Retinoic acid receptor RXR-alpha (Protein name
), RXRA_MOUSE from NCBI database.
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Gene name:
Rxra(Nr2b1);
Protein name:
Retinoic acid receptor RXR-alpha;
Alternative:
Retinoid X receptor alpha;Nuclear receptor subfamily 2 group B member 1;
Organism:
Mouse (Mus musculus).
General Annotation
Sub Unit:
Homodimer (By similarity). 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 (By similarity). Interacts with coactivator NCOA3, PELP1, SENP6, SFPQ, DNTTIP2 and RNF8. Interacts with PRMT2 (By similarity). Interacts with coactivator NCOA6, and FAM120B.
Function:
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 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.
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Cited for: NUCLEOTIDE SEQUENCE [MRNA];HETERODIMERIZATION WITH RARA;FUNCTION
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Cited for: NUCLEOTIDE SEQUENCE [MRNA];IDENTIFICATION OF LIGAND
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Cited for: PROTEIN SEQUENCE OF 5-16; 27-46; 291-307 AND 446-465;SUBUNIT
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Cited for: PHOSPHORYLATION AT SER-22; SER-61; SER-75; THR-87 AND SER-265;FUNCTION;MUTAGENESIS OF SER-22; SER-44; SER-48; SER-54; SER-61; SER-75; THR-87; SER-96; SER-101 AND SER-265
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Cited for: PHOSPHORYLATION AT SER-22;FUNCTION;MUTAGENESIS OF SER-22
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Cited for: INTERACTION WITH ASXL1 AND NCOA1;MUTAGENESIS OF 455-PHE-LEU-456 AND 459-MET-LEU-460
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Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 230-462 OF MUTANT ALA-318 IN COMPLEX WITH H.SAPIENS RARA
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Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 230-467 IN COMPLEX WITH RARB AND MED1