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Entry version 222 (02 Jun 2021)
Sequence version 1 (13 Aug 1987)
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Protein

Steroid 17-alpha-hydroxylase/17,20 lyase

Gene

CYP17A1

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 corticoid and androgen biosynthesis (PubMed:9452426, PubMed:27339894, PubMed:22266943, PubMed:25301938).

Catalyzes 17-alpha hydroxylation of C21 steroids, which is common for both pathways. A second oxidative step, required only for androgen synthesis, involves an acyl-carbon cleavage. The 17-alpha hydroxy intermediates, as part of adrenal glucocorticoids biosynthesis pathway, are precursors of cortisol (PubMed:9452426, PubMed:25301938) (Probable).

Hydroxylates steroid hormones, pregnenolone and progesterone to form 17-alpha hydroxy metabolites, followed by the cleavage of the C17-C20 bond to form C19 steroids, dehydroepiandrosterone (DHEA) and androstenedione (PubMed:9452426, PubMed:27339894, PubMed:22266943, PubMed:25301938).

Has 16-alpha hydroxylase activity. Catalyzes 16-alpha hydroxylation of 17-alpha hydroxy pregnenolone, followed by the cleavage of the C17-C20 bond to form 16-alpha-hydroxy DHEA. Also 16-alpha hydroxylates androgens, relevant for estriol synthesis (PubMed:27339894, PubMed:25301938).

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 (CPR; NADPH-ferrihemoprotein reductase) (PubMed:9452426, PubMed:27339894, PubMed:22266943, PubMed:25301938).

1 Publication4 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

heme2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Regulated predominantly by intracellular cAMP levels (PubMed:10720067). The 17,20-lyase activity is stimulated by cytochrome b5, which acts as an allosteric effector increasing the Vmax of the lyase activity (PubMed:9452426, PubMed:27339894).3 Publications

<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

kcat is 1.01 min(-1) with progesterone as substrate. kcat is 0.39 min(-1) with pregnenolone as substrate. kcat is 0.24 min(-1) with 17alpha-hydroxypregnenolone as substrate.
  1. KM=10.5 µM for progesterone (17-alpha hydroxylation)1 Publication
  2. KM=0.93 µM for pregnenolone (17-alpha hydroxylation)1 Publication
  3. KM=1.2 µM for 17alpha-hydroxypregnenolone (17,20 lyase activity)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: glucocorticoid biosynthesis

    This protein is involved in the pathway glucocorticoid biosynthesis, which is part of Steroid biosynthesis.2 Publications
    View all proteins of this organism that are known to be involved in the pathway glucocorticoid biosynthesis and in Steroid biosynthesis.

    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 sitei202Substrate1 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 bindingi442Iron (heme axial ligand)1

    <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

    • 17-alpha-hydroxyprogesterone aldolase activity Source: UniProtKB
    • heme binding Source: UniProtKB
    • iron ion binding Source: InterPro
    • oxygen binding Source: ProtInc
    • steroid 17-alpha-monooxygenase activity Source: UniProtKB

    GO - Biological processi

    <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 processSteroidogenesis
    LigandHeme, Iron, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:HS07560-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.14.14.19, 2681
    1.14.14.32, 2681

    Pathway Commons web resource for biological pathway data

    More...
    PathwayCommonsi
    P05093

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-193048, Androgen biosynthesis
    R-HSA-194002, Glucocorticoid biosynthesis
    R-HSA-5579028, Defective CYP17A1 causes Adrenal hyperplasia 5 (AH5)

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P05093

    SIGNOR Signaling Network Open Resource

    More...
    SIGNORi
    P05093

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

    More...
    UniPathwayi
    UPA00788

    Chemistry databases

    SwissLipids knowledge resource for lipid biology

    More...
    SwissLipidsi
    SLP:000001611

    <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:
    Steroid 17-alpha-hydroxylase/17,20 lyase1 Publication (EC:1.14.14.193 Publications)
    Alternative name(s):
    17-alpha-hydroxyprogesterone aldolase (EC:1.14.14.323 Publications)
    CYPXVII
    Cytochrome P450 17A11 Publication
    Cytochrome P450-C17
    Short name:
    Cytochrome P450c171 Publication
    Steroid 17-alpha-monooxygenase
    <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:CYP17A11 PublicationImported
    Synonyms:CYP17, S17AH
    <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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    <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 10

    Organism-specific databases

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:2593, CYP17A1

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    609300, gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_P05093

    Eukaryotic Pathogen, Vector and Host Database Resources

    More...
    VEuPathDBi
    HostDB:ENSG00000148795.5

    <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

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome

    <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

    <p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

    Adrenal hyperplasia 5 (AH5)19 Publications
    The disease is caused by variants affecting the gene represented in this entry.
    Disease descriptionA form of congenital adrenal hyperplasia, a common recessive disease due to defective synthesis of cortisol. Congenital adrenal hyperplasia is characterized by androgen excess leading to ambiguous genitalia in affected females, rapid somatic growth during childhood in both sexes with premature closure of the epiphyses and short adult stature. Four clinical types: 'salt wasting' (SW, the most severe type), 'simple virilizing' (SV, less severely affected patients), with normal aldosterone biosynthesis, 'non-classic form' or late-onset (NC or LOAH) and 'cryptic' (asymptomatic).
    Related information in OMIM
    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_02274535P → L in AH5; 38% 17alpha-hydroxylase activity and 33% 17,20-lyase activity. 1 Publication1
    Natural variantiVAR_00127053Missing in AH5; 10% 17alpha-hydroxylase activity and 13% 17,20-lyase activity. 3 Publications1
    Natural variantiVAR_00127164Y → S in AH5. 1 PublicationCorresponds to variant dbSNP:rs1183147390Ensembl.1
    Natural variantiVAR_01314793F → C in AH5. 1 PublicationCorresponds to variant dbSNP:rs104894146EnsemblClinVar.1
    Natural variantiVAR_07304396R → Q in AH5. 1 PublicationCorresponds to variant dbSNP:rs104894153EnsemblClinVar.1
    Natural variantiVAR_02274696R → W in AH5; 25% of both 17alpha-hydroxylase and 17,20-lyase activities. 3 PublicationsCorresponds to variant dbSNP:rs104894138EnsemblClinVar.1
    Natural variantiVAR_001272106S → P in AH5. 1 PublicationCorresponds to variant dbSNP:rs104894135EnsemblClinVar.1
    Natural variantiVAR_001273112I → II in AH5. 1 Publication1
    Natural variantiVAR_022747114F → V in AH5. 1 PublicationCorresponds to variant dbSNP:rs104894147EnsemblClinVar.1
    Natural variantiVAR_022748116D → V in AH5. 1 PublicationCorresponds to variant dbSNP:rs104894148EnsemblClinVar.1
    Natural variantiVAR_073044121W → R in AH5; partial loss of activity. 1 Publication1
    Natural variantiVAR_073045174A → E in AH5. 1 Publication1
    Natural variantiVAR_022749177N → D in AH5; 10% 17alpha-hydroxylase and 17,20-lyase activities. 1 Publication1
    Natural variantiVAR_022750329Y → D in AH5. 1 PublicationCorresponds to variant dbSNP:rs104894144EnsemblClinVar.1
    Natural variantiVAR_022751330Missing in AH5; complete loss of both 17alpha-hydroxylase and 17,20-lyase activities. 1 PublicationCorresponds to variant dbSNP:rs759060233Ensembl.1
    Natural variantiVAR_001274342P → T in AH5. 1 PublicationCorresponds to variant dbSNP:rs104894137EnsemblClinVar.1
    Natural variantiVAR_022752347R → C in AH5. 1 PublicationCorresponds to variant dbSNP:rs104894149EnsemblClinVar.1
    Natural variantiVAR_001275347R → H in AH5; selectively ablates 17,20-lyase activity, while preserving most 17alpha-hydroxylase activity. 3 PublicationsCorresponds to variant dbSNP:rs61754278EnsemblClinVar.1
    Natural variantiVAR_001276358R → Q in AH5; selectively ablates 17,20-lyase activity, while preserving most 17alpha-hydroxylase activity. 2 PublicationsCorresponds to variant dbSNP:rs104894139EnsemblClinVar.1
    Natural variantiVAR_022753362R → C in AH5. 1 PublicationCorresponds to variant dbSNP:rs104894142EnsemblClinVar.1
    Natural variantiVAR_001277373H → L in AH5. 2 PublicationsCorresponds to variant dbSNP:rs760695410EnsemblClinVar.1
    Natural variantiVAR_073046373H → N in AH5. 1 PublicationCorresponds to variant dbSNP:rs1423560123Ensembl.1
    Natural variantiVAR_073047406W → L in AH5; complete loss of both 17alpha-hydroxylase and 17,20-lyase activities. 1 Publication1
    Natural variantiVAR_022754406W → R in AH5. 1 PublicationCorresponds to variant dbSNP:rs104894143EnsemblClinVar.1
    Natural variantiVAR_022755417F → C in AH5; ablates both 17,20-lyase activity and 17alpha-hydroxylase activity; loss of heme-binding and loss of phosphorylation. 2 PublicationsCorresponds to variant dbSNP:rs104894140Ensembl.1
    Natural variantiVAR_022756428P → L in AH5. 1 PublicationCorresponds to variant dbSNP:rs104894145EnsemblClinVar.1
    Natural variantiVAR_001278440R → H in AH5. 1 PublicationCorresponds to variant dbSNP:rs777638364Ensembl.1
    Natural variantiVAR_001279487 – 489Missing in AH5. 1 Publication3
    Natural variantiVAR_001280496R → C in AH5. 1 PublicationCorresponds to variant dbSNP:rs1250463562Ensembl.1
    Natural variantiVAR_022757496R → H in AH5; 30% 17alpha-hydroxylase activity and 29% 17,20-lyase activity. 1 PublicationCorresponds to variant dbSNP:rs763398879Ensembl.1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi105A → L: Increases the affinity for progesterone, resulting in preferential hydroxylation of progesterone at C17 over C16; increases the catalytic efficiency in the 17,20 lyase reaction. 1 Publication1

    Keywords - Diseasei

    Congenital adrenal hyperplasia, Disease variant

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    1586

    MalaCards human disease database

    More...
    MalaCardsi
    CYP17A1
    MIMi202110, phenotype

    Open Targets

    More...
    OpenTargetsi
    ENSG00000148795

    Orphanet; a database dedicated to information on rare diseases and orphan drugs

    More...
    Orphaneti
    90796, 46,XY disorder of sex development due to isolated 17,20-lyase deficiency
    90793, Congenital adrenal hyperplasia due to 17-alpha-hydroxylase deficiency

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA27090

    Miscellaneous databases

    Pharos NIH Druggable Genome Knowledgebase

    More...
    Pharosi
    P05093, Tclin

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL3522

    Drug and drug target database

    More...
    DrugBanki
    DB05812, Abiraterone
    DB04630, Aldosterone
    DB01424, Aminophenazone
    DB09061, Cannabidiol
    DB00882, Clomifene
    DB01234, Dexamethasone
    DB14649, Dexamethasone acetate
    DB01026, Ketoconazole
    DB14009, Medical Cannabis
    DB14011, Nabiximols
    DB00157, NADH
    DB01708, Prasterone
    DB00396, Progesterone
    DB00421, Spironolactone
    DB02901, Stanolone

    DrugCentral

    More...
    DrugCentrali
    P05093

    IUPHAR/BPS Guide to PHARMACOLOGY

    More...
    GuidetoPHARMACOLOGYi
    1361

    Genetic variation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    CYP17A1

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    117283

    <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_00000519311 – 508Steroid 17-alpha-hydroxylase/17,20 lyaseAdd BLAST508

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Phosphorylation is necessary for 17,20-lyase, but not for 17-alpha-hydroxylase activity.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...
    MassIVEi
    P05093

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

    More...
    PaxDbi
    P05093

    PeptideAtlas

    More...
    PeptideAtlasi
    P05093

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P05093

    ProteomicsDB: a multi-organism proteome resource

    More...
    ProteomicsDBi
    51789

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P05093

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

    More...
    PhosphoSitePlusi
    P05093

    <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

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000148795, Expressed in adrenal gland and 121 other tissues

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P05093, baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P05093, HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    ENSG00000148795, Tissue enriched (adrenal)

    <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

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    107958, 14 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    P05093, 13 interactors

    Molecular INTeraction database

    More...
    MINTi
    P05093

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000358903

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P05093

    Miscellaneous databases

    RNAct, Protein-RNA interaction predictions for model organisms.

    More...
    RNActi
    P05093, 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

    1508
    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
    P05093

    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

    <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

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000155588

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_001570_22_0_1

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P05093

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    ICLPRES

    Database of Orthologous Groups

    More...
    OrthoDBi
    702827at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P05093

    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
    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
    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>Sequence (1+)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 has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

    P05093-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MWELVALLLL TLAYLFWPKR RCPGAKYPKS LLSLPLVGSL PFLPRHGHMH
    60 70 80 90 100
    NNFFKLQKKY GPIYSVRMGT KTTVIVGHHQ LAKEVLIKKG KDFSGRPQMA
    110 120 130 140 150
    TLDIASNNRK GIAFADSGAH WQLHRRLAMA TFALFKDGDQ KLEKIICQEI
    160 170 180 190 200
    STLCDMLATH NGQSIDISFP VFVAVTNVIS LICFNTSYKN GDPELNVIQN
    210 220 230 240 250
    YNEGIIDNLS KDSLVDLVPW LKIFPNKTLE KLKSHVKIRN DLLNKILENY
    260 270 280 290 300
    KEKFRSDSIT NMLDTLMQAK MNSDNGNAGP DQDSELLSDN HILTTIGDIF
    310 320 330 340 350
    GAGVETTTSV VKWTLAFLLH NPQVKKKLYE EIDQNVGFSR TPTISDRNRL
    360 370 380 390 400
    LLLEATIREV LRLRPVAPML IPHKANVDSS IGEFAVDKGT EVIINLWALH
    410 420 430 440 450
    HNEKEWHQPD QFMPERFLNP AGTQLISPSV SYLPFGAGPR SCIGEILARQ
    460 470 480 490 500
    ELFLIMAWLL QRFDLEVPDD GQLPSLEGIP KVVFLIDSFK VKIKVRQAWR

    EAQAEGST
    Length:508
    Mass (Da):57,371
    Last modified:August 13, 1987 - 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:iE5454E9E18F96B0E
    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 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    A0A1W2PRK7A0A1W2PRK7_HUMAN
    Steroid 17-alpha-hydroxylase/17,20 ...
    CYP17A1
    509Annotation score:

    Annotation score:2 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>
    A0A1W2PQT5A0A1W2PQT5_HUMAN
    Steroid 17-alpha-hydroxylase/17,20 ...
    CYP17A1
    479Annotation 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>
    A0A1W2PQ28A0A1W2PQ28_HUMAN
    Steroid 17-alpha-hydroxylase/17,20 ...
    CYP17A1
    356Annotation 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>
    A0A1W2PRY0A0A1W2PRY0_HUMAN
    Steroid 17-alpha-hydroxylase/17,20 ...
    CYP17A1
    407Annotation 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>

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_01175522C → W. Corresponds to variant dbSNP:rs762563Ensembl.1
    Natural variantiVAR_02274535P → L in AH5; 38% 17alpha-hydroxylase activity and 33% 17,20-lyase activity. 1 Publication1
    Natural variantiVAR_00127053Missing in AH5; 10% 17alpha-hydroxylase activity and 13% 17,20-lyase activity. 3 Publications1
    Natural variantiVAR_00127164Y → S in AH5. 1 PublicationCorresponds to variant dbSNP:rs1183147390Ensembl.1
    Natural variantiVAR_01314793F → C in AH5. 1 PublicationCorresponds to variant dbSNP:rs104894146EnsemblClinVar.1
    Natural variantiVAR_07304396R → Q in AH5. 1 PublicationCorresponds to variant dbSNP:rs104894153EnsemblClinVar.1
    Natural variantiVAR_02274696R → W in AH5; 25% of both 17alpha-hydroxylase and 17,20-lyase activities. 3 PublicationsCorresponds to variant dbSNP:rs104894138EnsemblClinVar.1
    Natural variantiVAR_001272106S → P in AH5. 1 PublicationCorresponds to variant dbSNP:rs104894135EnsemblClinVar.1
    Natural variantiVAR_001273112I → II in AH5. 1 Publication1
    Natural variantiVAR_022747114F → V in AH5. 1 PublicationCorresponds to variant dbSNP:rs104894147EnsemblClinVar.1
    Natural variantiVAR_022748116D → V in AH5. 1 PublicationCorresponds to variant dbSNP:rs104894148EnsemblClinVar.1
    Natural variantiVAR_073044121W → R in AH5; partial loss of activity. 1 Publication1
    Natural variantiVAR_073045174A → E in AH5. 1 Publication1
    Natural variantiVAR_022749177N → D in AH5; 10% 17alpha-hydroxylase and 17,20-lyase activities. 1 Publication1
    Natural variantiVAR_022750329Y → D in AH5. 1 PublicationCorresponds to variant dbSNP:rs104894144EnsemblClinVar.1
    Natural variantiVAR_022751330Missing in AH5; complete loss of both 17alpha-hydroxylase and 17,20-lyase activities. 1 PublicationCorresponds to variant dbSNP:rs759060233Ensembl.1
    Natural variantiVAR_001274342P → T in AH5. 1 PublicationCorresponds to variant dbSNP:rs104894137EnsemblClinVar.1
    Natural variantiVAR_022752347R → C in AH5. 1 PublicationCorresponds to variant dbSNP:rs104894149EnsemblClinVar.1
    Natural variantiVAR_001275347R → H in AH5; selectively ablates 17,20-lyase activity, while preserving most 17alpha-hydroxylase activity. 3 PublicationsCorresponds to variant dbSNP:rs61754278EnsemblClinVar.1
    Natural variantiVAR_001276358R → Q in AH5; selectively ablates 17,20-lyase activity, while preserving most 17alpha-hydroxylase activity. 2 PublicationsCorresponds to variant dbSNP:rs104894139EnsemblClinVar.1
    Natural variantiVAR_022753362R → C in AH5. 1 PublicationCorresponds to variant dbSNP:rs104894142EnsemblClinVar.1
    Natural variantiVAR_001277373H → L in AH5. 2 PublicationsCorresponds to variant dbSNP:rs760695410EnsemblClinVar.1
    Natural variantiVAR_073046373H → N in AH5. 1 PublicationCorresponds to variant dbSNP:rs1423560123Ensembl.1
    Natural variantiVAR_073047406W → L in AH5; complete loss of both 17alpha-hydroxylase and 17,20-lyase activities. 1 Publication1
    Natural variantiVAR_022754406W → R in AH5. 1 PublicationCorresponds to variant dbSNP:rs104894143EnsemblClinVar.1
    Natural variantiVAR_022755417F → C in AH5; ablates both 17,20-lyase activity and 17alpha-hydroxylase activity; loss of heme-binding and loss of phosphorylation. 2 PublicationsCorresponds to variant dbSNP:rs104894140Ensembl.1
    Natural variantiVAR_022756428P → L in AH5. 1 PublicationCorresponds to variant dbSNP:rs104894145EnsemblClinVar.1
    Natural variantiVAR_001278440R → H in AH5. 1 PublicationCorresponds to variant dbSNP:rs777638364Ensembl.1
    Natural variantiVAR_001279487 – 489Missing in AH5. 1 Publication3
    Natural variantiVAR_001280496R → C in AH5. 1 PublicationCorresponds to variant dbSNP:rs1250463562Ensembl.1
    Natural variantiVAR_022757496R → H in AH5; 30% 17alpha-hydroxylase activity and 29% 17,20-lyase activity. 1 PublicationCorresponds to variant dbSNP:rs763398879Ensembl.1

    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
    M14564 mRNA Translation: AAA52151.1
    M19489 Genomic DNA Translation: AAA36405.1
    M63871 Genomic DNA Translation: AAA59984.1
    M31153 M31152 Genomic DNA Translation: AAA52140.1 Sequence problems.
    BT020000 mRNA Translation: AAV38803.1
    AL358790 Genomic DNA No translation available.
    BC062997 mRNA Translation: AAH62997.1
    BC063388 mRNA Translation: AAH63388.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS7541.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A40921, A26366

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_000093.1, NM_000102.3

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000369887; ENSP00000358903; ENSG00000148795

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    1586

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:1586

    <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

    SHMPD

    The Singapore human mutation and polymorphism database

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M14564 mRNA Translation: AAA52151.1
    M19489 Genomic DNA Translation: AAA36405.1
    M63871 Genomic DNA Translation: AAA59984.1
    M31153 M31152 Genomic DNA Translation: AAA52140.1 Sequence problems.
    BT020000 mRNA Translation: AAV38803.1
    AL358790 Genomic DNA No translation available.
    BC062997 mRNA Translation: AAH62997.1
    BC063388 mRNA Translation: AAH63388.1
    CCDSiCCDS7541.1
    PIRiA40921, A26366
    RefSeqiNP_000093.1, NM_000102.3

    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
    2C17model-A48-501[»]
    3RUKX-ray2.60A/B/C/D24-508[»]
    3SWZX-ray2.40A/B/C/D24-508[»]
    4NKVX-ray2.65A/B/C/D24-508[»]
    4NKWX-ray2.50A/B/C/D24-508[»]
    4NKXX-ray2.79A/B/C/D24-508[»]
    4NKYX-ray2.55A/B/C/D24-508[»]
    4NKZX-ray3.00A/B/C/D24-508[»]
    5IRQX-ray2.20A/B/C/D24-508[»]
    5IRVX-ray3.10A/B/C/D24-508[»]
    5UYSX-ray2.39A/B/C/D24-508[»]
    6CHIX-ray2.70A/B/C/D24-508[»]
    6CIRX-ray2.65A/B/C/D24-508[»]
    6CIZX-ray2.60A/B/C/D24-508[»]
    SMRiP05093
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi107958, 14 interactors
    IntActiP05093, 13 interactors
    MINTiP05093
    STRINGi9606.ENSP00000358903

    Chemistry databases

    BindingDBiP05093
    ChEMBLiCHEMBL3522
    DrugBankiDB05812, Abiraterone
    DB04630, Aldosterone
    DB01424, Aminophenazone
    DB09061, Cannabidiol
    DB00882, Clomifene
    DB01234, Dexamethasone
    DB14649, Dexamethasone acetate
    DB01026, Ketoconazole
    DB14009, Medical Cannabis
    DB14011, Nabiximols
    DB00157, NADH
    DB01708, Prasterone
    DB00396, Progesterone
    DB00421, Spironolactone
    DB02901, Stanolone
    DrugCentraliP05093
    GuidetoPHARMACOLOGYi1361
    SwissLipidsiSLP:000001611

    PTM databases

    iPTMnetiP05093
    PhosphoSitePlusiP05093

    Genetic variation databases

    BioMutaiCYP17A1
    DMDMi117283

    Proteomic databases

    MassIVEiP05093
    PaxDbiP05093
    PeptideAtlasiP05093
    PRIDEiP05093
    ProteomicsDBi51789

    Protocols and materials databases

    Antibodypedia a portal for validated antibodies

    More...
    Antibodypediai
    31491, 615 antibodies

    The DNASU plasmid repository

    More...
    DNASUi
    1586

    Genome annotation databases

    EnsembliENST00000369887; ENSP00000358903; ENSG00000148795
    GeneIDi1586
    KEGGihsa:1586

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    1586
    DisGeNETi1586

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    CYP17A1
    HGNCiHGNC:2593, CYP17A1
    HPAiENSG00000148795, Tissue enriched (adrenal)
    MalaCardsiCYP17A1
    MIMi202110, phenotype
    609300, gene
    neXtProtiNX_P05093
    OpenTargetsiENSG00000148795
    Orphaneti90796, 46,XY disorder of sex development due to isolated 17,20-lyase deficiency
    90793, Congenital adrenal hyperplasia due to 17-alpha-hydroxylase deficiency
    PharmGKBiPA27090
    VEuPathDBiHostDB:ENSG00000148795.5

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG0156, Eukaryota
    GeneTreeiENSGT00940000155588
    HOGENOMiCLU_001570_22_0_1
    InParanoidiP05093
    OMAiICLPRES
    OrthoDBi702827at2759
    PhylomeDBiP05093
    TreeFamiTF105095

    Enzyme and pathway databases

    UniPathwayiUPA00788
    BioCyciMetaCyc:HS07560-MONOMER
    BRENDAi1.14.14.19, 2681
    1.14.14.32, 2681
    PathwayCommonsiP05093
    ReactomeiR-HSA-193048, Androgen biosynthesis
    R-HSA-194002, Glucocorticoid biosynthesis
    R-HSA-5579028, Defective CYP17A1 causes Adrenal hyperplasia 5 (AH5)
    SABIO-RKiP05093
    SIGNORiP05093

    Miscellaneous databases

    BioGRID ORCS database of CRISPR phenotype screens

    More...
    BioGRID-ORCSi
    1586, 5 hits in 993 CRISPR screens

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...
    ChiTaRSi
    CYP17A1, human

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    CYP17A1

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

    More...
    GenomeRNAii
    1586
    PharosiP05093, Tclin

    Protein Ontology

    More...
    PROi
    PR:P05093
    RNActiP05093, protein

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000148795, Expressed in adrenal gland and 121 other tissues
    ExpressionAtlasiP05093, baseline and differential
    GenevisibleiP05093, HS

    Family and domain databases

    Gene3Di1.10.630.10, 1 hit
    InterProiView protein in InterPro
    IPR001128, Cyt_P450
    IPR017972, Cyt_P450_CS
    IPR002401, Cyt_P450_E_grp-I
    IPR036396, Cyt_P450_sf
    PfamiView protein in Pfam
    PF00067, p450, 1 hit
    PRINTSiPR00463, EP450I
    PR00385, P450
    SUPFAMiSSF48264, SSF48264, 1 hit
    PROSITEiView protein in PROSITE
    PS00086, CYTOCHROME_P450, 1 hit

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCP17A_HUMAN
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P05093
    Secondary accession number(s): Q5TZV7
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: June 2, 2021
    This is version 222 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (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.

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with genetic variants
      List of human entries with genetic variants
    3. Human variants curated from literature reports
      Index of human variants curated from literature reports
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families
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