-related genes and commonly measured quantitative traits of 752 healthy Japanese subjects". J. Hum. Genet. 54 (6): 317–23. doi:10.1038/jhg.2009.31. PMID 19343046.
• Ross CJ, Katzov-Eckert H, Dubé MP, et al. (2009). "Genetic variants in TPMT and COMT are associated with hearing loss in children receiving cisplatin chemotherapy". Nat. Genet. 41 (12): 1345–9. doi:10.1038/ng.478. PMID 19898482.
• Mackenzie PI, Bock KW, Burchell B, et al. (2005). "Nomenclature update for the mammalian UDP glycosyltransferase (UGT) gene superfamily". Pharmacogenet. Genomics. 15 (10): 677–85. doi:10.1097/01.fpc.0000173483.13689.56. PMID 16141793.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.