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UniProtKB - P15538 (C11B1_HUMAN)

Entry version 204 (11 Dec 2019)
Sequence version 5 (25 Nov 2008)
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Protein

Cytochrome P450 11B1, mitochondrial

Gene

CYP11B1

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 biosynthesis of adrenal corticoids (PubMed:18215163). Catalyzes the hydroxylation of carbon hydrogen bond at 11-beta position of 11-deoxycortisol and 11-deoxycorticosterone/21-hydroxyprogesterone yielding cortisol or corticosterone, respectively (PubMed:18215163). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate and reducing the second into a water molecule. Two electrons are provided by NADPH via a two-protein mitochondrial transfer system comprising flavoprotein FDXR (adrenodoxin/ferredoxin reductase) and nonheme iron-sulfur protein FDX1 or FDX2 (adrenodoxin/ferredoxin) (PubMed:18215163).1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

hemeBy similarity

<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 1.67 sec(-1) with 11-deoxycortisol as substrate. kcat is 0.85 sec(-1) with 21-hydroxyprogesterone as substrate.1 Publication
  1. KM=338.4 µM for 11-deoxycortisol1 Publication
  2. KM=179.5 µM for 21-hydroxyprogesterone1 Publication

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

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

    Pathwayi: Steroid hormone biosynthesis

    This protein is involved in Steroid hormone biosynthesis.1 Publication
    View all proteins of this organism that are known to be involved in Steroid hormone biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi450Iron (heme axial ligand)By similarity1

    <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 functionMonooxygenase, Oxidoreductase
    Biological processLipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroidogenesis
    LigandHeme, Iron, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		MetaCyc:HS08547-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		1.14.15.4 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...    Reactomei    		R-HSA-194002 Glucocorticoid biosynthesis
    R-HSA-211976 Endogenous sterols
    R-HSA-5579017 Defective CYP11B1 causes Adrenal hyperplasia 4 (AH4)

    SIGNOR Signaling Network Open Resource

    More...    SIGNORi    		P15538

    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:000001197

    <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_and_taxonomy_section">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 11B1, mitochondrial
    Alternative name(s):
    CYPXIB1
    Cytochrome P-450c11
    Short name:
    Cytochrome P450C11
    Steroid 11-beta-hydroxylase, CYP11B11 Publication (EC:1.14.15.41 Publication)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:CYP11B11 PublicationImported
    Synonyms:S11BH
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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 8

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...    EuPathDBi    		HostDB:ENSG00000160882.11

    Human Gene Nomenclature Database

    More...    HGNCi    		HGNC:2591 CYP11B1

    Online Mendelian Inheritance in Man (OMIM)

    More...    MIMi    		610613 gene

    neXtProt; the human protein knowledge platform

    More...    neXtProti    		NX_P15538

    <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

    Membrane, 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

    <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 4 (AH4)12 Publications
    The disease is caused by mutations 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_07449342P → L in AH4; classic; highly decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs193922538EnsemblClinVar.1
    Natural variantiVAR_00126042P → S in AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity. 3 PublicationsCorresponds to variant dbSNP:rs104894069EnsemblClinVar.1
    Natural variantiVAR_01414643R → Q in AH4; decreases steroid 11-beta-hydroxylase activity. 4 PublicationsCorresponds to variant dbSNP:rs4534EnsemblClinVar.1
    Natural variantiVAR_07449479F → I in AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs1489638195EnsemblClinVar.1
    Natural variantiVAR_07449583L → S in AH4; highly decreases steroid 11-beta-hydroxylase activity. 1 Publication1
    Natural variantiVAR_07449688M → I in AH4; slightly decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs193922539EnsemblClinVar.1
    Natural variantiVAR_06566694P → L in AH4; almost abolishes steroid 11-beta-hydroxylase activity. 2 PublicationsCorresponds to variant dbSNP:rs104894070EnsemblClinVar.1
    Natural variantiVAR_074497116W → C in AH4; almost abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs772003869Ensembl.1
    Natural variantiVAR_074498116W → G in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs772733691EnsemblClinVar.1
    Natural variantiVAR_074499125H → R in AH4; slightly decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs757389720EnsemblClinVar.1
    Natural variantiVAR_074500129V → M in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs377423817EnsemblClinVar.1
    Natural variantiVAR_001261133N → H in AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity. 2 PublicationsCorresponds to variant dbSNP:rs104894067EnsemblClinVar.1
    Natural variantiVAR_074501135P → S in AH4; highly decreases steroid 11-beta-hydroxylase activity. 1 Publication1
    Natural variantiVAR_074502139F → L in AH4; decreases steroid 11-beta-hydroxylase activity. 1 Publication1
    Natural variantiVAR_075553141R → Q in AH4; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs267601810EnsemblClinVar.1
    Natural variantiVAR_074503143R → W in AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs140336749EnsemblClinVar.1
    Natural variantiVAR_074504150S → L in AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs142484434EnsemblClinVar.1
    Natural variantiVAR_074505158L → P in AH4; highly decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs1554653191EnsemblClinVar.1
    Natural variantiVAR_074506159P → L in AH4; decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs370266763Ensembl.1
    Natural variantiVAR_074507161Missing in AH4. 1 Publication1
    Natural variantiVAR_074508165A → D in AH4; almost abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs1554653185EnsemblClinVar.1
    Natural variantiVAR_074509196T → A in AH4; decreases steroid 11-beta-hydroxylase activity. 1 Publication1
    Natural variantiVAR_074510254 – 259Missing in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 Publication6
    Natural variantiVAR_074511267G → D in AH4. 1 Publication1
    Natural variantiVAR_074512299L → P in AH4; non-classic; almost abolishes steroid 11-beta-hydroxylase activity. 2 PublicationsCorresponds to variant dbSNP:rs387907573EnsemblClinVar.1
    Natural variantiVAR_074513306A → V in AH4; non-classic; almost abolishes steroid 11-beta-hydroxylase activity. 2 PublicationsCorresponds to variant dbSNP:rs387907572EnsemblClinVar.1
    Natural variantiVAR_074514310E → K in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs387907574EnsemblClinVar.1
    Natural variantiVAR_074515314G → R in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs1336285846Ensembl.1
    Natural variantiVAR_001262318T → M in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs104894061EnsemblClinVar.1
    Natural variantiVAR_074516318T → P in AH4. 1 PublicationCorresponds to variant dbSNP:rs1296969984Ensembl.1
    Natural variantiVAR_065667318T → R in AH4. 4 Publications1
    Natural variantiVAR_001263319T → M in AH4; non-classic; decreases steroid 11-beta-hydroxylase activity. 2 PublicationsCorresponds to variant dbSNP:rs104894068EnsemblClinVar.1
    Natural variantiVAR_074517321F → V in AH4. 1 PublicationCorresponds to variant dbSNP:rs1453371113Ensembl.1
    Natural variantiVAR_074518331A → V in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 Publication1
    Natural variantiVAR_075554332R → G in AH4; high reduction of steroid 11-beta-monooxygenase activity. 1 Publication1
    Natural variantiVAR_074519332R → Q in AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs149881706EnsemblClinVar.1
    Natural variantiVAR_074520341R → S in AH4. 1 PublicationCorresponds to variant dbSNP:rs372115638EnsemblClinVar.1
    Natural variantiVAR_074521366R → C in AH4; decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs773245244Ensembl.1
    Natural variantiVAR_074522368A → D in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs104894071EnsemblClinVar.1
    Natural variantiVAR_074523371E → G in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs368944209EnsemblClinVar.1
    Natural variantiVAR_001264374R → Q in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs104894062EnsemblClinVar.1
    Natural variantiVAR_065196379G → V in AH4. 1 Publication1
    Natural variantiVAR_074524384R → G in AH4. 1 Publication1
    Natural variantiVAR_074525384R → Q in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs764598023EnsemblClinVar.1
    Natural variantiVAR_074526401T → A in AH4; decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs201300785Ensembl.1
    Natural variantiVAR_074527427R → H in AH4. 1 PublicationCorresponds to variant dbSNP:rs754432887EnsemblClinVar.1
    Natural variantiVAR_074528438Missing in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 Publication1
    Natural variantiVAR_074529441V → G in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs772169059Ensembl.1
    Natural variantiVAR_074530444G → D in AH4. 1 PublicationCorresponds to variant dbSNP:rs779103938EnsemblClinVar.1
    Natural variantiVAR_074531448R → C in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs1221010438Ensembl.1
    Natural variantiVAR_001265448R → H in AH4; abolishes steroid 11-beta-hydroxylase activity. 5 PublicationsCorresponds to variant dbSNP:rs28934586EnsemblClinVar.1
    Natural variantiVAR_074532453R → Q in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs1447069098Ensembl.1
    Natural variantiVAR_065197454R → C in AH4. 1 Publication1
    Natural variantiVAR_074533463L → LL in AH4; classic; abolishes steroid 11-beta-hydroxylase activity. 1 Publication1
    Natural variantiVAR_074534489L → S in AH4. 1 PublicationCorresponds to variant dbSNP:rs750428278Ensembl.1
    Hyperaldosteronism, familial, 1 (HALD1)
    The disease is caused by mutations affecting the gene represented in this entry. The molecular defect causing hyperaldosteronism familial 1 is an anti-Lepore-type fusion of the CYP11B1 and CYP11B2 genes. The hybrid gene has the promoting part of CYP11B1, ACTH-sensitive, and the coding part of CYP11B2.
    Disease descriptionA disorder characterized by hypertension, variable hyperaldosteronism, and abnormal adrenal steroid production, including 18-oxocortisol and 18-hydroxycortisol. There is significant phenotypic heterogeneity, and some individuals never develop hypertension.
    Related information in OMIM

    Keywords - Diseasei

    Congenital adrenal hyperplasia, Disease mutation

    Organism-specific databases

    DisGeNET

    More...    DisGeNETi    		1584

    MalaCards human disease database

    More...    MalaCardsi    		CYP11B1
    MIMi103900 phenotype
    202010 phenotype

    Open Targets

    More...    OpenTargetsi    		ENSG00000160882

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

    More...    Orphaneti    		90795 Congenital adrenal hyperplasia due to 11-beta-hydroxylase deficiency
    403 Familial hyperaldosteronism type I

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...    PharmGKBi    		PA133

    Miscellaneous databases

    Pharos NIH Druggable Genome Knowledgebase

    More...    Pharosi    		P15538 Tclin

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...    ChEMBLi    		CHEMBL1908

    Drug and drug target database

    More...    DrugBanki    		DB04630 Aldosterone
    DB00501 Cimetidine
    DB00292 Etomidate
    DB00741 Hydrocortisone
    DB14538 Hydrocortisone aceponate
    DB14539 Hydrocortisone acetate
    DB14540 Hydrocortisone butyrate
    DB14541 Hydrocortisone cypionate
    DB14542 Hydrocortisone phosphate
    DB14543 Hydrocortisone probutate
    DB14545 Hydrocortisone succinate
    DB14544 Hydrocortisone valerate
    DB01026 Ketoconazole
    DB05667 Levoketoconazole
    DB01233 Metoclopramide
    DB01011 Metyrapone
    DB01388 Mibefradil
    DB01110 Miconazole
    DB00648 Mitotane
    DB00252 Phenytoin
    DB00421 Spironolactone

    DrugCentral

    More...    DrugCentrali    		P15538

    IUPHAR/BPS Guide to PHARMACOLOGY

    More...    GuidetoPHARMACOLOGYi    		1359

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...    BioMutai    		CYP11B1

    Domain mapping of disease mutations (DMDM)

    More...    DMDMi    		215274267

    <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 transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 24MitochondrionAdd BLAST24
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000359625 – 503Cytochrome P450 11B1, mitochondrialAdd BLAST479

    Proteomic databases

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...    MassIVEi    		P15538

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

    More...    PaxDbi    		P15538

    PeptideAtlas

    More...    PeptideAtlasi    		P15538

    PRoteomics IDEntifications database

    More...    PRIDEi    		P15538

    ProteomicsDB: a multi-organism proteome resource

    More...    ProteomicsDBi    		53185 [P15538-1]
    53186 [P15538-2]

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...    iPTMneti    		P15538

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

    More...    PhosphoSitePlusi    		P15538

    <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    		ENSG00000160882 Expressed in 86 organ(s), highest expression level in right adrenal gland

    ExpressionAtlas, Differential and Baseline Expression

    More...    ExpressionAtlasi    		P15538 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...    Genevisiblei    		P15538 HS

    Organism-specific databases

    Human Protein Atlas

    More...    HPAi    		HPA049171
    HPA056348
    HPA057752

    <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    		107956, 1 interactor

    STRING: functional protein association networks

    More...    STRINGi    		9606.ENSP00000292427

    Chemistry databases

    BindingDB database of measured binding affinities

    More...    BindingDBi    		P15538

    Miscellaneous databases

    RNAct, Protein-RNA interaction predictions for model organisms.

    More...    RNActi    		P15538 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

    1503
    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    		P15538

    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

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		KOG0159 Eukaryota
    COG2124 LUCA

    Ensembl GeneTree

    More...    GeneTreei    		ENSGT00940000163354

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000013161

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P15538

    KEGG Orthology (KO)

    More...    KOi    		K00497

    Database of Orthologous Groups

    More...    OrthoDBi    		1271528at2759

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P15538

    TreeFam database of animal gene trees

    More...    TreeFami    		TF105094

    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
    IPR002399 Cyt_P450_mitochondrial
    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    		PR00408 MITP450
    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_length">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 (2+)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 <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.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

    This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

    Isoform 1 (identifier: P15538-1) [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.

    « Hide
            10         20         30         40         50
    MALRAKAEVC MAVPWLSLQR AQALGTRAAR VPRTVLPFEA MPRRPGNRWL 
            60         70         80         90        100
    RLLQIWREQG YEDLHLEVHQ TFQELGPIFR YDLGGAGMVC VMLPEDVEKL 
           110        120        130        140        150
    QQVDSLHPHR MSLEPWVAYR QHRGHKCGVF LLNGPEWRFN RLRLNPEVLS 
           160        170        180        190        200
    PNAVQRFLPM VDAVARDFSQ ALKKKVLQNA RGSLTLDVQP SIFHYTIEAS 
           210        220        230        240        250
    NLALFGERLG LVGHSPSSAS LNFLHALEVM FKSTVQLMFM PRSLSRWTSP 
           260        270        280        290        300
    KVWKEHFEAW DCIFQYGDNC IQKIYQELAF SRPQQYTSIV AELLLNAELS 
           310        320        330        340        350
    PDAIKANSME LTAGSVDTTV FPLLMTLFEL ARNPNVQQAL RQESLAAAAS 
           360        370        380        390        400
    ISEHPQKATT ELPLLRAALK ETLRLYPVGL FLERVASSDL VLQNYHIPAG 
           410        420        430        440        450
    TLVRVFLYSL GRNPALFPRP ERYNPQRWLD IRGSGRNFYH VPFGFGMRQC 
           460        470        480        490        500
    LGRRLAEAEM LLLLHHVLKH LQVETLTQED IKMVYSFILR PSMFPLLTFR 

    AIN
    Length:503
    Mass (Da):57,573
    Last modified:November 25, 2008 - v5
    <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:i0B36D82513960EE9
    GO
    Isoform 2 (identifier: P15538-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         401-466: Missing.

    Show »
    Length:437
    Mass (Da):49,750
    Checksum:iF85180BFB83C9B5A
    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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    		Gene namesLengthAnnotation
    H0YBR4H0YBR4_HUMAN
    Cytochrome P450 11B1, mitochondrial
    CYP11B1
    		181Annotation 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>
    Q4VAR0Q4VAR0_HUMAN
    CYP11B1 protein
    CYP11B1
    		574Annotation 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_01414510C → Y1 PublicationCorresponds to variant dbSNP:rs6405Ensembl.1
    Natural variantiVAR_07449342P → L in AH4; classic; highly decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs193922538EnsemblClinVar.1
    Natural variantiVAR_00126042P → S in AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity. 3 PublicationsCorresponds to variant dbSNP:rs104894069EnsemblClinVar.1
    Natural variantiVAR_01414643R → Q in AH4; decreases steroid 11-beta-hydroxylase activity. 4 PublicationsCorresponds to variant dbSNP:rs4534EnsemblClinVar.1
    Natural variantiVAR_01463863D → H. Corresponds to variant dbSNP:rs5282EnsemblClinVar.1
    Natural variantiVAR_07449479F → I in AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs1489638195EnsemblClinVar.1
    Natural variantiVAR_07449583L → S in AH4; highly decreases steroid 11-beta-hydroxylase activity. 1 Publication1
    Natural variantiVAR_07449688M → I in AH4; slightly decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs193922539EnsemblClinVar.1
    Natural variantiVAR_06566694P → L in AH4; almost abolishes steroid 11-beta-hydroxylase activity. 2 PublicationsCorresponds to variant dbSNP:rs104894070EnsemblClinVar.1
    Natural variantiVAR_074497116W → C in AH4; almost abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs772003869Ensembl.1
    Natural variantiVAR_074498116W → G in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs772733691EnsemblClinVar.1
    Natural variantiVAR_074499125H → R in AH4; slightly decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs757389720EnsemblClinVar.1
    Natural variantiVAR_074500129V → M in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs377423817EnsemblClinVar.1
    Natural variantiVAR_001261133N → H in AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity. 2 PublicationsCorresponds to variant dbSNP:rs104894067EnsemblClinVar.1
    Natural variantiVAR_074501135P → S in AH4; highly decreases steroid 11-beta-hydroxylase activity. 1 Publication1
    Natural variantiVAR_074502139F → L in AH4; decreases steroid 11-beta-hydroxylase activity. 1 Publication1
    Natural variantiVAR_075553141R → Q in AH4; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs267601810EnsemblClinVar.1
    Natural variantiVAR_074503143R → W in AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs140336749EnsemblClinVar.1
    Natural variantiVAR_074504150S → L in AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs142484434EnsemblClinVar.1
    Natural variantiVAR_074505158L → P in AH4; highly decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs1554653191EnsemblClinVar.1
    Natural variantiVAR_074506159P → L in AH4; decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs370266763Ensembl.1
    Natural variantiVAR_014147160M → I1 PublicationCorresponds to variant dbSNP:rs5287Ensembl.1
    Natural variantiVAR_074507161Missing in AH4. 1 Publication1
    Natural variantiVAR_074508165A → D in AH4; almost abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs1554653185EnsemblClinVar.1
    Natural variantiVAR_014639173K → R. Corresponds to variant dbSNP:rs4539EnsemblClinVar.1
    Natural variantiVAR_074509196T → A in AH4; decreases steroid 11-beta-hydroxylase activity. 1 Publication1
    Natural variantiVAR_048462248T → I. Corresponds to variant dbSNP:rs34620645EnsemblClinVar.1
    Natural variantiVAR_074510254 – 259Missing in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 Publication6
    Natural variantiVAR_014640257F → L. Corresponds to variant dbSNP:rs5288Ensembl.1
    Natural variantiVAR_074511267G → D in AH4. 1 Publication1
    Natural variantiVAR_014641281S → N. Corresponds to variant dbSNP:rs5291Ensembl.1
    Natural variantiVAR_014148293L → V1 PublicationCorresponds to variant dbSNP:rs5292Ensembl.1
    Natural variantiVAR_074512299L → P in AH4; non-classic; almost abolishes steroid 11-beta-hydroxylase activity. 2 PublicationsCorresponds to variant dbSNP:rs387907573EnsemblClinVar.1
    Natural variantiVAR_074513306A → V in AH4; non-classic; almost abolishes steroid 11-beta-hydroxylase activity. 2 PublicationsCorresponds to variant dbSNP:rs387907572EnsemblClinVar.1
    Natural variantiVAR_074514310E → K in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs387907574EnsemblClinVar.1
    Natural variantiVAR_074515314G → R in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs1336285846Ensembl.1
    Natural variantiVAR_001262318T → M in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs104894061EnsemblClinVar.1
    Natural variantiVAR_074516318T → P in AH4. 1 PublicationCorresponds to variant dbSNP:rs1296969984Ensembl.1
    Natural variantiVAR_065667318T → R in AH4. 4 Publications1
    Natural variantiVAR_001263319T → M in AH4; non-classic; decreases steroid 11-beta-hydroxylase activity. 2 PublicationsCorresponds to variant dbSNP:rs104894068EnsemblClinVar.1
    Natural variantiVAR_074517321F → V in AH4. 1 PublicationCorresponds to variant dbSNP:rs1453371113Ensembl.1
    Natural variantiVAR_074518331A → V in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 Publication1
    Natural variantiVAR_075554332R → G in AH4; high reduction of steroid 11-beta-monooxygenase activity. 1 Publication1
    Natural variantiVAR_074519332R → Q in AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs149881706EnsemblClinVar.1
    Natural variantiVAR_074520341R → S in AH4. 1 PublicationCorresponds to variant dbSNP:rs372115638EnsemblClinVar.1
    Natural variantiVAR_014149348A → T1 PublicationCorresponds to variant dbSNP:rs6407EnsemblClinVar.1
    Natural variantiVAR_074521366R → C in AH4; decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs773245244Ensembl.1
    Natural variantiVAR_074522368A → D in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs104894071EnsemblClinVar.1
    Natural variantiVAR_074523371E → G in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs368944209EnsemblClinVar.1
    Natural variantiVAR_001264374R → Q in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs104894062EnsemblClinVar.1
    Natural variantiVAR_065196379G → V in AH4. 1 Publication1
    Natural variantiVAR_074524384R → G in AH4. 1 Publication1
    Natural variantiVAR_074525384R → Q in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs764598023EnsemblClinVar.1
    Natural variantiVAR_014150386A → V4 PublicationsCorresponds to variant dbSNP:rs4541EnsemblClinVar.1
    Natural variantiVAR_074526401T → A in AH4; decreases steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs201300785Ensembl.1
    Natural variantiVAR_048463404R → H. Corresponds to variant dbSNP:rs4998896Ensembl.1
    Natural variantiVAR_074527427R → H in AH4. 1 PublicationCorresponds to variant dbSNP:rs754432887EnsemblClinVar.1
    Natural variantiVAR_074528438Missing in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 Publication1
    Natural variantiVAR_014642439Y → H. Corresponds to variant dbSNP:rs5294Ensembl.1
    Natural variantiVAR_074529441V → G in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs772169059Ensembl.1
    Natural variantiVAR_074530444G → D in AH4. 1 PublicationCorresponds to variant dbSNP:rs779103938EnsemblClinVar.1
    Natural variantiVAR_074531448R → C in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs1221010438Ensembl.1
    Natural variantiVAR_001265448R → H in AH4; abolishes steroid 11-beta-hydroxylase activity. 5 PublicationsCorresponds to variant dbSNP:rs28934586EnsemblClinVar.1
    Natural variantiVAR_074532453R → Q in AH4; abolishes steroid 11-beta-hydroxylase activity. 1 PublicationCorresponds to variant dbSNP:rs1447069098Ensembl.1
    Natural variantiVAR_065197454R → C in AH4. 1 Publication1
    Natural variantiVAR_074533463L → LL in AH4; classic; abolishes steroid 11-beta-hydroxylase activity. 1 Publication1
    Natural variantiVAR_074534489L → S in AH4. 1 PublicationCorresponds to variant dbSNP:rs750428278Ensembl.1
    Natural variantiVAR_008687494F → C2 Publications1

    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_043308401 – 466Missing in isoform 2. 1 PublicationAdd BLAST66

    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
    		M32879, M32863, M32878 Genomic DNA Translation: AAA52149.1
    X55764 mRNA Translation: CAA39290.1
    D16153 Genomic DNA Translation: BAB71992.1
    D16155 Genomic DNA Translation: BAA03717.1
    EU332839 Genomic DNA Translation: ABY87528.1
    AC083841 Genomic DNA No translation available.
    CH471162 Genomic DNA Translation: EAW82293.1
    BC096286 mRNA Translation: AAH96286.1
    BC096287 mRNA Translation: AAH96287.1
    M24667 mRNA Translation: AAA52148.1 Sequence problems.
    D10169 Genomic DNA Translation: BAA01039.1

    The Consensus CDS (CCDS) project

    More...    CCDSi    		CCDS34953.1 [P15538-2]
    CCDS6392.1 [P15538-1]

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		S11338

    NCBI Reference Sequences

    More...    RefSeqi    		NP_000488.3, NM_000497.3 [P15538-1]
    NP_001021384.1, NM_001026213.1 [P15538-2]

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...    Ensembli    		ENST00000292427; ENSP00000292427; ENSG00000160882 [P15538-1]
    ENST00000517471; ENSP00000428043; ENSG00000160882 [P15538-2]

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		1584

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		hsa:1584

    UCSC genome browser

    More...    UCSCi    		uc003yxi.4 human [P15538-1]

    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

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    		M32879, M32863, M32878 Genomic DNA Translation: AAA52149.1
    X55764 mRNA Translation: CAA39290.1
    D16153 Genomic DNA Translation: BAB71992.1
    D16155 Genomic DNA Translation: BAA03717.1
    EU332839 Genomic DNA Translation: ABY87528.1
    AC083841 Genomic DNA No translation available.
    CH471162 Genomic DNA Translation: EAW82293.1
    BC096286 mRNA Translation: AAH96286.1
    BC096287 mRNA Translation: AAH96287.1
    M24667 mRNA Translation: AAA52148.1 Sequence problems.
    D10169 Genomic DNA Translation: BAA01039.1
    CCDSiCCDS34953.1 [P15538-2]
    CCDS6392.1 [P15538-1]
    PIRiS11338
    RefSeqiNP_000488.3, NM_000497.3 [P15538-1]
    NP_001021384.1, NM_001026213.1 [P15538-2]

    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
    6M7XX-ray2.10A/B31-503[»]
    SMRiP15538
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi107956, 1 interactor
    STRINGi9606.ENSP00000292427

    Chemistry databases

    BindingDBiP15538
    ChEMBLiCHEMBL1908
    DrugBankiDB04630 Aldosterone
    DB00501 Cimetidine
    DB00292 Etomidate
    DB00741 Hydrocortisone
    DB14538 Hydrocortisone aceponate
    DB14539 Hydrocortisone acetate
    DB14540 Hydrocortisone butyrate
    DB14541 Hydrocortisone cypionate
    DB14542 Hydrocortisone phosphate
    DB14543 Hydrocortisone probutate
    DB14545 Hydrocortisone succinate
    DB14544 Hydrocortisone valerate
    DB01026 Ketoconazole
    DB05667 Levoketoconazole
    DB01233 Metoclopramide
    DB01011 Metyrapone
    DB01388 Mibefradil
    DB01110 Miconazole
    DB00648 Mitotane
    DB00252 Phenytoin
    DB00421 Spironolactone
    DrugCentraliP15538
    GuidetoPHARMACOLOGYi1359
    SwissLipidsiSLP:000001197

    PTM databases

    iPTMnetiP15538
    PhosphoSitePlusiP15538

    Polymorphism and mutation databases

    BioMutaiCYP11B1
    DMDMi215274267

    Proteomic databases

    MassIVEiP15538
    PaxDbiP15538
    PeptideAtlasiP15538
    PRIDEiP15538
    ProteomicsDBi53185 [P15538-1]
    53186 [P15538-2]

    Genome annotation databases

    EnsembliENST00000292427; ENSP00000292427; ENSG00000160882 [P15538-1]
    ENST00000517471; ENSP00000428043; ENSG00000160882 [P15538-2]
    GeneIDi1584
    KEGGihsa:1584
    UCSCiuc003yxi.4 human [P15538-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...    CTDi    		1584
    DisGeNETi1584
    EuPathDBiHostDB:ENSG00000160882.11

    GeneCards: human genes, protein and diseases

    More...    GeneCardsi    		CYP11B1
    HGNCiHGNC:2591 CYP11B1
    HPAiHPA049171
    HPA056348
    HPA057752
    MalaCardsiCYP11B1
    MIMi103900 phenotype
    202010 phenotype
    610613 gene
    neXtProtiNX_P15538
    OpenTargetsiENSG00000160882
    Orphaneti90795 Congenital adrenal hyperplasia due to 11-beta-hydroxylase deficiency
    403 Familial hyperaldosteronism type I
    PharmGKBiPA133

    GenAtlas: human gene database

    More...    GenAtlasi    		Search...

    Phylogenomic databases

    eggNOGiKOG0159 Eukaryota
    COG2124 LUCA
    GeneTreeiENSGT00940000163354
    HOGENOMiHOG000013161
    InParanoidiP15538
    KOiK00497
    OrthoDBi1271528at2759
    PhylomeDBiP15538
    TreeFamiTF105094

    Enzyme and pathway databases

    UniPathwayiUPA00788
    BioCyciMetaCyc:HS08547-MONOMER
    BRENDAi1.14.15.4 2681
    ReactomeiR-HSA-194002 Glucocorticoid biosynthesis
    R-HSA-211976 Endogenous sterols
    R-HSA-5579017 Defective CYP11B1 causes Adrenal hyperplasia 4 (AH4)
    SIGNORiP15538

    Miscellaneous databases

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

    More...    ChiTaRSi    		CYP11B1 human

    The Gene Wiki collection of pages on human genes and proteins

    More...    GeneWikii    		Steroid_11-beta-hydroxylase

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

    More...    GenomeRNAii    		1584
    PharosiP15538 Tclin

    Protein Ontology

    More...    PROi    		PR:P15538
    RNActiP15538 protein

    The Stanford Online Universal Resource for Clones and ESTs

    More...    SOURCEi    		Search...

    Gene expression databases

    BgeeiENSG00000160882 Expressed in 86 organ(s), highest expression level in right adrenal gland
    ExpressionAtlasiP15538 baseline and differential
    GenevisibleiP15538 HS

    Family and domain databases

    Gene3Di1.10.630.10, 1 hit
    InterProiView protein in InterPro
    IPR001128 Cyt_P450
    IPR017972 Cyt_P450_CS
    IPR002399 Cyt_P450_mitochondrial
    IPR036396 Cyt_P450_sf
    PfamiView protein in Pfam
    PF00067 p450, 1 hit
    PRINTSiPR00408 MITP450
    PR00385 P450
    SUPFAMiSSF48264 SSF48264, 1 hit
    PROSITEiView protein in PROSITE
    PS00086 CYTOCHROME_P450, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...    ProtoNeti    		Search...

    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 nameiC11B1_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: P15538
    Secondary accession number(s): Q14095
    , Q4VAQ8, Q4VAQ9, Q9UML2
    <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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: November 25, 2008
    Last modified: December 11, 2019
    This is version 204 of the entry and version 5 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, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    4. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    5. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    6. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    7. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
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