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UniProtKB - P04798 (CP1A1_HUMAN)

Entry version 220 (17 Jun 2020)
Sequence version 1 (01 Apr 1988)
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Protein

Cytochrome P450 1A1

Gene

CYP1A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins (PubMed:11555828, PubMed:14559847, PubMed:12865317, PubMed:15805301, PubMed:15041462, PubMed:18577768, PubMed:19965576, PubMed:20972997, PubMed:10681376). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase) (PubMed:11555828, PubMed:14559847, PubMed:12865317, PubMed:15805301, PubMed:15041462, PubMed:18577768, PubMed:19965576, PubMed:20972997, PubMed:10681376). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2, as well as D-ring hydroxylated E1 and E2 at the C15-alpha and C16-alpha positions (PubMed:11555828, PubMed:14559847, PubMed:12865317, PubMed:15805301). Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation (PubMed:15041462, PubMed:18577768). Catalyzes the epoxidation of double bonds of certain PUFA (PubMed:15041462, PubMed:19965576, PubMed:20972997). Converts arachidonic acid toward epoxyeicosatrienoic acid (EET) regioisomers, 8,9-, 11,12-, and 14,15-EET, that function as lipid mediators in the vascular system (PubMed:20972997). Displays an absolute stereoselectivity in the epoxidation of eicosapentaenoic acid (EPA) producing the 17(R),18(S) enantiomer (PubMed:15041462). May play an important role in all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid (PubMed:10681376). May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent) (PubMed:21068195).10 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

heme1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=8 µM for all-trans retinol1 Publication
  2. KM=9.5 µM for 17beta-estradiol (2-hydroxylation)1 Publication
  3. KM=11.8 µM for 17beta-estradiol (4-hydroxylation)1 Publication
  4. KM=79 µM for 17beta-estradiol (6alpha-hydroxylation)1 Publication
  5. KM=19.6 µM for 17beta-estradiol (15alpha-hydroxylation)1 Publication
  6. KM=12.2 µM for estrone (2-hydroxylation)1 Publication
  7. KM=22.6 µM for estrone (4-hydroxylation)1 Publication
  8. KM=86 µM for estrone (6alpha-hydroxylation)1 Publication
  9. KM=85 µM for estrone (15alpha-hydroxylation)1 Publication
  1. Vmax=507 pmol/min/nmol enzyme toward all-trans retinol1 Publication
  2. Vmax=0.6 pmol/min/pmol enzyme toward 17beta-estradiol (2-hydroxylation)1 Publication
  3. Vmax=0.02 pmol/min/pmol enzyme toward 17beta-estradiol (4-hydroxylation)1 Publication
  4. Vmax=3.6 pmol/min/pmol enzyme toward 17beta-estradiol (6alpha-hydroxylation)1 Publication
  5. Vmax=0.9 pmol/min/pmol enzyme toward 17beta-estradiol (15alpha-hydroxylation)1 Publication
  6. Vmax=0.4 pmol/min/pmol enzyme toward estrone (2-hydroxylation)1 Publication
  7. Vmax=0.1 pmol/min/pmol enzyme toward estrone (4-hydroxylation)1 Publication
  8. Vmax=0.2 pmol/min/pmol enzyme toward estrone (6alpha-hydroxylation)1 Publication
  9. Vmax=1.2 pmol/min/pmol enzyme toward estrone (15alpha-hydroxylation)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: Steroid hormone biosynthesis

This protein is involved in Steroid hormone biosynthesis.4 Publications
View all proteins of this organism that are known to be involved in Steroid hormone biosynthesis.

Pathwayi: fatty acid metabolism

This protein is involved in the pathway fatty acid metabolism, which is part of Lipid metabolism.5 Publications
View all proteins of this organism that are known to be involved in the pathway fatty acid metabolism and in Lipid metabolism.

Pathwayi: retinol metabolism

This protein is involved in the pathway retinol metabolism, which is part of Cofactor metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway retinol metabolism and in Cofactor metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei224Substrate1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi457Iron (heme axial ligand)1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionLyase, Monooxygenase, Oxidoreductase
Biological processFatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis
LigandHeme, Iron, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-1989781 PPARA activates gene expression
R-HSA-211981 Xenobiotics
R-HSA-2142670 Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET)
R-HSA-2142816 Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE)
R-HSA-9018681 Biosynthesis of protectins

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P04798

SIGNOR Signaling Network Open Resource

More...SIGNORi		P04798

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00199
UPA00912

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...SwissLipidsi		SLP:000001329

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Cytochrome P450 1A11 Publication (EC:1.14.14.14 Publications)
Short name:
CYPIA11 Publication
Alternative name(s):
Cytochrome P450 form 6
Cytochrome P450-C
Cytochrome P450-P1
Hydroperoxy icosatetraenoate dehydratase1 Publication (EC:4.2.1.1521 Publication)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CYP1A11 PublicationImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 15

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000140465.13

Human Gene Nomenclature Database

More...HGNCi		HGNC:2595 CYP1A1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		108330 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P04798

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Microsome, Mitochondrion, Mitochondrion inner membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Organism-specific databases

DisGeNET

More...DisGeNETi		1543

Open Targets

More...OpenTargetsi		ENSG00000140465

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA27092

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P04798 Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2231

Drug and drug target database

More...DrugBanki		DB08496 (R)-warfarin
DB02342 2-Methoxyestradiol
DB00518 Albendazole
DB01118 Amiodarone
DB00381 Amlodipine
DB00613 Amodiaquine
DB00972 Azelastine
DB04957 Azimilide
DB04975 Banoxantrone
DB06770 Benzyl alcohol
DB01393 Bezafibrate
DB00201 Caffeine
DB09061 Cannabidiol
DB01136 Carvedilol
DB00608 Chloroquine
DB00356 Chlorzoxazone
DB00169 Cholecalciferol
DB00568 Cinnarizine
DB01407 Clenbuterol
DB00636 Clofibrate
DB00575 Clonidine
DB00363 Clozapine
DB00851 Dacarbazine
DB06292 Dapagliflozin
DB01254 Dasatinib
DB00694 Daunorubicin
DB04840 Debrisoquine
DB01234 Dexamethasone
DB00633 Dexmedetomidine
DB11511 Difloxacin
DB05928 Dovitinib
DB08846 Ellagic acid
DB00530 Erlotinib
DB00783 Estradiol
DB13952 Estradiol acetate
DB13953 Estradiol benzoate
DB13954 Estradiol cypionate
DB13955 Estradiol dienanthate
DB13956 Estradiol valerate
DB00655 Estrone
DB00898 Ethanol
DB04841 Flunarizine
DB00499 Flutamide
DB01095 Fluvastatin
DB00176 Fluvoxamine
DB00317 Gefitinib
DB00889 Granisetron
DB00502 Haloperidol
DB12379 Indirubin
DB01064 Isoprenaline
DB11757 Istradefylline
DB01167 Itraconazole
DB01026 Ketoconazole
DB00448 Lansoprazole
DB00455 Loratadine
DB04871 Lorcaserin
DB09238 Manidipine
DB00643 Mebendazole
DB14009 Medical Cannabis
DB01065 Melatonin
DB00170 Menadione
DB00553 Methoxsalen
DB14011 Nabiximols
DB00184 Nicotine
DB01115 Nifedipine
DB00325 Nitroprusside
DB01059 Norfloxacin
DB00338 Omeprazole
DB00738 Pentamidine
DB08922 Perospirone
DB03783 Phenacetin
DB01174 Phenobarbital
DB00466 Picrotoxin
DB01087 Primaquine
DB00396 Progesterone
DB00818 Propofol
DB00571 Propranolol
DB00550 Propylthiouracil
DB00165 Pyridoxine
DB00908 Quinidine
DB00468 Quinine
DB01129 Rabeprazole
DB02709 Resveratrol
DB00740 Riluzole
DB08931 Riociguat
DB06176 Romidepsin
DB06654 Safinamide
DB01591 Solifenacin
DB00428 Streptozocin
DB00605 Sulindac
DB00675 Tamoxifen
DB04905 Tesmilifene
DB00624 Testosterone
DB13943 Testosterone cypionate
DB13944 Testosterone enanthate
DB13946 Testosterone undecanoate
DB01041 Thalidomide
DB00277 Theophylline
DB00730 Thiabendazole
DB01685 Topiroxostat
DB00539 Toremifene
DB00755 Tretinoin
DB12245 Triclabendazole
DB11155 Triclocarban
DB00197 Troglitazone

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		1318

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		CYP1A1

Domain mapping of disease mutations (DMDM)

More...DMDMi		117139

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000516271 – 512Cytochrome P450 1A1Add BLAST512

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi67O-linked (GlcNAc) serineBy similarity1

Keywords - PTMi

Glycoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P04798

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P04798

MaxQB - The MaxQuant DataBase

More...MaxQBi		P04798

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P04798

PeptideAtlas

More...PeptideAtlasi		P04798

PRoteomics IDEntifications database

More...PRIDEi		P04798

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		51744 [P04798-1]
654
655

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P04798

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P04798

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Lung, lymphocytes and placenta.

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000140465 Expressed in liver and 110 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P04798 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P04798 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000140465 Group enriched (liver, lung, urinary bladder)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with cytosolic chaperones HSP70 and HSP90; this interaction is required for initial targeting to mitochondria.

Interacts (via mitochondrial targeting signal) with TOMM40 (via N-terminus); this interaction is required for translocation across the mitochondrial outer membrane.

By similarity

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		107923, 76 interactors

Protein interaction database and analysis system

More...IntActi		P04798, 48 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000369050

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P04798

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P04798 protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1512
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P04798

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni29 – 40Mitochondrial targeting signalBy similarityAdd BLAST12

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0156 Eukaryota
COG2124 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00950000183037

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_1209426_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P04798

KEGG Orthology (KO)

More...KOi		K07408

Identification of Orthologs from Complete Genome Data

More...OMAi		DLTPEYG

Database of Orthologous Groups

More...OrthoDBi		1389393at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P04798

TreeFam database of animal gene trees

More...TreeFami		TF105095

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.630.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001128 Cyt_P450
IPR017972 Cyt_P450_CS
IPR002401 Cyt_P450_E_grp-I
IPR008066 Cyt_P450_E_grp-I_CYP1
IPR036396 Cyt_P450_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00067 p450, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00463 EP450I
PR01683 EP450ICYP1A
PR00385 P450

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48264 SSF48264, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00086 CYTOCHROME_P450, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 3 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P04798-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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        10         20         30         40         50
MLFPISMSAT EFLLASVIFC LVFWVIRASR PQVPKGLKNP PGPWGWPLIG 
        60         70         80         90        100
HMLTLGKNPH LALSRMSQQY GDVLQIRIGS TPVVVLSGLD TIRQALVRQG 
       110        120        130        140        150
DDFKGRPDLY TFTLISNGQS MSFSPDSGPV WAARRRLAQN GLKSFSIASD 
       160        170        180        190        200
PASSTSCYLE EHVSKEAEVL ISTLQELMAG PGHFNPYRYV VVSVTNVICA 
       210        220        230        240        250
ICFGRRYDHN HQELLSLVNL NNNFGEVVGS GNPADFIPIL RYLPNPSLNA 
       260        270        280        290        300
FKDLNEKFYS FMQKMVKEHY KTFEKGHIRD ITDSLIEHCQ EKQLDENANV 
       310        320        330        340        350
QLSDEKIINI VLDLFGAGFD TVTTAISWSL MYLVMNPRVQ RKIQEELDTV 
       360        370        380        390        400
IGRSRRPRLS DRSHLPYMEA FILETFRHSS FVPFTIPHST TRDTSLKGFY 
       410        420        430        440        450
IPKGRCVFVN QWQINHDQKL WVNPSEFLPE RFLTPDGAID KVLSEKVIIF 
       460        470        480        490        500
GMGKRKCIGE TIARWEVFLF LAILLQRVEF SVPLGVKVDM TPIYGLTMKH 
       510 
ACCEHFQMQL RS
Length:512
Mass (Da):58,165
Last modified:April 1, 1988 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i3C62366044148EFD
GO
Isoform 2 (identifier: P04798-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     189-189: Y → T
     190-512: Missing.

Show »
Length:189
Mass (Da):20,788
Checksum:i6F774C4E9FC85427
GO
Isoform 3 (identifier: P04798-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-261: Missing.
     419-512: Missing.

Show »
Length:157
Mass (Da):18,441
Checksum:iD0AE3E0EEA55B854
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E7EMT5E7EMT5_HUMAN
Cytochrome P450 1A1
CYP1A1
483Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q5J9B1Q5J9B1_HUMAN
Cytochrome P450 1A1
CYP1A1
484Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A4F3V8A4F3V8_HUMAN
Cytochrome P450 1A1
CYP1A1
175Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti26I → M in AAA52139 (PubMed:3838385).Curated1
Sequence conflicti235D → E in AAA52139 (PubMed:3838385).Curated1
Sequence conflicti381F → L in CAA26458 (PubMed:2989797).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_02319445G → D3 PublicationsCorresponds to variant dbSNP:rs4646422Ensembl.1
Natural variantiVAR_03381766M → V. Corresponds to variant dbSNP:rs35035798Ensembl.1
Natural variantiVAR_02319578I → T2 PublicationsCorresponds to variant dbSNP:rs17861094Ensembl.1
Natural variantiVAR_02470693R → W1 PublicationCorresponds to variant dbSNP:rs2229150Ensembl.1
Natural variantiVAR_024707173T → R1 PublicationCorresponds to variant dbSNP:rs28399427Ensembl.1
Natural variantiVAR_009280279R → W1 PublicationCorresponds to variant dbSNP:rs34260157Ensembl.1
Natural variantiVAR_020122286I → T. Corresponds to variant dbSNP:rs4987133Ensembl.1
Natural variantiVAR_016937331M → I in allele CYP1A1*6. 1 PublicationCorresponds to variant dbSNP:rs56313657Ensembl.1
Natural variantiVAR_016938448I → N in allele CYP1A1*8. 1 PublicationCorresponds to variant dbSNP:rs72547509Ensembl.1
Natural variantiVAR_008342461T → N in allele CYP1A1*4; displays similar catalytic efficiency toward estrogens when compared to the wild-type enzyme.. 4 PublicationsCorresponds to variant dbSNP:rs1799814Ensembl.1
Natural variantiVAR_001243462I → V in allele CYP1A1*2B and allele CYP1A1*2C; displays 5.7- and 12-fold increase in catalytic efficiency in the formation of 2-hydroxylated estrogens, 17beta-estradiol and estrone respectively.. 3 PublicationsCorresponds to variant dbSNP:rs1048943Ensembl.1
Natural variantiVAR_016939464R → C in allele CYP1A1*9. 1 PublicationCorresponds to variant dbSNP:rs41279188Ensembl.1
Natural variantiVAR_016940464R → S in allele CYP1A1*5. 1 PublicationCorresponds to variant dbSNP:rs41279188Ensembl.1
Natural variantiVAR_033818470F → V. Corresponds to variant dbSNP:rs36121583Ensembl.1
Natural variantiVAR_016941477R → W in allele CYP1A1*10. 2 PublicationsCorresponds to variant dbSNP:rs56240201Ensembl.1
Natural variantiVAR_024708482V → M1 PublicationCorresponds to variant dbSNP:rs28399429Ensembl.1
Natural variantiVAR_016942492P → R in allele CYP1A1*11. 2 PublicationsCorresponds to variant dbSNP:rs28399430Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0533631 – 261Missing in isoform 3. 1 PublicationAdd BLAST261
Alternative sequenceiVSP_053364189Y → T in isoform 2. 1 Publication1
Alternative sequenceiVSP_053365190 – 512Missing in isoform 2. 1 PublicationAdd BLAST323
Alternative sequenceiVSP_053366419 – 512Missing in isoform 3. 1 PublicationAdd BLAST94

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
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

The Consensus CDS (CCDS) project

More...CCDSi		CCDS10268.1 [P04798-1]

Protein sequence database of the Protein Information Resource

More...PIRi		A24797 O4HU6

NCBI Reference Sequences

More...RefSeqi		NP_000490.1, NM_000499.4 [P04798-1]
NP_001306145.1, NM_001319216.1
NP_001306146.1, NM_001319217.1 [P04798-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000379727; 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]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		1543

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:1543

UCSC genome browser

More...UCSCi		uc002ayp.4 human [P04798-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Cytochrome P450 Allele Nomenclature Committee

CYP1A1 alleles

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

CYP1A1 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
CCDSiCCDS10268.1 [P04798-1]
PIRiA24797 O4HU6
RefSeqiNP_000490.1, NM_000499.4 [P04798-1]
NP_001306145.1, NM_001319216.1
NP_001306146.1, NM_001319217.1 [P04798-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4I8VX-ray2.60A/B/C/D35-512[»]
6DWMX-ray2.85A/B/C/D35-512[»]
6DWNX-ray3.00A/B/C/D35-512[»]
6O5YX-ray3.17A/B/C/D35-512[»]
SMRiP04798
ModBaseiSearch...
PDBe-KBi