LMPD Database

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LMP001137

UniProt Annotations

Entry Information
Gene Nameretinoid X receptor, alpha
Protein EntryQ6P3U7_HUMAN
UniProt IDQ6P3U7
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=1; IsoId=P19793-1; Sequence=Displayed; Name=2; IsoId=P19793-2; Sequence=VSP_056565; Note=No experimental confirmation available.;
DomainComposed of three domains: a modulating N-terminal domain (AF1 domain), a DNA-binding domain and a C-terminal ligand-binding domain (AF2 domain).
FunctionReceptor 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 RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. The high affinity ligand for RXRs is 9-cis retinoic acid. RXRA serves as a common heterodimeric partner for a number of nuclear receptors. 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 of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone acetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation. The RXRA/PPARA heterodimer is required for PPARA transcriptional activity on fatty acid oxidation genes such as ACOX1 and the P450 system genes. {ECO
InteractionQ03463:- (xeno); NbExp=3; IntAct=EBI-78598, EBI-9159704; Q71SY5:MED25; NbExp=4; IntAct=EBI-78598, EBI-394558; Q15788:NCOA1; NbExp=5; IntAct=EBI-78598, EBI-455189; Q9JLI4:Ncoa6 (xeno); NbExp=2; IntAct=EBI-78598, EBI-286271; P27986:PIK3R1; NbExp=8; IntAct=EBI-78598, EBI-79464; P10276:RARA; NbExp=4; IntAct=EBI-78598, EBI-413374; P42224:STAT1; NbExp=2; IntAct=EBI-78598, EBI-1057697;
PtmPhosphorylated on serine and threonine residues mainly in the N-terminal modulating domain. Constiutively phosphorylated on Ser- 21 in the presence or absence of ligand. 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. This phosphorylation is required for repression of cAMP- mediated transcriptional activity of RARA. {ECO
PtmSumoylation negatively regulates transcriptional activity. Desumoylated specifically by SENP6.
SimilarityBelongs to the nuclear hormone receptor family. NR2 subfamily.
SimilarityContains 1 nuclear receptor DNA-binding domain.
Subcellular LocationNucleus {ECO
SubunitHomodimer. Heterodimer with RARA; required for ligand- dependent retinoic acid receptor transcriptional activity. Heterodimer with PPARA (via the leucine-like zipper in the LBD); the interaction is required for PPARA transcriptional activity. Also heterodimerizes with PPARG. Interacts with NCOA3 and NCOA6 coactivators. Interacts with FAM120B (By similarity). Interacts with PELP1, SENP6, SFPQ, DNTTIP2 and RNF8. 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. Interacts with PRMT2. Interacts with ASXL1 (By similarity). Interacts with BHLHE40/DEC1, BHLHE41/DEC2, NCOR1 and NCOR2. Interacts in a ligand-dependent fashion with MED1 and NCOA1. {ECO
Tissue SpecificityHighly expressed in liver, also found in lung, kidney and heart.
Web ResourceName=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/rxra/";
Web ResourceName=Wikipedia; Note=Retinoid X receptor entry; URL="http://en.wikipedia.org/wiki/Retinoid_X_receptor";