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P13631

- RARG_HUMAN

UniProt

P13631 - RARG_HUMAN

Protein

Retinoic acid receptor gamma

Gene

RARG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 178 (01 Oct 2014)
      Sequence version 1 (01 Jan 1990)
      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. In the absence of ligand, acts mainly as an activator of gene expression due to weak binding to corepressors. Required for limb bud development. In concert with RARA or RARB, required for skeletal growth, matrix homeostasis and growth plate function By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi90 – 15566Nuclear receptorPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri90 – 11021NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri126 – 15025NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: BHF-UCL
    2. protein binding Source: UniProtKB
    3. retinoic acid receptor activity Source: Ensembl
    4. retinoid X receptor binding Source: BHF-UCL
    5. sequence-specific DNA binding Source: InterPro
    6. sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    7. steroid hormone receptor activity Source: InterPro
    8. zinc ion binding Source: InterPro

    GO - Biological processi

    1. anterior/posterior pattern specification Source: Ensembl
    2. canonical Wnt signaling pathway Source: BHF-UCL
    3. cellular response to retinoic acid Source: Ensembl
    4. embryonic eye morphogenesis Source: BHF-UCL
    5. embryonic hindlimb morphogenesis Source: BHF-UCL
    6. gene expression Source: Reactome
    7. growth plate cartilage chondrocyte growth Source: Ensembl
    8. Harderian gland development Source: Ensembl
    9. multicellular organism growth Source: Ensembl
    10. negative regulation of cartilage development Source: Ensembl
    11. negative regulation of cell proliferation Source: BHF-UCL
    12. negative regulation of chondrocyte differentiation Source: Ensembl
    13. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    14. positive regulation of apoptotic process Source: BHF-UCL
    15. positive regulation of cell proliferation Source: Ensembl
    16. positive regulation of programmed cell death Source: BHF-UCL
    17. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    18. prostate gland epithelium morphogenesis Source: Ensembl
    19. regulation of cell size Source: BHF-UCL
    20. regulation of myelination Source: Ensembl
    21. response to retinoic acid Source: BHF-UCL
    22. retinoic acid receptor signaling pathway Source: BHF-UCL
    23. trachea cartilage development Source: Ensembl
    24. transcription initiation from RNA polymerase II promoter Source: Reactome

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_15525. Nuclear Receptor transcription pathway.
    SignaLinkiP13631.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Retinoic acid receptor gamma
    Short name:
    RAR-gamma
    Alternative name(s):
    Nuclear receptor subfamily 1 group B member 3
    Gene namesi
    Name:RARG
    Synonyms:NR1B3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:9866. RARG.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: BHF-UCL
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB
    4. transcription factor complex Source: BHF-UCL

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34227.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 454454Retinoic acid receptor gammaPRO_0000053472Add
    BLAST

    Proteomic databases

    MaxQBiP13631.
    PaxDbiP13631.
    PRIDEiP13631.

    PTM databases

    PhosphoSiteiP13631.

    Expressioni

    Gene expression databases

    ArrayExpressiP13631.
    BgeeiP13631.
    CleanExiHS_RARG.
    GenevestigatoriP13631.

    Organism-specific databases

    HPAiHPA053883.

    Interactioni

    Subunit structurei

    Homodimer. Heterodimer with a RXR molecule. Binds DNA preferentially as a RAR/RXR heterodimer. Forms a complex with PUS1 and the SRA1 RNA in the nucleus.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SORBS3O60504-22EBI-2568901,EBI-1222956

    Protein-protein interaction databases

    BioGridi111851. 32 interactions.
    IntActiP13631. 13 interactions.
    MINTiMINT-3007936.
    STRINGi9606.ENSP00000332695.

    Structurei

    Secondary structure

    1
    454
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi184 – 20017
    Helixi204 – 2063
    Helixi224 – 24623
    Helixi251 – 2533
    Helixi256 – 27722
    Turni281 – 2844
    Beta strandi285 – 2873
    Beta strandi292 – 2954
    Helixi296 – 3027
    Helixi305 – 3073
    Helixi308 – 31811
    Helixi319 – 3213
    Helixi325 – 33612
    Helixi347 – 36822
    Helixi375 – 40127
    Beta strandi404 – 4063
    Helixi410 – 4167

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EXAX-ray1.59A178-423[»]
    1EXXX-ray1.67A178-423[»]
    1FCXX-ray1.47A183-417[»]
    1FCYX-ray1.30A183-417[»]
    1FCZX-ray1.38A183-417[»]
    1FD0X-ray1.38A183-417[»]
    2LBDX-ray2.06A178-423[»]
    3LBDX-ray2.40A178-423[»]
    4LBDX-ray2.50A178-423[»]
    ProteinModelPortaliP13631.
    SMRiP13631. Positions 89-417.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP13631.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 8989ModulatingAdd
    BLAST
    Regioni156 – 20146HingeAdd
    BLAST
    Regioni202 – 421220Ligand-bindingAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri90 – 11021NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri126 – 15025NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG297448.
    HOVERGENiHBG005606.
    InParanoidiP13631.
    KOiK08529.
    OMAiRSPQPDQ.
    OrthoDBiEOG738053.
    PhylomeDBiP13631.
    TreeFamiTF328382.

    Family and domain databases

    Gene3Di1.10.565.10. 1 hit.
    3.30.50.10. 1 hit.
    InterProiIPR008946. Nucl_hormone_rcpt_ligand-bd.
    IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
    IPR003078. Retinoic_acid_rcpt.
    IPR001723. Str_hrmn_rcpt.
    IPR001628. Znf_hrmn_rcpt.
    IPR013088. Znf_NHR/GATA.
    [Graphical view]
    PfamiPF00104. Hormone_recep. 1 hit.
    PF00105. zf-C4. 1 hit.
    [Graphical view]
    PRINTSiPR01292. RETNOICACIDR.
    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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Note: Isoforms differ only in their N-terminal regions.

    Isoform 1 (identifier: P13631-1) [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

    MATNKERLFA AGALGPGSGY PGAGFPFAFP GALRGSPPFE MLSPSFRGLG    50
    QPDLPKEMAS LSVETQSTSS EEMVPSSPSP PPPPRVYKPC FVCNDKSSGY 100
    HYGVSSCEGC KGFFRRSIQK NMVYTCHRDK NCIINKVTRN RCQYCRLQKC 150
    FEVGMSKEAV RNDRNKKKKE VKEEGSPDSY ELSPQLEELI TKVSKAHQET 200
    FPSLCQLGKY TTNSSADHRV QLDLGLWDKF SELATKCIIK IVEFAKRLPG 250
    FTGLSIADQI TLLKAACLDI LMLRICTRYT PEQDTMTFSD GLTLNRTQMH 300
    NAGFGPLTDL VFAFAGQLLP LEMDDTETGL LSAICLICGD RMDLEEPEKV 350
    DKLQEPLLEA LRLYARRRRP SQPYMFPRML MKITDLRGIS TKGAERAITL 400
    KMEIPGPMPP LIREMLENPE MFEDDSSQPG PHPNASSEDE VPGGQGKGGL 450
    KSPA 454
    Length:454
    Mass (Da):50,342
    Last modified:January 1, 1990 - v1
    Checksum:i1EE27B22772D4AFD
    GO
    Isoform 2 (identifier: P13631-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-61: MATNKERLFA...PDLPKEMASL → MYDCMETFAP...FAWPQPASLQ

    Show »
    Length:443
    Mass (Da):49,308
    Checksum:i4D709194F5111E86
    GO
    Isoform 3 (identifier: P13631-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-72: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:382
    Mass (Da):42,926
    Checksum:i37AF909319A4B140
    GO
    Isoform 4 (identifier: P13631-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-111: MATNKERLFA...YGVSSCEGCK → MLALPLPPCW...LPGRNPPACN

    Note: No experimental confirmation available.

    Show »
    Length:432
    Mass (Da):47,931
    Checksum:iAA332A06D720ADB8
    GO

    Sequence cautioni

    The sequence CAA40548.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti118 – 1181I → T in CAB60726. 1 PublicationCurated
    Sequence conflicti172 – 1721K → R in AAG41594. 1 PublicationCurated
    Sequence conflicti252 – 2521T → A in CAB60726. 1 PublicationCurated
    Sequence conflicti342 – 3421M → V in BAH12478. (PubMed:14702039)Curated
    Sequence conflicti421 – 4211M → L in CAB60726. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti427 – 4271S → L.
    Corresponds to variant rs2229774 [ dbSNP | Ensembl ].
    VAR_038554
    Natural varianti430 – 4301G → S in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036061

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 111111MATNK…CEGCK → MLALPLPPCWSGAPPGEEGE SAAGPWCFQHPVSLQAGSRC TTVWKRLPRVRDGCTGRPGP GPACCAEPPAAPVSPDLNLL PGRNPPACN in isoform 4. 1 PublicationVSP_044776Add
    BLAST
    Alternative sequencei1 – 7272Missing in isoform 3. 1 PublicationVSP_044777Add
    BLAST
    Alternative sequencei1 – 6161MATNK…EMASL → MYDCMETFAPGPRRLYGAAG PGAGLLRRATGGSCFAGLES FAWPQPASLQ in isoform 2. 2 PublicationsVSP_031080Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24857 mRNA. Translation: AAA52692.1.
    M57707 mRNA. Translation: AAA63254.1.
    M38258 mRNA. Translation: AAA60254.1.
    AK297023 mRNA. Translation: BAH12478.1.
    AK297277 mRNA. Translation: BAH12537.1.
    AK316259 mRNA. Translation: BAH14630.1.
    AC021072 Genomic DNA. No translation available.
    AC073573 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW96676.1.
    BC093727 mRNA. Translation: AAH93727.1.
    BC093729 mRNA. Translation: AAH93729.1.
    M32074 mRNA. Translation: AAA60253.1.
    X57280 Genomic DNA. Translation: CAA40548.1. Sequence problems.
    AJ250835 Genomic DNA. Translation: CAB60726.1.
    AY013703 Genomic DNA. Translation: AAG41594.2.
    AY013704 Genomic DNA. Translation: AAG41595.1.
    CCDSiCCDS41790.1. [P13631-2]
    CCDS58236.1. [P13631-3]
    CCDS58237.1. [P13631-4]
    CCDS8850.1. [P13631-1]
    PIRiA33903.
    C35991.
    RefSeqiNP_000957.1. NM_000966.5. [P13631-1]
    NP_001036193.1. NM_001042728.2. [P13631-2]
    NP_001230659.1. NM_001243730.1. [P13631-3]
    NP_001230661.1. NM_001243732.1. [P13631-4]
    XP_005269113.1. XM_005269056.2. [P13631-1]
    XP_005269114.1. XM_005269057.1. [P13631-1]
    UniGeneiHs.1497.
    Hs.733399.

    Genome annotation databases

    EnsembliENST00000338561; ENSP00000343698; ENSG00000172819. [P13631-2]
    ENST00000394426; ENSP00000377947; ENSG00000172819. [P13631-1]
    ENST00000425354; ENSP00000388510; ENSG00000172819. [P13631-1]
    ENST00000543726; ENSP00000444335; ENSG00000172819. [P13631-4]
    GeneIDi5916.
    KEGGihsa:5916.
    UCSCiuc001sce.3. human. [P13631-1]
    uc010sob.2. human.

    Polymorphism databases

    DMDMi133498.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Retinoic acid receptor entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24857 mRNA. Translation: AAA52692.1 .
    M57707 mRNA. Translation: AAA63254.1 .
    M38258 mRNA. Translation: AAA60254.1 .
    AK297023 mRNA. Translation: BAH12478.1 .
    AK297277 mRNA. Translation: BAH12537.1 .
    AK316259 mRNA. Translation: BAH14630.1 .
    AC021072 Genomic DNA. No translation available.
    AC073573 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW96676.1 .
    BC093727 mRNA. Translation: AAH93727.1 .
    BC093729 mRNA. Translation: AAH93729.1 .
    M32074 mRNA. Translation: AAA60253.1 .
    X57280 Genomic DNA. Translation: CAA40548.1 . Sequence problems.
    AJ250835 Genomic DNA. Translation: CAB60726.1 .
    AY013703 Genomic DNA. Translation: AAG41594.2 .
    AY013704 Genomic DNA. Translation: AAG41595.1 .
    CCDSi CCDS41790.1. [P13631-2 ]
    CCDS58236.1. [P13631-3 ]
    CCDS58237.1. [P13631-4 ]
    CCDS8850.1. [P13631-1 ]
    PIRi A33903.
    C35991.
    RefSeqi NP_000957.1. NM_000966.5. [P13631-1 ]
    NP_001036193.1. NM_001042728.2. [P13631-2 ]
    NP_001230659.1. NM_001243730.1. [P13631-3 ]
    NP_001230661.1. NM_001243732.1. [P13631-4 ]
    XP_005269113.1. XM_005269056.2. [P13631-1 ]
    XP_005269114.1. XM_005269057.1. [P13631-1 ]
    UniGenei Hs.1497.
    Hs.733399.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EXA X-ray 1.59 A 178-423 [» ]
    1EXX X-ray 1.67 A 178-423 [» ]
    1FCX X-ray 1.47 A 183-417 [» ]
    1FCY X-ray 1.30 A 183-417 [» ]
    1FCZ X-ray 1.38 A 183-417 [» ]
    1FD0 X-ray 1.38 A 183-417 [» ]
    2LBD X-ray 2.06 A 178-423 [» ]
    3LBD X-ray 2.40 A 178-423 [» ]
    4LBD X-ray 2.50 A 178-423 [» ]
    ProteinModelPortali P13631.
    SMRi P13631. Positions 89-417.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111851. 32 interactions.
    IntActi P13631. 13 interactions.
    MINTi MINT-3007936.
    STRINGi 9606.ENSP00000332695.

    Chemistry

    BindingDBi P13631.
    ChEMBLi CHEMBL2363071.
    DrugBanki DB00459. Acitretin.
    DB00210. Adapalene.
    DB00523. Alitretinoin.
    DB00926. Etretinate.
    DB00799. Tazarotene.
    DB00755. Tretinoin.
    GuidetoPHARMACOLOGYi 592.

    PTM databases

    PhosphoSitei P13631.

    Polymorphism databases

    DMDMi 133498.

    Proteomic databases

    MaxQBi P13631.
    PaxDbi P13631.
    PRIDEi P13631.

    Protocols and materials databases

    DNASUi 5916.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000338561 ; ENSP00000343698 ; ENSG00000172819 . [P13631-2 ]
    ENST00000394426 ; ENSP00000377947 ; ENSG00000172819 . [P13631-1 ]
    ENST00000425354 ; ENSP00000388510 ; ENSG00000172819 . [P13631-1 ]
    ENST00000543726 ; ENSP00000444335 ; ENSG00000172819 . [P13631-4 ]
    GeneIDi 5916.
    KEGGi hsa:5916.
    UCSCi uc001sce.3. human. [P13631-1 ]
    uc010sob.2. human.

    Organism-specific databases

    CTDi 5916.
    GeneCardsi GC12M053604.
    H-InvDB HIX0129677.
    HGNCi HGNC:9866. RARG.
    HPAi HPA053883.
    MIMi 180190. gene.
    neXtProti NX_P13631.
    PharmGKBi PA34227.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG297448.
    HOVERGENi HBG005606.
    InParanoidi P13631.
    KOi K08529.
    OMAi RSPQPDQ.
    OrthoDBi EOG738053.
    PhylomeDBi P13631.
    TreeFami TF328382.

    Enzyme and pathway databases

    Reactomei REACT_15525. Nuclear Receptor transcription pathway.
    SignaLinki P13631.

    Miscellaneous databases

    EvolutionaryTracei P13631.
    GeneWikii Retinoic_acid_receptor_gamma.
    GenomeRNAii 5916.
    NextBioi 23030.
    PROi P13631.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P13631.
    Bgeei P13631.
    CleanExi HS_RARG.
    Genevestigatori P13631.

    Family and domain databases

    Gene3Di 1.10.565.10. 1 hit.
    3.30.50.10. 1 hit.
    InterProi IPR008946. Nucl_hormone_rcpt_ligand-bd.
    IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
    IPR003078. Retinoic_acid_rcpt.
    IPR001723. Str_hrmn_rcpt.
    IPR001628. Znf_hrmn_rcpt.
    IPR013088. Znf_NHR/GATA.
    [Graphical view ]
    Pfami PF00104. Hormone_recep. 1 hit.
    PF00105. zf-C4. 1 hit.
    [Graphical view ]
    PRINTSi PR01292. RETNOICACIDR.
    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "A functional retinoic acid receptor encoded by the gene on human chromosome 12."
      Ishikawa T., Umesono K., Mangelsdorf D.J., Aburatani H., Stanger B.Z., Shibasaki Y., Imawari M., Evans R.M., Takaku F.
      Mol. Endocrinol. 4:837-844(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Genomic organization of the retinoic acid receptor gamma gene."
      Lehmann J.M., Hoffmann B., Pfahl M.
      Nucleic Acids Res. 19:573-578(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING.
      Tissue: Placenta.
    4. "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] (ISOFORMS 2; 3 AND 4).
      Tissue: Brain, Tongue and Umbilical cord blood.
    5. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Colon.
    8. "Murine isoforms of retinoic acid receptor gamma with specific patterns of expression."
      Kastner P., Krust A., Mendelsohn C., Garnier J.-M., Zelent A., Leroy P., Staub A., Chambon P.
      Proc. Natl. Acad. Sci. U.S.A. 87:2700-2704(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-63 (ISOFORM 2).
    9. "RAR-gamma-2 expression is regulated through a retinoic acid response element embedded in Sp1 sites."
      Lehmann J.M., Zhang X.K., Pfahl M.
      Mol. Cell. Biol. 12:2976-2985(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55, ALTERNATIVE SPLICING.
      Tissue: Placenta.
    10. Gebhard W.
      Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 74-454.
      Tissue: Lung carcinoma.
    11. "Genomic organization of the human retinoic acid receptor gamma gene."
      Xu H., Clifford J.L.
      Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-191 AND 394-411.
    12. "Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid."
      Renaud J.-P., Rochel N., Ruff M., Vivat V., Chambon P., Gronemeyer H., Moras D.
      Nature 378:681-689(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 178-423.
    13. "Conformational adaptation of agonists to the human nuclear receptor RAR gamma."
      Klaholz B.P., Renaud J.-P., Mitschler A., Zusi C., Chambon P., Gronemeyer H., Moras D.
      Nat. Struct. Biol. 5:199-202(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 178-423.
    14. Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-430.

    Entry informationi

    Entry nameiRARG_HUMAN
    AccessioniPrimary (citable) accession number: P13631
    Secondary accession number(s): B7Z492
    , B7Z4F1, B7ZAE4, J3KNP6, P22932, Q15281, Q52LZ8, Q9BYX8, Q9H1I3, Q9UJ38
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 1, 1990
    Last modified: October 1, 2014
    This is version 178 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 12
      Human chromosome 12: 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