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UniProtKB - P08235 (MCR_HUMAN)

Entry version 227 (02 Dec 2020)
Sequence version 2 (12 Sep 2018)
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Protein

Mineralocorticoid receptor

Gene

NR3C2

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

Receptor for both mineralocorticoids (MC) such as aldosterone and glucocorticoids (GC) such as corticosterone or cortisol. Binds to mineralocorticoid response elements (MRE) and transactivates target genes. The effect of MC is to increase ion and water transport and thus raise extracellular fluid volume and blood pressure and lower potassium levels.1 Publication

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 sitei770Steroid1
Binding sitei776Steroid1
Binding sitei817Steroid1
Binding sitei945Steroid1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi603 – 668Nuclear receptorPROSITE-ProRule annotationAdd BLAST66
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri603 – 623NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri639 – 663NR C4-typePROSITE-ProRule annotationAdd BLAST25

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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding, Receptor
Biological processTranscription, Transcription regulation
LigandLipid-binding, Metal-binding, Steroid-binding, Zinc

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P08235

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-3371497, HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-HSA-383280, Nuclear Receptor transcription pathway
R-HSA-4090294, SUMOylation of intracellular receptors

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		P08235

SIGNOR Signaling Network Open Resource

More...SIGNORi		P08235

<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:
Mineralocorticoid receptor
Short name:
MR
Alternative name(s):
Nuclear receptor subfamily 3 group C member 2
<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:NR3C2
Synonyms:MCR, MLR
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%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 4

Organism-specific databases

Eukaryotic Pathogen and Host Database Resources

More...EuPathDBi		HostDB:ENSG00000151623.14

Human Gene Nomenclature Database

More...HGNCi		HGNC:7979, NR3C2

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		600983, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P08235

<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

Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

<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

Pseudohypoaldosteronism 1, autosomal dominant (PHA1A)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA salt wasting disease resulting from target organ unresponsiveness to mineralocorticoids. PHA1A is a mild form characterized by target organ defects confined to kidney. Patients may present with neonatal renal salt wasting with hyperkalaemic acidosis despite high aldosterone levels. These patients improve with age and usually become asymptomatic without treatment.
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_031268633G → R in PHA1A; reduces transcription transactivation upon aldosterone binding. 1 PublicationCorresponds to variant dbSNP:rs121912566EnsemblClinVar.1
Natural variantiVAR_031269645C → S in PHA1A. 1 Publication1
Natural variantiVAR_031270659R → S in PHA1A. 1 Publication1
Natural variantiVAR_031271759P → S in PHA1A. 1 Publication1
Natural variantiVAR_031272769L → P in PHA1A. 1 Publication1
Natural variantiVAR_031273770N → K in PHA1A. 1 Publication1
Natural variantiVAR_031274776Q → R in PHA1A; reduces aldosterone binding. 1 PublicationCorresponds to variant dbSNP:rs121912565EnsemblClinVar.1
Natural variantiVAR_031275805S → P in PHA1A. 1 Publication1
Natural variantiVAR_031276815S → R in PHA1A. 1 Publication1
Natural variantiVAR_031277818S → L in PHA1A; abolishes translocation to the nucleus and transcription transactivation upon aldosterone binding. 1 PublicationCorresponds to variant dbSNP:rs121912573EnsemblClinVar.1
Natural variantiVAR_015627924L → P in PHA1A; abolishes transcription transactivation upon aldosterone binding. 2 PublicationsCorresponds to variant dbSNP:rs121912563EnsemblClinVar.1
Natural variantiVAR_031278972E → G in PHA1A; reduces affinity for aldosterone and transcription transactivation. 1 PublicationCorresponds to variant dbSNP:rs121912574EnsemblClinVar.1
Natural variantiVAR_031279979L → P in PHA1A; loss of aldosterone binding and transcription transactivation. 1 PublicationCorresponds to variant dbSNP:rs121912567EnsemblClinVar.1
Early-onset hypertension with severe exacerbation in pregnancy (EOHSEP)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionInheritance is autosomal dominant. The disease is characterized by the onset of severe hypertension before the age of 20, and by suppression of aldosterone secretion.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_015626810S → L in EOHSEP; alters receptor specificity and leads to constitutive activation. 3 PublicationsCorresponds to variant dbSNP:rs41511344EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi767S → N: Loss of transcription transactivation. 1 Publication1
Mutagenesisi767S → Q: Strong decrease of transcription transactivation. 1 Publication1
Mutagenesisi770N → A, D, H, Q, S or T: Abolishes aldosterone binding and transcription transactivation. 2 Publications1
Mutagenesisi776Q → A: Reduces aldosterone binding and transcription transactivation. 2 Publications1
Mutagenesisi782K → E: Decreased coactivator binding. 1 Publication1
Mutagenesisi785K → E: Loss of coactivator binding. 1 Publication1
Mutagenesisi796E → R: Decreased coactivator binding. 1 Publication1
Mutagenesisi808C → S: Increases aldosterone-binding. 1 Publication1
Mutagenesisi810S → M: Alters receptor specificity. 1 Publication1
Mutagenesisi817R → A: Reduces aldosterone binding and transcription transactivation. 2 Publications1
Mutagenesisi849C → S: Strongly decreases affinity for aldosterone and transcription transactivation. 1 Publication1
Mutagenesisi942C → S: Abolishes steroid binding and transcription transactivation. 1 Publication1
Mutagenesisi945T → A: Decreases aldosterone-binding and cortisol-binding. 2 Publications1
Mutagenesisi952L → A: Reduces transcription transactivation. 1 Publication1
Mutagenesisi953K → A: Slightly reduces aldosterone binding and abolishes transcription transactivation. 1 Publication1
Mutagenesisi954V → A: Reduces aldosterone binding and abolishes transcription transactivation. 1 Publication1
Mutagenesisi956F → A: Abolishes aldosterone binding and transcription transactivation. 1 Publication1
Mutagenesisi957P → A: Slightly reduces aldosterone binding and transcription transactivation. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...DisGeNETi		4306

MalaCards human disease database

More...MalaCardsi		NR3C2
MIMi177735, phenotype
605115, phenotype

Open Targets

More...OpenTargetsi		ENSG00000151623

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

More...Orphaneti		171871, Renal pseudohypoaldosteronism type 1

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA242

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P08235, Tclin

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1994

Drug and drug target database

More...DrugBanki		DB04630, Aldosterone
DB01013, Clobetasol propionate
DB04652, Corticosterone
DB06780, Desoxycorticosterone acetate
DB01134, Desoxycorticosterone pivalate
DB01395, Drospirenone
DB00700, Eplerenone
DB01023, Felodipine
DB00687, Fludrocortisone
DB13867, Fluticasone
DB08906, Fluticasone furoate
DB00588, Fluticasone propionate
DB02998, Metribolone
DB00393, Nimodipine
DB00396, Progesterone
DB00421, Spironolactone
DB02901, Stanolone
DB13951, Stanolone acetate
DB00624, Testosterone
DB13943, Testosterone cypionate
DB13944, Testosterone enanthate
DB13946, Testosterone undecanoate

DrugCentral

More...DrugCentrali		P08235

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		626

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		NR3C2

Domain mapping of disease mutations (DMDM)

More...DMDMi		126885

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000536821 – 984Mineralocorticoid receptorAdd BLAST984

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei250PhosphoserineBy similarity1
Modified residuei259PhosphoserineBy similarity1
Modified residuei283PhosphoserineBy similarity1
Modified residuei287PhosphoserineBy similarity1
Modified residuei299PhosphoserineBy similarity1

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

Phosphorylated.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P08235

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P08235

MaxQB - The MaxQuant DataBase

More...MaxQBi		P08235

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

More...PaxDbi		P08235

PeptideAtlas

More...PeptideAtlasi		P08235

PRoteomics IDEntifications database

More...PRIDEi		P08235

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		2889
2891
52088 [P08235-1]
52089 [P08235-2]
52090 [P08235-3]
52091 [P08235-4]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P08235

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

More...PhosphoSitePlusi		P08235

<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

Ubiquitous. Highly expressed in distal tubules, convoluted tubules and cortical collecting duct in kidney, and in sweat glands. Detected at lower levels in cardiomyocytes, in epidermis and in colon enterocytes.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000151623, Expressed in colonic mucosa and 230 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P08235, baseline and differential

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000151623, Low tissue specificity

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Heteromultimeric cytoplasmic complex with HSP90, HSP70, and FKBP4, in the absence of ligand. After ligand binding, it translocates to the nucleus and binds to DNA as a homodimer and as a heterodimer with NR3C1. May interact with HSD11B2 in the absence of ligand. Binds the coactivators NCOA1, NCOA2, TIF1 and NRIP1.

4 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		110451, 32 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P08235

Protein interaction database and analysis system

More...IntActi		P08235, 7 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000350815

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P08235

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P08235, 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

1984
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P08235

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P08235

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini726 – 964NR LBDPROSITE-ProRule annotationAdd BLAST239

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>Regioni1 – 602ModulatingAdd BLAST602
Regioni669 – 725HingeAdd BLAST57
Regioni782 – 785Important for coactivator binding4

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.

<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 nuclear hormone receptor family. NR3 subfamily.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri603 – 623NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri639 – 663NR C4-typePROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3575, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000159333

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P08235

Identification of Orthologs from Complete Genome Data

More...OMAi		SFDGNCE

Database of Orthologous Groups

More...OrthoDBi		146963at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P08235

Family and domain databases

Database of protein disorder

More...DisProti		DP01561

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.565.10, 1 hit
3.30.50.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR035500, NHR-like_dom_sf
IPR000536, Nucl_hrmn_rcpt_lig-bd
IPR001628, Znf_hrmn_rcpt
IPR013088, Znf_NHR/GATA

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00104, Hormone_recep, 1 hit
PF00105, zf-C4, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00047, STROIDFINGER

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00430, HOLI, 1 hit
SM00399, ZnF_C4, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48508, SSF48508, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51843, NR_LBD, 1 hit
PS00031, NUCLEAR_REC_DBD_1, 1 hit
PS51030, NUCLEAR_REC_DBD_2, 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>Sequences (4)i

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

This entry describes 4 <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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P08235-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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METKGYHSLP EGLDMERRWG QVSQAVERSS LGPTERTDEN NYMEIVNVSC 
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VSGAIPNNST QGSSKEKQEL LPCLQQDNNR PGILTSDIKT ELESKELSAT 
       110        120        130        140        150
VAESMGLYMD SVRDADYSYE QQNQQGSMSP AKIYQNVEQL VKFYKGNGHR 
       160        170        180        190        200
PSTLSCVNTP LRSFMSDSGS SVNGGVMRAV VKSPIMCHEK SPSVCSPLNM 
       210        220        230        240        250
TSSVCSPAGI NSVSSTTASF GSFPVHSPIT QGTPLTCSPN VENRGSRSHS 
       260        270        280        290        300
PAHASNVGSP LSSPLSSMKS SISSPPSHCS VKSPVSSPNN VTLRSSVSSP 
       310        320        330        340        350
ANINNSRCSV SSPSNTNNRS TLSSPAASTV GSICSPVNNA FSYTASGTSA 
       360        370        380        390        400
GSSTLRDVVP SPDTQEKGAQ EVPFPKTEEV ESAISNGVTG QLNIVQYIKP 
       410        420        430        440        450
EPDGAFSSSC LGGNSKINSD SSFSVPIKQE STKHSCSGTS FKGNPTVNPF 
       460        470        480        490        500
PFMDGSYFSF MDDKDYYSLS GILGPPVPGF DGNCEGSGFP VGIKQEPDDG 
       510        520        530        540        550
SYYPEASIPS SAIVGVNSGG QSFHYRIGAQ GTISLSRSAR DQSFQHLSSF 
       560        570        580        590        600
PPVNTLVESW KSHGDLSSRR SDGYPVLEYI PENVSSSTLR SVSTGSSRPS 
       610        620        630        640        650
KICLVCGDEA SGCHYGVVTC GSCKVFFKRA VEGQHNYLCA GRNDCIIDKI 
       660        670        680        690        700
RRKNCPACRL QKCLQAGMNL GARKSKKLGK LKGIHEEQPQ QQQPPPPPPP 
       710        720        730        740        750
PQSPEEGTTY IAPAKEPSVN TALVPQLSTI SRALTPSPVM VLENIEPEIV 
       760        770        780        790        800
YAGYDSSKPD TAENLLSTLN RLAGKQMIQV VKWAKVLPGF KNLPLEDQIT 
       810        820        830        840        850
LIQYSWMCLS SFALSWRSYK HTNSQFLYFA PDLVFNEEKM HQSAMYELCQ 
       860        870        880        890        900
GMHQISLQFV RLQLTFEEYT IMKVLLLLST IPKDGLKSQA AFEEMRTNYI 
       910        920        930        940        950
KELRKMVTKC PNNSGQSWQR FYQLTKLLDS MHDLVSDLLE FCFYTFRESH 
       960        970        980 
ALKVEFPAML VEIISDQLPK VESGNAKPLY FHRK
Length:984
Mass (Da):107,082
Last modified:September 12, 2018 - 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:i833D900F2CB27390
GO
Isoform 2 (identifier: P08235-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     672-706: ARKSKKLGKLKGIHEEQPQQQQPPPPPPPPQSPEE → ERRCISLPCMNYARGCTKSAFSSFDCSSPLKNTPS
     707-984: Missing.

Note: Lacks steroid-binding activity and acts as ligand-independent transactivator.Curated
Show »
Length:706
Mass (Da):75,066
Checksum:i03CF63D0ACEE981C
GO
Isoform 3 (identifier: P08235-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     633-633: G → GKCSW

Show »
Length:988
Mass (Da):107,586
Checksum:iFDA63FAC05757193
GO
Isoform 4 (identifier: P08235-4) [UniParc]FASTAAdd to basket
Also known as: Delta

The sequence of this isoform differs from the canonical sequence as follows:
     672-788: Missing.

Show »
Length:867
Mass (Da):94,373
Checksum:i0F5055BFD6337578
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 conflicti946F → I in AAI11759 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0360637H → Q in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_014623180V → I Common polymorphism; decreased mineralocorticoid receptor activity. 3 PublicationsCorresponds to variant dbSNP:rs5522EnsemblClinVar.1
Natural variantiVAR_015625241V → A Polymorphism; changed mineralocorticoid receptor activity; changed response curve to aldosterone stimulation. 2 Publications1
Natural variantiVAR_014624444N → T1 PublicationCorresponds to variant dbSNP:rs5523EnsemblClinVar.1
Natural variantiVAR_014625537R → Q1 PublicationCorresponds to variant dbSNP:rs5526Ensembl.1
Natural variantiVAR_014626554N → S1 PublicationCorresponds to variant dbSNP:rs5527EnsemblClinVar.1
Natural variantiVAR_031268633G → R in PHA1A; reduces transcription transactivation upon aldosterone binding. 1 PublicationCorresponds to variant dbSNP:rs121912566EnsemblClinVar.1
Natural variantiVAR_031269645C → S in PHA1A. 1 Publication1
Natural variantiVAR_031270659R → S in PHA1A. 1 Publication1
Natural variantiVAR_031271759P → S in PHA1A. 1 Publication1
Natural variantiVAR_031272769L → P in PHA1A. 1 Publication1
Natural variantiVAR_031273770N → K in PHA1A. 1 Publication1
Natural variantiVAR_031274776Q → R in PHA1A; reduces aldosterone binding. 1 PublicationCorresponds to variant dbSNP:rs121912565EnsemblClinVar.1
Natural variantiVAR_031275805S → P in PHA1A. 1 Publication1
Natural variantiVAR_015626810S → L in EOHSEP; alters receptor specificity and leads to constitutive activation. 3 PublicationsCorresponds to variant dbSNP:rs41511344EnsemblClinVar.1
Natural variantiVAR_031276815S → R in PHA1A. 1 Publication1
Natural variantiVAR_031277818S → L in PHA1A; abolishes translocation to the nucleus and transcription transactivation upon aldosterone binding. 1 PublicationCorresponds to variant dbSNP:rs121912573EnsemblClinVar.1
Natural variantiVAR_029311826F → Y. Corresponds to variant dbSNP:rs13306592Ensembl.1
Natural variantiVAR_015627924L → P in PHA1A; abolishes transcription transactivation upon aldosterone binding. 2 PublicationsCorresponds to variant dbSNP:rs121912563EnsemblClinVar.1
Natural variantiVAR_031278972E → G in PHA1A; reduces affinity for aldosterone and transcription transactivation. 1 PublicationCorresponds to variant dbSNP:rs121912574EnsemblClinVar.1
Natural variantiVAR_031279979L → P in PHA1A; loss of aldosterone binding and transcription transactivation. 1 PublicationCorresponds to variant dbSNP:rs121912567EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_007357633G → GKCSW in isoform 3. Curated1
Alternative sequenceiVSP_007360672 – 788Missing in isoform 4. 2 PublicationsAdd BLAST117
Alternative sequenceiVSP_007358672 – 706ARKSK…QSPEE → ERRCISLPCMNYARGCTKSA FSSFDCSSPLKNTPS in isoform 2. 1 PublicationAdd BLAST35
Alternative sequenceiVSP_007359707 – 984Missing in isoform 2. 1 PublicationAdd BLAST278

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
M16801 mRNA Translation: AAA59571.1
AJ315514 mRNA Translation: CAC67405.1
AJ315515 mRNA Translation: CAC67406.1
EU326312 Genomic DNA Translation: ACA05924.1
EU326312 Genomic DNA Translation: ACA05925.1
FJ515829 Genomic DNA Translation: ACS13716.1
FJ515829 Genomic DNA Translation: ACS13717.1
AC069272 Genomic DNA No translation available.
AC093678 Genomic DNA No translation available.
AC093881 Genomic DNA No translation available.
AC104691 Genomic DNA No translation available.
AC106899 Genomic DNA No translation available.
BC111758 mRNA Translation: AAI11759.1
AH006913 Genomic DNA Translation: AAC63513.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS3772.1 [P08235-1]
CCDS54811.1 [P08235-4]

Protein sequence database of the Protein Information Resource

More...PIRi		A29513

NCBI Reference Sequences

More...RefSeqi		NP_000892.2, NM_000901.4 [P08235-1]
NP_001159576.1, NM_001166104.1 [P08235-4]
XP_011530277.1, XM_011531975.1 [P08235-3]
XP_011530278.1, XM_011531976.2
XP_011530279.1, XM_011531977.2
XP_016863706.1, XM_017008217.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000342437; ENSP00000343907; ENSG00000151623 [P08235-2]
ENST00000344721; ENSP00000341390; ENSG00000151623 [P08235-1]
ENST00000358102; ENSP00000350815; ENSG00000151623 [P08235-1]
ENST00000511528; ENSP00000421481; ENSG00000151623 [P08235-3]
ENST00000512865; ENSP00000423510; ENSG00000151623 [P08235-4]
ENST00000625323; ENSP00000486719; ENSG00000151623 [P08235-3]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		4306

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:4306

UCSC genome browser

More...UCSCi		uc003ilk.5, human [P08235-1]

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

<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

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Wikipedia

Mineralocorticoid receptor entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16801 mRNA Translation: AAA59571.1
AJ315514 mRNA Translation: CAC67405.1
AJ315515 mRNA Translation: CAC67406.1
EU326312 Genomic DNA Translation: ACA05924.1
EU326312 Genomic DNA Translation: ACA05925.1
FJ515829 Genomic DNA Translation: ACS13716.1
FJ515829 Genomic DNA Translation: ACS13717.1
AC069272 Genomic DNA No translation available.
AC093678 Genomic DNA No translation available.
AC093881 Genomic DNA No translation available.
AC104691 Genomic DNA No translation available.
AC106899 Genomic DNA No translation available.
BC111758 mRNA Translation: AAI11759.1
AH006913 Genomic DNA Translation: AAC63513.1
CCDSiCCDS3772.1 [P08235-1]
CCDS54811.1 [P08235-4]
PIRiA29513
RefSeqiNP_000892.2, NM_000901.4 [P08235-1]
NP_001159576.1, NM_001166104.1 [P08235-4]
XP_011530277.1, XM_011531975.1 [P08235-3]
XP_011530278.1, XM_011531976.2
XP_011530279.1, XM_011531977.2
XP_016863706.1, XM_017008217.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y9RX-ray1.96A/B731-984[»]
1YA3X-ray2.34A/B/C731-984[»]
2A3IX-ray1.95A732-984[»]
2AA2X-ray1.95A712-984[»]
2AA5X-ray2.20A/B712-984[»]
2AA6X-ray1.95A/B712-984[»]
2AA7X-ray2.20A712-984[»]
2AAXX-ray1.75A/B712-984[»]
2AB2X-ray1.85A/B712-984[»]
2ABIX-ray2.33A/B/C731-984[»]
2OAXX-ray2.29A/B/C/D/E/F731-984[»]
3VHUX-ray2.11A712-984[»]
3VHVX-ray1.35A727-984[»]
3WFFX-ray2.05A712-984[»]
3WFGX-ray1.40A712-984[»]
4PF3X-ray1.10A712-984[»]
4TNTX-ray2.39A/B593-671[»]
4UDAX-ray2.03A735-984[»]
4UDBX-ray2.36A735-984[»]
5HCVX-ray2.50A/B/C732-984[»]
5L7EX-ray1.86A735-984[»]
5L7GX-ray2.01A735-984[»]
5L7HX-ray1.84A735-984[»]
5MWPX-ray1.82A735-984[»]
5MWYX-ray1.75A735-984[»]
6GEVX-ray1.54A735-984[»]
6GG8X-ray1.80A735-984[»]
6GGGX-ray1.71A735-984[»]
6L88X-ray3.00A/B/C/D735-984[»]
SMRiP08235
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi110451, 32 interactors
CORUMiP08235
IntActiP08235, 7 interactors
STRINGi9606.ENSP00000350815

Chemistry databases

BindingDBiP08235
ChEMBLiCHEMBL1994
DrugBankiDB04630, Aldosterone
DB01013, Clobetasol propionate
DB04652, Corticosterone
DB06780, Desoxycorticosterone acetate
DB01134, Desoxycorticosterone pivalate
DB01395, Drospirenone
DB00700, Eplerenone
DB01023, Felodipine
DB00687, Fludrocortisone
DB13867, Fluticasone
DB08906, Fluticasone furoate
DB00588, Fluticasone propionate
DB02998, Metribolone
DB00393, Nimodipine
DB00396, Progesterone
DB00421, Spironolactone
DB02901, Stanolone
DB13951, Stanolone acetate
DB00624, Testosterone
DB13943, Testosterone cypionate
DB13944, Testosterone enanthate
DB13946, Testosterone undecanoate
DrugCentraliP08235
GuidetoPHARMACOLOGYi626

PTM databases

iPTMnetiP08235
PhosphoSitePlusiP08235

Polymorphism and mutation databases

BioMutaiNR3C2
DMDMi126885

Proteomic databases

jPOSTiP08235
MassIVEiP08235
MaxQBiP08235
PaxDbiP08235
PeptideAtlasiP08235
PRIDEiP08235
ProteomicsDBi2889
2891
52088 [P08235-1]
52089 [P08235-2]
52090 [P08235-3]
52091 [P08235-4]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		3971, 291 antibodies

Genome annotation databases

EnsembliENST00000342437; ENSP00000343907; ENSG00000151623 [P08235-2]
ENST00000344721; ENSP00000341390; ENSG00000151623 [P08235-1]
ENST00000358102; ENSP00000350815; ENSG00000151623 [P08235-1]
ENST00000511528; ENSP00000421481; ENSG00000151623 [P08235-3]
ENST00000512865; ENSP00000423510; ENSG00000151623 [P08235-4]
ENST00000625323; ENSP00000486719; ENSG00000151623 [P08235-3]
GeneIDi4306
KEGGihsa:4306
UCSCiuc003ilk.5, human [P08235-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		4306
DisGeNETi4306
EuPathDBiHostDB:ENSG00000151623.14

GeneCards: human genes, protein and diseases

More...GeneCardsi		NR3C2
HGNCiHGNC:7979, NR3C2
HPAiENSG00000151623, Low tissue specificity
MalaCardsiNR3C2
MIMi177735, phenotype
600983, gene
605115, phenotype
neXtProtiNX_P08235
OpenTargetsiENSG00000151623
Orphaneti171871, Renal pseudohypoaldosteronism type 1
PharmGKBiPA242

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3575, Eukaryota
GeneTreeiENSGT00940000159333
InParanoidiP08235
OMAiSFDGNCE
OrthoDBi146963at2759
PhylomeDBiP08235

Enzyme and pathway databases

PathwayCommonsiP08235
ReactomeiR-HSA-3371497, HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-HSA-383280, Nuclear Receptor transcription pathway
R-HSA-4090294, SUMOylation of intracellular receptors
SignaLinkiP08235
SIGNORiP08235

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		4306, 5 hits in 871 CRISPR screens

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

More...ChiTaRSi		NR3C2, human
EvolutionaryTraceiP08235

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Mineralocorticoid_receptor

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

More...GenomeRNAii		4306
PharosiP08235, Tclin

Protein Ontology

More...PROi		PR:P08235
RNActiP08235, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000151623, Expressed in colonic mucosa and 230 other tissues
ExpressionAtlasiP08235, baseline and differential

Family and domain databases

DisProtiDP01561
Gene3Di1.10.565.10, 1 hit
3.30.50.10, 1 hit
InterProiView protein in InterPro
IPR035500, NHR-like_dom_sf
IPR000536, Nucl_hrmn_rcpt_lig-bd
IPR001628, Znf_hrmn_rcpt
IPR013088, Znf_NHR/GATA
PfamiView protein in Pfam
PF00104, Hormone_recep, 1 hit
PF00105, zf-C4, 1 hit
PRINTSiPR00047, STROIDFINGER
SMARTiView protein in SMART
SM00430, HOLI, 1 hit
SM00399, ZnF_C4, 1 hit
SUPFAMiSSF48508, SSF48508, 1 hit
PROSITEiView protein in PROSITE
PS51843, NR_LBD, 1 hit
PS00031, NUCLEAR_REC_DBD_1, 1 hit
PS51030, NUCLEAR_REC_DBD_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

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

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMCR_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: P08235
Secondary accession number(s): B0ZBF5
, B0ZBF7, Q2NKL1, Q96KQ8, Q96KQ9
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: September 12, 2018
Last modified: December 2, 2020
This is version 227 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

3D-structure, Reference proteome

Documents

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