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P18911

- RARG_MOUSE

UniProt

P18911 - RARG_MOUSE

Protein

Retinoic acid receptor gamma

Gene

Rarg

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 3 (05 Feb 2008)
      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 By similarity. Required for limb bud development. In concert with RARA or RARB, required for skeletal growth, matrix homeostasis and growth plate function.By similarity2 Publications

    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: MGI
    3. retinoic acid receptor activity Source: Ensembl
    4. retinoid X receptor binding Source: BHF-UCL
    5. RNA polymerase II regulatory region sequence-specific DNA binding Source: MGI
    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: MGI
    2. bone development Source: UniProtKB
    3. bone morphogenesis Source: MGI
    4. camera-type eye development Source: MGI
    5. cellular response to retinoic acid Source: MGI
    6. chondrocyte development Source: UniProtKB
    7. embryonic camera-type eye development Source: MGI
    8. embryonic eye morphogenesis Source: MGI
    9. embryonic hindlimb morphogenesis Source: MGI
    10. epithelium development Source: MGI
    11. face development Source: MGI
    12. gland development Source: MGI
    13. glandular epithelial cell development Source: MGI
    14. growth plate cartilage chondrocyte growth Source: UniProtKB
    15. growth plate cartilage development Source: MGI
    16. Harderian gland development Source: MGI
    17. limb development Source: UniProtKB
    18. multicellular organism growth Source: MGI
    19. negative regulation of apoptotic process Source: MGI
    20. negative regulation of cartilage development Source: MGI
    21. negative regulation of cell differentiation Source: MGI
    22. negative regulation of cell proliferation Source: MGI
    23. negative regulation of chondrocyte differentiation Source: MGI
    24. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    25. neural tube closure Source: MGI
    26. positive regulation of apoptotic process Source: MGI
    27. positive regulation of cell proliferation Source: MGI
    28. positive regulation of gene expression Source: MGI
    29. positive regulation of programmed cell death Source: MGI
    30. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    31. prostate gland epithelium morphogenesis Source: MGI
    32. regulation of gene expression Source: MGI
    33. regulation of myelination Source: Ensembl
    34. reproductive structure development Source: MGI
    35. retina development in camera-type eye Source: MGI
    36. retinal pigment epithelium development Source: MGI
    37. retinoic acid receptor signaling pathway Source: MGI
    38. trachea cartilage development Source: MGI

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:97858. Rarg.

    Subcellular locationi

    Nucleus 1 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

    1. nucleus Source: MGI
    2. transcription factor complex Source: BHF-UCL

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Rarg and Rarb double null mice exhibit growth retardation 3 weeks after birth. Defects are found in the growth plates with deficiency in cartilage. Growth retardation was noticable in limb sketal elements such as femurs. Early lethality and male sterility due to squamous metaplasia of the seminal vesicles and prostate are also observed. Isoform 2 mutants appear normal. The Rarg and Cyp26b1 double null mutation is able to partially rescue limb skeletal morphology without restoring normal expression of proximo-distal patterning genes.3 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 458458Retinoic acid receptor gammaPRO_0000053474Add
    BLAST

    Proteomic databases

    PRIDEiP18911.

    PTM databases

    PhosphoSiteiP18911.

    Expressioni

    Developmental stagei

    In E9.5-E12.5 embryos, expression throughout limb bud mesenchyme. This expression overlaps with that of CYP26B1. Also strongly expressed in the caudal and craniofacial regions.1 Publication

    Gene expression databases

    ArrayExpressiP18911.
    BgeeiP18911.
    CleanExiMM_RARG.
    GenevestigatoriP18911.

    Interactioni

    Subunit structurei

    Homodimer By similarity. Heterodimer with a RXR molecule By similarity. Binds DNA preferentially as a RAR/RXR heterodimer By similarity. Forms a complex with PUS1 and the SRA1 RNA in the nucleus.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi202595. 4 interactions.
    DIPiDIP-42822N.
    IntActiP18911. 1 interaction.
    MINTiMINT-2834553.

    Structurei

    3D structure databases

    ProteinModelPortaliP18911.
    SMRiP18911. Positions 89-419.
    ModBaseiSearch...
    MobiDBiSearch...

    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.
    GeneTreeiENSGT00740000114969.
    HOGENOMiHOG000010312.
    HOVERGENiHBG005606.
    InParanoidiP18911.
    KOiK08529.
    OMAiRSPQPDQ.
    OrthoDBiEOG738053.
    PhylomeDBiP18911.
    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P18911-1) [UniParc]FASTAAdd to Basket

    Also known as: A

    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 PGALGPGSGY 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 MFEDDSSKPG PHPKASSEDE APGGQGKRGQ 450
    SPQPDQGP 458
    Length:458
    Mass (Da):50,891
    Last modified:February 5, 2008 - v3
    Checksum:i1D13D2F1482D7194
    GO
    Isoform 2 (identifier: P18911-2) [UniParc] [UniParc]FASTAAdd to Basket

    Also known as: B

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

    Show »
    Length:447
    Mass (Da):49,849
    Checksum:i75E0BCB50BC9AD3B
    GO
    Isoform 3 (identifier: P18911-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-62: MATNKERLFA...DLPKEMASLS → MHKGDNSGHQ...LSSHAAFHSA

    Show »
    Length:434
    Mass (Da):48,708
    Checksum:iD0885E92CB7B2966
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti63 – 631V → E in BAE28323. (PubMed:16141072)Curated
    Sequence conflicti78 – 781P → A in BAE28323. (PubMed:16141072)Curated
    Sequence conflicti176 – 1761S → L in AAH13709. (PubMed:15489334)Curated
    Sequence conflicti369 – 3724RPSQ → DPAK in AAA40035. (PubMed:2157970)Curated
    Sequence conflicti369 – 3724RPSQ → DPAK in AAA40036. (PubMed:2157970)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6262MATNK…MASLS → MHKGDNSGHQQVPRKRGHGM RVLLLSFCLSSHAAFHSA in isoform 3. 1 PublicationVSP_031081Add
    BLAST
    Alternative sequencei1 – 6161MATNK…EMASL → MYDCMESFVPGPRRLYGAAG PGAGLLRRATGSSCFAGLES FAWAQPASLQ in isoform 2. 2 PublicationsVSP_031082Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15848 mRNA. Translation: CAA33845.1.
    M34475 mRNA. Translation: AAA40036.1.
    M34476 mRNA. Translation: AAA40035.1.
    AK148064 mRNA. Translation: BAE28323.1.
    BC012923 mRNA. Translation: AAH12923.1.
    BC013709 mRNA. Translation: AAH13709.1.
    M32068 mRNA. Translation: AAA40032.1.
    M32069 mRNA. Translation: AAA40033.1.
    M32070 mRNA. Translation: AAA40034.1.
    CCDSiCCDS27875.1. [P18911-1]
    CCDS37226.1. [P18911-2]
    PIRiB34714.
    S05052. A34714.
    RefSeqiNP_001036192.1. NM_001042727.2. [P18911-2]
    NP_035374.3. NM_011244.4. [P18911-1]
    XP_006520712.1. XM_006520649.1. [P18911-1]
    XP_006520713.1. XM_006520650.1. [P18911-1]
    UniGeneiMm.1273.

    Genome annotation databases

    EnsembliENSMUST00000043172; ENSMUSP00000048838; ENSMUSG00000001288. [P18911-1]
    ENSMUST00000063339; ENSMUSP00000067266; ENSMUSG00000001288. [P18911-2]
    GeneIDi19411.
    KEGGimmu:19411.
    UCSCiuc007xvc.1. mouse. [P18911-2]
    uc007xvd.1. mouse. [P18911-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15848 mRNA. Translation: CAA33845.1 .
    M34475 mRNA. Translation: AAA40036.1 .
    M34476 mRNA. Translation: AAA40035.1 .
    AK148064 mRNA. Translation: BAE28323.1 .
    BC012923 mRNA. Translation: AAH12923.1 .
    BC013709 mRNA. Translation: AAH13709.1 .
    M32068 mRNA. Translation: AAA40032.1 .
    M32069 mRNA. Translation: AAA40033.1 .
    M32070 mRNA. Translation: AAA40034.1 .
    CCDSi CCDS27875.1. [P18911-1 ]
    CCDS37226.1. [P18911-2 ]
    PIRi B34714.
    S05052. A34714.
    RefSeqi NP_001036192.1. NM_001042727.2. [P18911-2 ]
    NP_035374.3. NM_011244.4. [P18911-1 ]
    XP_006520712.1. XM_006520649.1. [P18911-1 ]
    XP_006520713.1. XM_006520650.1. [P18911-1 ]
    UniGenei Mm.1273.

    3D structure databases

    ProteinModelPortali P18911.
    SMRi P18911. Positions 89-419.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202595. 4 interactions.
    DIPi DIP-42822N.
    IntActi P18911. 1 interaction.
    MINTi MINT-2834553.

    Chemistry

    BindingDBi P18911.
    ChEMBLi CHEMBL4177.
    GuidetoPHARMACOLOGYi 592.

    PTM databases

    PhosphoSitei P18911.

    Proteomic databases

    PRIDEi P18911.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000043172 ; ENSMUSP00000048838 ; ENSMUSG00000001288 . [P18911-1 ]
    ENSMUST00000063339 ; ENSMUSP00000067266 ; ENSMUSG00000001288 . [P18911-2 ]
    GeneIDi 19411.
    KEGGi mmu:19411.
    UCSCi uc007xvc.1. mouse. [P18911-2 ]
    uc007xvd.1. mouse. [P18911-1 ]

    Organism-specific databases

    CTDi 5916.
    MGIi MGI:97858. Rarg.

    Phylogenomic databases

    eggNOGi NOG297448.
    GeneTreei ENSGT00740000114969.
    HOGENOMi HOG000010312.
    HOVERGENi HBG005606.
    InParanoidi P18911.
    KOi K08529.
    OMAi RSPQPDQ.
    OrthoDBi EOG738053.
    PhylomeDBi P18911.
    TreeFami TF328382.

    Miscellaneous databases

    NextBioi 296533.
    PROi P18911.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P18911.
    Bgeei P18911.
    CleanExi MM_RARG.
    Genevestigatori P18911.

    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. "Cloning of murine alpha and beta retinoic acid receptors and a novel receptor gamma predominantly expressed in skin."
      Zelent A., Krust A., Petkovich M., Kastner P., Chambon P.
      Nature 339:714-717(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    2. "Identification of a novel isoform of the retinoic acid receptor gamma expressed in the mouse embryo."
      Giguere V., Shago M., Zirngibl R., Tate P., Rossant J., Varmuza S.
      Mol. Cell. Biol. 10:2335-2340(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: C57BL/6J.
    4. "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).
      Strain: Czech II.
      Tissue: Mammary tumor.
    5. "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 1-74 (ISOFORMS 1; 2 AND 3).
    6. "Function of retinoic acid receptor gamma in the mouse."
      Lohnes D., Kastner P., Dierich A., Mark M., LeMeur M., Chambon P.
      Cell 73:643-658(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION.
    7. "Regulation of nuclear receptor activity by a pseudouridine synthase through posttranscriptional modification of steroid receptor RNA activator."
      Zhao X., Patton J.R., Davis S.L., Florence B., Ames S.J., Spanjaard R.A.
      Mol. Cell 15:549-558(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH PUS1 AND SRA1, SUBCELLULAR LOCATION.
    8. "Retinoic acid receptors are required for skeletal growth, matrix homeostasis and growth plate function in postnatal mouse."
      Williams J.A., Kondo N., Okabe T., Takeshita N., Pilchak D.M., Koyama E., Ochiai T., Jensen D., Chu M.L., Kane M.A., Napoli J.L., Enomoto-Iwamoto M., Ghyselinck N., Chambon P., Pacifici M., Iwamoto M.
      Dev. Biol. 328:315-327(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION.
    9. "Analysis of Cyp26b1/Rarg compound-null mice reveals two genetically separable effects of retinoic acid on limb outgrowth."
      Pennimpede T., Cameron D.A., MacLean G.A., Petkovich M.
      Dev. Biol. 339:179-186(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, POSSIBLE FUNCTION, DEVELOPMENTAL STAGE.

    Entry informationi

    Entry nameiRARG_MOUSE
    AccessioniPrimary (citable) accession number: P18911
    Secondary accession number(s): P20787
    , Q3UG86, Q62149, Q91VK5, Q91YX2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 153 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3