Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Corticosteroid 11-beta-dehydrogenase isozyme 2

Gene

HSD11B2

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

Catalyzes the conversion of cortisol to the inactive metabolite cortisone. Modulates intracellular glucocorticoid levels, thus protecting the nonselective mineralocorticoid receptor from occupation by glucocorticoids.

Miscellaneous

Consumption of large amounts of liquorice can lead to apparent mineralocorticoid excess and hypertension.

<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 describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by glycyrrhetinic acid (derived from liquorice), carbenoloxone and 11-alpha-OH-progesterone.By 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

  1. KM=26.1 nM for cortisol2 Publications
  2. KM=785 nM for cortisol2 Publications
  3. KM=77 nM for cortisterone2 Publications
  1. Vmax=64.1 nmol/h/mg enzyme toward cortisterone2 Publications
  2. Vmax=66 nmol/h/mg enzyme toward cortisol2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei219SubstrateBy similarity1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei232Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi82 – 111NADBy similarityAdd BLAST30

<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 functionOxidoreductase
LigandNAD

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.1.1.B40 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-194002 Glucocorticoid biosynthesis

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P80365

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P80365

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000000810

<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:
Corticosteroid 11-beta-dehydrogenase isozyme 2 (EC:1.1.1.-)
Alternative name(s):
11-beta-hydroxysteroid dehydrogenase type 2
Short name:
11-DH2
Short name:
11-beta-HSD2
11-beta-hydroxysteroid dehydrogenase type II
Short name:
11-HSD type II
Short name:
11-beta-HSD type II
NAD-dependent 11-beta-hydroxysteroid dehydrogenase
Short name:
11-beta-HSD
Short chain dehydrogenase/reductase family 9C member 3
<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:HSD11B2
Synonyms:HSD11K1 Publication, SDR9C3
<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 16

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000176387.6

Human Gene Nomenclature Database

More...
HGNCi
HGNC:5209 HSD11B2

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
614232 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P80365

<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

Endoplasmic reticulum, Microsome

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

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

Apparent mineralocorticoid excess (AME)12 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive form of low-renin hypertension. It is usually diagnosed within the first years of life and is characterized by polyuria and polydipsia, failure to thrive, hypernatremia, severe hypertension with low renin and aldosterone levels, profound hypokalemia with metabolic alkalosis, and most often nephrocalcinosis.
See also OMIM:218030
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_015634114 – 115Missing in AME; reduces enzyme activity by at least 95%. 1 Publication2
Natural variantiVAR_015635179L → R in AME; abolishes enzyme activity. 1 Publication1
Natural variantiVAR_015636180S → F in AME; reduces enzyme activity. 1 Publication1
Natural variantiVAR_015637186R → C in AME. 2 PublicationsCorresponds to variant dbSNP:rs768507002Ensembl.1
Natural variantiVAR_006958208R → C in AME; reduces enzyme activity by at least 95%. 3 PublicationsCorresponds to variant dbSNP:rs121917780EnsemblClinVar.1
Natural variantiVAR_015638208R → H in AME; abolishes enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs28934592EnsemblClinVar.1
Natural variantiVAR_006959213R → C in AME; reduces enzyme activity by 90%. 3 PublicationsCorresponds to variant dbSNP:rs28934591EnsemblClinVar.1
Natural variantiVAR_066514223D → N in AME; reduces enzyme activity to about 6% of wild type. 1 PublicationCorresponds to variant dbSNP:rs121917833EnsemblClinVar.1
Natural variantiVAR_015640237A → V in AME; reduces enzyme activity. 1 Publication1
Natural variantiVAR_015641244D → N in AME; associated with R-250. 1 Publication1
Natural variantiVAR_015643250 – 251LL → PS in AME; abolishes enzyme activity. 2
Natural variantiVAR_015642250L → R in AME; associated with N-244. 1 Publication1
Natural variantiVAR_015644279R → C in AME; decreases enzyme activity by 33%. 1 PublicationCorresponds to variant dbSNP:rs28934594EnsemblClinVar.1
Natural variantiVAR_015645328A → V in AME; abolishes enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs1453036708Ensembl.1
Natural variantiVAR_015647337 – 338RY → H in AME; abolishes enzyme activity. 4 Publications2
Natural variantiVAR_066515337R → C in AME; decreased half-life from 21 to 4 hours compared to wild-type, probably due to degradation via the proteasomal pathway. 3 PublicationsCorresponds to variant dbSNP:rs121917781EnsemblClinVar.1
Natural variantiVAR_015646338Y → H in AME; abolishes enzyme activity; decreased half-life from 21 to 3 hours compared to wild-type, probably due to degradation via the proteasomal pathway. 1 PublicationCorresponds to variant dbSNP:rs387907117EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi115E → K or Q: Abolishes cofactor specificity. 1 Publication1
Mutagenesisi335R → A or Q: Reduced enzyme activity. 1 Publication1
Mutagenesisi335R → K: No effect on enzyme activity. 1 Publication1
Mutagenesisi336R → A or Q: Almost complete loss of enzyme activity. 1 Publication1
Mutagenesisi336R → K: Reduced enzyme activity. 1 Publication1
Mutagenesisi337R → A or Q: Almost complete loss of enzyme activity. 1 Publication1
Mutagenesisi337R → K: Reduced enzyme activity. 1 Publication1
Mutagenesisi338Y → F or A: Complete loss of enzyme activity. 1 Publication1
Mutagenesisi339Y → A, F or H: Reduced enzyme activity. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
3291

MalaCards human disease database

More...
MalaCardsi
HSD11B2
MIMi218030 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000176387

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

More...
Orphaneti
320 Apparent mineralocorticoid excess

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA29477

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3746

Drug and drug target database

More...
DrugBanki
DB01569 Formebolone
DB00157 NADH

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
HSD11B2

Domain mapping of disease mutations (DMDM)

More...
DMDMi
30316367

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000546271 – 405Corticosteroid 11-beta-dehydrogenase isozyme 2Add BLAST405

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P80365

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P80365

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

More...
PaxDbi
P80365

PeptideAtlas

More...
PeptideAtlasi
P80365

PRoteomics IDEntifications database

More...
PRIDEi
P80365

ProteomicsDB human proteome resource

More...
ProteomicsDBi
57680

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P80365

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

More...
PhosphoSitePlusi
P80365

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

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

Expressed in kidney, pancreas, prostate, ovary, small intestine and colon. At midgestation, expressed at high levels in placenta and in fetal kidney and, at much lower levels, in fetal lung and testis (PubMed:8530071).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000176387 Expressed in 113 organ(s), highest expression level in adult mammalian kidney

CleanEx database of gene expression profiles

More...
CleanExi
HS_HSD11B2

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P80365 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P80365 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB032443
HPA042186
HPA056385

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

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

Interacts with ligand-free cytoplasmic NR3C2.1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
109524, 6 interactors

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000316786

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P80365

<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

More...
ProteinModelPortali
P80365

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni335 – 339Essential for protein stability5

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1610 Eukaryota
ENOG410Y7FK LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000159716

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG005482

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P80365

KEGG Orthology (KO)

More...
KOi
K00071

Identification of Orthologs from Complete Genome Data

More...
OMAi
FPCLAAY

Database of Orthologous Groups

More...
OrthoDBi
EOG091G0LMI

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P80365

TreeFam database of animal gene trees

More...
TreeFami
TF325617

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036291 NAD(P)-bd_dom_sf
IPR020904 Sc_DH/Rdtase_CS
IPR002347 SDR_fam

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00106 adh_short, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00081 GDHRDH

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51735 SSF51735, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00061 ADH_SHORT, 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>Sequence (1+)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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P80365-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MERWPWPSGG AWLLVAARAL LQLLRSDLRL GRPLLAALAL LAALDWLCQR
60 70 80 90 100
LLPPPAALAV LAAAGWIALS RLARPQRLPV ATRAVLITGC DSGFGKETAK
110 120 130 140 150
KLDSMGFTVL ATVLELNSPG AIELRTCCSP RLRLLQMDLT KPGDISRVLE
160 170 180 190 200
FTKAHTTSTG LWGLVNNAGH NEVVADAELS PVATFRSCME VNFFGALELT
210 220 230 240 250
KGLLPLLRSS RGRIVTVGSP AGDMPYPCLG AYGTSKAAVA LLMDTFSCEL
260 270 280 290 300
LPWGVKVSII QPGCFKTESV RNVGQWEKRK QLLLANLPQE LLQAYGKDYI
310 320 330 340 350
EHLHGQFLHS LRLAMSDLTP VVDAITDALL AARPRRRYYP GQGLGLMYFI
360 370 380 390 400
HYYLPEGLRR RFLQAFFISH CLPRALQPGQ PGTTPPQDAA QDPNLSPGPS

PAVAR
Length:405
Mass (Da):44,127
Last modified:April 30, 2003 - v2
<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:i4AB269E269982D24
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
R4GN04R4GN04_HUMAN
Corticosteroid 11-beta-dehydrogenas...
HSD11B2
58Annotation score:

Annotation score:1 out of 5

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti148V → F in AAB48544 (PubMed:8530071).Curated1
Sequence conflicti148V → L in AAA91969 (PubMed:7859916).Curated1
Sequence conflicti350I → T in AAH64536 (PubMed:15489334).Curated1
Sequence conflicti392D → G in AAH36780 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_015634114 – 115Missing in AME; reduces enzyme activity by at least 95%. 1 Publication2
Natural variantiVAR_052317147R → H. Corresponds to variant dbSNP:rs13306425EnsemblClinVar.1
Natural variantiVAR_015635179L → R in AME; abolishes enzyme activity. 1 Publication1
Natural variantiVAR_015636180S → F in AME; reduces enzyme activity. 1 Publication1
Natural variantiVAR_015637186R → C in AME. 2 PublicationsCorresponds to variant dbSNP:rs768507002Ensembl.1
Natural variantiVAR_006958208R → C in AME; reduces enzyme activity by at least 95%. 3 PublicationsCorresponds to variant dbSNP:rs121917780EnsemblClinVar.1
Natural variantiVAR_015638208R → H in AME; abolishes enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs28934592EnsemblClinVar.1
Natural variantiVAR_006959213R → C in AME; reduces enzyme activity by 90%. 3 PublicationsCorresponds to variant dbSNP:rs28934591EnsemblClinVar.1
Natural variantiVAR_066514223D → N in AME; reduces enzyme activity to about 6% of wild type. 1 PublicationCorresponds to variant dbSNP:rs121917833EnsemblClinVar.1
Natural variantiVAR_015639227P → L in hypertension; decreases affinity for cortisol. 1 PublicationCorresponds to variant dbSNP:rs121917782EnsemblClinVar.1
Natural variantiVAR_015640237A → V in AME; reduces enzyme activity. 1 Publication1
Natural variantiVAR_015641244D → N in AME; associated with R-250. 1 Publication1
Natural variantiVAR_015643250 – 251LL → PS in AME; abolishes enzyme activity. 2
Natural variantiVAR_015642250L → R in AME; associated with N-244. 1 Publication1
Natural variantiVAR_015644279R → C in AME; decreases enzyme activity by 33%. 1 PublicationCorresponds to variant dbSNP:rs28934594EnsemblClinVar.1
Natural variantiVAR_015645328A → V in AME; abolishes enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs1453036708Ensembl.1
Natural variantiVAR_015647337 – 338RY → H in AME; abolishes enzyme activity. 4 Publications2
Natural variantiVAR_066515337R → C in AME; decreased half-life from 21 to 4 hours compared to wild-type, probably due to degradation via the proteasomal pathway. 3 PublicationsCorresponds to variant dbSNP:rs121917781EnsemblClinVar.1
Natural variantiVAR_015646338Y → H in AME; abolishes enzyme activity; decreased half-life from 21 to 3 hours compared to wild-type, probably due to degradation via the proteasomal pathway. 1 PublicationCorresponds to variant dbSNP:rs387907117EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U14631 mRNA Translation: AAA91969.1
U27317 Genomic DNA Translation: AAB48544.1
U26726 mRNA Translation: AAC50356.1
EF694683 Genomic DNA Translation: ABS29267.1
FJ515828 Genomic DNA Translation: ACS13714.1
CH471092 Genomic DNA Translation: EAW83134.1
BC036780 mRNA Translation: AAH36780.1
BC064536 mRNA Translation: AAH64536.1
AY046280 Genomic DNA Translation: AAK91586.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS10837.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S62789

NCBI Reference Sequences

More...
RefSeqi
NP_000187.3, NM_000196.3

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.1376

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000326152; ENSP00000316786; ENSG00000176387

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
3291

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:3291

UCSC genome browser

More...
UCSCi
uc002etd.4 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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14631 mRNA Translation: AAA91969.1
U27317 Genomic DNA Translation: AAB48544.1
U26726 mRNA Translation: AAC50356.1
EF694683 Genomic DNA Translation: ABS29267.1
FJ515828 Genomic DNA Translation: ACS13714.1
CH471092 Genomic DNA Translation: EAW83134.1
BC036780 mRNA Translation: AAH36780.1
BC064536 mRNA Translation: AAH64536.1
AY046280 Genomic DNA Translation: AAK91586.1
CCDSiCCDS10837.1
PIRiS62789
RefSeqiNP_000187.3, NM_000196.3
UniGeneiHs.1376

3D structure databases

ProteinModelPortaliP80365
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109524, 6 interactors
STRINGi9606.ENSP00000316786

Chemistry databases

BindingDBiP80365
ChEMBLiCHEMBL3746
DrugBankiDB01569 Formebolone
DB00157 NADH
SwissLipidsiSLP:000000810

PTM databases

iPTMnetiP80365
PhosphoSitePlusiP80365

Polymorphism and mutation databases

BioMutaiHSD11B2
DMDMi30316367

Proteomic databases

EPDiP80365
MaxQBiP80365
PaxDbiP80365
PeptideAtlasiP80365
PRIDEiP80365
ProteomicsDBi57680

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000326152; ENSP00000316786; ENSG00000176387
GeneIDi3291
KEGGihsa:3291
UCSCiuc002etd.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3291
DisGeNETi3291
EuPathDBiHostDB:ENSG00000176387.6

GeneCards: human genes, protein and diseases

More...
GeneCardsi
HSD11B2
HGNCiHGNC:5209 HSD11B2
HPAiCAB032443
HPA042186
HPA056385
MalaCardsiHSD11B2
MIMi218030 phenotype
614232 gene
neXtProtiNX_P80365
OpenTargetsiENSG00000176387
Orphaneti320 Apparent mineralocorticoid excess
PharmGKBiPA29477

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1610 Eukaryota
ENOG410Y7FK LUCA
GeneTreeiENSGT00940000159716
HOVERGENiHBG005482
InParanoidiP80365
KOiK00071
OMAiFPCLAAY
OrthoDBiEOG091G0LMI
PhylomeDBiP80365
TreeFamiTF325617

Enzyme and pathway databases

BRENDAi1.1.1.B40 2681
ReactomeiR-HSA-194002 Glucocorticoid biosynthesis
SABIO-RKiP80365
SIGNORiP80365

Miscellaneous databases

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

More...
ChiTaRSi
HSD11B2 human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Corticosteroid_11-beta-dehydrogenase_isozyme_2

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

More...
GenomeRNAii
3291

Protein Ontology

More...
PROi
PR:P80365

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000176387 Expressed in 113 organ(s), highest expression level in adult mammalian kidney
CleanExiHS_HSD11B2
ExpressionAtlasiP80365 baseline and differential
GenevisibleiP80365 HS

Family and domain databases

InterProiView protein in InterPro
IPR036291 NAD(P)-bd_dom_sf
IPR020904 Sc_DH/Rdtase_CS
IPR002347 SDR_fam
PfamiView protein in Pfam
PF00106 adh_short, 1 hit
PRINTSiPR00081 GDHRDH
SUPFAMiSSF51735 SSF51735, 1 hit
PROSITEiView protein in PROSITE
PS00061 ADH_SHORT, 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 nameiDHI2_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: P80365
Secondary accession number(s): A7LB28
, C5HTY7, Q13194, Q6P2G9, Q8N439, Q96QN8, Q9UC50, Q9UC51, Q9UCW5, Q9UCW6, Q9UCW7, Q9UCW8
<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: February 1, 1995
Last sequence update: April 30, 2003
Last modified: December 5, 2018
This is version 180 of the entry and version 2 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. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again