Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P28700

- RXRA_MOUSE

UniProt

P28700 - RXRA_MOUSE

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 1 (01 Dec 1992)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. protein binding Source: UniProtKB
    6. retinoic acid-responsive element binding Source: Ensembl
    7. sequence-specific DNA binding Source: MGI
    8. sequence-specific DNA binding transcription factor activity Source: MGI
    9. steroid hormone receptor activity Source: InterPro
    10. transcription factor binding Source: UniProtKB
    11. vitamin D response element binding Source: Ensembl
    12. 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

    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_205251. Transcriptional activation of mitochondrial biogenesis.
    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

    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. 3 Publications
    Mutagenesisi44 – 441S → A: No effect on constituitive phosphorylation. 2 Publications
    Mutagenesisi48 – 481S → A: No effect on constituitive phosphorylation. 2 Publications
    Mutagenesisi54 – 541S → A: No effect on constituitive phosphorylation. 2 Publications
    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. 2 Publications
    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. 2 Publications
    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. 2 Publications
    Mutagenesisi96 – 961S → A: No effect on constituitive phosphorylation. 2 Publications
    Mutagenesisi101 – 1011S → A: No effect on constituitive phosphorylation. 2 Publications
    Mutagenesisi265 – 2651S → A: No effect on constiuitive phosphorylation but loss of stress-induced phosphorylation. No effect on RXRA transcriptional activity. 2 Publications
    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

    ArrayExpressiP28700.
    BgeeiP28700.
    CleanExiMM_RXRA.
    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 – 2344
    Helixi237 – 24610
    Helixi269 – 28214
    Helixi284 – 2896
    Turni292 – 2965
    Helixi299 – 32123
    Beta strandi323 – 3308
    Beta strandi336 – 3383
    Helixi339 – 3446
    Helixi348 – 35710
    Helixi359 – 3646
    Helixi369 – 38012
    Helixi391 – 41222
    Helixi419 – 4246
    Helixi426 – 43813
    Turni439 – 4435
    Helixi447 – 4493
    Helixi452 – 46110

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    GeneTreeiENSGT00740000115010.
    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

    MDTKHFLPLD FSTQVNSSSL NSPTGRGSMA VPSLHPSLGP GIGSPLGSPG    50
    QLHSPISTLS SPINGMGPPF SVISSPMGPH SMSVPTTPTL GFGTGSPQLN 100
    SPMNPVSSTE DIKPPLGLNG VLKVPAHPSG NMASFTKHIC AICGDRSSGK 150
    HYGVYSCEGC KGFFKRTVRK DLTYTCRDNK DCLIDKRQRN RCQYCRYQKC 200
    LAMGMKREAV QEERQRGKDR NENEVESTSS ANEDMPVEKI LEAELAVEPK 250
    TETYVEANMG LNPSSPNDPV TNICQAADKQ LFTLVEWAKR IPHFSELPLD 300
    DQVILLRAGW NELLIASFSH RSIAVKDGIL LATGLHVHRN SAHSAGVGAI 350
    FDRVLTELVS KMRDMQMDKT ELGCLRAIVL FNPDSKGLSN PAEVEALREK 400
    VYASLEAYCK HKYPEQPGRF AKLLLRLPAL RSIGLKCLEH LFFFKLIGDT 450
    PIDTFLMEML EAPHQAT 467
    Length:467
    Mass (Da):51,217
    Last modified:December 1, 1992 - v1
    Checksum:i0AF62396BCDC87DB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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 ENSGT00740000115010.
    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_205251. Transcriptional activation of mitochondrial biogenesis.
    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

    ArrayExpressi P28700.
    Bgeei P28700.
    CleanExi MM_RXRA.
    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: October 1, 2014
    This is version 151 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