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Entry version 247 (17 Jun 2020)
Sequence version 2 (01 Oct 1989)
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Protein

Retinoic acid receptor alpha

Gene

RARA

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 (PubMed:19850744, PubMed:16417524, PubMed:20215566). 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 (PubMed:28167758). The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 (PubMed:28167758). In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone deacetylation, chromatin condensation and transcriptional suppression (PubMed:16417524). On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation (PubMed:9267036, PubMed:19850744, PubMed:20215566). Formation of a complex with histone deacetylases might lead to inhibition of RARE DNA element binding and to transcriptional repression (PubMed:28167758). Transcriptional activation and RARE DNA element binding might be supported by the transcription factor KLF2 (PubMed:28167758). RARA plays an essential role in the regulation of retinoic acid-induced germ cell development during spermatogenesis (By similarity). Has a role in the survival of early spermatocytes at the beginning prophase of meiosis (By similarity). In Sertoli cells, may promote the survival and development of early meiotic prophase spermatocytes (By similarity). In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function (By similarity). Together with RXRA, positively regulates microRNA-10a expression, thereby inhibiting the GATA6/VCAM1 signaling response to pulsatile shear stress in vascular endothelial cells (PubMed:28167758). In association with HDAC3, HDAC5 and HDAC7 corepressors, plays a role in the repression of microRNA-10a and thereby promotes the inflammatory response (PubMed:28167758).By similarity5 Publications

Caution

Was originally thought to be part of the MLL5-L complex, at least composed of KMT2E, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT (PubMed:19377461). However, the corresponding article has been retracted (PubMed:24336203).2 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

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 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-4090294 SUMOylation of intracellular receptors
R-HSA-5362517 Signaling by Retinoic Acid
R-HSA-5617472 Activation of anterior HOX genes in hindbrain development during early embryogenesis
R-HSA-9616222 Transcriptional regulation of granulopoiesis

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

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SignaLinki
P10276

SIGNOR Signaling Network Open Resource

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SIGNORi
P10276

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

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MoonDBi
P10276 Predicted

<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 alpha
Short name:
RAR-alpha
Alternative name(s):
Nuclear receptor subfamily 1 group B member 1
<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:RARA
Synonyms:NR1B1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 17

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000131759.17

Human Gene Nomenclature Database

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HGNCi
HGNC:9864 RARA

Online Mendelian Inheritance in Man (OMIM)

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MIMi
180240 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P10276

<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

Chromosomal aberrations involving RARA are commonly found in acute promyelocytic leukemia. Translocation t(11;17)(q32;q21) with ZBTB16/PLZF; translocation t(15;17)(q21;q21) with PML; translocation t(5;17)(q32;q11) with NPM. The PML-RARA oncoprotein requires both the PML ring structure and coiled-coil domain for both interaction with UBE2I, nuclear microspeckle location and sumoylation. In addition, the coiled-coil domain functions in blocking RA-mediated transactivation and cell differentiation.3 Publications

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>Mutagenesisi95S → A: No effect on PKB/AKT1-mediated phosphorylation. Repressed transactivation. 1 Publication1
Mutagenesisi96S → A: Abolishes PKB/AKT1-mediated phosphorylation. Repressed transactivation. 1 Publication1
Mutagenesisi147K → R: Abrogates sumoylation in the presence or absence of ATRA and primarily nuclear localization and enhanced ATRA-mediated transcriptional activity; when associated with R-166; R-171 and R-399. 1 Publication1
Mutagenesisi154S → A: No effect on PKB/AKT1-mediated phosphorylation. No repression of transactivation. 1 Publication1
Mutagenesisi157S → A: No effect on PKB/AKT1-mediated phosphorylation. Repressed transactivation. 1 Publication1
Mutagenesisi166K → R: Cytoplasmic in the absence of ATRA and reduced transcriptional activity in the presence of ATRA. Low sumoylation levels in the presence of ATRA; when associated with R-399. Nuclear localization and enhanced transcriptional activity; when associated with R-171 and R-399. Primarily nuclear localization and enhanced ATRA-mediated transcriptional activity; when associated with R-147; R-171 and R-399. 1 Publication1
Mutagenesisi171K → R: Cytoplasmic in the absence of ATRA and reduced transcriptional activity in the presence of ATRA. Low sumoylation levels in the presence of ATRA; when associated with R-399. Nuclear localization and enhanced transcriptional activity; when associated with R-166 and R-399. Primarily nuclear localization and enhanced ATRA-mediated transcriptional activity; when associated with R-147; R-166 and R-399. 1 Publication1
Mutagenesisi219S → A: No effect on heterodimerization with RARA. On ATRA treatment, localizes to the nucleus, and increased protein levels; when associated with A-369. 1 Publication1
Mutagenesisi219S → E: No effect on heterodimerization with RARA. On ATRA treatment, localizes to both nucleus and cytoplasm, no increase in protein levels, and decrease in RARA-mediated transcriptional activity; when associated with E-369. 1 Publication1
Mutagenesisi369S → A: No effect on heterodimerization with RARA. On ATRA treatment, localizes to the nucleus, and increased protein levels; when associated with A-219. 1 Publication1
Mutagenesisi369S → E: Some inhibition of heterodimerization with RARA. On ATRA treatment, localizes to both nucleus and cytoplasm, increase in protein levels, and decrease in RARA-mediated transcriptional activity; when associated with E-219. 1 Publication1
Mutagenesisi396I → E: Abrogates interaction with NCOR1 or NCOR2. Increased affinity for NCOR1 and NCOR2 in the presence of BMS493. Increased transcriptional activity in the presence of agonist and decreased activity in the presence of neutral antagonist. 1 Publication1
Mutagenesisi399K → R in the absence of ATRA, abolishes sumoylation and is mainly nuclear. In the presence of ATRA, some sumoylation, cytoplasmic location, reduced transcriptional activity and no SENP6 binding. Low sumoylation levels in the presence of ATRA and nuclear location in the absence of ATRA; when associated with R-166 or with R-171. Primarily nuclear localization and enhanced ATRA-mediated transcriptional activity; when associated with R-147; R-166 and R-171. 1 Publication1
Mutagenesisi409 – 410LI → AA: Abolishes interaction with ASXL1 and NCOA1. 1 Publication2
Mutagenesisi412E → Q: Impairs interaction with ASXL1 and NCOA1; when associated with Q-415. 1 Publication1
Mutagenesisi413 – 414ML → AA: Abolishes interaction with ASXL1 and NCOA1. 1 Publication2
Mutagenesisi415E → Q: Impairs interaction with ASXL1 and NCOA1; when associated with Q-412. 1 Publication1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei60 – 61Breakpoint for translocation to form PLZF-RAR-alpha, RAR-alpha1-PLZF and PML-RAR-alpha oncogenes2

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNET

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DisGeNETi
5914

MalaCards human disease database

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MalaCardsi
RARA
MIMi612376 phenotype

Open Targets

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OpenTargetsi
ENSG00000131759

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

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Orphaneti
520 Acute promyelocytic leukemia

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA34225

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
P10276 Tclin

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2055

Drug and drug target database

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DrugBanki
DB00459 Acitretin
DB00210 Adapalene
DB00523 Alitretinoin
DB00926 Etretinate
DB00982 Isotretinoin
DB05785 LGD-1550
DB04942 Tamibarotene
DB00799 Tazarotene
DB00755 Tretinoin
DB12808 Trifarotene

DrugCentral

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DrugCentrali
P10276

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
590

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
RARA

Domain mapping of disease mutations (DMDM)

More...
DMDMi
133483

<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_00000534611 – 462Retinoic acid receptor alphaAdd BLAST462

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 residuei77Phosphoserine; by CDK7By similarity1
Modified residuei96Phosphoserine; by PKB/AKT11 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki166Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki171Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei219Phosphoserine; by PKA1 Publication1
Modified residuei369Phosphoserine; by PKA1 Publication1
Cross-linki399Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication

<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 on serine and threonine residues. Phosphorylation does not change during cell cycle. Phosphorylation on Ser-77 is crucial for transcriptional activity (By similarity). Phosphorylation by AKT1 is required for the repressor activity but has no effect on DNA binding, protein stability nor subcellular localization. Phosphorylated by PKA in vitro. This phosphorylation on Ser-219 and Ser-369 is critical for ligand binding, nuclear localization and transcriptional activity in response to FSH signaling.By similarity2 Publications
Sumoylated with SUMO2, mainly on Lys-399 which is also required for SENP6 binding. On all-trans retinoic acid (ATRA) binding, a confromational change may occur that allows sumoylation on two additional site, Lys-166 and Lys-171. Probably desumoylated by SENP6. Sumoylation levels determine nuclear localization and regulate ATRA-mediated transcriptional activity.2 Publications
Trimethylation enhances heterodimerization with RXRA and positively modulates the transcriptional activation.
Ubiquitinated.
Acetylated; acetylation is increased upon pulsatile shear stress and decreased upon oscillatory shear stress.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P10276

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
P10276

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

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PaxDbi
P10276

PeptideAtlas

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PeptideAtlasi
P10276

PRoteomics IDEntifications database

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PRIDEi
P10276

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
52592 [P10276-1]
52593 [P10276-2]
52594 [P10276-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P10276

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

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PhosphoSitePlusi
P10276

SwissPalm database of S-palmitoylation events

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SwissPalmi
P10276

<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 monocytes.1 Publication

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Down-regulated by aging (PubMed:26463675). Induced by pulsatile shear stress (PubMed:28167758).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000131759 Expressed in nasal cavity epithelium and 216 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P10276 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P10276 HS

Organism-specific databases

Human Protein Atlas

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HPAi
ENSG00000131759 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

Heterodimer; with RXRA (via C-terminus); association with RXRA is enhanced by pulsatile shear stress (PubMed:28167758, PubMed:10698945, PubMed:10882070, PubMed:20215566, PubMed:15509776). Binds DNA preferentially as a heterodimer (PubMed:10698945, PubMed:28167758). RXRA serves as enhancer to induce RARA binding to RARE (PubMed:30468856).

Interacts with RXRG (PubMed:28167758).

Interacts with coactivators NCOA3 and NCOA6 (PubMed:9267036, PubMed:10567404).

Interacts with NCOA7; the interaction requires ligand-binding (PubMed:11971969).

Interacts (via the ligand-binding domain) with PRAME; the interaction is ligand (retinoic acid)-dependent (PubMed:16179254).

Interacts with AKT1; the interaction phosphorylates RARA and represses transactivation (PubMed:16417524).

Interacts with PRKAR1A; the interaction negatively regulates RARA transcriptional activity (PubMed:20215566).

Interacts with NCOR1 and NCOR2 (PubMed:20543827).

Interacts with PRMT2 (PubMed:12039952).

Interacts with LRIF1 (PubMed:17455211).

Interacts with ASXL1 and NCOA1 (PubMed:16606617).

Interacts with ACTN4 (PubMed:22351778). In a complex with HDAC3, HDAC5 and HDAC7; the HDACs serve as corepressors of RARA, causing its deacetylation and inhibition of RARE DNA element binding; association with HDAC3, HDAC5 and HDAC7 is increased upon oscillatory shear stress (PubMed:28167758).

Interacts with CDK7 (By similarity). In the absence of hormonal ligand, interacts with TACC1 (PubMed:20078863).

By similarity17 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

Hide details
P10276
With#Exp.IntAct
ACTN4 - isoform 1 [O43707-1]2EBI-413374,EBI-15971664
ALOX15B [O15296]3EBI-413374,EBI-12150557
ALX1 [Q15699]3EBI-413374,EBI-750671
BBS4 [Q96RK4]3EBI-413374,EBI-1805814
CCNDBP1 [O95273]3EBI-413374,EBI-748961
CCNH [P51946]2EBI-413374,EBI-741406
EZH2 [Q15910]2EBI-413374,EBI-530054
GNAQ [P50148]4EBI-413374,EBI-3909604
ITGB1BP2 [Q9UKP3]2EBI-413374,EBI-5659717
MCRS1 [Q96EZ8]3EBI-413374,EBI-348259
MED1 [Q15648]6EBI-413374,EBI-394459
MED25 [Q71SY5]10EBI-413374,EBI-394558
NCOA1 [Q15788]7EBI-413374,EBI-455189
NCOA3 [Q9Y6Q9]2EBI-413374,EBI-81196
NCOR1 [O75376]6EBI-413374,EBI-347233
NCOR2 [Q9Y618]4EBI-413374,EBI-80830
NFE2L2 [Q16236]2EBI-413374,EBI-2007911
NR2C1 - isoform 2 [P13056-2]3EBI-413374,EBI-18764867
NRIP1 [P48552]4EBI-413374,EBI-746484
PHF8 - isoform 2 [Q9UPP1-2]2EBI-413374,EBI-6601215
PLEKHF2 [Q9H8W4]3EBI-413374,EBI-742388
PPARG [P37231]3EBI-413374,EBI-781384
PRKDC [P78527]3EBI-413374,EBI-352053
RXRA [P19793]14EBI-413374,EBI-78598
RXRB [P28702]15EBI-413374,EBI-748576
RXRB - isoform 2 [P28702-3]3EBI-413374,EBI-16429492
RXRG [P48443]17EBI-413374,EBI-712405
SIRT1 [Q96EB6]3EBI-413374,EBI-1802965
SUMO1 [P63165]5EBI-413374,EBI-80140
TEKT4 [Q8WW24]4EBI-413374,EBI-750487
ZNF423 [Q2M1K9]2EBI-413374,EBI-950016
Ajuba [Q91XC0] from Mus musculus.7EBI-413374,EBI-1565930
Asxl1 [P59598] from Mus musculus.4EBI-413374,EBI-5743705
Isoform Alpha-2 [P10276-2]
With#Exp.IntAct
NRIP1 [P48552]3EBI-10197061,EBI-746484
RXRB [P28702]4EBI-10197061,EBI-748576
RXRG [P48443]6EBI-10197061,EBI-712405
TEKT4 [Q8WW24]3EBI-10197061,EBI-750487

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
111849, 149 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-508 RXRalpha-RARalpha retinoic acid receptor complex
CPX-525 RARalpha-NCOA1 activated retinoic acid receptor complex
CPX-666 RARalpha-NCOA2 activated retinoic acid receptor complex
CPX-816 RXRalpha-RARalpha-NCOA2 retinoic acid receptor complex

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P10276

Database of interacting proteins

More...
DIPi
DIP-34N

Protein interaction database and analysis system

More...
IntActi
P10276, 71 interactors

Molecular INTeraction database

More...
MINTi
P10276

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000254066

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P10276

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P10276 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

1462
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
P10276

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
P10276

<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
Regioni404 – 419Required for binding corepressor NCOR1Add BLAST16

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi408 – 4169aaTAD1 Publication9

<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 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.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

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
ENSGT00940000159997

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_007368_18_2_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P10276

KEGG Orthology (KO)

More...
KOi
K08527

Identification of Orthologs from Complete Genome Data

More...
OMAi
AECSESY

Database of Orthologous Groups

More...
OrthoDBi
1165737at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P10276

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

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...
IDEALi
IID00365

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 (3+)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 3 <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 3 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform Alpha-1 (identifier: P10276-1) [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
MASNSSSCPT PGGGHLNGYP VPPYAFFFPP MLGGLSPPGA LTTLQHQLPV
60 70 80 90 100
SGYSTPSPAT IETQSSSSEE IVPSPPSPPP LPRIYKPCFV CQDKSSGYHY
110 120 130 140 150
GVSACEGCKG FFRRSIQKNM VYTCHRDKNC IINKVTRNRC QYCRLQKCFE
160 170 180 190 200
VGMSKESVRN DRNKKKKEVP KPECSESYTL TPEVGELIEK VRKAHQETFP
210 220 230 240 250
ALCQLGKYTT NNSSEQRVSL DIDLWDKFSE LSTKCIIKTV EFAKQLPGFT
260 270 280 290 300
TLTIADQITL LKAACLDILI LRICTRYTPE QDTMTFSDGL TLNRTQMHNA
310 320 330 340 350
GFGPLTDLVF AFANQLLPLE MDDAETGLLS AICLICGDRQ DLEQPDRVDM
360 370 380 390 400
LQEPLLEALK VYVRKRRPSR PHMFPKMLMK ITDLRSISAK GAERVITLKM
410 420 430 440 450
EIPGSMPPLI QEMLENSEGL DTLSGQPGGG GRDGGGLAPP PGSCSPSLSP
460
SSNRSSPATH SP
Length:462
Mass (Da):50,771
Last modified:October 1, 1989 - 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:iE8D1CF9A1E57CB99
GO
Isoform Alpha-2 (identifier: P10276-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: MASNSSSCPT...SGYSTPSPAT → MYESVEVGGP...TPLWNGSNHS

Show »
Length:457
Mass (Da):50,742
Checksum:i1E328ED7945D1F95
GO
Isoform Alpha-1-deltaBC (identifier: P10276-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     61-157: Missing.

Note: Does not bind nor transactivate RARE on its own but may do so as a heterodimer with Alpha-1.Curated
Show »
Length:365
Mass (Da):39,700
Checksum:iD24F282D50E9953E
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A8MUP8A8MUP8_HUMAN
Retinoic acid receptor alpha
RARA hCG_2007196
478Annotation score:

Annotation score:3 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>
J3KSJ4J3KSJ4_HUMAN
Retinoic acid receptor alpha
RARA
186Annotation 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>
J3QRM2J3QRM2_HUMAN
Retinoic acid receptor alpha
RARA
66Annotation 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>

<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 AAB00112 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAB00113 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAB62809 differs from that shown. Reason: Erroneous initiation.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 conflicti241E → D in AAD05222 (PubMed:10337631).Curated1

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_0036291 – 60MASNS…PSPAT → MYESVEVGGPTPNPFLVVDF YNQNRACLLPEKGLPAPGPY STPLRTPLWNGSNHS in isoform Alpha-2. 1 PublicationAdd BLAST60
Alternative sequenceiVSP_04314361 – 157Missing in isoform Alpha-1-deltaBC. 1 PublicationAdd BLAST97

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
X06614 mRNA Translation: CAA29829.1
X06538 mRNA Translation: CAA29787.1
AF088895 AF088894 Genomic DNA Translation: AAD05222.1
FJ487576 mRNA Translation: ACK86665.1
AC080112 Genomic DNA No translation available.
BC008727 mRNA Translation: AAH08727.1
BC071733 mRNA Translation: AAH71733.1
X56058, X58685 mRNA Translation: CAA39533.1
X58685 mRNA Translation: CAA41532.1
U41742 mRNA Translation: AAB00112.1 Different initiation.
U41743 mRNA Translation: AAB00113.1 Different initiation.
AF283809 Genomic DNA Translation: AAF87249.1
AB067754 mRNA Translation: BAB62809.1 Different initiation.

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS11366.1 [P10276-1]
CCDS42317.1 [P10276-2]
CCDS45671.1 [P10276-3]

Protein sequence database of the Protein Information Resource

More...
PIRi
A29491

NCBI Reference Sequences

More...
RefSeqi
NP_000955.1, NM_000964.3 [P10276-1]
NP_001019980.1, NM_001024809.3 [P10276-2]
NP_001138773.1, NM_001145301.2 [P10276-1]
NP_001138774.1, NM_001145302.2 [P10276-3]
XP_005257610.1, XM_005257553.1 [P10276-1]
XP_005257611.1, XM_005257554.1 [P10276-1]
XP_011523397.1, XM_011525095.1 [P10276-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000254066; ENSP00000254066; ENSG00000131759 [P10276-1]
ENST00000394081; ENSP00000377643; ENSG00000131759 [P10276-2]
ENST00000394089; ENSP00000377649; ENSG00000131759 [P10276-1]
ENST00000425707; ENSP00000389993; ENSG00000131759 [P10276-3]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5914

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:5914

UCSC genome browser

More...
UCSCi
uc002hun.3 human [P10276-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

<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

Retinoic acid receptor entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06614 mRNA Translation: CAA29829.1
X06538 mRNA Translation: CAA29787.1
AF088895 AF088894 Genomic DNA Translation: AAD05222.1
FJ487576 mRNA Translation: ACK86665.1
AC080112 Genomic DNA No translation available.
BC008727 mRNA Translation: AAH08727.1
BC071733 mRNA Translation: AAH71733.1
X56058, X58685 mRNA Translation: CAA39533.1
X58685 mRNA Translation: CAA41532.1
U41742 mRNA Translation: AAB00112.1 Different initiation.
U41743 mRNA Translation: AAB00113.1 Different initiation.
AF283809 Genomic DNA Translation: AAF87249.1
AB067754 mRNA Translation: BAB62809.1 Different initiation.
CCDSiCCDS11366.1 [P10276-1]
CCDS42317.1 [P10276-2]
CCDS45671.1 [P10276-3]
PIRiA29491
RefSeqiNP_000955.1, NM_000964.3 [P10276-1]
NP_001019980.1, NM_001024809.3 [P10276-2]
NP_001138773.1, NM_001145301.2 [P10276-1]
NP_001138774.1, NM_001145302.2 [P10276-3]
XP_005257610.1, XM_005257553.1 [P10276-1]
XP_005257611.1, XM_005257554.1 [P10276-1]
XP_011523397.1, XM_011525095.1 [P10276-1]

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
1DKFX-ray2.50B182-416[»]
1DSZX-ray1.70A82-167[»]
3A9EX-ray2.75B153-421[»]
3KMRX-ray1.80A176-421[»]
3KMZX-ray2.10A/B176-421[»]
4DQMX-ray2.75A/C182-415[»]
5K13X-ray1.85A181-426[»]
SMRiP10276
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi111849, 149 interactors
ComplexPortaliCPX-508 RXRalpha-RARalpha retinoic acid receptor complex
CPX-525 RARalpha-NCOA1 activated retinoic acid receptor complex
CPX-666 RARalpha-NCOA2 activated retinoic acid receptor complex
CPX-816 RXRalpha-RARalpha-NCOA2 retinoic acid receptor complex
CORUMiP10276
DIPiDIP-34N
IntActiP10276, 71 interactors
MINTiP10276
STRINGi9606.ENSP00000254066

Chemistry databases

BindingDBiP10276
ChEMBLiCHEMBL2055
DrugBankiDB00459 Acitretin
DB00210 Adapalene
DB00523 Alitretinoin
DB00926 Etretinate
DB00982 Isotretinoin
DB05785 LGD-1550
DB04942 Tamibarotene
DB00799 Tazarotene
DB00755 Tretinoin
DB12808 Trifarotene
DrugCentraliP10276
GuidetoPHARMACOLOGYi590

Protein family/group databases

MoonDBiP10276 Predicted

PTM databases

iPTMnetiP10276
PhosphoSitePlusiP10276
SwissPalmiP10276

Polymorphism and mutation databases

BioMutaiRARA
DMDMi133483

Proteomic databases

jPOSTiP10276
MassIVEiP10276
PaxDbiP10276
PeptideAtlasiP10276
PRIDEiP10276
ProteomicsDBi52592 [P10276-1]
52593 [P10276-2]
52594 [P10276-3]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
16473 750 antibodies

The DNASU plasmid repository

More...
DNASUi
5914

Genome annotation databases

EnsembliENST00000254066; ENSP00000254066; ENSG00000131759 [P10276-1]
ENST00000394081; ENSP00000377643; ENSG00000131759 [P10276-2]
ENST00000394089; ENSP00000377649; ENSG00000131759 [P10276-1]
ENST00000425707; ENSP00000389993; ENSG00000131759 [P10276-3]
GeneIDi5914
KEGGihsa:5914
UCSCiuc002hun.3 human [P10276-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5914
DisGeNETi5914
EuPathDBiHostDB:ENSG00000131759.17

GeneCards: human genes, protein and diseases

More...
GeneCardsi
RARA
HGNCiHGNC:9864 RARA
HPAiENSG00000131759 Low tissue specificity
MalaCardsiRARA
MIMi180240 gene
612376 phenotype
neXtProtiNX_P10276
OpenTargetsiENSG00000131759
Orphaneti520 Acute promyelocytic leukemia
PharmGKBiPA34225

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3575 Eukaryota
ENOG410XRZC LUCA
GeneTreeiENSGT00940000159997
HOGENOMiCLU_007368_18_2_1
InParanoidiP10276
KOiK08527
OMAiAECSESY
OrthoDBi1165737at2759
PhylomeDBiP10276
TreeFamiTF328382

Enzyme and pathway databases

ReactomeiR-HSA-383280 Nuclear Receptor transcription pathway
R-HSA-4090294 SUMOylation of intracellular receptors
R-HSA-5362517 Signaling by Retinoic Acid
R-HSA-5617472 Activation of anterior HOX genes in hindbrain development during early embryogenesis
R-HSA-9616222 Transcriptional regulation of granulopoiesis
SignaLinkiP10276
SIGNORiP10276

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
5914 13 hits in 809 CRISPR screens

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

More...
ChiTaRSi
RARA human
EvolutionaryTraceiP10276

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Retinoic_acid_receptor_alpha

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

More...
GenomeRNAii
5914
PharosiP10276 Tclin

Protein Ontology

More...
PROi
PR:P10276
RNActiP10276 protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000131759 Expressed in nasal cavity epithelium and 216 other tissues
ExpressionAtlasiP10276 baseline and differential
GenevisibleiP10276 HS

Family and domain databases

Gene3Di1.10.565.10, 1 hit
3.30.50.10, 1 hit
IDEALiIID00365
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 nameiRARA_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: P10276
Secondary accession number(s): B8Y636
, P78456, Q13440, Q13441, Q96S41, Q9NQS0
<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: October 1, 1989
Last modified: June 17, 2020
This is version 247 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
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