RXRA
entrez
6256
canonical
uniprot
P19793
canonical
ensembl
ENSG00000186350
resolver
ensp
ENSP00000419692
resolver
ensp
ENSP00000500402
resolver
enst
ENST00000672570
resolver
genesymbol
NR2B1
resolver
genesymbol
RXRA
resolver
genesymbol_syn
NR2B1
resolver
hgnc
HGNC:10477
resolver
uniprot
A0A5F9ZHH6
resolver
uniprot
B3KY83
resolver
uniprot
F1D8Q5
resolver
uniprot
Q2NL52
resolver
uniprot
Q2V504
resolver
uniprot
Q6P3U7
resolver
uniprot_entry
A0A5F9ZHH6_HUMAN
resolver
uniprot_entry
F1D8Q5_HUMAN
resolver
uniprot_entry
Q6P3U7_HUMAN
resolver
uniprot_entry
RXRA_HUMAN
resolver
uniprot_sec
B3KY83
resolver
uniprot_sec
Q2NL52
resolver
uniprot_sec
Q2V504
resolver
amino_acid_sequence
MDTKHFLPLDFSTQVNSSLTSPTGRGSMAAPSLHPSLGPGIGSPGQLHSPISTLSSPINGMGPPFSVISSPMGPHSMSVPTTPTLGFSTGSPQLSSPMNPVSSSEDIKPPLGLNGVLKVPAHPSGNMASFTKHICAICGDRSSGKHYGVYSCEGCKGFFKRTVRKDLTYTCRDNKDCLIDKRQRNRCQYCRYQKCLAMGMKREAVQEERQRGKDRNENEVESTSSANEDMPVERILEAELAVEPKTETYVEANMGLNPSSPNDPVTNICQAADKQLFTLVEWAKRIPHFSELPLDDQVILLRAGWNELLIASFSHRSIAVKDGILLATGLHVHRNSAHSAGVGAIFDRVLTELVSKMRDMQMDKTELGCLRAIVLFNPDSKGLSNPAEVEALREKVYASLEAYCKHKYPEQPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQMT
uniprot
proteins
function
FUNCTION: 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). {ECO:0000269|PubMed:10195690, ECO:0000269|PubMed:10874028, ECO:0000269|PubMed:11162439, ECO:0000269|PubMed:11915042, ECO:0000269|PubMed:12145331, ECO:0000269|PubMed:1310260, ECO:0000269|PubMed:15509776, ECO:0000269|PubMed:16107141, ECO:0000269|PubMed:17761950, ECO:0000269|PubMed:18800767, ECO:0000269|PubMed:19167885, ECO:0000269|PubMed:20215566, ECO:0000269|PubMed:25417649, ECO:0000269|PubMed:26463675, ECO:0000269|PubMed:28167758, ECO:0000269|PubMed:29021580, ECO:0000269|PubMed:30216632, ECO:0000269|PubMed:37478846, ECO:0000269|PubMed:9267036}.
uniprot
proteins
mass_dalton
50811
uniprot
proteins
mutagenesis
MUTAGEN 27; /note="S->A: Abolishes phosphorylation. No change in increase of RARA-mediated transcriptional activity."; /evidence="ECO:0000269|PubMed:11162439, ECO:0000269|PubMed:20215566"; MUTAGEN 27; /note="S->A: Increase in RARA-mediated transcriptional activity."; /evidence="ECO:0000269|PubMed:11162439, ECO:0000269|PubMed:20215566"; MUTAGEN 133..156; /note="Missing: Abolishes acetylation by EP300."; /evidence="ECO:0000269|PubMed:17761950"; MUTAGEN 145; /note="K->R: Abolishes acetylation by EP300, DNA binding and transcriptional activity. Impairs interaction with EP300."; /evidence="ECO:0000269|PubMed:17761950"; MUTAGEN 158..159; /note="FF->AA: Abolishes nuclear export."; /evidence="ECO:0000269|PubMed:12145331"; MUTAGEN 160..165; /note="KRTVRK->QGTVGQ: Abolishes nuclear localization and transcriptional activity."; /evidence="ECO:0000269|PubMed:12145331"; MUTAGEN 206..216; /note="Missing: No impact on acetylation by EP300."; /evidence="ECO:0000269|PubMed:17761950"; MUTAGEN 280; /note="V->A: Abolished ubiquitination and degradation by UBR5."; /evidence="ECO:0000269|PubMed:37478846"; MUTAGEN 352..462; /note="Missing: No impact on acetylation by EP300."; /evidence="ECO:0000269|PubMed:17761950"; MUTAGEN 357..360; /note="MRDM->ARDA: Abolishes nuclear export."; /evidence="ECO:0000269|PubMed:15509776"; MUTAGEN 418..430; /note="LLLRLPALRSIGL->ALARLPALRSIGA: Abolishes nuclear localization."; /evidence="ECO:0000269|PubMed:15509776"; MUTAGEN 434; /note="E->N,Q,K,A: As a heterodimer with NR1H4, impairs interaction with coactivator NCOA1. Impairs transcriptional activity."; /evidence="ECO:0000269|PubMed:30275017
uniprot
proteins
post_translational_modification
PTM: Acetylated by EP300; acetylation enhances DNA binding and transcriptional activity. {ECO:0000269|PubMed:17761950}.; PTM: 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). {ECO:0000250|UniProtKB:P28700, ECO:0000269|PubMed:11162439}.; PTM: 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). {ECO:0000269|PubMed:37478846}.; PTM: Sumoylation negatively regulates transcriptional activity. Desumoylated specifically by SENP6. {ECO:0000269|PubMed:16912044}.
uniprot
proteins
protein_family
NR2 subfamily
uniprot
proteins
protein_family
Nuclear hormone receptor family
uniprot
proteins
pubmed
10195690
uniprot
proteins
pubmed
10567404
uniprot
proteins
pubmed
10669605
uniprot
proteins
pubmed
10698945
uniprot
proteins
pubmed
10835357
uniprot
proteins
pubmed
10874028
uniprot
proteins
pubmed
10882139
uniprot
proteins
pubmed
10970886
uniprot
proteins
pubmed
11162439
uniprot
proteins
pubmed
11259580
uniprot
proteins
pubmed
11698662
uniprot
proteins
pubmed
11915042
uniprot
proteins
pubmed
12039952
uniprot
proteins
pubmed
12145331
uniprot
proteins
pubmed
1310260
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14981089
uniprot
proteins
pubmed
15047147
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15509776
uniprot
proteins
pubmed
15610733
uniprot
proteins
pubmed
16107141
uniprot
proteins
pubmed
16574651
uniprot
proteins
pubmed
16912044
uniprot
proteins
pubmed
17205979
uniprot
proteins
pubmed
17761950
uniprot
proteins
pubmed
18619963
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18800767
uniprot
proteins
pubmed
19167885
uniprot
proteins
pubmed
19786558
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20078863
uniprot
proteins
pubmed
20215566
uniprot
proteins
pubmed
2159111
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25417649
uniprot
proteins
pubmed
26463675
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28167758
uniprot
proteins
pubmed
28698609
uniprot
proteins
pubmed
29021580
uniprot
proteins
pubmed
30216632
uniprot
proteins
pubmed
30275017
uniprot
proteins
pubmed
37478846
uniprot
proteins
pubmed
7746322
uniprot
proteins
pubmed
7760929
uniprot
proteins
pubmed
7925381
uniprot
proteins
pubmed
9267036
uniprot
proteins
pubmed
9698548
uniprot
proteins
sequence_length
462
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:10874028, ECO:0000269|PubMed:11915042, ECO:0000269|PubMed:12145331, ECO:0000269|PubMed:15509776, ECO:0000269|PubMed:17761950, ECO:0000269|PubMed:28167758}. Cytoplasm {ECO:0000269|PubMed:12145331, ECO:0000269|PubMed:15509776}. Mitochondrion {ECO:0000269|PubMed:17761950}. Note=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). {ECO:0000269|PubMed:12145331, ECO:0000269|PubMed:15509776, ECO:0000269|PubMed:17761950, ECO:0000269|PubMed:28167758}.
uniprot
proteins