Retinoic acid receptor RXR-alpha (Protein name
), RXRA_HUMAN from NCBI database.
top
|
General Annotation
|
Antigen Annotation
|
3D
|
Predicted Eptitope
|
Vaild Sequence
|
Related Databases
|
Feedback
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:
Human (Homo sapiens).
General Annotation
Sub Unit:
Homodimer. 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.
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.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);DNA-BINDING
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2)
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: PHOSPHORYLATION AT SER-27;FUNCTION;MUTAGENESIS OF SER-27
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: INTERACTION WITH HCV CORE PROTEIN AND PPARA;SUBCELLULAR LOCATION;FUNCTION
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: INTERACTION WITH BHLHE40/DEC1; BHLHE41/DEC2; NCOA1; MED1; NCOR1 AND NCOR2
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: HETERODIMERIZATION WITH RARA;FUNCTION;MUTAGENESIS OF SER-27
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 130-209
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 225-462
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 129-209 IN COMPLEX WITH RARA AND DNA
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 224-462 OF APO AND HOLO FORMS
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 225-462 OF APO AND HOLO FORMS
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 129-212 IN COMPLEX WITH DNA
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 225-462 IN COMPLEX WITH PPARG; COACTIVATOR NCOA1; RETINOIC ACID AND SYNTHETIC ANTIDIABETIC AGONISTS ROSIGLITAZONE AND GI262570
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 225-462 IN COMPLEX WITH PPARA OR PPARG; 9-CIS RETINOIC ACID; COACTIVATOR NCOA1 AND PPAR SYNTHETIC AGONIST GW409544
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF 227-458 IN COMPLEX WITH M.MUSCULUS NR1I13; R.NORVEGICUS NCOA2 AND AGONIST INSECTICIDE CONTAMINANT TCPOBOP