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Entry version 206 (22 Apr 2020)
Sequence version 3 (15 Jul 1998)
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Protein

Cytochrome P450 11B2, mitochondrial

Gene

CYP11B2

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 that catalyzes the biosynthesis of adrenal mineralocorticoid aldosterone (PubMed:11856349, PubMed:23322723, PubMed:1594605, PubMed:9814506). Catalyzes three sequential oxidative reactions of 11-deoxycorticosterone/21-hydroxyprogesterone, namely 11-beta hydroxylation followed with two successive oxidations at C18 to yield 18-hydroxy and then 18-aldehyde derivatives, resulting in the formation of aldosterone (PubMed:11856349, PubMed:23322723, PubMed:1594605, PubMed:9814506). 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:11856349, PubMed:23322723, PubMed:1594605, PubMed:9814506).4 Publications

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

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

heme1 Publication

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

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei38111-deoxycorticosterone; via carbonyl oxygenCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi450Iron (heme axial ligand)Combined sources1 Publication1

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

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

More...
BioCyci
MetaCyc:HS11355-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-193993 Mineralocorticoid biosynthesis
R-HSA-194002 Glucocorticoid biosynthesis
R-HSA-211976 Endogenous sterols
R-HSA-5579009 Defective CYP11B2 causes Corticosterone methyloxidase 1 deficiency (CMO-1 deficiency)

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P19099

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000001198

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Cytochrome P450 11B2, mitochondrial
Alternative name(s):
Aldosterone synthase1 Publication
Short name:
ALDOS
Aldosterone-synthesizing enzyme
CYPXIB2
Corticosterone 18-monooxygenase, CYP11B2 (EC:1.14.15.54 Publications)
Cytochrome P-450Aldo
Cytochrome P-450C18
Steroid 11-beta-hydroxylase, CYP11B21 Publication (EC:1.14.15.41 Publication)
Steroid 18-hydroxylase1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CYP11B21 PublicationImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 8

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:2592 CYP11B2

Online Mendelian Inheritance in Man (OMIM)

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MIMi
124080 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P19099

<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

Corticosterone methyloxidase 1 deficiency (CMO-1 deficiency)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal recessive disorder of aldosterone biosynthesis. There are two biochemically different forms of selective aldosterone deficiency be termed corticosterone methyloxidase (CMO) deficiency type 1 and type 2. In CMO-1 deficiency, aldosterone is undetectable in plasma, while its immediate precursor, 18-hydroxycorticosterone, is low or normal.
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_018470140N → NRL in CMO-1 deficiency; the enzyme is inactive. 1
Natural variantiVAR_018472461L → P in CMO-1 deficiency; abolishes the 18-hydroxylase activity required for conversion of 11-deoxycorticosterone to aldosterone. 1 PublicationCorresponds to variant dbSNP:rs72554627EnsemblClinVar.1
Corticosterone methyloxidase 2 deficiency (CMO-2 deficiency)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal recessive disorder of aldosterone biosynthesis. In CMO-2 deficiency, aldosterone can be low or normal, but at the expense of increased secretion of 18-hydroxycorticosterone. Consequently, patients have a greatly increased ratio of 18-hydroxycorticosterone to aldosterone and a low ratio of corticosterone to 18-hydroxycorticosterone in serum.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_001267181R → W in CMO-2 deficiency; reduces 18-hydroxylase and abolishes 18-oxidase activities; leaves 11 beta-hydroxylase activity intact. 2 PublicationsCorresponds to variant dbSNP:rs28931609EnsemblClinVar.1
Natural variantiVAR_018471185T → I in CMO-2 deficiency. 2 PublicationsCorresponds to variant dbSNP:rs121912978EnsemblClinVar.1
Natural variantiVAR_001268198E → D in CMO-2 deficiency; slightly reduced 11-beta-hydroxylase activity, greatly decreased 18-hydroxylase activity and absent 18-oxidase activity when associated with A-386.. 1 PublicationCorresponds to variant dbSNP:rs104894072EnsemblClinVar.1
Natural variantiVAR_001269386V → A in CMO-2 deficiency; small but consistent reduction in the production of 18-hydroxycorticosterone; slightly reduced 11-beta-hydroxylase activity, greatly decreased 18-hydroxylase activity and absent 18-oxidase activity when associated with D-198.. 5 PublicationsCorresponds to variant dbSNP:rs61757294EnsemblClinVar.1
Natural variantiVAR_018473498T → A in CMO-2 deficiency. 1 PublicationCorresponds to variant dbSNP:rs72554626EnsemblClinVar.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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi112I → P: Increases 11-beta- and 18-hydroxylase activites toward 11-deoxycorticosterone; increases 11-beta-hydroxylase activity toward 11-deoxycortisol. 1 Publication1
Mutagenesisi147D → E: Increases 11-beta-hydroxylase activity toward 11-deoxycorticosterone and 11-deoxycortisol. 1 Publication1
Mutagenesisi152K → N: No significant effect on hydroxylase activities toward 11-deoxycorticosterone and 11-deoxycortisol. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
1585

MalaCards human disease database

More...
MalaCardsi
CYP11B2
MIMi103900 phenotype
203400 phenotype
610600 phenotype

Open Targets

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OpenTargetsi
ENSG00000179142

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

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Orphaneti
403 Familial hyperaldosteronism type I
427 Familial hypoaldosteronism

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA134

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
P19099 Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2722

Drug and drug target database

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DrugBanki
DB04630 Aldosterone
DB00700 Eplerenone
DB00292 Etomidate
DB00741 Hydrocortisone
DB14539 Hydrocortisone acetate
DB14540 Hydrocortisone butyrate
DB14543 Hydrocortisone probutate
DB14545 Hydrocortisone succinate
DB14544 Hydrocortisone valerate
DB01011 Metyrapone
DB01388 Mibefradil
DB00421 Spironolactone
DB06281 Torcetrapib

DrugCentral

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DrugCentrali
P19099

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1360

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
CYP11B2

Domain mapping of disease mutations (DMDM)

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DMDMi
3041666

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000359725 – 503Cytochrome P450 11B2, mitochondrialAdd BLAST479

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P19099

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
P19099

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

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PaxDbi
P19099

PeptideAtlas

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PeptideAtlasi
P19099

PRoteomics IDEntifications database

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PRIDEi
P19099

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
53632

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P19099

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

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PhosphoSitePlusi
P19099

<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
ENSG00000179142 Expressed in left adrenal gland and 41 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P19099 HS

Organism-specific databases

Human Protein Atlas

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HPAi
ENSG00000179142 Tissue enriched (adrenal)

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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
107957, 7 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000325822

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P19099

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
P19099 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

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SMRi
P19099

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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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

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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
CLU_001570_28_4_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P19099

KEGG Orthology (KO)

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KOi
K07433

Identification of Orthologs from Complete Genome Data

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OMAi
HTGRNGW

Database of Orthologous Groups

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OrthoDBi
481145at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P19099

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

More...
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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

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

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is 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.

P19099-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MALRAKAEVC VAAPWLSLQR ARALGTRAAR APRTVLPFEA MPQHPGNRWL
60 70 80 90 100
RLLQIWREQG YEHLHLEMHQ TFQELGPIFR YNLGGPRMVC VMLPEDVEKL
110 120 130 140 150
QQVDSLHPCR MILEPWVAYR QHRGHKCGVF LLNGPEWRFN RLRLNPDVLS
160 170 180 190 200
PKAVQRFLPM VDAVARDFSQ ALKKKVLQNA RGSLTLDVQP SIFHYTIEAS
210 220 230 240 250
NLALFGERLG LVGHSPSSAS LNFLHALEVM FKSTVQLMFM PRSLSRWISP
260 270 280 290 300
KVWKEHFEAW DCIFQYGDNC IQKIYQELAF NRPQHYTGIV AELLLKAELS
310 320 330 340 350
LEAIKANSME LTAGSVDTTA FPLLMTLFEL ARNPDVQQIL RQESLAAAAS
360 370 380 390 400
ISEHPQKATT ELPLLRAALK ETLRLYPVGL FLERVVSSDL VLQNYHIPAG
410 420 430 440 450
TLVQVFLYSL GRNAALFPRP ERYNPQRWLD IRGSGRNFHH VPFGFGMRQC
460 470 480 490 500
LGRRLAEAEM LLLLHHVLKH FLVETLTQED IKMVYSFILR PGTSPLLTFR

AIN
Length:503
Mass (Da):57,560
Last modified:July 15, 1998 - v3
<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:i42BA671704CEE35D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti17S → C in AAA35741 (PubMed:2592361).Curated1
Sequence conflicti55I → M in AAA35741 (PubMed:2592361).Curated1
Sequence conflicti119Y → I in AAA35741 (PubMed:2592361).Curated1
Sequence conflicti249S → R in CAA38539 (PubMed:2256920).Curated1
Sequence conflicti342Q → K in AAA35741 (PubMed:2592361).Curated1
Sequence conflicti438F → L in AAA35741 (PubMed:2592361).Curated1
Sequence conflicti470H → R in AAA35741 (PubMed:2592361).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01415129A → T1 PublicationCorresponds to variant dbSNP:rs6438Ensembl.1
Natural variantiVAR_01415230R → Q1 PublicationCorresponds to variant dbSNP:rs6441EnsemblClinVar.1
Natural variantiVAR_018470140N → NRL in CMO-1 deficiency; the enzyme is inactive. 1
Natural variantiVAR_001266173K → R3 PublicationsCorresponds to variant dbSNP:rs4539EnsemblClinVar.1
Natural variantiVAR_001267181R → W in CMO-2 deficiency; reduces 18-hydroxylase and abolishes 18-oxidase activities; leaves 11 beta-hydroxylase activity intact. 2 PublicationsCorresponds to variant dbSNP:rs28931609EnsemblClinVar.1
Natural variantiVAR_018471185T → I in CMO-2 deficiency. 2 PublicationsCorresponds to variant dbSNP:rs121912978EnsemblClinVar.1
Natural variantiVAR_001268198E → D in CMO-2 deficiency; slightly reduced 11-beta-hydroxylase activity, greatly decreased 18-hydroxylase activity and absent 18-oxidase activity when associated with A-386.. 1 PublicationCorresponds to variant dbSNP:rs104894072EnsemblClinVar.1
Natural variantiVAR_014643222N → T. Corresponds to variant dbSNP:rs5308Ensembl.1
Natural variantiVAR_014153248I → T2 PublicationsCorresponds to variant dbSNP:rs4547Ensembl.1
Natural variantiVAR_014154281N → S2 PublicationsCorresponds to variant dbSNP:rs4537EnsemblClinVar.1
Natural variantiVAR_014155339I → T2 PublicationsCorresponds to variant dbSNP:rs4544EnsemblClinVar.1
Natural variantiVAR_014644383E → V. Corresponds to variant dbSNP:rs5312Ensembl.1
Natural variantiVAR_001269386V → A in CMO-2 deficiency; small but consistent reduction in the production of 18-hydroxycorticosterone; slightly reduced 11-beta-hydroxylase activity, greatly decreased 18-hydroxylase activity and absent 18-oxidase activity when associated with D-198.. 5 PublicationsCorresponds to variant dbSNP:rs61757294EnsemblClinVar.1
Natural variantiVAR_014645403V → E. Corresponds to variant dbSNP:rs5315Ensembl.1
Natural variantiVAR_014156435G → S2 PublicationsCorresponds to variant dbSNP:rs4545EnsemblClinVar.1
Natural variantiVAR_018472461L → P in CMO-1 deficiency; abolishes the 18-hydroxylase activity required for conversion of 11-deoxycorticosterone to aldosterone. 1 PublicationCorresponds to variant dbSNP:rs72554627EnsemblClinVar.1
Natural variantiVAR_014646487F → V. Corresponds to variant dbSNP:rs5317Ensembl.1
Natural variantiVAR_018473498T → A in CMO-2 deficiency. 1 PublicationCorresponds to variant dbSNP:rs72554626EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M32881, M32864, M32880 Genomic DNA Translation: AAA35741.1
X54741 mRNA Translation: CAA38539.1
D13752 Genomic DNA Translation: BAA02899.1
EU326306 Genomic DNA Translation: ACA05912.1
CH471162 Genomic DNA Translation: EAW82292.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS6393.1

Protein sequence database of the Protein Information Resource

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PIRi
B34181

NCBI Reference Sequences

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RefSeqi
NP_000489.3, NM_000498.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000323110; ENSP00000325822; ENSG00000179142

Database of genes from NCBI RefSeq genomes

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GeneIDi
1585

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:1585

UCSC genome browser

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UCSCi
uc003yxk.1 human

Keywords - Coding sequence diversityi

Polymorphism

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

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

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

Wikipedia

CYP11B2 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32881, M32864, M32880 Genomic DNA Translation: AAA35741.1
X54741 mRNA Translation: CAA38539.1
D13752 Genomic DNA Translation: BAA02899.1
EU326306 Genomic DNA Translation: ACA05912.1
CH471162 Genomic DNA Translation: EAW82292.1
CCDSiCCDS6393.1
PIRiB34181
RefSeqiNP_000489.3, NM_000498.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4DVQX-ray2.49A/B/C/D/E/F/G/H/I/J/K/L34-503[»]
4FDHX-ray2.71A/B/C/D/E/F/G/H/I/J/K/L34-503[»]
4ZGXX-ray3.20A/B/C/D/E/F/G/H/I/J/K/L28-503[»]
SMRiP19099
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi107957, 7 interactors
STRINGi9606.ENSP00000325822

Chemistry databases

BindingDBiP19099
ChEMBLiCHEMBL2722
DrugBankiDB04630 Aldosterone
DB00700 Eplerenone
DB00292 Etomidate
DB00741 Hydrocortisone
DB14539 Hydrocortisone acetate
DB14540 Hydrocortisone butyrate
DB14543 Hydrocortisone probutate
DB14545 Hydrocortisone succinate
DB14544 Hydrocortisone valerate
DB01011 Metyrapone
DB01388 Mibefradil
DB00421 Spironolactone
DB06281 Torcetrapib
DrugCentraliP19099
GuidetoPHARMACOLOGYi1360
SwissLipidsiSLP:000001198

PTM databases

iPTMnetiP19099
PhosphoSitePlusiP19099

Polymorphism and mutation databases

BioMutaiCYP11B2
DMDMi3041666

Proteomic databases

jPOSTiP19099
MassIVEiP19099
PaxDbiP19099
PeptideAtlasiP19099
PRIDEiP19099
ProteomicsDBi53632

Protocols and materials databases

Antibodypedia a portal for validated antibodies

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Antibodypediai
14554 225 antibodies

The DNASU plasmid repository

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DNASUi
1585

Genome annotation databases

EnsembliENST00000323110; ENSP00000325822; ENSG00000179142
GeneIDi1585
KEGGihsa:1585
UCSCiuc003yxk.1 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
1585
DisGeNETi1585

GeneCards: human genes, protein and diseases

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GeneCardsi
CYP11B2
HGNCiHGNC:2592 CYP11B2
HPAiENSG00000179142 Tissue enriched (adrenal)
MalaCardsiCYP11B2
MIMi103900 phenotype
124080 gene
203400 phenotype
610600 phenotype
neXtProtiNX_P19099
OpenTargetsiENSG00000179142
Orphaneti403 Familial hyperaldosteronism type I
427 Familial hypoaldosteronism
PharmGKBiPA134

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0159 Eukaryota
COG2124 LUCA
GeneTreeiENSGT00940000163354
HOGENOMiCLU_001570_28_4_1
InParanoidiP19099
KOiK07433
OMAiHTGRNGW
OrthoDBi481145at2759
PhylomeDBiP19099
TreeFamiTF105094

Enzyme and pathway databases

BioCyciMetaCyc:HS11355-MONOMER
BRENDAi1.14.15.4 2681
ReactomeiR-HSA-193993 Mineralocorticoid biosynthesis
R-HSA-194002 Glucocorticoid biosynthesis
R-HSA-211976 Endogenous sterols
R-HSA-5579009 Defective CYP11B2 causes Corticosterone methyloxidase 1 deficiency (CMO-1 deficiency)
SIGNORiP19099

Miscellaneous databases

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
Aldosterone_synthase

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

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GenomeRNAii
1585
PharosiP19099 Tchem

Protein Ontology

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PROi
PR:P19099
RNActiP19099 protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000179142 Expressed in left adrenal gland and 41 other tissues
GenevisibleiP19099 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

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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 nameiC11B2_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: P19099
Secondary accession number(s): B0ZBE4, Q16726
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: July 15, 1998
Last modified: April 22, 2020
This is version 206 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

3D-structure, Reference proteome

Documents

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