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P19793

- RXRA_HUMAN

UniProt

P19793 - RXRA_HUMAN

Protein

Retinoic acid receptor RXR-alpha

Gene

RXRA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 176 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      Previous versions | rss
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    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.4 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi135 – 20066Nuclear receptorPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri135 – 15521NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri171 – 19525NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. 9-cis retinoic acid receptor activity Source: ProtInc
    2. chromatin DNA binding Source: Ensembl
    3. DNA binding Source: MGI
    4. enzyme binding Source: UniProtKB
    5. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: BHF-UCL
    6. protein binding Source: UniProtKB
    7. protein heterodimerization activity Source: UniProtKB
    8. retinoic acid receptor activity Source: BHF-UCL
    9. retinoic acid-responsive element binding Source: UniProtKB
    10. RNA polymerase II regulatory region sequence-specific DNA binding Source: MGI
    11. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    12. steroid hormone receptor activity Source: InterPro
    13. transcription coactivator activity Source: ProtInc
    14. vitamin D receptor binding Source: BHF-UCL
    15. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cardiac muscle cell proliferation Source: Ensembl
    2. cellular lipid metabolic process Source: Reactome
    3. cholesterol metabolic process Source: BHF-UCL
    4. embryo implantation Source: Ensembl
    5. gene expression Source: Reactome
    6. in utero embryonic development Source: Ensembl
    7. maternal placenta development Source: Ensembl
    8. modulation by virus of host morphology or physiology Source: UniProtKB
    9. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    10. peroxisome proliferator activated receptor signaling pathway Source: UniProtKB
    11. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    12. protein homotetramerization Source: MGI
    13. regulation of branching involved in prostate gland morphogenesis Source: Ensembl
    14. response to retinoic acid Source: BHF-UCL
    15. retinoic acid receptor signaling pathway Source: BHF-UCL
    16. secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development Source: Ensembl
    17. small molecule metabolic process Source: Reactome
    18. transcription initiation from RNA polymerase II promoter Source: Reactome
    19. ventricular cardiac muscle cell differentiation Source: Ensembl
    20. ventricular cardiac muscle tissue morphogenesis Source: Ensembl
    21. vitamin metabolic process Source: ProtInc

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Host-virus interaction, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_116145. PPARA activates gene expression.
    REACT_118659. RORA activates circadian gene expression.
    REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
    REACT_118789. REV-ERBA represses gene expression.
    REACT_147904. Activation of gene expression by SREBF (SREBP).
    REACT_15525. Nuclear Receptor transcription pathway.
    REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
    REACT_200608. Transcriptional activation of mitochondrial biogenesis.
    REACT_24941. Circadian Clock.
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.
    SignaLinkiP19793.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:10477. RXRA.

    Subcellular locationi

    Nucleus 1 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

    1. nuclear chromatin Source: BHF-UCL
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi27 – 271S → A: Abolishes phosphorylation. No change in increase of RARA-mediated transcriptional activity. 2 Publications
    Mutagenesisi27 – 271S → A: Increase in RARA-mediated transcriptional activity. 2 Publications

    Organism-specific databases

    PharmGKBiPA34890.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 462462Retinoic acid receptor RXR-alphaPRO_0000053566Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei21 – 211PhosphoserineBy similarity
    Modified residuei27 – 271Phosphoserine1 Publication
    Modified residuei56 – 561Phosphoserine; by MAPK8 and MAPK9By similarity
    Modified residuei70 – 701Phosphoserine; by MAPK8 and MAPK9By similarity
    Modified residuei82 – 821Phosphothreonine; by MAPK8 and MAPK9By similarity
    Cross-linki108 – 108Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei260 – 2601Phosphoserine; by MAPK8 and MAPK9By similarity

    Post-translational modificationi

    Phosphorylated on serine and threonine residues mainly in the N-terminal modulating domain. Constiutively phosphorylated on Ser-21 in the presence or absence of ligand. 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. This phosphorylation is required for repression of cAMP-mediated transcriptional activity of RARA.By similarity1 Publication
    Sumoylation negatively regulates transcriptional activity. Desumoylated specifically by SENP6.1 Publication

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP19793.
    PaxDbiP19793.
    PRIDEiP19793.

    PTM databases

    PhosphoSiteiP19793.

    Miscellaneous databases

    PMAP-CutDBP19793.

    Expressioni

    Tissue specificityi

    Highly expressed in liver, also found in lung, kidney and heart.

    Gene expression databases

    ArrayExpressiP19793.
    BgeeiP19793.
    CleanExiHS_RXRA.
    GenevestigatoriP19793.

    Organism-specific databases

    HPAiCAB004565.
    CAB005352.

    Interactioni

    Subunit structurei

    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 By similarity. 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 By similarity. Interacts with BHLHE40/DEC1, BHLHE41/DEC2, NCOR1 and NCOR2. Interacts in a ligand-dependent fashion with MED1 and NCOA1.By similarity15 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q034633EBI-78598,EBI-9159704From a different organism.
    MED25Q71SY54EBI-78598,EBI-394558
    NCOA1Q157885EBI-78598,EBI-455189
    Ncoa6Q9JLI42EBI-78598,EBI-286271From a different organism.
    PIK3R1P279868EBI-78598,EBI-79464
    RARAP102764EBI-78598,EBI-413374
    STAT1P422242EBI-78598,EBI-1057697

    Protein-protein interaction databases

    BioGridi112168. 107 interactions.
    DIPiDIP-641N.
    IntActiP19793. 39 interactions.
    MINTiMINT-98407.
    STRINGi9606.ENSP00000419692.

    Structurei

    Secondary structure

    1
    462
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi130 – 1334
    Turni136 – 1383
    Beta strandi141 – 1466
    Beta strandi147 – 1504
    Helixi153 – 16513
    Beta strandi172 – 1754
    Turni181 – 1866
    Helixi188 – 19710
    Helixi202 – 2043
    Helixi226 – 2294
    Helixi232 – 24211
    Helixi246 – 2505
    Turni251 – 2533
    Beta strandi258 – 2614
    Helixi264 – 28421
    Helixi289 – 2913
    Helixi294 – 31623
    Turni317 – 3193
    Beta strandi320 – 3256
    Turni327 – 3293
    Beta strandi331 – 3333
    Helixi334 – 3385
    Turni339 – 3413
    Helixi343 – 35210
    Helixi354 – 3596
    Helixi364 – 37512
    Beta strandi380 – 3823
    Helixi386 – 40722
    Helixi414 – 4196
    Helixi422 – 44221
    Helixi449 – 4546

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BY4X-ray2.10A/B/C/D129-209[»]
    1DSZX-ray1.70B129-212[»]
    1FBYX-ray2.25A/B224-462[»]
    1FM6X-ray2.10A/U225-462[»]
    1FM9X-ray2.10A225-462[»]
    1G1UX-ray2.50A/B/C/D225-462[»]
    1G5YX-ray2.00A/B/C/D225-462[»]
    1K74X-ray2.30A225-462[»]
    1LBDX-ray2.70A201-460[»]
    1MV9X-ray1.90A223-462[»]
    1MVCX-ray1.90A223-462[»]
    1MZNX-ray1.90A/C/E/G223-462[»]
    1R0NX-ray2.60A130-206[»]
    1RDTX-ray2.40A225-462[»]
    1RXRNMR-A130-212[»]
    1XLSX-ray2.96A/B/C/D227-458[»]
    1XV9X-ray2.70A/C227-462[»]
    1XVPX-ray2.60A/C227-462[»]
    1YNWX-ray3.00B130-228[»]
    2ACLX-ray2.80A/C/E/G225-462[»]
    2NLLX-ray1.90A135-200[»]
    2P1TX-ray1.80A223-462[»]
    2P1UX-ray2.20A223-462[»]
    2P1VX-ray2.20A223-462[»]
    2ZXZX-ray3.00A223-462[»]
    2ZY0X-ray2.90A/C223-462[»]
    3DZUX-ray3.20A11-462[»]
    3DZYX-ray3.10A11-462[»]
    3E00X-ray3.10A11-462[»]
    3E94X-ray1.90A223-462[»]
    3FALX-ray2.36A/C225-462[»]
    3FC6X-ray2.06A/C225-462[»]
    3FUGX-ray2.00A223-462[»]
    3H0AX-ray2.10A228-455[»]
    3KWYX-ray2.30A223-462[»]
    3NSPX-ray2.90A/B223-462[»]
    3NSQX-ray2.60A/B223-462[»]
    3OAPX-ray2.05A228-458[»]
    3OZJX-ray2.10A/C225-462[»]
    3PCUX-ray2.00A229-458[»]
    3R29X-ray2.90A/B223-462[»]
    3R2AX-ray3.00A/B/C/D223-462[»]
    3R5MX-ray2.80A/C223-462[»]
    3UVVX-ray2.95B225-462[»]
    4J5WX-ray2.80C/D227-462[»]
    4J5XX-ray2.80C/D227-462[»]
    4K4JX-ray2.00A228-458[»]
    4K6IX-ray2.10A228-458[»]
    4M8EX-ray2.40A228-458[»]
    4M8HX-ray2.20A228-458[»]
    4N5GX-ray2.11A/B/C/D223-462[»]
    4N8RX-ray2.03A/B/C/D223-462[»]
    4NQAX-ray3.10A/H98-462[»]
    4POHX-ray2.30A228-458[»]
    4POJX-ray2.00A228-458[»]
    4PP3X-ray2.00A228-458[»]
    4PP5X-ray2.00A228-458[»]
    DisProtiDP00062.
    ProteinModelPortaliP19793.
    SMRiP19793. Positions 127-459.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19793.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 134134ModulatingBy similarityAdd
    BLAST
    Regioni201 – 22424HingeAdd
    BLAST
    Regioni225 – 462238Ligand-bindingAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri135 – 15521NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri171 – 19525NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG327099.
    HOVERGENiHBG005606.
    InParanoidiP19793.
    KOiK08524.
    OMAiKHFLPLD.
    PhylomeDBiP19793.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P19793-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDTKHFLPLD FSTQVNSSLT SPTGRGSMAA PSLHPSLGPG IGSPGQLHSP    50
    ISTLSSPING MGPPFSVISS PMGPHSMSVP TTPTLGFSTG SPQLSSPMNP 100
    VSSSEDIKPP LGLNGVLKVP AHPSGNMASF TKHICAICGD RSSGKHYGVY 150
    SCEGCKGFFK RTVRKDLTYT CRDNKDCLID KRQRNRCQYC RYQKCLAMGM 200
    KREAVQEERQ RGKDRNENEV ESTSSANEDM PVERILEAEL AVEPKTETYV 250
    EANMGLNPSS PNDPVTNICQ AADKQLFTLV EWAKRIPHFS ELPLDDQVIL 300
    LRAGWNELLI ASFSHRSIAV KDGILLATGL HVHRNSAHSA GVGAIFDRVL 350
    TELVSKMRDM QMDKTELGCL RAIVLFNPDS KGLSNPAEVE ALREKVYASL 400
    EAYCKHKYPE QPGRFAKLLL RLPALRSIGL KCLEHLFFFK LIGDTPIDTF 450
    LMEMLEAPHQ MT 462
    Length:462
    Mass (Da):50,811
    Last modified:February 1, 1991 - v1
    Checksum:i7F952B580AD84C42
    GO
    Isoform 2 (identifier: P19793-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-97: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:365
    Mass (Da):41,060
    Checksum:i6F0D30787329986D
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti261 – 2611P → L.
    Corresponds to variant rs2234960 [ dbSNP | Ensembl ].
    VAR_014620
    Natural varianti327 – 3271A → S.
    Corresponds to variant rs1805345 [ dbSNP | Ensembl ].
    VAR_050582
    Natural varianti336 – 3361S → I.
    Corresponds to variant rs1805345 [ dbSNP | Ensembl ].
    VAR_014621
    Natural varianti398 – 3981A → V.
    Corresponds to variant rs11542209 [ dbSNP | Ensembl ].
    VAR_050583

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9797Missing in isoform 2. 1 PublicationVSP_056565Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52773 mRNA. Translation: CAA36982.1.
    AB307705 mRNA. Translation: BAH02296.1.
    AK131192 mRNA. Translation: BAG54745.1.
    AC156789 Genomic DNA. No translation available.
    AL354796, AL669970 Genomic DNA. Translation: CAH70571.1.
    AL669970, AL354796 Genomic DNA. Translation: CAM45733.1.
    AL683798 Genomic DNA. No translation available.
    CH471090 Genomic DNA. Translation: EAW88123.1.
    BC110998 mRNA. Translation: AAI10999.1.
    DQ303444 Genomic DNA. Translation: ABB96254.1.
    CCDSiCCDS35172.1.
    PIRiS09592.
    RefSeqiNP_001278850.1. NM_001291921.1.
    NP_002948.1. NM_002957.5.
    UniGeneiHs.590886.

    Genome annotation databases

    EnsembliENST00000481739; ENSP00000419692; ENSG00000186350.
    ENST00000540193; ENSP00000442123; ENSG00000186350.
    GeneIDi6256.
    KEGGihsa:6256.
    UCSCiuc004cfb.2. human.

    Polymorphism databases

    DMDMi133701.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Wikipedia

    Retinoid X receptor entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52773 mRNA. Translation: CAA36982.1 .
    AB307705 mRNA. Translation: BAH02296.1 .
    AK131192 mRNA. Translation: BAG54745.1 .
    AC156789 Genomic DNA. No translation available.
    AL354796 , AL669970 Genomic DNA. Translation: CAH70571.1 .
    AL669970 , AL354796 Genomic DNA. Translation: CAM45733.1 .
    AL683798 Genomic DNA. No translation available.
    CH471090 Genomic DNA. Translation: EAW88123.1 .
    BC110998 mRNA. Translation: AAI10999.1 .
    DQ303444 Genomic DNA. Translation: ABB96254.1 .
    CCDSi CCDS35172.1.
    PIRi S09592.
    RefSeqi NP_001278850.1. NM_001291921.1.
    NP_002948.1. NM_002957.5.
    UniGenei Hs.590886.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BY4 X-ray 2.10 A/B/C/D 129-209 [» ]
    1DSZ X-ray 1.70 B 129-212 [» ]
    1FBY X-ray 2.25 A/B 224-462 [» ]
    1FM6 X-ray 2.10 A/U 225-462 [» ]
    1FM9 X-ray 2.10 A 225-462 [» ]
    1G1U X-ray 2.50 A/B/C/D 225-462 [» ]
    1G5Y X-ray 2.00 A/B/C/D 225-462 [» ]
    1K74 X-ray 2.30 A 225-462 [» ]
    1LBD X-ray 2.70 A 201-460 [» ]
    1MV9 X-ray 1.90 A 223-462 [» ]
    1MVC X-ray 1.90 A 223-462 [» ]
    1MZN X-ray 1.90 A/C/E/G 223-462 [» ]
    1R0N X-ray 2.60 A 130-206 [» ]
    1RDT X-ray 2.40 A 225-462 [» ]
    1RXR NMR - A 130-212 [» ]
    1XLS X-ray 2.96 A/B/C/D 227-458 [» ]
    1XV9 X-ray 2.70 A/C 227-462 [» ]
    1XVP X-ray 2.60 A/C 227-462 [» ]
    1YNW X-ray 3.00 B 130-228 [» ]
    2ACL X-ray 2.80 A/C/E/G 225-462 [» ]
    2NLL X-ray 1.90 A 135-200 [» ]
    2P1T X-ray 1.80 A 223-462 [» ]
    2P1U X-ray 2.20 A 223-462 [» ]
    2P1V X-ray 2.20 A 223-462 [» ]
    2ZXZ X-ray 3.00 A 223-462 [» ]
    2ZY0 X-ray 2.90 A/C 223-462 [» ]
    3DZU X-ray 3.20 A 11-462 [» ]
    3DZY X-ray 3.10 A 11-462 [» ]
    3E00 X-ray 3.10 A 11-462 [» ]
    3E94 X-ray 1.90 A 223-462 [» ]
    3FAL X-ray 2.36 A/C 225-462 [» ]
    3FC6 X-ray 2.06 A/C 225-462 [» ]
    3FUG X-ray 2.00 A 223-462 [» ]
    3H0A X-ray 2.10 A 228-455 [» ]
    3KWY X-ray 2.30 A 223-462 [» ]
    3NSP X-ray 2.90 A/B 223-462 [» ]
    3NSQ X-ray 2.60 A/B 223-462 [» ]
    3OAP X-ray 2.05 A 228-458 [» ]
    3OZJ X-ray 2.10 A/C 225-462 [» ]
    3PCU X-ray 2.00 A 229-458 [» ]
    3R29 X-ray 2.90 A/B 223-462 [» ]
    3R2A X-ray 3.00 A/B/C/D 223-462 [» ]
    3R5M X-ray 2.80 A/C 223-462 [» ]
    3UVV X-ray 2.95 B 225-462 [» ]
    4J5W X-ray 2.80 C/D 227-462 [» ]
    4J5X X-ray 2.80 C/D 227-462 [» ]
    4K4J X-ray 2.00 A 228-458 [» ]
    4K6I X-ray 2.10 A 228-458 [» ]
    4M8E X-ray 2.40 A 228-458 [» ]
    4M8H X-ray 2.20 A 228-458 [» ]
    4N5G X-ray 2.11 A/B/C/D 223-462 [» ]
    4N8R X-ray 2.03 A/B/C/D 223-462 [» ]
    4NQA X-ray 3.10 A/H 98-462 [» ]
    4POH X-ray 2.30 A 228-458 [» ]
    4POJ X-ray 2.00 A 228-458 [» ]
    4PP3 X-ray 2.00 A 228-458 [» ]
    4PP5 X-ray 2.00 A 228-458 [» ]
    DisProti DP00062.
    ProteinModelPortali P19793.
    SMRi P19793. Positions 127-459.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112168. 107 interactions.
    DIPi DIP-641N.
    IntActi P19793. 39 interactions.
    MINTi MINT-98407.
    STRINGi 9606.ENSP00000419692.

    Chemistry

    BindingDBi P19793.
    ChEMBLi CHEMBL2363071.
    DrugBanki DB00459. Acitretin.
    DB00210. Adapalene.
    DB00523. Alitretinoin.
    DB00926. Etretinate.
    GuidetoPHARMACOLOGYi 610.

    PTM databases

    PhosphoSitei P19793.

    Polymorphism databases

    DMDMi 133701.

    Proteomic databases

    MaxQBi P19793.
    PaxDbi P19793.
    PRIDEi P19793.

    Protocols and materials databases

    DNASUi 6256.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000481739 ; ENSP00000419692 ; ENSG00000186350 .
    ENST00000540193 ; ENSP00000442123 ; ENSG00000186350 .
    GeneIDi 6256.
    KEGGi hsa:6256.
    UCSCi uc004cfb.2. human.

    Organism-specific databases

    CTDi 6256.
    GeneCardsi GC09P137208.
    HGNCi HGNC:10477. RXRA.
    HPAi CAB004565.
    CAB005352.
    MIMi 180245. gene.
    neXtProti NX_P19793.
    PharmGKBi PA34890.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG327099.
    HOVERGENi HBG005606.
    InParanoidi P19793.
    KOi K08524.
    OMAi KHFLPLD.
    PhylomeDBi P19793.
    TreeFami TF352097.

    Enzyme and pathway databases

    Reactomei REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_116145. PPARA activates gene expression.
    REACT_118659. RORA activates circadian gene expression.
    REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
    REACT_118789. REV-ERBA represses gene expression.
    REACT_147904. Activation of gene expression by SREBF (SREBP).
    REACT_15525. Nuclear Receptor transcription pathway.
    REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
    REACT_200608. Transcriptional activation of mitochondrial biogenesis.
    REACT_24941. Circadian Clock.
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.
    SignaLinki P19793.

    Miscellaneous databases

    EvolutionaryTracei P19793.
    GeneWikii Retinoid_X_receptor_alpha.
    GenomeRNAii 6256.
    NextBioi 24295.
    PMAP-CutDB P19793.
    PROi P19793.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P19793.
    Bgeei P19793.
    CleanExi HS_RXRA.
    Genevestigatori P19793.

    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. "Nuclear receptor that identifies a novel retinoic acid response pathway."
      Mangelsdorf D.J., Ong E.S., Dyck J.A., Evans R.M.
      Nature 345:224-229(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Kidney.
    2. "DNA-binding profiling of human hormone nuclear receptors via fluorescence correlation spectroscopy in a cell-free system."
      Kobayashi T., Kodani Y., Nozawa A., Endo Y., Sawasaki T.
      FEBS Lett. 582:2737-2744(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DNA-BINDING.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Amygdala.
    4. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Ovary.
    7. NIEHS SNPs program
      Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-462.
    8. "9-cis retinoic acid is a high affinity ligand for the retinoid X receptor."
      Heyman R.A., Mangelsdorf D.J., Dyck J.A., Stein R.B., Eichele G., Evans R.M., Thaller C.
      Cell 68:397-406(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF LIGAND.
    9. "Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300."
      Chen H., Lin R.J., Schiltz R.L., Chakravarti D., Nash A., Nagy L., Privalsky M.L., Nakatani Y., Evans R.M.
      Cell 90:569-580(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NCOA3.
    10. "A nuclear factor ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo."
      Lee S.-K., Anzick S.L., Choi J.-E., Bubendorf L., Guan X.-Y., Jung Y.-K., Kallioniemi O.-P., Kononen J., Trent J.M., Azorsa D., Jhun B.-H., Cheong J.H., Lee Y.C., Meltzer P.S., Lee J.W.
      J. Biol. Chem. 274:34283-34293(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NCOA6.
    11. "Conserved amino acids in the ligand-binding and tau(i) domains of the peroxisome proliferator-activated receptor alpha are necessary for heterodimerization with RXR."
      Gorla-Bajszczak A., Juge-Aubry C., Pernin A., Burger A.G., Meier C.A.
      Mol. Cell. Endocrinol. 147:37-47(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: HETERODIMERIZATION WITH PPARA, FUNCTION.
    12. "Serine 27, a human retinoid X receptor alpha residue, phosphorylated by protein kinase A is essential for cyclicAMP-mediated downregulation of RXRalpha function."
      Harish S., Ashok M.S., Khanam T., Rangarajan P.N.
      Biochem. Biophys. Res. Commun. 279:853-857(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-27, FUNCTION, MUTAGENESIS OF SER-27.
    13. "PSF is a novel corepressor that mediates its effect through Sin3A and the DNA binding domain of nuclear hormone receptors."
      Mathur M., Tucker P.W., Samuels H.H.
      Mol. Cell. Biol. 21:2298-2311(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SFPQ.
    14. "Interaction of hepatitis C virus core protein with retinoid X receptor alpha modulates its transcriptional activity."
      Tsutsumi T., Suzuki T., Shimoike T., Suzuki R., Moriya K., Shintani Y., Fujie H., Matsuura Y., Koike K., Miyamura T.
      Hepatology 35:937-946(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HCV CORE PROTEIN AND PPARA, SUBCELLULAR LOCATION, FUNCTION.
    15. "Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha."
      Qi C., Chang J., Zhu Y., Yeldandi A.V., Rao S.M., Zhu Y.-J.
      J. Biol. Chem. 277:28624-28630(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRMT2.
    16. "ERBP, a novel estrogen receptor binding protein enhancing the activity of estrogen receptor."
      Bu H., Kashireddy P., Chang J., Zhu Y.T., Zhang Z., Zheng W., Rao S.M., Zhu Y.-J.
      Biochem. Biophys. Res. Commun. 317:54-59(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DNTTIP2.
    17. "The RING finger protein, RNF8, interacts with retinoid X receptor alpha and enhances its transcription-stimulating activity."
      Takano Y., Adachi S., Okuno M., Muto Y., Yoshioka T., Matsushima-Nishiwaki R., Tsurumi H., Ito K., Friedman S.L., Moriwaki H., Kojima S., Okano Y.
      J. Biol. Chem. 279:18926-18934(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RNF8.
    18. "9-cis-retinoic acid up-regulates expression of transcriptional coregulator PELP1, a novel coactivator of the retinoid X receptor alpha pathway."
      Singh R.R., Gururaj A.E., Vadlamudi R.K., Kumar R.
      J. Biol. Chem. 281:15394-15404(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PELP1.
    19. "Negative modulation of RXRalpha transcriptional activity by small ubiquitin-related modifier (SUMO) modification and its reversal by SUMO-specific protease SUSP1."
      Choi S.J., Chung S.S., Rho E.J., Lee H.W., Lee M.H., Choi H.S., Seol J.H., Baek S.H., Bang O.S., Chung C.H.
      J. Biol. Chem. 281:30669-30677(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-108, INTERACTION WITH SENP6.
    20. "Lysine trimethylation of retinoic acid receptor-alpha: a novel means to regulate receptor function."
      Huq M.D., Tsai N.-P., Khan S.A., Wei L.-N.
      Mol. Cell. Proteomics 6:677-688(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: HETERODIMERIZATION WITH RARA.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. "The basic helix-loop-helix proteins differentiated embryo chondrocyte (DEC) 1 and DEC2 function as corepressors of retinoid X receptors."
      Cho Y., Noshiro M., Choi M., Morita K., Kawamoto T., Fujimoto K., Kato Y., Makishima M.
      Mol. Pharmacol. 76:1360-1369(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BHLHE40/DEC1; BHLHE41/DEC2; NCOA1; MED1; NCOR1 AND NCOR2.
    23. "Activity of retinoic acid receptor-alpha is directly regulated at its protein kinase A sites in response to follicle-stimulating hormone signaling."
      Santos N.C., Kim K.H.
      Endocrinology 151:2361-2372(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: HETERODIMERIZATION WITH RARA, FUNCTION, MUTAGENESIS OF SER-27.
    24. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. "NMR assignments and secondary structure of the retinoid X receptor alpha DNA-binding domain. Evidence for the novel C-terminal helix."
      Lee M.S., Sem D.S., Kliewer S.A., Provencal J., Evans R.M., Wright P.E.
      Eur. J. Biochem. 224:639-650(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 130-223.
    26. "Structural determinants of nuclear receptor assembly on DNA direct repeats."
      Rastinejad F., Perlmann T., Evans R.M., Sigler P.B.
      Nature 375:203-211(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 130-209.
    27. "Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha."
      Bourguet W., Ruff M., Chambon P., Gronemeyer H., Moras D.
      Nature 375:377-382(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 225-462.
    28. "High-resolution solution structure of the retinoid X receptor DNA-binding domain."
      Holmbeck S.M., Foster M.P., Casimiro D.R., Sem D.S., Dyson H.J., Wright P.E.
      J. Mol. Biol. 281:271-284(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 130-212.
    29. "Structure of the RXR-RAR DNA-binding complex on the retinoic acid response element DR1."
      Rastinejad F., Wagner T., Zhao Q., Khorasanizadeh S.
      EMBO J. 19:1045-1054(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 129-209 IN COMPLEX WITH RARA AND DNA.
    30. "Crystal structure of the human RXRalpha ligand-binding domain bound to its natural ligand: 9-cis retinoic acid."
      Egea P.F., Mitschler A., Rochel N., Ruff M., Chambon P., Moras D.
      EMBO J. 19:2592-2601(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 224-462 OF APO AND HOLO FORMS.
    31. "Structural basis for autorepression of retinoid X receptor by tetramer formation and the AF-2 helix."
      Gampe R.T. Jr., Montana V.G., Lambert M.H., Wisely G.B., Milburn M.V., Xu H.E.
      Genes Dev. 14:2229-2241(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 225-462 OF APO AND HOLO FORMS.
    32. Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 129-212 IN COMPLEX WITH DNA.
    33. "Asymmetry in the PPARgamma/RXRalpha crystal structure reveals the molecular basis of heterodimerization among nuclear receptors."
      Gampe R.T. Jr., Montana V.G., Lambert M.H., Miller A.B., Bledsoe R.K., Milburn M.V., Kliewer S.A., Willson T.M., Xu H.E.
      Mol. Cell 5:545-555(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 225-462 IN COMPLEX WITH PPARG; COACTIVATOR NCOA1; RETINOIC ACID AND SYNTHETIC ANTIDIABETIC AGONISTS ROSIGLITAZONE AND GI262570.
    34. "Structural determinants of ligand binding selectivity between the peroxisome proliferator-activated receptors."
      Xu H.E., Lambert M.H., Montana V.G., Plunket K.D., Moore L.B., Collins J.L., Oplinger J.A., Kliewer S.A., Gampe R.T. Jr., McKee D.D., Moore J.T., Willson T.M.
      Proc. Natl. Acad. Sci. U.S.A. 98:13919-13924(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 225-462 IN COMPLEX WITH PPARA OR PPARG; 9-CIS RETINOIC ACID; COACTIVATOR NCOA1 AND PPAR SYNTHETIC AGONIST GW409544.
    35. "The nuclear xenobiotic receptor CAR: structural determinants of constitutive activation and heterodimerization."
      Suino K., Peng L., Reynolds R., Li Y., Cha J.Y., Repa J.J., Kliewer S.A., Xu H.E.
      Mol. Cell 16:893-905(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF 227-458 IN COMPLEX WITH M.MUSCULUS NR1I13; R.NORVEGICUS NCOA2 AND AGONIST INSECTICIDE CONTAMINANT TCPOBOP.

    Entry informationi

    Entry nameiRXRA_HUMAN
    AccessioniPrimary (citable) accession number: P19793
    Secondary accession number(s): B3KY83, Q2NL52, Q2V504
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 176 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3