Skip Header

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

UniProtKB - P10826 (RARB_HUMAN)

Entry version 236 (22 Apr 2020)
Sequence version 2 (16 Nov 2001)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Retinoic acid receptor beta

Gene

RARB

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 retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence or presence of hormone ligand, acts mainly as an activator of gene expression due to weak binding to corepressors (PubMed:12554770). The RXRA/RARB heterodimer can act as a repressor on the DR1 element and as an activator on the DR5 element (PubMed:29021580). In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function (By similarity).By similarity2 Publications

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 bindingi88 – 153Nuclear 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 fingeri88 – 108NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri124 – 148NR 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
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-383280 Nuclear Receptor transcription pathway
R-HSA-5362517 Signaling by Retinoic Acid
R-HSA-5617472 Activation of anterior HOX genes in hindbrain development during early embryogenesis

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

More...SignaLinki		P10826

SIGNOR Signaling Network Open Resource

More...SIGNORi		P10826

<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:
Retinoic acid receptor beta
Short name:
RAR-beta
Alternative name(s):
HBV-activated protein
Nuclear receptor subfamily 1 group B member 2
RAR-epsilon
<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:RARB
Synonyms:HAP, NR1B2
<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 3

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:9865 RARB

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		180220 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P10826

<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, 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

Microphthalmia, syndromic, 12 (MCOPS12)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of microphthalmia, a disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues (anophthalmia). In many cases, microphthalmia/anophthalmia occurs in association with syndromes that include non-ocular abnormalities. MCOPS12 patients manifest variable features, including diaphragmatic hernia, pulmonary hypoplasia, and cardiac abnormalities.
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_077141220L → P in MCOPS12; increased transcriptional response to retinoic acid ligands. 1 Publication1
Natural variantiVAR_077142303G → A in MCOPS12; increased transcriptional response to retinoic acid ligands. 1 Publication1
Natural variantiVAR_070780394R → C in MCOPS12; increased transcriptional response to retinoic acid ligands. 2 Publications1
Natural variantiVAR_070781394R → S in MCOPS12; increases transcriptional response to retinoic acid. 1 Publication1

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>Mutagenesisi106E → A: As a heterodimer with RXRA, abolishes transcriptional repression on DR1, reduces transcriptional activation on DR5 and binding affinity for DR1 and DR5 DNA elements. 1 Publication1
Mutagenesisi113R → A: As a heterodimer with RXRA, abolishes transcriptional repression on DR1 and reduces transcriptional activation on DR5. 1 Publication1
Mutagenesisi120M → E: As a heterodimer with RXRA, reduces transcriptional repression on DR1 and reduces transcriptional activation on DR5. Reduces binding affinity for DR1 and DR5 DNA elements; when associated with E-366. 1 Publication1
Mutagenesisi123T → V: Reduces transcriptional repression on DR1 and reduces transcriptional activation on DR5; when associated with E-369 and E-370. 1
Mutagenesisi188T → I: No effect on transcriptional activation in the absence of hormone. 1 Publication1
Mutagenesisi191I → V: No effect on transcriptional activation in the absence of hormone. 1 Publication1
Mutagenesisi222L → I: Reduced transcriptional activation in the absence of hormone. Even greater reduction in transcriptional activation in the absence of hormone; when associated with D-223 or S-232. Great reduction in transcriptional activation in the absence of hormone; when associated with D-223 and S-232. 1 Publication1
Mutagenesisi223G → D: Greatly reduced transcriptional activation in the absence of hormone. Even greater reduction in transcriptional activation in the absence of hormone; when associated with I-222 or S-232. Great reduction in transcriptional activation in the absence of hormone; when associated with I-222 and S-232. 1 Publication1
Mutagenesisi232A → S: Reduced transcriptional activation in the absence of hormone. Some further reduction of transcriptional activity in the absence of hormone; when associated with I-222 or D-223. Great reduction in transcriptional activation in the absence of hormone; when associated with I-222 and D-223. 1 Publication1
Mutagenesisi365K → E: As a heterodimer with RXRA, reduces transcriptional repression on DR1 and reduces transcriptional activation on DR5. Reduces transcriptional repression on DR1 and reduces transcriptional activation on DR5; when associated with E-366 and E-367. 1 Publication1
Mutagenesisi366R → E: As a heterodimer with RXRA, reduces binding affinity for DR5 DNA element and no change in binding to DR1. Reduces transcriptional repression on DR1 and reduces transcriptional activation on DR5; when associated with E-365 and E-367. Reduces binding affinity for DR1 and DR5 DNA elements; when associated with E-120. 1 Publication1
Mutagenesisi367R → E: As a heterodimer with RXRA, reduces transcriptional repression on DR1 and reduces transcriptional activation on DR5. Reduces transcriptional repression on DR1 and reduces transcriptional activation on DR5; when associated with E-365 and E-366. 1 Publication1
Mutagenesisi369S → E: Reduces transcriptional repression on DR1 and reduces transcriptional activation on DR5; when associated with V-123 and E-370. 1
Mutagenesisi370K → E: Reduces transcriptional repression on DR1 and reduced transcriptional activation on DR5; when associated with V-123 and E-369. 1

Keywords - Diseasei

Disease mutation, Microphthalmia, Proto-oncogene

Organism-specific databases

DisGeNET

More...DisGeNETi		5915

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...GeneReviewsi		RARB

MalaCards human disease database

More...MalaCardsi		RARB
MIMi615524 phenotype

Open Targets

More...OpenTargetsi		ENSG00000077092

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

More...Orphaneti		2470 Matthew-Wood syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA34226

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P10826 Tclin

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2008

Drug and drug target database

More...DrugBanki		DB00459 Acitretin
DB00210 Adapalene
DB00523 Alitretinoin
DB02877 Arotinoid acid
DB00926 Etretinate
DB05785 LGD-1550
DB04942 Tamibarotene
DB00799 Tazarotene
DB00755 Tretinoin
DB12808 Trifarotene

DrugCentral

More...DrugCentrali		P10826

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		591

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		RARB

Domain mapping of disease mutations (DMDM)

More...DMDMi		17380507

<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_00000534671 – 455Retinoic acid receptor betaAdd BLAST455

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 residuei77PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P10826

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P10826

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

More...PaxDbi		P10826

PeptideAtlas

More...PeptideAtlasi		P10826

PRoteomics IDEntifications database

More...PRIDEi		P10826

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		52654 [P10826-1]
52655 [P10826-2]
52656 [P10826-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P10826

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

More...PhosphoSitePlusi		P10826

<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 aortic endothelial cells (at protein level).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000077092 Expressed in forebrain and 152 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P10826 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P10826 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000077092 Tissue enhanced (retina)

<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

Homodimer (By similarity). Heterodimer; with a RXR molecule (By similarity). Binds DNA preferentially as a RAR/RXR heterodimer (By similarity). Heterodimerizes (via NR LBD) with RXRA (PubMed:29021580).

Interacts weakly with NCOR2 (PubMed:12554770).

By similarity2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Show more details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		111850, 23 interactors

Protein interaction database and analysis system

More...IntActi		P10826, 20 interactors

Molecular INTeraction database

More...MINTi		P10826

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000332296

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P10826

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P10826 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

1455
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		P10826

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		P10826

<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>Domaini183 – 417NR LBDPROSITE-ProRule annotationAdd BLAST235

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 – 87ModulatingAdd BLAST87
Regioni154 – 182HingeAdd BLAST29

<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.
The DNA-binding nuclear receptor domain and the NR LBD domain are required for binding of the RARB/RXRA heterodimer to both DR1 and DR5 DNA elements.1 Publication

<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. NR1 subfamily.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri88 – 108NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri124 – 148NR C4-typePROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3575 Eukaryota
ENOG410XRZC LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000156196

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_007368_18_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P10826

KEGG Orthology (KO)

More...KOi		K08528

Identification of Orthologs from Complete Genome Data

More...OMAi		WTENILK

Database of Orthologous Groups

More...OrthoDBi		1165737at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P10826

TreeFam database of animal gene trees

More...TreeFami		TF328382

Family and domain databases

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
IPR001723 Nuclear_hrmn_rcpt
IPR003078 Retinoic_acid_rcpt
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		PR01292 RETNOICACIDR
PR00398 STRDHORMONER
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

This entry has 4 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform Beta-1 (identifier: P10826-1) [UniParc]FASTAAdd to basket

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

« Hide
        10         20         30         40         50
MTTSGHACPV PAVNGHMTHY PATPYPLLFP PVIGGLSLPP LHGLHGHPPP 
        60         70         80         90        100
SGCSTPSPAT IETQSTSSEE LVPSPPSPLP PPRVYKPCFV CQDKSSGYHY 
       110        120        130        140        150
GVSACEGCKG FFRRSIQKNM IYTCHRDKNC VINKVTRNRC QYCRLQKCFE 
       160        170        180        190        200
VGMSKESVRN DRNKKKKETS KQECTESYEM TAELDDLTEK IRKAHQETFP 
       210        220        230        240        250
SLCQLGKYTT NSSADHRVRL DLGLWDKFSE LATKCIIKIV EFAKRLPGFT 
       260        270        280        290        300
GLTIADQITL LKAACLDILI LRICTRYTPE QDTMTFSDGL TLNRTQMHNA 
       310        320        330        340        350
GFGPLTDLVF TFANQLLPLE MDDTETGLLS AICLICGDRQ DLEEPTKVDK 
       360        370        380        390        400
LQEPLLEALK IYIRKRRPSK PHMFPKILMK ITDLRSISAK GAERVITLKM 
       410        420        430        440        450
EIPGSMPPLI QEMLENSEGH EPLTPSSSGN TAEHSPSISP SSVENSGVSQ 

SPLVQ
Length:455
Mass (Da):50,489
Last modified:November 16, 2001 - 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:i8813263AD0495D5A
GO
Isoform Beta-2 (identifier: P10826-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: MTTSGHACPV...SGCSTPSPAT → MFDCMDVLSV...EWQHRHTAQS

Show »
Length:448
Mass (Da):50,344
Checksum:i844A298AD32F46A8
GO
Isoform Beta-3 (identifier: P10826-4)
Sequence is not available
Length:–
Mass (Da):–
Isoform Beta-4 (identifier: P10826-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-119: Missing.

Show »
Length:336
Mass (Da):37,932
Checksum:iD248E5CAB87DA44E
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
D6RBI3D6RBI3_HUMAN
Retinoic acid receptor beta
RARB
402Annotation score:

Annotation score:2 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>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence CAA27637 differs from that shown. Reason: Erroneous gene model prediction.Curated

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 conflicti206G → A in CAA68398 (PubMed:2825037).Curated1
Sequence conflicti317L → Q in CAA30262 (PubMed:2836738).Curated1
Sequence conflicti414L → M in CAA68398 (PubMed:2825037).Curated1
Sequence conflicti454V → L in CAA30262 (PubMed:2836738).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03606090V → I in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_077141220L → P in MCOPS12; increased transcriptional response to retinoic acid ligands. 1 Publication1
Natural variantiVAR_077142303G → A in MCOPS12; increased transcriptional response to retinoic acid ligands. 1 Publication1
Natural variantiVAR_070780394R → C in MCOPS12; increased transcriptional response to retinoic acid ligands. 2 Publications1
Natural variantiVAR_070781394R → S in MCOPS12; increases transcriptional response to retinoic acid. 1 Publication1

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_0036351 – 119Missing in isoform Beta-4. 1 PublicationAdd BLAST119
Alternative sequenceiVSP_0036341 – 60MTTSG…PSPAT → MFDCMDVLSVSPGQILDFYT ASPSSCMLQEKALKACFSGL TQTEWQHRHTAQS in isoform Beta-2. 3 PublicationsAdd BLAST60

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
X07282 mRNA Translation: CAA30262.1
Y00291 mRNA Translation: CAA68398.1
AF157483 mRNA Translation: AAD45688.1
BC060794 mRNA Translation: AAH60794.1
X56849 Genomic DNA No translation available.
X77664 Genomic DNA Translation: CAA54740.1
X04014 Genomic DNA Translation: CAA27637.1 Sequence problems.
M57445 Genomic DNA Translation: AAA58728.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS2642.1 [P10826-2]
CCDS46775.1 [P10826-3]

Protein sequence database of the Protein Information Resource

More...PIRi		S02827
S49021

NCBI Reference Sequences

More...RefSeqi		NP_000956.2, NM_000965.4 [P10826-2]
NP_001277145.1, NM_001290216.2 [P10826-1]
NP_001277146.1, NM_001290217.1 [P10826-3]
NP_001277195.1, NM_001290266.1
NP_001277205.1, NM_001290276.1 [P10826-3]
NP_057236.1, NM_016152.3 [P10826-3]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000330688; ENSP00000332296; ENSG00000077092 [P10826-2]
ENST00000437042; ENSP00000398840; ENSG00000077092 [P10826-3]
ENST00000458646; ENSP00000391391; ENSG00000077092 [P10826-3]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		5915

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:5915

UCSC genome browser

More...UCSCi		uc003cdh.4 human [P10826-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07282 mRNA Translation: CAA30262.1
Y00291 mRNA Translation: CAA68398.1
AF157483 mRNA Translation: AAD45688.1
BC060794 mRNA Translation: AAH60794.1
X56849 Genomic DNA No translation available.
X77664 Genomic DNA Translation: CAA54740.1
X04014 Genomic DNA Translation: CAA27637.1 Sequence problems.
M57445 Genomic DNA Translation: AAA58728.1
CCDSiCCDS2642.1 [P10826-2]
CCDS46775.1 [P10826-3]
PIRiS02827
S49021
RefSeqiNP_000956.2, NM_000965.4 [P10826-2]
NP_001277145.1, NM_001290216.2 [P10826-1]
NP_001277146.1, NM_001290217.1 [P10826-3]
NP_001277195.1, NM_001290266.1
NP_001277205.1, NM_001290276.1 [P10826-3]
NP_057236.1, NM_016152.3 [P10826-3]

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
1HRANMR-A82-160[»]
1XAPX-ray2.10A176-421[»]
4DM6X-ray1.90A/B176-421[»]
4DM8X-ray2.30A/B176-421[»]
4JYGX-ray2.35A/B176-421[»]
4JYHX-ray2.60A/B176-421[»]
4JYIX-ray1.90A/B176-421[»]
5UANX-ray3.51B80-455[»]
6SSQX-ray2.30A/B176-421[»]
SMRiP10826
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi111850, 23 interactors
IntActiP10826, 20 interactors
MINTiP10826
STRINGi9606.ENSP00000332296

Chemistry databases

BindingDBiP10826
ChEMBLiCHEMBL2008
DrugBankiDB00459 Acitretin
DB00210 Adapalene
DB00523 Alitretinoin
DB02877 Arotinoid acid
DB00926 Etretinate
DB05785 LGD-1550
DB04942 Tamibarotene
DB00799 Tazarotene
DB00755 Tretinoin
DB12808 Trifarotene
DrugCentraliP10826
GuidetoPHARMACOLOGYi591

PTM databases

iPTMnetiP10826
PhosphoSitePlusiP10826

Polymorphism and mutation databases

BioMutaiRARB
DMDMi17380507

Proteomic databases

jPOSTiP10826
MassIVEiP10826
PaxDbiP10826
PeptideAtlasiP10826
PRIDEiP10826
ProteomicsDBi52654 [P10826-1]
52655 [P10826-2]
52656 [P10826-3]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		934 496 antibodies

The DNASU plasmid repository

More...DNASUi		5915

Genome annotation databases

EnsembliENST00000330688; ENSP00000332296; ENSG00000077092 [P10826-2]
ENST00000437042; ENSP00000398840; ENSG00000077092 [P10826-3]
ENST00000458646; ENSP00000391391; ENSG00000077092 [P10826-3]
GeneIDi5915
KEGGihsa:5915
UCSCiuc003cdh.4 human [P10826-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5915
DisGeNETi5915

GeneCards: human genes, protein and diseases

More...GeneCardsi		RARB
GeneReviewsiRARB
HGNCiHGNC:9865 RARB
HPAiENSG00000077092 Tissue enhanced (retina)
MalaCardsiRARB
MIMi180220 gene
615524 phenotype
neXtProtiNX_P10826
OpenTargetsiENSG00000077092
Orphaneti2470 Matthew-Wood syndrome
PharmGKBiPA34226

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3575 Eukaryota
ENOG410XRZC LUCA
GeneTreeiENSGT00940000156196
HOGENOMiCLU_007368_18_0_1
InParanoidiP10826
KOiK08528
OMAiWTENILK
OrthoDBi1165737at2759
PhylomeDBiP10826
TreeFamiTF328382

Enzyme and pathway databases

ReactomeiR-HSA-383280 Nuclear Receptor transcription pathway
R-HSA-5362517 Signaling by Retinoic Acid
R-HSA-5617472 Activation of anterior HOX genes in hindbrain development during early embryogenesis
SignaLinkiP10826
SIGNORiP10826

Miscellaneous databases

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

More...ChiTaRSi		RARB human
EvolutionaryTraceiP10826

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Retinoic_acid_receptor_beta

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

More...GenomeRNAii		5915
PharosiP10826 Tclin

Protein Ontology

More...PROi		PR:P10826
RNActiP10826 protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000077092 Expressed in forebrain and 152 other tissues
ExpressionAtlasiP10826 baseline and differential
GenevisibleiP10826 HS

Family and domain databases

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
IPR001723 Nuclear_hrmn_rcpt
IPR003078 Retinoic_acid_rcpt
IPR001628 Znf_hrmn_rcpt
IPR013088 Znf_NHR/GATA
PfamiView protein in Pfam
PF00104 Hormone_recep, 1 hit
PF00105 zf-C4, 1 hit
PRINTSiPR01292 RETNOICACIDR
PR00398 STRDHORMONER
PR00047 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 nameiRARB_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: P10826
Secondary accession number(s): P12891
, Q00989, Q15298, Q9UN48
<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: July 1, 1989
Last sequence update: November 16, 2001
Last modified: April 22, 2020
This is version 236 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. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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