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Protein Page:
RXRA (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
RXRA 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. 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. 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 and NCOA1. Highly expressed in liver, also found in lung, kidney and heart. Belongs to the nuclear hormone receptor family. NR2 subfamily. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; DNA binding protein; Nuclear receptor
Chromosomal Location of Human Ortholog: 9q34.3
Cellular Component: nucleoplasm; nuclear chromatin; nucleus
Molecular Function: ligand-dependent nuclear receptor activity; zinc ion binding; chromatin DNA binding; transcription coactivator activity; protein binding; enzyme binding; DNA binding; vitamin D receptor binding; retinoid-X receptor activity; protein heterodimerization activity; steroid hormone receptor activity; retinoic acid receptor activity; transcription factor activity
Biological Process: retinoic acid receptor signaling pathway; transcription initiation from RNA polymerase II promoter; cholesterol metabolic process; response to retinoic acid; vitamin metabolic process; in utero embryonic development; ventricular cardiac muscle cell differentiation; cardiac muscle cell proliferation; cellular lipid metabolic process; negative regulation of transcription from RNA polymerase II promoter; protein homotetramerization; virus-host interaction; ventricular cardiac muscle morphogenesis; steroid hormone mediated signaling; positive regulation of transcription from RNA polymerase II promoter; gene expression; embryo implantation; maternal placenta development
Reference #:  P19793 (UniProtKB)
Alt. Names/Synonyms: FLJ00280; FLJ00318; FLJ16020; FLJ16733; MGC102720; NR2B1; Nuclear receptor subfamily 2 group B member 1; Retinoic acid receptor RXR-alpha; Retinoid X receptor alpha; retinoid X receptor, alpha; RXR-alpha; RXRA
Gene Symbols: RXRA
Molecular weight: 50,811 Da
Basal Isoelectric point: 7.92  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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RXRA

Protein Structure Not Found.


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Sites Implicated In
transcription, altered: S27‑p, Y249‑p, S260‑p
transcription, inhibited: S32‑p, T82‑p, Y249‑p, S260‑p
activity, inhibited: S27‑p, S32‑p, Y249‑p, S260‑p
intracellular localization: S260‑p
molecular association, regulation: S32‑p, T82‑p
protein stabilization: S260‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 K4 ____MDTKHFLPLDF
0 1 S17-p DFSTQVNsSLtsPTG
0 1 T20-p TQVNsSLtsPTGRGs
2 8 S21-p QVNsSLtsPTGRGsM
1 0 S27-p tsPTGRGsMAAPsLH
2 0 S32-p RGsMAAPsLHPSLGP
1 0 S56 SPISTLSSPINGMGP
1 0 S70 PPFSVISSPMGPHSM
3 0 T82-p HSMSVPTtPTLGFST
2 0 K108-sm VSSSEDIkPPLGLNG
0 1 S129-p HPSGNMAsFTKHICA
0 2 Y150-p SGKHYGVySCEGCKG
2 0 Y249-p VEPKTETyVEANMGL
0 1 S259-p ANMGLNPssPNDPVt
8 1 S260-p NMGLNPssPNDPVtN
0 1 T266-p ssPNDPVtNICQAAD
0 1 K381 VLFNPDSKGLSNPAE
0 1 Y397-p EALREKVyASLEAyC
0 1 Y403-p VyASLEAyCKHKYPE
0 2 K417-ub EQPGRFAkLLLRLPA
  mouse

 
K4-ub ____MDTkHFLPLDF
S17 DFSTQVNSSSLNsPT
N21 QVNSSSLNsPTGRGS
S22-p VNSSSLNsPTGRGSM
S28 NsPTGRGSMAVPSLH
S33 RGSMAVPSLHPSLGP
S61-p SPISTLSsPINGMGP
S75-p PPFSVISsPMGPHSM
T87-p HSMSVPTtPTLGFGT
K113 VSSTEDIKPPLGLNG
S134 HPSGNMASFTKHICA
Y155 SGKHYGVYSCEGCKG
Y254 VEPKTETYVEANMGL
S264 ANMGLNPSsPNDPVT
S265-p NMGLNPSsPNDPVTN
T271 SsPNDPVTNICQAAD
K386-ub VLFNPDSkGLSNPAE
Y402 EALREKVYASLEAYC
Y408 VYASLEAYCKHKYPE
K422-ub EQPGRFAkLLLRLPA
  rat

 
K4 ____MDTKHFLPLDF
S17 DFSTQVNSSSLSsPT
S21 QVNSSSLSsPTGRGS
S22-p VNSSSLSsPTGRGSM
S28 SsPTGRGSMAAPSLH
S33 RGSMAAPSLHPSLGP
S61 SPISTLSSPINGMGP
S75 PPFSVISSPMGPHSM
T87 HSMSVPTTPTLGFET
K113 VSSSEDIKPPLGLNG
S134 HPSGNMSSFTKHICA
Y155 SGKHYGVYSCEGCKG
Y254 VEPKTETYVEANMGL
S264 ANMGLNPSSPNDPVT
S265 NMGLNPSSPNDPVTN
T271 SSPNDPVTNICQAAD
K386 VLFNPDSKGLSNPAE
Y402 EALREKVYASLEAYC
Y408 VYASLEAYCKHKYPE
K422 EQPGRFAKLLLRLPA
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