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P04798 (CP1A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 165. 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 1A1

EC=1.14.14.1
Alternative name(s):
CYPIA1
Cytochrome P450 form 6
Cytochrome P450-C
Cytochrome P450-P1
Gene names
Name:CYP1A1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length512 AA.
Sequence statusComplete.
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.

Catalytic activity

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

Cofactor

Heme group. Ref.11

Subcellular location

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

Tissue specificity

Lung, lymphocytes and placenta.

Induction

By 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD).

Sequence similarities

Belongs to the cytochrome P450 family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandHeme
Iron
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process9-cis-retinoic acid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

aging

Inferred from electronic annotation. Source: Ensembl

amine metabolic process

Inferred from electronic annotation. Source: Ensembl

arachidonic acid metabolic process

Traceable author statement. Source: Reactome

camera-type eye development

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Inferred from electronic annotation. Source: Ensembl

cellular lipid metabolic process

Traceable author statement. Source: Reactome

coumarin metabolic process

Inferred from electronic annotation. Source: Ensembl

dibenzo-p-dioxin catabolic process

Inferred from electronic annotation. Source: Ensembl

digestive tract development

Inferred from electronic annotation. Source: Ensembl

drug metabolic process

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

embryo development ending in birth or egg hatching

Inferred from electronic annotation. Source: Ensembl

epoxygenase P450 pathway

Traceable author statement. Source: Reactome

flavonoid metabolic process

Inferred from electronic annotation. Source: Ensembl

hepatocyte differentiation

Inferred from electronic annotation. Source: Ensembl

hydrogen peroxide biosynthetic process

Inferred from electronic annotation. Source: Ensembl

insecticide metabolic process

Inferred from electronic annotation. Source: Ensembl

maternal process involved in parturition

Inferred from electronic annotation. Source: Ensembl

omega-hydroxylase P450 pathway

Traceable author statement. Source: Reactome

oxidation-reduction process

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

porphyrin-containing compound metabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of G1/S transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

response to antibiotic

Inferred from electronic annotation. Source: Ensembl

response to arsenic-containing substance

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to food

Inferred from electronic annotation. Source: Ensembl

response to herbicide

Inferred from electronic annotation. Source: Ensembl

response to hyperoxia

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to iron(III) ion

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to nematode

Inferred from electronic annotation. Source: Ensembl

response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

response to virus

Inferred from electronic annotation. Source: Ensembl

response to vitamin A

Inferred from electronic annotation. Source: Ensembl

response to wounding

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

vitamin D metabolic process

Inferred by curator PubMed 15546903. Source: BHF-UCL

xenobiotic metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentendoplasmic reticulum membrane

Traceable author statement. Source: Reactome

mitochondrion

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionaromatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

demethylase activity

Inferred from electronic annotation. Source: Ensembl

flavonoid 3'-monooxygenase activity

Inferred from electronic annotation. Source: Ensembl

heme binding

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: InterPro

oxidoreductase activity

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

oxidoreductase activity, acting on diphenols and related substances as donors

Inferred from electronic annotation. Source: Ensembl

oxygen binding

Traceable author statement PubMed 1691986. Source: ProtInc

steroid hydroxylase activity

Inferred from electronic annotation. Source: Ensembl

vitamin D 24-hydroxylase activity

Inferred from direct assay PubMed 15546903. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P04798-1)

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: P04798-2)

The sequence of this isoform differs from the canonical sequence as follows:
     189-189: Y → T
     190-512: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P04798-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-261: Missing.
     419-512: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 512512Cytochrome P450 1A1
PRO_0000051627

Sites

Metal binding4571Iron (heme axial ligand)
Binding site2241Substrate

Natural variations

Alternative sequence1 – 261261Missing in isoform 3.
VSP_053363
Alternative sequence1891Y → T in isoform 2.
VSP_053364
Alternative sequence190 – 512323Missing in isoform 2.
VSP_053365
Alternative sequence419 – 51294Missing in isoform 3.
VSP_053366
Natural variant451G → D. Ref.6 Ref.17 Ref.18
Corresponds to variant rs4646422 [ dbSNP | Ensembl ].
VAR_023194
Natural variant661M → V.
Corresponds to variant rs35035798 [ dbSNP | Ensembl ].
VAR_033817
Natural variant781I → T. Ref.17 Ref.18
Corresponds to variant rs17861094 [ dbSNP | Ensembl ].
VAR_023195
Natural variant931R → W. Ref.17
Corresponds to variant rs2229150 [ dbSNP | Ensembl ].
VAR_024706
Natural variant1731T → R. Ref.17
Corresponds to variant rs28399427 [ dbSNP | Ensembl ].
VAR_024707
Natural variant2791R → W. Ref.14
Corresponds to variant rs34260157 [ dbSNP | Ensembl ].
VAR_009280
Natural variant2861I → T.
Corresponds to variant rs4987133 [ dbSNP | Ensembl ].
VAR_020122
Natural variant3311M → I in allele CYP1A1*6. Ref.15
Corresponds to variant rs56313657 [ dbSNP | Ensembl ].
VAR_016937
Natural variant4481I → N in allele CYP1A1*8. Ref.16
VAR_016938
Natural variant4611T → N in allele CYP1A1*4. Ref.13 Ref.17 Ref.18
Corresponds to variant rs1799814 [ dbSNP | Ensembl ].
VAR_008342
Natural variant4621I → V in allele CYP1A1*2B and allele CYP1A1*2C. Ref.12 Ref.18
Corresponds to variant rs1048943 [ dbSNP | Ensembl ].
VAR_001243
Natural variant4641R → C in allele CYP1A1*9. Ref.16
VAR_016939
Natural variant4641R → S in allele CYP1A1*5. Ref.15
Corresponds to variant rs41279188 [ dbSNP | Ensembl ].
VAR_016940
Natural variant4701F → V.
Corresponds to variant rs36121583 [ dbSNP | Ensembl ].
VAR_033818
Natural variant4771R → W in allele CYP1A1*10. Ref.16 Ref.19
Corresponds to variant rs56240201 [ dbSNP | Ensembl ].
VAR_016941
Natural variant4821V → M. Ref.17
Corresponds to variant rs28399429 [ dbSNP | Ensembl ].
VAR_024708
Natural variant4921P → R in allele CYP1A1*11. Ref.16 Ref.17
Corresponds to variant rs28399430 [ dbSNP | Ensembl ].
VAR_016942

Experimental info

Sequence conflict261I → M in AAA52139. Ref.2
Sequence conflict2351D → E in AAA52139. Ref.2
Sequence conflict3811F → L in CAA26458. Ref.1

Secondary structure

.............................................................................. 512
Helix Strand Turn

Details...

Sequences

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

Last modified April 1, 1988. Version 1.
Checksum: 3C62366044148EFD

FASTA51258,165
        10         20         30         40         50         60 
MLFPISMSAT EFLLASVIFC LVFWVIRASR PQVPKGLKNP PGPWGWPLIG HMLTLGKNPH 

        70         80         90        100        110        120 
LALSRMSQQY GDVLQIRIGS TPVVVLSGLD TIRQALVRQG DDFKGRPDLY TFTLISNGQS 

       130        140        150        160        170        180 
MSFSPDSGPV WAARRRLAQN GLKSFSIASD PASSTSCYLE EHVSKEAEVL ISTLQELMAG 

       190        200        210        220        230        240 
PGHFNPYRYV VVSVTNVICA ICFGRRYDHN HQELLSLVNL NNNFGEVVGS GNPADFIPIL 

       250        260        270        280        290        300 
RYLPNPSLNA FKDLNEKFYS FMQKMVKEHY KTFEKGHIRD ITDSLIEHCQ EKQLDENANV 

       310        320        330        340        350        360 
QLSDEKIINI VLDLFGAGFD TVTTAISWSL MYLVMNPRVQ RKIQEELDTV IGRSRRPRLS 

       370        380        390        400        410        420 
DRSHLPYMEA FILETFRHSS FVPFTIPHST TRDTSLKGFY IPKGRCVFVN QWQINHDQKL 

       430        440        450        460        470        480 
WVNPSEFLPE RFLTPDGAID KVLSEKVIIF GMGKRKCIGE TIARWEVFLF LAILLQRVEF 

       490        500        510 
SVPLGVKVDM TPIYGLTMKH ACCEHFQMQL RS 

« Hide

Isoform 2 [UniParc].

Checksum: 6F774C4E9FC85427
Show »

FASTA18920,788
Isoform 3 [UniParc].

Checksum: D0AE3E0EEA55B854
Show »

FASTA15718,441

References

« Hide 'large scale' references
[1]"Human P1-450 gene sequence and correlation of mRNA with genetic differences in benzo[a]pyrene metabolism."
Jaiswal A.K., Gonzales F.J., Nebert D.W.
Nucleic Acids Res. 13:4503-4520(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Human dioxin-inducible cytochrome P1-450: complementary DNA and amino acid sequence."
Jaiswal A.K., Gonzalez F.J., Nebert D.W.
Science 228:80-83(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Structure and drug inducibility of the human cytochrome P-450c gene."
Kawajiri K., Watanabe J., Gotoh O., Tagashira Y., Sogawa K., Fujii-Kuriyama Y.
Eur. J. Biochem. 159:219-225(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Placenta.
[4]"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].
[5]"Cloning and sequencing of new alternative splicing variants of human CYP1A1 gene."
Graebsch C., Bauer M.
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
Tissue: Blood.
[6]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ASP-45.
[7]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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 1).
Tissue: Cervix.
[9]"Identification of cytochrome P450 1A1 in human brain."
Yun C.H., Park H.J., Kim S.J., Kim H.K.
Biochem. Biophys. Res. Commun. 243:808-810(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 282-425 (ISOFORM 1).
Tissue: Brain.
[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 295-484 (ISOFORM 1).
[11]"Human cytochrome P450 1A1 structure and utility in understanding drug and xenobiotic metabolism."
Walsh A.A., Szklarz G.D., Scott E.E.
J. Biol. Chem. 288:12932-12943(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 35-512 IN COMPLEX WITH HEME AND INHIBITOR ALPHA-NAPHTOFLAVONE, COFACTOR.
[12]"Genetic linkage of lung cancer-associated MspI polymorphisms with amino acid replacement in the heme binding region of the human cytochrome P450IA1 gene."
Hayashi S., Watanabe J., Nakachi K., Kawajiri K.
J. Biochem. 110:407-411(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VAL-462.
[13]"A C4887A polymorphism in exon 7 of human CYP1A1: population frequency, mutation linkages, and impact on lung cancer susceptibility."
Cascorbi I., Brockmoller J., Roots I.
Cancer Res. 56:4965-4969(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ASN-461.
[14]"Variation in induced CYP1A1 levels: relationship to CYP1A1, Ah receptor and GSTM1 polymorphisms."
Smart J., Daly A.K.
Pharmacogenetics 10:11-24(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TRP-279.
[15]"Detection of known and two novel (M331I and R464S) missense mutations in the human CYP1A1 gene in a French Caucasian population."
Chevalier D., Allorge D., Lo-Guidice J.-M., Cauffiez C., Lhermitte M., Lafitte J.-J., Broly F.
Hum. Mutat. 17:355-355(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ILE-331 AND SER-464.
[16]"Novel nonsynonymous polymorphisms of the CYP1A1 Gene in Japanese."
Saito M., Egashira M., Kiyotani K., Fujieda M., Yamazaki H., Kiyohara C., Kunitoh H., Kamataki T.
Drug Metab. Pharmacokinet. 18:218-222(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ASN-448; CYS-464; TRP-477 AND ARG-492.
[17]"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 ASP-45; THR-78; TRP-93; ARG-173; ASN-461; MET-482 AND ARG-492.
[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: VARIANTS ASP-45; THR-78; ASN-461 AND VAL-462.
[19]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] TRP-477.
+Additional computationally mapped references.

Web resources

Cytochrome P450 Allele Nomenclature Committee

CYP1A1 alleles

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

CYP1A1 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02612 Genomic DNA. Translation: CAA26458.1.
K03191 mRNA. Translation: AAA52139.1.
X04300 Genomic DNA. Translation: CAA27843.1.
AF253322 Genomic DNA. Translation: AAK25727.1.
AM233518 mRNA. Translation: CAJ80721.1.
AM233519 mRNA. Translation: CAJ80722.1.
AM233520 mRNA. Translation: CAJ80723.1.
AK223113 mRNA. Translation: BAD96833.1.
AC091230 Genomic DNA. No translation available.
BC023019 mRNA. Translation: AAH23019.1.
M12079 mRNA. Translation: AAA52152.1.
AF040259 mRNA. Translation: AAD10199.1.
PIRO4HU6. A24797.
RefSeqNP_000490.1. NM_000499.3.
XP_005254242.1. XM_005254185.1.
UniGeneHs.72912.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4I8VX-ray2.60A/B/C/D35-512[»]
ProteinModelPortalP04798.
SMRP04798. Positions 36-512.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000369050.

Chemistry

BindingDBP04798.
ChEMBLCHEMBL2231.
DrugBankDB01169. Arsenic trioxide.
DB00865. Benzphetamine.
DB00290. Bleomycin.
DB00356. Chlorzoxazone.
DB00851. Dacarbazine.
DB00970. Dactinomycin.
DB00736. Esomeprazole.
DB00655. Estrone.
DB01095. Fluvastatin.
DB00176. Fluvoxamine.
DB01404. Ginseng.
DB00889. Granisetron.
DB01026. Ketoconazole.
DB00170. Menadione.
DB00466. Picrotoxin.
DB01087. Primaquine.
DB00908. Quinidine.
DB00468. Quinine.
DB00730. Thiabendazole.

PTM databases

PhosphoSiteP04798.

Polymorphism databases

DMDM117139.

Proteomic databases

PaxDbP04798.
PRIDEP04798.

Protocols and materials databases

DNASU1543.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379727; ENSP00000369050; ENSG00000140465. [P04798-1]
ENST00000395048; ENSP00000378488; ENSG00000140465. [P04798-1]
ENST00000562201; ENSP00000455340; ENSG00000140465. [P04798-2]
ENST00000564596; ENSP00000457668; ENSG00000140465. [P04798-3]
ENST00000567032; ENSP00000456585; ENSG00000140465. [P04798-1]
ENST00000569630; ENSP00000455051; ENSG00000140465. [P04798-2]
GeneID1543.
KEGGhsa:1543.
UCSCuc002ayp.4. human. [P04798-1]

Organism-specific databases

CTD1543.
GeneCardsGC15M075011.
HGNCHGNC:2595. CYP1A1.
HPACAB018654.
MIM108330. gene.
neXtProtNX_P04798.
PharmGKBPA27092.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2124.
HOGENOMHOG000036991.
HOVERGENHBG106944.
InParanoidP04798.
KOK07408.
OMAHLPYMEA.
OrthoDBEOG7RBZ85.
PhylomeDBP04798.
TreeFamTF105095.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
SABIO-RKP04798.

Gene expression databases

ArrayExpressP04798.
BgeeP04798.
CleanExHS_CYP1A1.
GenevestigatorP04798.

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

ChiTaRSCYP1A1. human.
GeneWikiCytochrome_P450,_family_1,_member_A1.
GenomeRNAi1543.
NextBio35461723.
PROP04798.
SOURCESearch...

Entry information

Entry nameCP1A1_HUMAN
AccessionPrimary (citable) accession number: P04798
Secondary accession number(s): A4F3V9, A4F3W0, Q53G18
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: April 1, 1988
Last modified: April 16, 2014
This is version 165 of the entry and version 1 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