Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Retinoic acid receptor RXR-alpha

Gene

Rxra

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi140 – 20566Nuclear receptorPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri140 – 16021NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri176 – 20025NR C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • 9-cis retinoic acid receptor activity Source: MGI
  • chromatin DNA binding Source: MGI
  • DNA binding Source: MGI
  • enzyme binding Source: MGI
  • ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: MGI
  • protein heterodimerization activity Source: MGI
  • retinoic acid-responsive element binding Source: MGI
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: MGI
  • sequence-specific DNA binding Source: MGI
  • sequence-specific DNA binding transcription factor activity Source: MGI
  • steroid hormone receptor activity Source: InterPro
  • transcription factor binding Source: UniProtKB
  • vitamin D receptor binding Source: MGI
  • vitamin D response element binding Source: Ensembl
  • zinc ion binding Source: InterPro

GO - Biological processi

  • angiogenesis involved in coronary vascular morphogenesis Source: DFLAT
  • camera-type eye development Source: MGI
  • cardiac muscle cell differentiation Source: DFLAT
  • cardiac muscle cell proliferation Source: DFLAT
  • embryo implantation Source: MGI
  • heart development Source: DFLAT
  • heart morphogenesis Source: DFLAT
  • in utero embryonic development Source: MGI
  • maternal placenta development Source: MGI
  • mesenchyme development Source: DFLAT
  • modulation by virus of host morphology or physiology Source: MGI
  • negative regulation of gene expression Source: DFLAT
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • peroxisome proliferator activated receptor signaling pathway Source: MGI
  • placenta development Source: MGI
  • positive regulation of transcription, DNA-templated Source: DFLAT
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus Source: MGI
  • positive regulation of translational initiation by iron Source: MGI
  • protein homotetramerization Source: MGI
  • regulation of branching involved in prostate gland morphogenesis Source: MGI
  • regulation of transcription, DNA-templated Source: MGI
  • regulation of transcription from RNA polymerase II promoter Source: MGI
  • response to retinoic acid Source: MGI
  • retinoic acid receptor signaling pathway Source: MGI
  • secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development Source: MGI
  • ventricular cardiac muscle cell differentiation Source: MGI
  • ventricular cardiac muscle tissue morphogenesis Source: MGI
  • visceral serous pericardium development Source: DFLAT
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
REACT_276696. Nuclear Receptor transcription pathway.
REACT_278177. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_281686. Endogenous sterols.
REACT_283453. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
REACT_293784. Import of palmitoyl-CoA into the mitochondrial matrix.
REACT_300927. Recycling of bile acids and salts.
REACT_306383. Signaling by Retinoic Acid.
REACT_309805. Transcriptional regulation of white adipocyte differentiation.
REACT_314031. Synthesis of bile acids and bile salts.
REACT_325766. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_332733. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).

Names & Taxonomyi

Protein namesi
Recommended name:
Retinoic acid receptor RXR-alpha
Alternative name(s):
Nuclear receptor subfamily 2 group B member 1
Retinoid X receptor alpha
Gene namesi
Name:Rxra
Synonyms:Nr2b1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:98214. Rxra.

Subcellular locationi

GO - Cellular componenti

  • nuclear chromatin Source: MGI
  • nucleoplasm Source: Reactome
  • nucleus Source: MGI
  • receptor complex Source: MGI
  • RNA polymerase II transcription factor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi22 – 221S → A: Loss of constituitive phosphorylation. No effect on RXRA transcriptional activity. 2 Publications
Mutagenesisi44 – 441S → A: No effect on constituitive phosphorylation. 1 Publication
Mutagenesisi48 – 481S → A: No effect on constituitive phosphorylation. 1 Publication
Mutagenesisi54 – 541S → A: No effect on constituitive phosphorylation. 1 Publication
Mutagenesisi61 – 611S → A: No effect on constituitive phosphorylation, decreased stress-induced phosphorylation but no effect on RXRA transcriptional activity. Abolishes stress-induced phosphorylation but no effect on RXRA transcriptional activity; when associated with A-75 and A-87. No effect on RXRA transcriptional activity. 1 Publication
Mutagenesisi75 – 751S → A: No effect on constituitive phosphorylation, decreased stress-induced phosphorylation but no effect on RXRA transcriptional activity. Abolishes stress-induced phosphorylation but no effect on RXRA transcriptional activity; when associated with A-61 and A-87. 1 Publication
Mutagenesisi87 – 871T → A: No effect on constituitive phosphorylation, decreased stress-induced phosphorylation but no effect on RXRA transcriptional activity. Abolishes stress-induced phosphorylation but no effect on RXRA transcriptional activity; when associated with A-61 and A-75. phosphorylation. No effect on RXRA transcriptional activity. 1 Publication
Mutagenesisi96 – 961S → A: No effect on constituitive phosphorylation. 1 Publication
Mutagenesisi101 – 1011S → A: No effect on constituitive phosphorylation. 1 Publication
Mutagenesisi265 – 2651S → A: No effect on constiuitive phosphorylation but loss of stress-induced phosphorylation. No effect on RXRA transcriptional activity. 1 Publication
Mutagenesisi455 – 4562FL → AA: Abolishes interaction with ASXL1 and NCOA1. 1 Publication
Mutagenesisi459 – 4602ML → AA: Abolishes interaction with ASXL1 and NCOA1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 467467Retinoic acid receptor RXR-alphaPRO_0000053567Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei22 – 221Phosphoserine2 Publications
Modified residuei28 – 281PhosphoserineBy similarity
Modified residuei61 – 611Phosphoserine; by MAPK8 and MAPK91 Publication
Modified residuei75 – 751Phosphoserine; by MAPK8 and MAPK91 Publication
Modified residuei87 – 871Phosphothreonine; by MAPK8 and MAPK91 Publication
Cross-linki113 – 113Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei264 – 2641PhosphoserineBy similarity
Modified residuei265 – 2651Phosphoserine; by MAPK8 and MAPK91 Publication

Post-translational modificationi

Phosphorylated on serine and threonine residues mainly in the N-terminal modulating domain. Phosphorylated on Ser-28, in vitro, by PKA. This phosphorylation is required for repression of cAMP-mediated transcriptional activity of RARA (By similarity). Constiutively phosphorylated on Ser-22 in the presence or absence of ligand. Under stress conditions, hyperphosphorylated by activated JNK on Ser-61, Ser-75, Thr-87 and Ser-265.By similarity2 Publications
Sumoylation negatively regulates transcriptional activity. Desumoylated specifically by SENP6 (By similarity).By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP28700.
PaxDbiP28700.
PRIDEiP28700.

PTM databases

PhosphoSiteiP28700.

Expressioni

Gene expression databases

BgeeiP28700.
CleanExiMM_RXRA.
ExpressionAtlasiP28700. baseline and differential.
GenevisibleiP28700. MM.

Interactioni

Subunit structurei

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. Interacts with BHLHE40/DEC1, BHLHE41/DEC2, NCOR1 and NCOR2. Interacts in a ligand-dependent fashion with MED1 (By similarity). Interacts with coactivator NCOA6, and FAM120B. Interacts with ASXL1. Interacts in a ligand-dependent fashion with NCOA1.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ASXL1Q8IXJ92EBI-346715,EBI-1646500From a different organism.
Asxl1P595982EBI-346715,EBI-5743705
MED25Q71SY53EBI-346715,EBI-394558From a different organism.
SFPQP23246-13EBI-346715,EBI-355463From a different organism.

Protein-protein interaction databases

BioGridi203038. 16 interactions.
IntActiP28700. 14 interactions.
MINTiMINT-2775018.
STRINGi10090.ENSMUSP00000076491.

Structurei

Secondary structure

1
467
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi231 – 2344Combined sources
Helixi237 – 24610Combined sources
Helixi269 – 28214Combined sources
Helixi284 – 2896Combined sources
Turni292 – 2965Combined sources
Helixi299 – 32123Combined sources
Beta strandi323 – 3308Combined sources
Beta strandi336 – 3383Combined sources
Helixi339 – 3446Combined sources
Helixi348 – 35710Combined sources
Helixi359 – 3646Combined sources
Helixi369 – 38012Combined sources
Helixi391 – 41222Combined sources
Helixi419 – 4246Combined sources
Helixi426 – 43813Combined sources
Turni439 – 4435Combined sources
Helixi447 – 4493Combined sources
Helixi452 – 46110Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DKFX-ray2.50A230-462[»]
1XDKX-ray2.90A/E230-467[»]
3A9EX-ray2.75A228-467[»]
ProteinModelPortaliP28700.
SMRiP28700. Positions 132-464.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28700.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 139139Modulating domainBy similarityAdd
BLAST
Regioni206 – 22924HingeAdd
BLAST
Regioni230 – 467238Ligand-binding domainAdd
BLAST

Domaini

Composed of three domains: a modulating N-terminal or AF1 domain, a DNA-binding domain and a C-terminal ligand-binding or AF2 domain.

Sequence similaritiesi

Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri140 – 16021NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri176 – 20025NR C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG327099.
GeneTreeiENSGT00760000118948.
HOGENOMiHOG000260821.
HOVERGENiHBG005606.
InParanoidiP28700.
KOiK08524.
OMAiKHFLPLD.
PhylomeDBiP28700.
TreeFamiTF352097.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR021780. Nuc_recep-AF1.
IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR000003. Retinoid-X_rcpt/HNF4.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF00104. Hormone_recep. 1 hit.
PF11825. Nuc_recep-AF1. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR00545. RETINOIDXR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P28700-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDTKHFLPLD FSTQVNSSSL NSPTGRGSMA VPSLHPSLGP GIGSPLGSPG
60 70 80 90 100
QLHSPISTLS SPINGMGPPF SVISSPMGPH SMSVPTTPTL GFGTGSPQLN
110 120 130 140 150
SPMNPVSSTE DIKPPLGLNG VLKVPAHPSG NMASFTKHIC AICGDRSSGK
160 170 180 190 200
HYGVYSCEGC KGFFKRTVRK DLTYTCRDNK DCLIDKRQRN RCQYCRYQKC
210 220 230 240 250
LAMGMKREAV QEERQRGKDR NENEVESTSS ANEDMPVEKI LEAELAVEPK
260 270 280 290 300
TETYVEANMG LNPSSPNDPV TNICQAADKQ LFTLVEWAKR IPHFSELPLD
310 320 330 340 350
DQVILLRAGW NELLIASFSH RSIAVKDGIL LATGLHVHRN SAHSAGVGAI
360 370 380 390 400
FDRVLTELVS KMRDMQMDKT ELGCLRAIVL FNPDSKGLSN PAEVEALREK
410 420 430 440 450
VYASLEAYCK HKYPEQPGRF AKLLLRLPAL RSIGLKCLEH LFFFKLIGDT
460
PIDTFLMEML EAPHQAT
Length:467
Mass (Da):51,217
Last modified:December 1, 1992 - v1
Checksum:i0AF62396BCDC87DB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84817 mRNA. Translation: AAA40080.1.
X66223 mRNA. Translation: CAA46962.1.
CCDSiCCDS15830.1.
PIRiS26668.
RefSeqiNP_035435.1. NM_011305.3.
UniGeneiMm.24624.

Genome annotation databases

EnsembliENSMUST00000077257; ENSMUSP00000076491; ENSMUSG00000015846.
ENSMUST00000166775; ENSMUSP00000133044; ENSMUSG00000015846.
GeneIDi20181.
KEGGimmu:20181.
UCSCiuc008ixs.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84817 mRNA. Translation: AAA40080.1.
X66223 mRNA. Translation: CAA46962.1.
CCDSiCCDS15830.1.
PIRiS26668.
RefSeqiNP_035435.1. NM_011305.3.
UniGeneiMm.24624.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DKFX-ray2.50A230-462[»]
1XDKX-ray2.90A/E230-467[»]
3A9EX-ray2.75A228-467[»]
ProteinModelPortaliP28700.
SMRiP28700. Positions 132-464.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203038. 16 interactions.
IntActiP28700. 14 interactions.
MINTiMINT-2775018.
STRINGi10090.ENSMUSP00000076491.

Chemistry

BindingDBiP28700.
ChEMBLiCHEMBL3084.
GuidetoPHARMACOLOGYi610.

PTM databases

PhosphoSiteiP28700.

Proteomic databases

MaxQBiP28700.
PaxDbiP28700.
PRIDEiP28700.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000077257; ENSMUSP00000076491; ENSMUSG00000015846.
ENSMUST00000166775; ENSMUSP00000133044; ENSMUSG00000015846.
GeneIDi20181.
KEGGimmu:20181.
UCSCiuc008ixs.1. mouse.

Organism-specific databases

CTDi6256.
MGIiMGI:98214. Rxra.

Phylogenomic databases

eggNOGiNOG327099.
GeneTreeiENSGT00760000118948.
HOGENOMiHOG000260821.
HOVERGENiHBG005606.
InParanoidiP28700.
KOiK08524.
OMAiKHFLPLD.
PhylomeDBiP28700.
TreeFamiTF352097.

Enzyme and pathway databases

ReactomeiREACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
REACT_276696. Nuclear Receptor transcription pathway.
REACT_278177. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_281686. Endogenous sterols.
REACT_283453. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
REACT_293784. Import of palmitoyl-CoA into the mitochondrial matrix.
REACT_300927. Recycling of bile acids and salts.
REACT_306383. Signaling by Retinoic Acid.
REACT_309805. Transcriptional regulation of white adipocyte differentiation.
REACT_314031. Synthesis of bile acids and bile salts.
REACT_325766. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_332733. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).

Miscellaneous databases

ChiTaRSiRxra. mouse.
EvolutionaryTraceiP28700.
NextBioi297705.
PROiP28700.
SOURCEiSearch...

Gene expression databases

BgeeiP28700.
CleanExiMM_RXRA.
ExpressionAtlasiP28700. baseline and differential.
GenevisibleiP28700. MM.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR021780. Nuc_recep-AF1.
IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR000003. Retinoid-X_rcpt/HNF4.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF00104. Hormone_recep. 1 hit.
PF11825. Nuc_recep-AF1. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR00545. RETINOIDXR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Purification, cloning, and RXR identity of the HeLa cell factor with which RAR or TR heterodimerizes to bind target sequences efficiently."
    Leid M., Kastner P., Lyons R., Nakshatri H., Saunders M., Zacharewsi T., Chen J.Y., Staub A., Garnier J.-M., Mader S., Chambon P.
    Cell 68:377-395(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], HETERODIMERIZATION WITH RARA, FUNCTION.
  2. "Characterization of three RXR genes that mediate the action of 9-cis retinoic acid."
    Mangelsdorf D.J., Borgmeyer U., Heyman R.A., Zhou J.Y., Ong E.S., Oro A.E., Kakizuka A., Evans R.M.
    Genes Dev. 6:329-344(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION OF LIGAND.
  3. "Adipocyte-specific transcription factor ARF6 is a heterodimeric complex of two nuclear hormone receptors, PPAR gamma and RXR alpha."
    Tontonoz P., Graves R.A., Budavari A.I., Erdjument-Bromage H., Lui M., Hu E., Tempst P., Spiegelman B.M.
    Nucleic Acids Res. 22:5628-5634(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 5-16; 27-46; 291-307 AND 446-465, SUBUNIT.
    Tissue: Adipose tissue.
  4. "Hyperphosphorylation of the retinoid X receptor alpha by activated c-Jun NH2-terminal kinases."
    Adam-Stitah S., Penna L., Chambon P., Rochette-Egly C.
    J. Biol. Chem. 274:18932-18941(1999) [PubMed] [Europe PMC] [Abstract]
    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.
  5. "Isolation and characterization of peroxisome proliferator-activated receptor (PPAR) interacting protein (PRIP) as a coactivator for PPAR."
    Zhu Y.-J., Kan L., Qi C., Kanwar Y.S., Yeldandi A.V., Rao M.S., Reddy J.K.
    J. Biol. Chem. 275:13510-13516(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NCOA6.
  6. "The phosphorylation site located in the A region of retinoic X receptor alpha is required for the antiproliferative effect of retinoic acid (RA) and the activation of RA target genes in F9 cells."
    Bastien J., Adam-Stitah S., Plassat J.L., Chambon P., Rochette-Egly C.
    J. Biol. Chem. 277:28683-28689(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-22, FUNCTION, MUTAGENESIS OF SER-22.
  7. "Additional sex comb-like 1 (ASXL1), in cooperation with SRC-1, acts as a ligand-dependent coactivator for retinoic acid receptor."
    Cho Y.S., Kim E.J., Park U.H., Sin H.S., Um S.J.
    J. Biol. Chem. 281:17588-17598(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ASXL1 AND NCOA1, MUTAGENESIS OF 455-PHE-LEU-456 AND 459-MET-LEU-460.
  8. "Constitutive coactivator of peroxisome proliferator-activated receptor (PPARgamma), a novel coactivator of PPARgamma that promotes adipogenesis."
    Li D., Kang Q., Wang D.-M.
    Mol. Endocrinol. 21:2320-2333(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FAM120B.
  9. "Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains."
    Bourguet W., Vivat V., Wurtz J.M., Chambon P., Gronemeyer H., Moras D.
    Mol. Cell 5:289-298(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 230-462 OF MUTANT ALA-318 IN COMPLEX WITH H.SAPIENS RARA.
  10. "Characterization of the interaction between retinoic acid receptor/retinoid X receptor (RAR/RXR) heterodimers and transcriptional coactivators through structural and fluorescence anisotropy studies."
    Pogenberg V., Guichou J.F., Vivat-Hannah V., Kammerer S., Perez E., Germain P., de Lera A.R., Gronemeyer H., Royer C.A., Bourguet W.
    J. Biol. Chem. 280:1625-1633(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 230-467 IN COMPLEX WITH RARB AND MED1.

Entry informationi

Entry nameiRXRA_MOUSE
AccessioniPrimary (citable) accession number: P28700
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: June 24, 2015
This is version 159 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.