CYP2A13

Cytochrome P450 2A13 is a protein that in humans is encoded by the CYP2A13 gene.

CYP2A13
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2P85, 2PG5, 2PG6, 2PG7, 3T3S, 4EJG, 4EJH, 4EJI
Identifiers
Aliases	CYP2A13, CPAD, CYP2A, CYPIIA13, cytochrome P450 family 2 subfamily A member 13
External IDs	OMIM: 608055; MGI: 88597; HomoloGene: 85917; GeneCards: CYP2A13; OMA:CYP2A13 - orthologs
Gene location (Human) Chr. Chromosome 19 (human) Band 19q13.2 Start 41,088,451 bp End 41,096,195 bp
Gene location (Mouse) Chr. Chromosome 7 (mouse) Band 7 A3|7 15.54 cM Start 26,534,730 bp End 26,542,973 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in nasal epithelium olfactory zone of nasal mucosa Brodmann area 10 quadriceps femoris muscle paraflocculus of cerebellum mucosa of paranasal sinus middle frontal gyrus frontal pole epithelium of bronchus bronchial epithelial cell Top expressed in proximal tubule human kidney right kidney hepatobiliary system liver esophagus respiratory epithelium thymus nasal epithelium olfactory epithelium More reference expression data BioGPS More reference expression data
Gene ontology Molecular function iron ion binding oxidoreductase activity aromatase activity arachidonic acid epoxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen heme binding oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen metal ion binding coumarin 7-hydroxylase activity steroid hydroxylase activity monooxygenase activity Cellular component organelle membrane endoplasmic reticulum membrane endoplasmic reticulum membrane intracellular membrane-bounded organelle cytoplasm Biological process xenobiotic metabolic process epoxygenase P450 pathway coumarin metabolic process organic acid metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 1553 13087 Ensembl ENSG00000197838 ENSMUSG00000005547 UniProt Q16696 P20852 RefSeq (mRNA) NM_000766 NM_007812 RefSeq (protein) NP_000757 n/a Location (UCSC) Chr 19: 41.09 – 41.1 Mb Chr 7: 26.53 – 26.54 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This protein localizes to the endoplasmic reticulum. Although its endogenous substrate has not been determined, it is known to metabolize 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone, a major nitrosamine specific to tobacco. This gene is part of a large cluster of cytochrome P450 genes from the CYP2A, CYP2B and CYP2F subfamilies on chromosome 19q.

External links

• Human CYP2A13 genome location and CYP2A13 gene details page in the UCSC Genome Browser.

Further reading

• Fernandez-Salguero P, Gonzalez FJ (1995). "The CYP2A gene subfamily: species differences, regulation, catalytic activities and role in chemical carcinogenesis". Pharmacogenetics. 5 (Special Issue): S123–8. doi:10.1097/00008571-199512001-00013. PMID 7581481.
• Smith G, Stubbins MJ, Harries LW, Wolf CR (1999). "Molecular genetics of the human cytochrome P450 monooxygenase superfamily". Xenobiotica. 28 (12): 1129–65. doi:10.1080/004982598238868. PMID 9890157.
• Hoffman SM, Fernandez-Salguero P, Gonzalez FJ, Mohrenweiser HW (1996). "Organization and evolution of the cytochrome P450 CYP2A-2B-2F subfamily gene cluster on human chromosome 19". J. Mol. Evol. 41 (6): 894–900. doi:10.1007/bf00173169. PMID 8587134. S2CID 12153961.
• Koskela S, Hakkola J, Hukkanen J, et al. (1999). "Expression of CYP2A genes in human liver and extrahepatic tissues". Biochem. Pharmacol. 57 (12): 1407–13. doi:10.1016/S0006-2952(99)00015-5. PMID 10353262.
• Su T, Bao Z, Zhang QY, et al. (2000). "Human cytochrome P450 CYP2A13: predominant expression in the respiratory tract and its high efficiency metabolic activation of a tobacco-specific carcinogen, 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone". Cancer Res. 60 (18): 5074–9. PMID 11016631.
• Zhang X, Su T, Zhang QY, et al. (2002). "Genetic polymorphisms of the human CYP2A13 gene: identification of single-nucleotide polymorphisms and functional characterization of an Arg257Cys variant". J. Pharmacol. Exp. Ther. 302 (2): 416–23. doi:10.1124/jpet.302.2.416. PMID 12130698.
• Saito S, Iida A, Sekine A, et al. (2003). "Catalog of 680 variations among eight cytochrome p450 ( CYP) genes, nine esterase genes, and two other genes in the Japanese population". J. Hum. Genet. 48 (5): 249–70. doi:10.1007/s10038-003-0021-7. PMID 12721789.
• Wang H, Tan W, Hao B, et al. (2004). "Substantial reduction in risk of lung adenocarcinoma associated with genetic polymorphism in CYP2A13, the most active cytochrome P450 for the metabolic activation of tobacco-specific carcinogen NNK". Cancer Res. 63 (22): 8057–61. PMID 14633739.
• Cauffiez C, Lo-Guidice JM, Quaranta S, et al. (2004). "Genetic polymorphism of the human cytochrome CYP2A13 in a French population: implication in lung cancer susceptibility". Biochem. Biophys. Res. Commun. 317 (2): 662–9. doi:10.1016/j.bbrc.2004.03.092. PMID 15063809.
• Cheng XY, Chen GL, Zhang WX, et al. (2004). "Arg257Cys polymorphism of CYP2A13 in a Chinese population". Clin. Chim. Acta. 343 (1–2): 213–6. doi:10.1016/j.cccn.2004.01.017. PMID 15115698.
• He XY, Shen J, Ding X, et al. (2005). "Identification of critical amino acid residues of human CYP2A13 for the metabolic activation of 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone, a tobacco-specific carcinogen". Drug Metab. Dispos. 32 (12): 1516–21. doi:10.1124/dmd.104.001370. PMID 15333516. S2CID 26225467.
• Fujieda M, Yamazaki H, Kiyotani K, et al. (2005). "Eighteen novel polymorphisms of the CYP2A13 gene in Japanese". Drug Metab. Pharmacokinet. 18 (1): 86–90. doi:10.2133/dmpk.18.86. PMID 15618722.
• Smith BD, Sanders JL, Porubsky PR, et al. (2007). "Structure of the human lung cytochrome P450 2A13". J. Biol. Chem. 282 (23): 17306–13. doi:10.1074/jbc.M702361200. PMID 17428784.