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P05177 (CP1A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytochrome P450 1A2

EC=1.14.14.1
Alternative name(s):
CYPIA2
Cytochrome P(3)450
Cytochrome P450 4
Cytochrome P450-P3
Gene names
Name:CYP1A2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length515 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Most active in catalyzing 2-hydroxylation. Caffeine is metabolized primarily by cytochrome CYP1A2 in the liver through an initial N3-demethylation. Also acts in the metabolism of aflatoxin B1 and acetaminophen. Participates in the bioactivation of carcinogenic aromatic and heterocyclic amines. Catalizes the N-hydroxylation of heterocyclic amines and the O-deethylation of phenacetin. Ref.11

Catalytic activity

RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O.

Cofactor

Heme group.

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.

Tissue specificity

Liver.

Induction

By nicotine, omeprazole, phenobarbital, primidone and rifampicin.

Polymorphism

The CYP1A2*1F allele which is quite common (40 to 50%) is due to a substitution of a base in the non-coding region of the CYP1A2 gene and has the effect of decreasing the enzyme inducibility. Individuals who are homozygous for the CYP1A2*1F allele are 'slow' caffeine metabolizers. Thus for these individual increased intake of caffeine seems to be associated with a concomitant increase in the risk of non-fatal myocardial infraction (MI).

Sequence similarities

Belongs to the cytochrome P450 family.

Biophysicochemical properties

Kinetic parameters:

KM=4 µM for 2-amino-6-methyldipyrido[1,2-a:3',2'-d]imidazole Ref.11

KM=21 µM for 2-amino-3-methylimidazo[4,5-f]quinoline

KM=26 µM for 2-amino-2,4-dimethylimidazo[4,5-f]quinoline

KM=27 µM for 2-amino-3,8-dimethylimidazo[4,5-f]quinoxaline

KM=71 µM for 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine

KM=25 µM for phenacetin

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandHeme
Iron
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processalkaloid metabolic process

Inferred from direct assay PubMed 11511187. Source: BHF-UCL

arachidonic acid metabolic process

Traceable author statement. Source: Reactome

cellular respiration

Inferred from electronic annotation. Source: Ensembl

cellular response to cadmium ion

Inferred from electronic annotation. Source: Ensembl

dibenzo-p-dioxin metabolic process

Inferred from electronic annotation. Source: Ensembl

drug catabolic process

Inferred from mutant phenotype PubMed 18356043. Source: BHF-UCL

drug metabolic process

Inferred from direct assay PubMed 15327587PubMed 19219744. Source: BHF-UCL

epoxygenase P450 pathway

Traceable author statement. Source: Reactome

exogenous drug catabolic process

Inferred from direct assay PubMed 18619574. Source: BHF-UCL

heterocycle metabolic process

Inferred from direct assay PubMed 15327587. Source: BHF-UCL

hydrogen peroxide biosynthetic process

Inferred from electronic annotation. Source: Ensembl

lung development

Inferred from electronic annotation. Source: Ensembl

methylation

Traceable author statement. Source: Reactome

monocarboxylic acid metabolic process

Inferred from direct assay PubMed 19651758. Source: BHF-UCL

monoterpenoid metabolic process

Inferred from direct assay PubMed 16401082. Source: BHF-UCL

omega-hydroxylase P450 pathway

Traceable author statement. Source: Reactome

oxidation-reduction process

Inferred from direct assay PubMed 16401082PubMed 19219744. Source: BHF-UCL

oxidative deethylation

Inferred from direct assay PubMed 19029318. Source: BHF-UCL

oxidative demethylation

Inferred from direct assay PubMed 18619574. Source: BHF-UCL

porphyrin-containing compound metabolic process

Inferred from electronic annotation. Source: Ensembl

post-embryonic development

Inferred from electronic annotation. Source: Ensembl

regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

steroid catabolic process

Inferred from mutant phenotype PubMed 18356043. Source: BHF-UCL

toxin biosynthetic process

Inferred from direct assay PubMed 11511187. Source: BHF-UCL

xenobiotic metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentendoplasmic reticulum membrane

Traceable author statement. Source: Reactome

intracellular membrane-bounded organelle

Inferred from direct assay PubMed 2813353. Source: UniProtKB

   Molecular_functionaromatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

caffeine oxidase activity

Inferred from direct assay PubMed 18619574. Source: BHF-UCL

demethylase activity

Inferred from direct assay PubMed 2813353. Source: UniProtKB

electron carrier activity

Traceable author statement PubMed 2813353. Source: UniProtKB

enzyme binding

Inferred from physical interaction PubMed 15680923. Source: BHF-UCL

heme binding

Inferred from direct assay Ref.12. Source: UniProtKB

iron ion binding

Inferred from electronic annotation. Source: InterPro

monooxygenase activity

Inferred from direct assay PubMed 15327587PubMed 19651758. Source: BHF-UCL

oxidoreductase activity

Inferred from direct assay PubMed 16401082PubMed 19219744. Source: BHF-UCL

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

Inferred from mutant phenotype PubMed 2813353. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P05177-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P05177-2)

The sequence of this isoform differs from the canonical sequence as follows:
     510-510: R → RL

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 515514Cytochrome P450 1A2
PRO_0000051651

Sites

Metal binding4581Iron (heme axial ligand)
Binding site2261Substrate Probable

Natural variations

Alternative sequence5101R → RL in isoform 2.
VSP_017123
Natural variant181S → C. Ref.16 Ref.18
Corresponds to variant rs17861152 [ dbSNP | Ensembl ].
VAR_023196
Natural variant211F → L in allele CYP1A2*2. Ref.13
Corresponds to variant rs56160784 [ dbSNP | Ensembl ].
VAR_008349
Natural variant421P → R in allele CYP1A2*15. Ref.17
VAR_025182
Natural variant731G → R. Ref.7
Corresponds to variant rs45565238 [ dbSNP | Ensembl ].
VAR_025183
Natural variant831T → M in allele CYP1A2*9. Ref.15
VAR_020848
Natural variant1041D → N. Ref.7
Corresponds to variant rs34067076 [ dbSNP | Ensembl ].
VAR_025184
Natural variant1111L → F. Ref.7
Corresponds to variant rs45442197 [ dbSNP | Ensembl ].
VAR_025185
Natural variant1681E → Q in allele CYP1A2*10. Ref.15
VAR_020849
Natural variant1861F → L in allele CYP1A2*11; drastic reduction in O-deethylation of phenacetin and 7-ethoxyresorufin; has a Vmax of approximately 5% of that of the wild-type and 5-fold lower Km value. Ref.15
VAR_020850
Natural variant2051F → V. Ref.7
Corresponds to variant rs45540640 [ dbSNP | Ensembl ].
VAR_025186
Natural variant2121S → C in allele CYP1A2*12. Ref.15
VAR_020851
Natural variant2811R → W. Ref.7
Corresponds to variant rs45468096 [ dbSNP | Ensembl ].
VAR_025187
Natural variant2981S → R. Ref.16
Corresponds to variant rs17861157 [ dbSNP | Ensembl ].
VAR_024709
Natural variant2991G → S in allele CYP1A2*13. Ref.15
Corresponds to variant rs35796837 [ dbSNP | Ensembl ].
VAR_020852
Natural variant3141I → V. Ref.5 Ref.16
Corresponds to variant rs28399418 [ dbSNP | Ensembl ].
VAR_024710
Natural variant3481D → N in allele CYP1A2*3; increases N-hydroxylation activity of heterocyclic amines; reduces phenacetin O-deethylation activity. Ref.11 Ref.14
Corresponds to variant rs56276455 [ dbSNP | Ensembl ].
VAR_020793
Natural variant3771R → Q in allele CYP1A2*16. Ref.17
VAR_025188
Natural variant3861I → F in allele CYP1A2*4; increases catalytic efficiency of N-hydroxylation towards some heterocyclic amines and reduces towards others; reduces catalytic efficiency of phenacetin O-deethylation due to a high decrease in the affinity for phenacetin. Ref.11 Ref.14
VAR_020794
Natural variant4061C → Y in allele CYP1A2*5; increases N-hydroxylation activity of heterocyclic amines; reduces catalytic efficiency of phenacetin O-deethylation. Ref.11 Ref.14
Corresponds to variant rs55889066 [ dbSNP | Ensembl ].
VAR_020795
Natural variant4311R → W in allele CYP1A2*6; not detected when expressed in heterologous system as it may be critical for maintenance of protein tertiary structure. Ref.11 Ref.14 Ref.16
Corresponds to variant rs28399424 [ dbSNP | Ensembl ].
VAR_020796
Natural variant4381T → I in allele CYP1A2*14. Ref.7 Ref.15
Corresponds to variant rs45486893 [ dbSNP | Ensembl ].
VAR_020853
Natural variant4561R → H in allele CYP1A2*8. Ref.17
VAR_025189
Natural variant4571R → W.
Corresponds to variant rs34151816 [ dbSNP | Ensembl ].
VAR_055563

Experimental info

Sequence conflict791R → S in AAA35738. Ref.2
Sequence conflict811G → D in AAH67427. Ref.8
Sequence conflict1701K → M in AAF13599. Ref.5
Sequence conflict3111V → L in AAA52154. Ref.10
Sequence conflict450 – 4512LF → MLV in AAA52154. Ref.10
Sequence conflict4921T → I in AAF13599. Ref.5
Sequence conflict5111R → LP in AAA35738. Ref.2

Secondary structure

........................................................................... 515
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 23AEFEEBDF6806AB

FASTA51558,294
        10         20         30         40         50         60 
MALSQSVPFS ATELLLASAI FCLVFWVLKG LRPRVPKGLK SPPEPWGWPL LGHVLTLGKN 

        70         80         90        100        110        120 
PHLALSRMSQ RYGDVLQIRI GSTPVLVLSR LDTIRQALVR QGDDFKGRPD LYTSTLITDG 

       130        140        150        160        170        180 
QSLTFSTDSG PVWAARRRLA QNALNTFSIA SDPASSSSCY LEEHVSKEAK ALISRLQELM 

       190        200        210        220        230        240 
AGPGHFDPYN QVVVSVANVI GAMCFGQHFP ESSDEMLSLV KNTHEFVETA SSGNPLDFFP 

       250        260        270        280        290        300 
ILRYLPNPAL QRFKAFNQRF LWFLQKTVQE HYQDFDKNSV RDITGALFKH SKKGPRASGN 

       310        320        330        340        350        360 
LIPQEKIVNL VNDIFGAGFD TVTTAISWSL MYLVTKPEIQ RKIQKELDTV IGRERRPRLS 

       370        380        390        400        410        420 
DRPQLPYLEA FILETFRHSS FLPFTIPHST TRDTTLNGFY IPKKCCVFVN QWQVNHDPEL 

       430        440        450        460        470        480 
WEDPSEFRPE RFLTADGTAI NKPLSEKMML FGMGKRRCIG EVLAKWEIFL FLAILLQQLE 

       490        500        510 
FSVPPGVKVD LTPIYGLTMK HARCEHVQAR RFSIN 

« Hide

Isoform 2 [UniParc].

Checksum: 8557AB02860C4806
Show »

FASTA51658,407

References

« Hide 'large scale' references
[1]"Human P3(450): cDNA and complete amino acid sequence."
Jaiswal A.K., Nebert D.W., Gonzalez F.J.
Nucleic Acids Res. 14:6773-6774(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Human cytochrome P-450 4 mRNA and gene: part of a multigene family that contains Alu sequences in its mRNA."
Quattrochi L.C., Pendurthi U.R., Okino S.T., Potenza C., Tukey R.H.
Proc. Natl. Acad. Sci. U.S.A. 83:6731-6735(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[3]"Human CYP1A2: sequence, gene structure, comparison with the mouse and rat orthologous gene, and differences in liver 1A2 mRNA expression."
Ikeya K., Jaiswal A.K., Owens R.A., Jones J.E., Nebert D.W., Kimura S.
Mol. Endocrinol. 3:1399-1408(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Human P(3)450: cDNA and complete protein sequence, repetitive Alu sequences in the 3' nontranslated region, and localization of gene to chromosome 15."
Jaiswal A.K., Nebert D.W., McBride O.W., Gonzalez F.J.
J. Exp. Pathol. 3:1-17(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[5]"Sequence of a new human cytochrome P450-1A2 cDNA."
Zhuge J., Qian Y., Xie H., Yu Y.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT VAL-314.
Tissue: Liver.
[6]"Organization of the CYP1A cluster on human chromosome 15: implications for gene regulation."
Corchero J., Pimprale S., Kimura S., Gonzalez F.J.
Pharmacogenetics 11:1-6(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]NIEHS SNPs program
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-73; ASN-104; PHE-111; VAL-205; TRP-281 AND ILE-438.
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[9]"Identification of a human liver cytochrome P-450 homologous to the major isosafrole-inducible cytochrome P-450 in the rat."
Wrighton S.A., Campanile C., Thomas P.E., Maines S.L., Watkins P.B., Parker G., Mendez-Picon G., Haniu M., Shively J.E., Levin W., Guzelian P.S.
Mol. Pharmacol. 29:405-410(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-19.
[10]"Cloning and isolation of human cytochrome P-450 cDNAs homologous to dioxin-inducible rabbit mRNAs encoding P-450 4 and P-450 6."
Quattrochi L.C., Okino S.T., Pendurthi U.R., Tukey R.H.
DNA 4:395-400(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 295-485.
Tissue: Liver.
[11]"Functional characterization of four allelic variants of human cytochrome P450 1A2."
Zhou H., Josephy P.D., Kim D., Guengerich F.P.
Arch. Biochem. Biophys. 422:23-30(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION OF VARIANTS ASN-348; PHE-386; TYR-406 AND TRP-431.
[12]"Adaptations for the oxidation of polycyclic aromatic hydrocarbons exhibited by the structure of human P450 1A2."
Sansen S., Yano J.K., Reynald R.L., Schoch G.A., Griffin K.J., Stout C.D., Johnson E.F.
J. Biol. Chem. 282:14348-14355(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 27-515 IN COMPLEX WITH THE INHIBITOR ALPHA-NAPHTHOFLAVONE AND HEME.
[13]"Detection of a novel cytochrome P-450 1A2 polymorphism (F21L) in Chinese."
Huang J.D., Guo W.C., Lai M.D., Guo Y.L., Lambert G.H.
Drug Metab. Dispos. 27:98-101(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LEU-21.
[14]"Five novel natural allelic variants-951A->C, 1042G->A (D348N), 1156A->T (I386F), 1217G->A (C406Y) and 1291C->T (C431Y)-of the human CYP1A2 gene in a French Caucasian population."
Chevalier D., Cauffiez C., Allorge D., Lo-Guidice J.-M., Lhermitte M., Lafitte J.-J., Broly F.
Hum. Mutat. 17:355-356(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ASN-348; PHE-386; TYR-406 AND TRP-431.
[15]"Six novel nonsynonymous CYP1A2 gene polymorphisms: catalytic activities of the naturally occurring variant enzymes."
Murayama N., Soyama A., Saito Y., Nakajima Y., Komamura K., Ueno K., Kamakura S., Kitakaze M., Kimura H., Goto Y., Saitoh O., Katoh M., Ohnuma T., Kawai M., Sugai K., Ohtsuki T., Suzuki C., Minami N., Ozawa S., Sawada J.
J. Pharmacol. Exp. Ther. 308:300-306(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MET-83; GLN-168; LEU-186; CYS-212; SER-299 AND ILE-438.
[16]"Genetic variation in eleven phase I drug metabolism genes in an ethnically diverse population."
Solus J.F., Arietta B.J., Harris J.R., Sexton D.P., Steward J.Q., McMunn C., Ihrie P., Mehall J.M., Edwards T.L., Dawson E.P.
Pharmacogenomics 5:895-931(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CYS-18; ARG-298; VAL-314 AND TRP-431.
[17]"Single nucleotide polymorphisms and haplotypes of CYP1A2 in a Japanese population."
Soyama A., Saito Y., Hanioka N., Maekawa K., Komamura K., Kamakura S., Kitakaze M., Tomoike H., Ueno K., Goto Y., Kimura H., Katoh M., Sugai K., Saitoh O., Kawai M., Ohnuma T., Ohtsuki T., Suzuki C. expand/collapse author list , Minami N., Kamatani N., Ozawa S., Sawada J.
Drug Metab. Pharmacokinet. 20:24-33(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ARG-42; GLN-377 AND HIS-456.
[18]"Toward the evaluation of function in genetic variability: characterizing human SNP frequencies and establishing BAC-transgenic mice carrying the human CYP1A1_CYP1A2 locus."
Jiang Z., Dalton T.P., Jin L., Wang B., Tsuneoka Y., Shertzer H.G., Deka R., Nebert D.W.
Hum. Mutat. 25:196-206(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CYS-18.
[19]"Coffee, CYP1A2 genotype, and risk of myocardial infarction."
Cornelis M.C., El-Sohemy A., Kabagambe E.K., Campos H.
JAMA 295:1135-1141(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: EFFECT OF CAFFEINE METABOLISM ON RISKS OF MYOCARDIAL INFARCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z00036 mRNA. Translation: CAA77335.1.
L00389 expand/collapse EMBL AC list , L00384, L00385, L00386, L00388, L00387 Genomic DNA. Translation: AAA35738.1.
M31667 expand/collapse EMBL AC list , M31664, M31665, M31666 Genomic DNA. Translation: AAA52163.1.
M12078 mRNA. Translation: AAA52154.1.
AF182274 mRNA. Translation: AAF13599.1.
AF253322 Genomic DNA. Translation: AAK25728.1.
DQ022432 Genomic DNA. Translation: AAY26399.1.
BC067424 mRNA. Translation: AAH67424.1.
BC067425 mRNA. Translation: AAH67425.1.
BC067426 mRNA. Translation: AAH67426.1.
BC067427 mRNA. Translation: AAH67427.1.
BC067428 mRNA. Translation: AAH67428.1.
M55053 mRNA. Translation: AAA52146.1.
PIRO4HU4. S16718.
RefSeqNP_000752.2. NM_000761.4.
UniGeneHs.1361.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HI4X-ray1.95A25-515[»]
ProteinModelPortalP05177.
SMRP05177. Positions 34-513.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107924. 2 interactions.
STRING9606.ENSP00000342007.

Chemistry

BindingDBP05177.
ChEMBLCHEMBL3356.
DrugBankDB01418. Acenocoumarol.
DB00316. Acetaminophen.
DB00787. Aciclovir.
DB00969. Alosetron.
DB01424. Aminophenazone.
DB00321. Amitriptyline.
DB00261. Anagrelide.
DB00972. Azelastine.
DB00188. Bortezomib.
DB00201. Caffeine.
DB00262. Carmustine.
DB00475. Chlordiazepoxide.
DB00477. Chlorpromazine.
DB00356. Chlorzoxazone.
DB00501. Cimetidine.
DB01012. Cinacalcet.
DB00537. Ciprofloxacin.
DB01242. Clomipramine.
DB00257. Clotrimazole.
DB00363. Clozapine.
DB00286. Conjugated Estrogens.
DB00924. Cyclobenzaprine.
DB00851. Dacarbazine.
DB00967. Desloratadine.
DB00829. Diazepam.
DB00527. Dibucaine.
DB00586. Diclofenac.
DB00476. Duloxetine.
DB00467. Enoxacin.
DB00736. Esomeprazole.
DB00783. Estradiol.
DB00655. Estrone.
DB00544. Fluorouracil.
DB00499. Flutamide.
DB00176. Fluvoxamine.
DB00998. Frovatriptan.
DB00365. Grepafloxacin.
DB00502. Haloperidol.
DB01094. Hesperetin.
DB00458. Imipramine.
DB01026. Ketoconazole.
DB01097. Leflunomide.
DB01002. Levobupivacaine.
DB01137. Levofloxacin.
DB00281. Lidocaine.
DB00978. Lomefloxacin.
DB01065. Melatonin.
DB00532. Mephenytoin.
DB00379. Mexiletine.
DB00370. Mirtazapine.
DB01059. Norfloxacin.
DB00540. Nortriptyline.
DB01165. Ofloxacin.
DB00334. Olanzapine.
DB00904. Ondansetron.
DB00377. Palonosetron.
DB00213. Pantoprazole.
DB00487. Pefloxacin.
DB01100. Pimozide.
DB01182. Propafenone.
DB00571. Propranolol.
DB00908. Quinidine.
DB00980. Ramelteon.
DB00863. Ranitidine.
DB01367. Rasagiline.
DB01045. Rifampin.
DB00740. Riluzole.
DB00533. Rofecoxib.
DB00268. Ropinirole.
DB00296. Ropivacaine.
DB00382. Tacrine.
DB00976. Telithromycin.
DB00342. Terfenadine.
DB00277. Theophylline.
DB00730. Thiabendazole.
DB00697. Tizanidine.
DB01124. Tolbutamide.
DB00661. Verapamil.
DB00682. Warfarin.
DB00744. Zileuton.
DB00315. Zolmitriptan.

PTM databases

PhosphoSiteP05177.

Polymorphism databases

DMDM117144.

Proteomic databases

PaxDbP05177.
PRIDEP05177.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000343932; ENSP00000342007; ENSG00000140505. [P05177-2]
GeneID1544.
KEGGhsa:1544.
UCSCuc002ayr.1. human. [P05177-2]

Organism-specific databases

CTD1544.
GeneCardsGC15P075041.
HGNCHGNC:2596. CYP1A2.
HPACAB016531.
MIM108330. gene.
124060. gene+phenotype.
neXtProtNX_P05177.
Orphanet284121. Susceptibility to adverse reaction due to clozapine.
PharmGKBPA27093.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2124.
HOVERGENHBG106944.
InParanoidP05177.
KOK07409.
OMAHARCEHV.
OrthoDBEOG7RBZ85.
PhylomeDBP05177.
TreeFamTF105095.

Enzyme and pathway databases

BioCycMetaCyc:HS06728-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP05177.

Gene expression databases

BgeeP05177.
CleanExHS_CYP1A2.
GenevestigatorP05177.

Family and domain databases

Gene3D1.10.630.10. 1 hit.
InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
IPR008066. Cyt_P450_E_grp-I_CYP1.
[Graphical view]
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00463. EP450I.
PR01683. EP450ICYP1A.
PR00385. P450.
SUPFAMSSF48264. SSF48264. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP05177.
GeneWikiCYP1A2.
GenomeRNAi1544.
NextBio6391.
PROP05177.
SOURCESearch...

Entry information

Entry nameCP1A2_HUMAN
AccessionPrimary (citable) accession number: P05177
Secondary accession number(s): Q16754 expand/collapse secondary AC list , Q6NWU5, Q9BXX7, Q9UK49
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 152 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM