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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

Has steroid 11-beta-hydroxylase activity. In addition to this activity, the 18 or 19-hydroxylation of steroids and the aromatization of androstendione to estrone have also been ascribed to cytochrome P450 XIB.

<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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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

  • corticosterone 18-monooxygenase activity Source: GO_Central
  • heme binding Source: BHF-UCL
  • iron ion binding Source: InterPro
  • steroid 11-beta-monooxygenase activity Source: BHF-UCL

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

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:HS08547-MONOMER

BRENDA Comprehensive Enzyme Information System

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BRENDAi
1.14.15.4 2681

Reactome - a knowledgebase of biological pathways and processes

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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

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SIGNORi
P15538

Chemistry databases

SwissLipids knowledge resource for lipid biology

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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 (EC:1.14.15.4)
<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:CYP11B1
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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

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EuPathDBi
HostDB:ENSG00000160882.11

Human Gene Nomenclature Database

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HGNCi
HGNC:2591 CYP11B1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
610613 gene

neXtProt; the human protein knowledge platform

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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; Source: COMPARTMENTS

Keywords - Cellular componenti

Membrane, Mitochondrion

<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).
See also OMIM:202010
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 Publication1
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 Publication1
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:rs142484434Ensembl.1
Natural variantiVAR_074505158L → P in AH4; highly decreases steroid 11-beta-hydroxylase activity. 1 Publication1
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 Publication1
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 Publication1
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 Publication1
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 Publication1
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 Publication1
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 Publication1
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.
See also OMIM:103900

Keywords - Diseasei

Congenital adrenal hyperplasia, Disease mutation

Organism-specific databases

DisGeNET

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DisGeNETi
1584

MalaCards human disease database

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MalaCardsi
CYP11B1
MIMi103900 phenotype
202010 phenotype

Open Targets

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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

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PharmGKBi
PA133

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL1908

Drug and drug target database

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DrugBanki
DB04630 Aldosterone
DB00501 Cimetidine
DB00257 Clotrimazole
DB00292 Etomidate
DB00196 Fluconazole
DB00741 Hydrocortisone
DB01026 Ketoconazole
DB01233 Metoclopramide
DB01011 Metyrapone
DB01388 Mibefradil
DB01110 Miconazole
DB00648 Mitotane
DB00252 Phenytoin
DB00421 Spironolactone

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1359

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
CYP11B1

Domain mapping of disease mutations (DMDM)

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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

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

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PaxDbi
P15538

PeptideAtlas

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PeptideAtlasi
P15538

PRoteomics IDEntifications database

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PRIDEi
P15538

ProteomicsDB human proteome resource

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ProteomicsDBi
53185
53186 [P15538-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P15538

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

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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

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

CleanEx database of gene expression profiles

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CleanExi
HS_CYP11B1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P15538 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P15538 HS

Organism-specific databases

Human Protein Atlas

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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)

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BioGridi
107956, 1 interactor

STRING: functional protein association networks

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STRINGi
9606.ENSP00000292427

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P15538

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P15538

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

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SMRi
P15538

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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

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eggNOGi
KOG0159 Eukaryota
COG2124 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000163354

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000013161

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG051098

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P15538

KEGG Orthology (KO)

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KOi
K00497

Database for complete collections of gene phylogenies

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PhylomeDBi
P15538

TreeFam database of animal gene trees

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TreeFami
TF105094

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.630.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR001128 Cyt_P450
IPR017972 Cyt_P450_CS
IPR002399 Cyt_P450_mitochondrial
IPR036396 Cyt_P450_sf

Pfam protein domain database

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Pfami
View protein in Pfam
PF00067 p450, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00408 MITP450
PR00385 P450

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48264 SSF48264, 1 hit

PROSITE; a protein domain and family database

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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>.<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 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« 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.

Note: No experimental confirmation available.
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
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>
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>

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 Publication1
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 Publication1
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:rs142484434Ensembl.1
Natural variantiVAR_074505158L → P in AH4; highly decreases steroid 11-beta-hydroxylase activity. 1 Publication1
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 Publication1
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 Publication1
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 Publication1
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 Publication1
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 Publication1
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 Publication1
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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<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]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.184927

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]
UniGeneiHs.184927

3D structure databases

ProteinModelPortaliP15538
SMRiP15538
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107956, 1 interactor
STRINGi9606.ENSP00000292427

Chemistry databases

BindingDBiP15538
ChEMBLiCHEMBL1908
DrugBankiDB04630 Aldosterone
DB00501 Cimetidine
DB00257 Clotrimazole
DB00292 Etomidate
DB00196 Fluconazole
DB00741 Hydrocortisone
DB01026 Ketoconazole
DB01233 Metoclopramide
DB01011 Metyrapone
DB01388 Mibefradil
DB01110 Miconazole
DB00648 Mitotane
DB00252 Phenytoin
DB00421 Spironolactone
GuidetoPHARMACOLOGYi1359
SwissLipidsiSLP:000001197

PTM databases

iPTMnetiP15538
PhosphoSitePlusiP15538

Polymorphism and mutation databases

BioMutaiCYP11B1
DMDMi215274267

Proteomic databases

PaxDbiP15538
PeptideAtlasiP15538
PRIDEiP15538
ProteomicsDBi53185
53186 [P15538-2]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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
HOVERGENiHBG051098
InParanoidiP15538
KOiK00497
PhylomeDBiP15538
TreeFamiTF105094

Enzyme and pathway databases

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

Protein Ontology

More...
PROi
PR:P15538

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
CleanExiHS_CYP11B1
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...

<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 5, 2018
This is version 198 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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