CYP1A1 - cytochrome P450, family 1, subfamily A, polypeptide 1
Entrez Gene Name: cytochrome P450, family 1, subfamily A, polypeptide 1
Entrez GeneID: Human(1543)
, Mouse(13076)
, Rat(24296)
Synonyms: AHH, AHRR, CP11, CYP1, CYP1A1, Cyp1a2, Cyp45c, Cypc45c, CYPIA1, Cytochrome p1-450, CYTOCHROME P4501A1, Erod, P-450bnf-b, P-450MC, P1-450, P450 IA1, P450-1, P450-C, P450-P1, P4501a1, P450DX
Gene Summary
- Human (1543): This gene, CYP1A1, 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 and its expression is induced by some polycyclic aromatic hydrocarbons (PAHs), some of which are found in cigarette smoke. The enzyme's endogenous substrate is unknown; however, it is able to metabolize some PAHs to carcinogenic intermediates. The gene has been associated with lung cancer risk. A related family member, CYP1A2, is located approximately 25 kb away from CYP1A1 on chromosome 15. [provided by RefSeq]
- Rat (24296): monooxygenase that plays a role in dioxin metabolism and detoxification which is 3-methylcholanthrene-inducible [RGD]
Molecular Functions | Biological Process | Cellular Components | Protein Domains | Subcellular Locations | Pathways | Literature References | IPA Extras
Cell Regulation
Biological Process
cellular amine metabolic process, dibenzo-p-dioxin metabolic process, heterocycle metabolic process, hydrogen peroxide biosynthetic process, oxidation reduction, toxin metabolic process
Literature References
- 17283379
Korashy HM, Shayeganpour A, Brocks DR, El-Kadi AO. Induction of Cytochrome P450 1A1 by Ketoconazole and Itraconazole but not Fluconazole in Murine and Human Hepatoma Cell Lines.Toxicol Sci 2007 May 01;97(1):32-43 - 16567799
Kang HJ, Kim HJ, Kim SK, Barouki R, Cho CH, Khanna KK, Rosen EM, Bae I. BRCA1 modulates xenobiotic stress-inducible gene expression by interacting with ARNT in human breast cancer cells.J Biol Chem 2006 May 26;281(21):14654-62 - 16595894
Nishihashi H, Kanno Y, Tomuro K, Nakahama T, Inouye Y. Primary structure and organ-specific expression of the rat aryl hydrocarbon receptor repressor gene.Biol Pharm Bull 2006 Apr 01;29(4):640-7 View 1830 categorized literature findings and their references in IPA
Molecular Functions
electron carrier activity, heme binding, iron ion binding, metal ion binding, monooxygenase activity, oxidoreductase 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, oxygen binding
Subcellular Locations
cell surface, cytoplasm, endoplasmic reticulum membrane, microsomal fraction, microsome, mitochondria, mitochondrial fraction, mitochondrial membrane, nuclear fraction, nucleus, plasma membrane



