CYP1A2
Cytochrome P450 1A2
Also known as: CP12, CP1A2_HUMAN, P3-450
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P05177
- Gene
- CYP1A2
- Ensembl
- ENSG00000140505
- Chromosome
- 15
- Canonical length
- 516 aa
- Protein class
- Cancer-related genes, Enzymes, Metabolic proteins, Predicted membrane proteins
- Quaternary structure
- Homodimer
OverviewNCBI Gene
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. The protein encoded by this gene 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. Other xenobiotic substrates for this enzyme include caffeine, aflatoxin B1, and acetaminophen. The transcript from this gene contains four Alu sequences flanked by direct repeats in the 3' untranslated region. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
516 residues, UniProt reviewed canonical sequence.
>P05177|CYP1A2
1 MALSQSVPFS ATELLLASAI FCLVFWVLKG LRPRVPKGLK SPPEPWGWPL LGHVLTLGKN
61 PHLALSRMSQ RYGDVLQIRI GSTPVLVLSR LDTIRQALVR QGDDFKGRPD LYTSTLITDG
121 QSLTFSTDSG PVWAARRRLA QNALNTFSIA SDPASSSSCY LEEHVSKEAK ALISRLQELM
181 AGPGHFDPYN QVVVSVANVI GAMCFGQHFP ESSDEMLSLV KNTHEFVETA SSGNPLDFFP
241 ILRYLPNPAL QRFKAFNQRF LWFLQKTVQE HYQDFDKNSV RDITGALFKH SKKGPRASGN
301 LIPQEKIVNL VNDIFGAGFD TVTTAISWSL MYLVTKPEIQ RKIQKELDTV IGRERRPRLS
361 DRPQLPYLEA FILETFRHSS FLPFTIPHST TRDTTLNGFY IPKKCCVFVN QWQVNHDPEL
421 WEDPSEFRPE RFLTADGTAI NKPLSEKMML FGMGKRRCIG EVLAKWEIFL FLAILLQQLE
481 FSVPPGVKVD LTPIYGLTMK HARCEHVQAR LRFSINLocalizationUniProt · AlphaFold · HPA
Whether an antibody against CYP1A2 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Other membrane
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.24
- Highest tissue expression
- 478 nTPM
Expression across tissuesHPA
Tissue
- liver: 478 nTPM
- thyroid gland: 2 nTPM
- bone marrow: 1 nTPM
- placenta: 0.7 nTPM
- skin: 0.6 nTPM
- epididymis: 0.5 nTPM
Single-cell type
- hepatocytes: 756 nCPM
- epididymal clear cells: 96 nCPM
- cholangiocytes: 8.7 nCPM
- kupffer cells: 2 nCPM
- alveolar cells type 1: 1.1 nCPM
- epididymal basal cells: 1.1 nCPM
Immune cell
- neutrophil: 2.1 nTPM
- basophil: 1.4 nTPM
- eosinophil: 0.5 nTPM
- naive B-cell: 0.5 nTPM
- NK-cell: 0.4 nTPM
- plasmacytoid DC: 0.4 nTPM
Brain region
- cerebellum: 8 nTPM
- white matter: 7.5 nTPM
- cerebral cortex: 6.4 nTPM
- medulla oblongata: 6.3 nTPM
- pons: 6.1 nTPM
- hippocampal formation: 6 nTPM
ReferencesPubMed · IEDB
Publications for CYP1A2 from three distinct lines of evidence, kept separate because they answer different questions: whether antibodies are directed at the protein, whether a B-cell epitope has been mapped on it, and whether a T-cell epitope has. Each is labelled with its source.
Reference: AutoantibodyPubMed
4 publications
- Interactions of dihydralazine with cytochromes P4501A: a possible explanation for the appearance of anti-cytochrome P4501A2 autoantibodies.
1994 · Mol Pharmacol · RCR 2.7 · 73 citations - Increased incidence of anti-LKM autoantibodies in a consecutive cohort of hepatitis C patients from central Greece.
2002 · Eur J Gastroenterol Hepatol · RCR 1.1 · 40 citations - Cytochrome P450 enzymes and UDP-glucuronosyltransferases as hepatocellular autoantigens.
1996 · Mol Biol Rep · RCR 0.4 · 11 citations - High levels of autoantibodies against drug-metabolizing enzymes in SLA/LP-positive AIH-1 sera.
2004 · Autoimmunity · RCR 0.2 · 6 citations
Sources: PubMed — antigen-level antibody evidence from a custom retrieval. Records matching a controlled set of autoantibody terms (the MeSH descriptors Autoantibodies and Autoantigens, with title and abstract term variants) were obtained through NCBI E-utilities, and their titles and abstracts parsed for constructions that direct an antibody at a named protein rather than for co-occurrence. Captured names were resolved against UniProt nomenclature and each antigen adjudicated individually against the source text. Bibliographic records from PubMed and MeSH, U.S. National Library of Medicine; citation metrics from NIH iCite (Hutchins et al., PLoS Biology 2016). Titles link to PubMed; abstracts are not reproduced here. The NLM does not endorse this analysis.
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 1.34
- gnomAD pLI
- 0
- gnomAD missense Z
- -0.42
- DepMap mean gene effect
- -0.01
- DepMap dependency class
- none
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 2% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- aflatoxin metabolic process
- alkaloid metabolic process
- cellular respiration
- cellular response to cadmium ion
- cholesterol metabolic process
- dibenzo-p-dioxin metabolic process
- epoxygenase P450 pathway
- estrogen metabolic process
- hydrogen peroxide biosynthetic process
- long-chain fatty acid biosynthetic process
- lung development
- methylation
- monocarboxylic acid metabolic process
- monoterpenoid metabolic process
- omega-hydroxylase P450 pathway
- oxidative demethylation
- porphyrin-containing compound metabolic process
- post-embryonic development
- regulation of gene expression
- retinol metabolic process
- steroid catabolic process
- toxin metabolic process
- xenobiotic catabolic process
- xenobiotic metabolic process
- toxin biosynthetic process
Molecular functions
- caffeine oxidase activity
- demethylase activity
- electron transfer activity
- enzyme binding
- estrogen 16-alpha-hydroxylase activity
- estrogen 2-hydroxylase activity
- heme binding
- hydroperoxy icosatetraenoate dehydratase activity
- iron 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
- steroid hydroxylase activity
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of CYP1A2 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads CYP1A2 as an antibody target. Whether an autoantibody or antibody against CYP1A2 could matter depends on whether native CYP1A2 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
CYP1A2 is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.
Annotation status
The present source text does not explicitly label CYP1A2 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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