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P28700

- RXRA_MOUSE

UniProt

P28700 - RXRA_MOUSE

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Protein

Retinoic acid receptor RXR-alpha

Gene

Rxra

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

  1. 9-cis retinoic acid receptor activity Source: MGI
  2. chromatin DNA binding Source: MGI
  3. DNA binding Source: MGI
  4. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: MGI
  5. retinoic acid-responsive element binding Source: Ensembl
  6. sequence-specific DNA binding Source: MGI
  7. sequence-specific DNA binding transcription factor activity Source: MGI
  8. steroid hormone receptor activity Source: InterPro
  9. transcription factor binding Source: UniProtKB
  10. vitamin D response element binding Source: Ensembl
  11. zinc ion binding Source: InterPro

GO - Biological processi

  1. angiogenesis involved in coronary vascular morphogenesis Source: DFLAT
  2. camera-type eye development Source: MGI
  3. cardiac muscle cell differentiation Source: DFLAT
  4. cardiac muscle cell proliferation Source: DFLAT
  5. embryo implantation Source: MGI
  6. heart development Source: DFLAT
  7. heart morphogenesis Source: DFLAT
  8. in utero embryonic development Source: MGI
  9. maternal placenta development Source: MGI
  10. mesenchyme development Source: DFLAT
  11. modulation by virus of host morphology or physiology Source: Ensembl
  12. negative regulation of gene expression Source: DFLAT
  13. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  14. peroxisome proliferator activated receptor signaling pathway Source: Ensembl
  15. placenta development Source: MGI
  16. positive regulation of transcription, DNA-templated Source: DFLAT
  17. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  18. positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus Source: MGI
  19. regulation of branching involved in prostate gland morphogenesis Source: MGI
  20. regulation of transcription, DNA-templated Source: MGI
  21. regulation of transcription from RNA polymerase II promoter Source: MGI
  22. response to retinoic acid Source: Ensembl
  23. retinoic acid receptor signaling pathway Source: MGI
  24. secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development Source: MGI
  25. ventricular cardiac muscle cell differentiation Source: MGI
  26. ventricular cardiac muscle tissue morphogenesis Source: MGI
  27. 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_118837. Rora activates circadian gene expression.
REACT_196516. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
REACT_198351. RORA activates circadian gene expression.
REACT_198352. REV-ERBA represses gene expression.
REACT_198602. PPARA activates gene expression.
REACT_198969. Activation of gene expression by SREBF (SREBP).
REACT_203193. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_205251. Transcriptional activation of mitochondrial biogenesis.
REACT_207530. Synthesis of bile acids and bile salts.
REACT_226284. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_226440. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
REACT_227038. Endogenous sterols.
REACT_234105. Nuclear Receptor transcription pathway.
REACT_239346. Recycling of bile acids and salts.
REACT_241925. Circadian Clock.
REACT_252217. Transcriptional regulation of white adipocyte differentiation.
REACT_257219. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
REACT_257268. Import of palmitoyl-CoA into the mitochondrial matrix.
REACT_268398. Orphan transporters.
REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

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: Chromosome 2

Organism-specific databases

MGIiMGI:98214. Rxra.

Subcellular locationi

GO - Cellular componenti

  1. nuclear chromatin Source: Ensembl
  2. nucleoplasm Source: Reactome
  3. nucleus Source: MGI
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 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.
GenevestigatoriP28700.

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. 15 interactions.
IntActiP28700. 14 interactions.
MINTiMINT-2775018.

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 .
CCDSi CCDS15830.1.
PIRi S26668.
RefSeqi NP_035435.1. NM_011305.3.
UniGenei Mm.24624.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DKF X-ray 2.50 A 230-462 [» ]
1XDK X-ray 2.90 A/E 230-467 [» ]
3A9E X-ray 2.75 A 228-467 [» ]
ProteinModelPortali P28700.
SMRi P28700. Positions 132-464.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 203038. 15 interactions.
IntActi P28700. 14 interactions.
MINTi MINT-2775018.

Chemistry

BindingDBi P28700.
ChEMBLi CHEMBL3084.
GuidetoPHARMACOLOGYi 610.

PTM databases

PhosphoSitei P28700.

Proteomic databases

MaxQBi P28700.
PaxDbi P28700.
PRIDEi P28700.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000077257 ; ENSMUSP00000076491 ; ENSMUSG00000015846 .
ENSMUST00000166775 ; ENSMUSP00000133044 ; ENSMUSG00000015846 .
GeneIDi 20181.
KEGGi mmu:20181.
UCSCi uc008ixs.1. mouse.

Organism-specific databases

CTDi 6256.
MGIi MGI:98214. Rxra.

Phylogenomic databases

eggNOGi NOG327099.
GeneTreei ENSGT00760000118948.
HOGENOMi HOG000260821.
HOVERGENi HBG005606.
InParanoidi P28700.
KOi K08524.
OMAi KHFLPLD.
PhylomeDBi P28700.
TreeFami TF352097.

Enzyme and pathway databases

Reactomei REACT_118837. Rora activates circadian gene expression.
REACT_196516. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
REACT_198351. RORA activates circadian gene expression.
REACT_198352. REV-ERBA represses gene expression.
REACT_198602. PPARA activates gene expression.
REACT_198969. Activation of gene expression by SREBF (SREBP).
REACT_203193. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_205251. Transcriptional activation of mitochondrial biogenesis.
REACT_207530. Synthesis of bile acids and bile salts.
REACT_226284. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_226440. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
REACT_227038. Endogenous sterols.
REACT_234105. Nuclear Receptor transcription pathway.
REACT_239346. Recycling of bile acids and salts.
REACT_241925. Circadian Clock.
REACT_252217. Transcriptional regulation of white adipocyte differentiation.
REACT_257219. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
REACT_257268. Import of palmitoyl-CoA into the mitochondrial matrix.
REACT_268398. Orphan transporters.
REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Miscellaneous databases

ChiTaRSi Rxra. mouse.
EvolutionaryTracei P28700.
NextBioi 297705.
PROi P28700.
SOURCEi Search...

Gene expression databases

Bgeei P28700.
CleanExi MM_RXRA.
ExpressionAtlasi P28700. baseline and differential.
Genevestigatori P28700.

Family and domain databases

Gene3Di 1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProi IPR021780. 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 ]
Pfami PF00104. Hormone_recep. 1 hit.
PF11825. Nuc_recep-AF1. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view ]
PRINTSi PR00545. RETINOIDXR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTi SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view ]
SUPFAMi SSF48508. SSF48508. 1 hit.
PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: November 26, 2014
This is version 153 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