{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P19793","secondaryAccessions":["B3KY83","Q2NL52","Q2V504"],"uniProtkbId":"RXRA_HUMAN","entryAudit":{"firstPublicDate":"1991-02-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1991-02-01","entryVersion":263,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Retinoic acid receptor RXR-alpha"}},"alternativeNames":[{"fullName":{"value":"Nuclear receptor subfamily 2 group B member 1"}},{"fullName":{"value":"Retinoid X receptor alpha"}}]},"genes":[{"geneName":{"value":"RXRA"},"synonyms":[{"value":"NR2B1"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10195690"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10874028"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11162439"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11915042"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12145331"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1310260"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15509776"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16107141"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17761950"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18800767"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19167885"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20215566"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25417649"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26463675"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28167758"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29021580"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30216632"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37478846"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9267036"}],"value":"Receptor for retinoic acid that acts as a transcription factor (PubMed:10874028, PubMed:11162439, PubMed:11915042, PubMed:37478846). Forms homo- or heterodimers with retinoic acid receptors (RARs) and binds to target response elements in response to their ligands, all-trans or 9-cis retinoic acid, to regulate gene expression in various biological processes (PubMed:10195690, PubMed:11162439, PubMed:11915042, PubMed:16107141, PubMed:17761950, PubMed:18800767, PubMed:19167885, PubMed:28167758, PubMed:37478846). The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 to regulate transcription (PubMed:10195690, PubMed:11162439, PubMed:11915042, PubMed:17761950, PubMed:28167758). The high affinity ligand for retinoid X receptors (RXRs) is 9-cis retinoic acid (PubMed:1310260). 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:20215566). On ligand binding, the corepressors dissociate from the receptors and coactivators are recruited leading to transcriptional activation (PubMed:20215566, PubMed:37478846, PubMed:9267036). Serves as a common heterodimeric partner for a number of nuclear receptors, such as RARA, RARB and PPARA (PubMed:10195690, PubMed:11915042, PubMed:28167758, PubMed:29021580). The RXRA/RARB heterodimer can act as a transcriptional repressor or transcriptional activator, depending on the RARE DNA element context (PubMed:29021580). The RXRA/PPARA heterodimer is required for PPARA transcriptional activity on fatty acid oxidation genes such as ACOX1 and the P450 system genes (PubMed:10195690). Together with RARA, positively regulates microRNA-10a expression, thereby inhibiting the GATA6/VCAM1 signaling response to pulsatile shear stress in vascular endothelial cells (PubMed:28167758). Acts as an enhancer of RARA binding to RARE DNA element (PubMed:28167758). May facilitate the nuclear import of heterodimerization partners such as VDR and NR4A1 (PubMed:12145331, PubMed:15509776). Promotes myelin debris phagocytosis and remyelination by macrophages (PubMed:26463675). Plays a role in the attenuation of the innate immune system in response to viral infections, possibly by negatively regulating the transcription of antiviral genes such as type I IFN genes (PubMed:25417649). Involved in the regulation of calcium signaling by repressing ITPR2 gene expression, thereby controlling cellular senescence (PubMed:30216632)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P28700"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10195690"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10567404"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10669605"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10698945"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10874028"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10882139"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11259580"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11698662"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11915042"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12039952"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14981089"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15047147"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15509776"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16574651"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16912044"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17761950"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19786558"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20078863"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28167758"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28698609"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29021580"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30275017"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9267036"}],"value":"Homodimer (PubMed:10669605, PubMed:17761950). Heterodimer (via C-terminus) with RARA; required for ligand-dependent retinoic acid receptor transcriptional activity; association with RARA is enhanced by pulsatile shear stress (PubMed:10698945, PubMed:15509776, PubMed:28167758). Heterodimer with PPARA (via the leucine-like zipper in the LBD); the interaction is required for PPARA transcriptional activity (PubMed:10195690, PubMed:11698662, PubMed:11915042). Heterodimerizes with PPARG (PubMed:10882139, PubMed:11698662). Heterodimerizes (via NR LBD) with RARB (PubMed:29021580). Heterodimerizes with NR1H4; the heterodimerization enhances the binding affinity for LXXLL motifs from coactivators (PubMed:30275017). Interacts with NCOA3 and NCOA6 coactivators (PubMed:10567404, PubMed:9267036). Interacts with coactivator FAM120B (By similarity). Interacts with coactivator PELP1, SENP6, SFPQ, DNTTIP2 and RNF8 (PubMed:11259580, PubMed:14981089, PubMed:15047147, PubMed:16574651, PubMed:16912044). Interacts with PRMT2 (PubMed:12039952). Interacts with ASXL1 (By similarity). Interacts with BHLHE40/DEC1, BHLHE41/DEC2, NCOR1 and NCOR2 (PubMed:19786558). Interacts in a ligand-dependent fashion with MED1 and NCOA1 (PubMed:10882139, PubMed:11698662, PubMed:19786558). Interacts with VDR (PubMed:28698609). Interacts with EP300; the interaction is decreased by 9-cis retinoic acid (PubMed:17761950). Heterodimer (via C-terminus) with NR4A1 (via DNA-binding domain); DNA-binding of the heterodimer is enhanced by 9-cis retinoic acid (PubMed:15509776, PubMed:17761950). NR4A1 competes with EP300 for interaction with RXRA and thereby attenuates EP300 mediated acetylation of RXRA (PubMed:17761950). In the absence of hormonal ligand, interacts with TACC1 (PubMed:20078863). Interacts ith IGFBP3 (PubMed:10874028)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11915042"}],"value":"(Microbial infection) Interacts (via the DNA binding domain) with HCV core protein; the interaction enhances the transcriptional activities of the RXRA/RARA and the RXRA/PPARA heterodimers"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P19793","intActId":"EBI-78598"},"interactantTwo":{"uniProtKBAccession":"O14503","geneName":"BHLHE40","intActId":"EBI-711810"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P19793","intActId":"EBI-78598"},"interactantTwo":{"uniProtKBAccession":"P35637","geneName":"FUS","intActId":"EBI-400434"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P19793","intActId":"EBI-78598"},"interactantTwo":{"uniProtKBAccession":"Q15648","geneName":"MED1","intActId":"EBI-394459"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P19793","intActId":"EBI-78598"},"interactantTwo":{"uniProtKBAccession":"Q71SY5","geneName":"MED25","intActId":"EBI-394558"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P19793","intActId":"EBI-78598"},"interactantTwo":{"uniProtKBAccession":"Q15788","geneName":"NCOA1","intActId":"EBI-455189"},"numberOfExperiments":14,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P19793","intActId":"EBI-78598"},"interactantTwo":{"uniProtKBAccession":"Q15596","geneName":"NCOA2","intActId":"EBI-81236"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P19793","intActId":"EBI-78598"},"interactantTwo":{"uniProtKBAccession":"P55055","geneName":"NR1H2","intActId":"EBI-745354"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P19793","intActId":"EBI-78598"},"interactantTwo":{"uniProtKBAccession":"P55055-1","geneName":"NR1H2","intActId":"EBI-21458417"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P19793","intActId":"EBI-78598"},"interactantTwo":{"uniProtKBAccession":"Q13133","geneName":"NR1H3","intActId":"EBI-781356"},"numberOfExperiments":8,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P19793","intActId":"EBI-78598"},"interactantTwo":{"uniProtKBAccession":"P27986","geneName":"PIK3R1","intActId":"EBI-79464"},"numberOfExperiments":8,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P19793","intActId":"EBI-78598"},"interactantTwo":{"uniProtKBAccession":"P37231","geneName":"PPARG","intActId":"EBI-781384"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P19793","intActId":"EBI-78598"},"interactantTwo":{"uniProtKBAccession":"P37231-1","geneName":"PPARG","intActId":"EBI-15664691"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P19793","intActId":"EBI-78598"},"interactantTwo":{"uniProtKBAccession":"P10276","geneName":"RARA","intActId":"EBI-413374"},"numberOfExperiments":14,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P19793","intActId":"EBI-78598"},"interactantTwo":{"uniProtKBAccession":"P42224","geneName":"STAT1","intActId":"EBI-1057697"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P19793","intActId":"EBI-78598"},"interactantTwo":{"uniProtKBAccession":"P11473","geneName":"VDR","intActId":"EBI-286357"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P19793","intActId":"EBI-78598"},"interactantTwo":{"uniProtKBAccession":"P97792-1","geneName":"Cxadr","intActId":"EBI-15903843"},"numberOfExperiments":2,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P19793","intActId":"EBI-78598"},"interactantTwo":{"uniProtKBAccession":"Q9JLI4","geneName":"Ncoa6","intActId":"EBI-286271"},"numberOfExperiments":2,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P19793","intActId":"EBI-78598"},"interactantTwo":{"uniProtKBAccession":"P04625","geneName":"THRA","intActId":"EBI-286261"},"numberOfExperiments":4,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P19793","intActId":"EBI-78598"},"interactantTwo":{"uniProtKBAccession":"Q03463","chainId":"PRO_0000278730","intActId":"EBI-9159704"},"numberOfExperiments":3,"organismDiffer":true}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12145331"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15509776"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17761950"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28167758"}],"value":"Localization to the nucleus is enhanced by vitamin D3 (PubMed:15509776). Nuclear localization may be enhanced by the interaction with heterodimerization partner VDR (PubMed:12145331). Translocation to the mitochondrion upon interaction with NR4A1 (PubMed:15509776, PubMed:17761950). Increased nuclear localization upon pulsatile shear stress (PubMed:28167758)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00407"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10874028"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11915042"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12145331"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15509776"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17761950"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28167758"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12145331"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15509776"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17761950"}],"value":"Mitochondrion","id":"SL-0173"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["P19793-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["P19793-2"],"sequenceIds":["VSP_056565"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14702039"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2159111"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24275569"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26463675"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30216632"}],"value":"Expressed in lung fibroblasts (at protein level) (PubMed:30216632). Expressed in monocytes (PubMed:26463675). Highly expressed in liver, also found in kidney and brain (PubMed:14702039, PubMed:2159111, PubMed:24275569)"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26463675"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28167758"}],"value":"Down-regulated by aging (PubMed:26463675). Induced by pulsatile shear stress (PubMed:28167758)"}],"commentType":"INDUCTION"},{"texts":[{"value":"Composed of three domains: a modulating N-terminal domain (AF1 domain), a DNA-binding domain and a C-terminal ligand-binding domain (AF2 domain)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17761950"}],"value":"Acetylated by EP300; acetylation enhances DNA binding and transcriptional activity"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P28700"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11162439"}],"value":"Phosphorylated on serine and threonine residues mainly in the N-terminal modulating domain (By similarity). Constitutively phosphorylated on Ser-21 in the presence or absence of ligand (By similarity). Under stress conditions, hyperphosphorylated by activated JNK on Ser-56, Ser-70, Thr-82 and Ser-260 (By similarity). Phosphorylated on Ser-27, in vitro, by PKA (PubMed:11162439). This phosphorylation is required for repression of cAMP-mediated transcriptional activity of RARA (PubMed:11162439)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37478846"}],"value":"Ubiquitinated by UBR5, leading to its degradation: UBR5 specifically recognizes and binds ligand-bound RXRA when it is not associated with coactivators (NCOAs) (PubMed:37478846). In presence of NCOAs, the UBR5-degron is not accessible, preventing its ubiquitination and degradation (PubMed:37478846)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16912044"}],"value":"Sumoylation negatively regulates transcriptional activity. Desumoylated specifically by SENP6"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the nuclear hormone receptor family. NR2 subfamily"}],"commentType":"SIMILARITY"},{"commentType":"WEB RESOURCE","resourceName":"Wikipedia","resourceUrl":"https://en.wikipedia.org/wiki/Retinoid_X_receptor","ftp":false,"note":"Retinoid X receptor entry"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":462,"modifier":"EXACT"}},"description":"Retinoic acid receptor RXR-alpha","featureId":"PRO_0000053566"},{"type":"Domain","location":{"start":{"value":227,"modifier":"EXACT"},"end":{"value":458,"modifier":"EXACT"}},"description":"NR LBD","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01189"}]},{"type":"DNA binding","location":{"start":{"value":135,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"Nuclear receptor","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00407"}]},{"type":"Zinc 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