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P11416

- RARA_MOUSE

UniProt

P11416 - RARA_MOUSE

Protein

Retinoic acid receptor alpha

Gene

Rara

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 1 (01 Oct 1989)
      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 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. Regulates expression of target genes in a ligand-dependent manner by recruiting chromatin complexes containing KMT2E/MLL5. Mediates retinoic acid-induced granulopoiesis. RARA plays an essential role in the regulation of retinoic acid-induced germ cell development during spermatogenesis. Has a role in the survival of early spermatocytes at the beginning prophase of meiosis. In Sertoli cells, may promote the survival and development of early meiotic prophase spermatocytes. In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function.7 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi88 – 15366Nuclear receptorPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri88 – 10821NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri124 – 14825NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin DNA binding Source: Ensembl
    2. DNA binding Source: MGI
    3. drug binding Source: Ensembl
    4. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: MGI
    5. mRNA 5'-UTR binding Source: Ensembl
    6. phosphatidylinositol 3-kinase regulator activity Source: Ensembl
    7. protein binding Source: UniProtKB
    8. retinoic acid binding Source: Ensembl
    9. retinoic acid receptor activity Source: MGI
    10. retinoic acid-responsive element binding Source: Ensembl
    11. RNA polymerase II regulatory region DNA binding Source: MGI
    12. RNA polymerase II regulatory region sequence-specific DNA binding Source: MGI
    13. sequence-specific DNA binding Source: MGI
    14. sequence-specific DNA binding transcription factor activity Source: MGI
    15. steroid hormone receptor activity Source: InterPro
    16. transcription coactivator activity Source: Ensembl
    17. transcription corepressor activity Source: Ensembl
    18. transcription factor binding Source: UniProtKB
    19. transcription regulatory region DNA binding Source: UniProtKB
    20. translation repressor activity, nucleic acid binding Source: Ensembl
    21. zinc ion binding Source: InterPro

    GO - Biological processi

    1. apoptotic cell clearance Source: Ensembl
    2. bone development Source: MGI
    3. cellular response to estrogen stimulus Source: Ensembl
    4. cellular response to lipopolysaccharide Source: UniProtKB
    5. cellular response to retinoic acid Source: Ensembl
    6. chondroblast differentiation Source: MGI
    7. embryonic camera-type eye development Source: MGI
    8. face development Source: MGI
    9. female pregnancy Source: Ensembl
    10. germ cell development Source: UniProtKB
    11. glandular epithelial cell development Source: MGI
    12. growth plate cartilage development Source: MGI
    13. intracellular estrogen receptor signaling pathway Source: Ensembl
    14. limb development Source: MGI
    15. liver development Source: Ensembl
    16. multicellular organism growth Source: MGI
    17. negative regulation of apoptotic process Source: MGI
    18. negative regulation of cartilage development Source: MGI
    19. negative regulation of cell differentiation Source: MGI
    20. negative regulation of cell proliferation Source: Ensembl
    21. negative regulation of gene expression Source: MGI
    22. negative regulation of granulocyte differentiation Source: Ensembl
    23. negative regulation of interferon-gamma production Source: Ensembl
    24. negative regulation of transcription, DNA-templated Source: MGI
    25. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    26. negative regulation of translational initiation Source: MGI
    27. negative regulation of tumor necrosis factor production Source: Ensembl
    28. neural tube closure Source: MGI
    29. outflow tract septum morphogenesis Source: MGI
    30. positive regulation of binding Source: Ensembl
    31. positive regulation of cell cycle Source: Ensembl
    32. positive regulation of cell proliferation Source: MGI
    33. positive regulation of ERK1 and ERK2 cascade Source: Ensembl
    34. positive regulation of gene expression Source: UniProtKB
    35. positive regulation of interleukin-13 production Source: Ensembl
    36. positive regulation of interleukin-4 production Source: Ensembl
    37. positive regulation of interleukin-5 production Source: Ensembl
    38. positive regulation of neuron differentiation Source: Ensembl
    39. positive regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
    40. positive regulation of protein kinase B signaling Source: Ensembl
    41. positive regulation of T-helper 2 cell differentiation Source: Ensembl
    42. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    43. prostate gland development Source: Ensembl
    44. protein phosphorylation Source: Ensembl
    45. regulation of granulocyte differentiation Source: MGI
    46. regulation of myelination Source: Ensembl
    47. regulation of synaptic plasticity Source: Ensembl
    48. regulation of transcription, DNA-templated Source: MGI
    49. response to cytokine Source: Ensembl
    50. response to estradiol Source: Ensembl
    51. response to ethanol Source: Ensembl
    52. response to retinoic acid Source: MGI
    53. response to vitamin A Source: Ensembl
    54. Sertoli cell fate commitment Source: UniProtKB
    55. spermatogenesis Source: MGI
    56. trachea cartilage development Source: MGI
    57. ureteric bud development Source: MGI
    58. ventricular cardiac muscle cell differentiation 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 alpha
    Short name:
    RAR-alpha
    Alternative name(s):
    Nuclear receptor subfamily 1 group B member 1
    Gene namesi
    Name:Rara
    Synonyms:Nr1b1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:97856. Rara.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Nuclear localization depends on ligand binding, phosphorylation and sumoylation. Transloaction to the nucleus is dependent on activation of PKC and the downstream MAPK phosphorylation.

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. dendrite Source: MGI
    3. neuronal cell body Source: MGI
    4. nuclear chromatin Source: Ensembl
    5. nucleus Source: UniProtKB
    6. perinuclear region of cytoplasm Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Seminiferous tubules of 6 month-old animals display varying degrees of testicular degeneration, with moderate to severe levels of germ-cell degeneration. Epithelial cells in the epididymis show general disorganization. Sperm count is reduced to about 1.7% of wild-type and sperm mobility reduced by half. Rara and Rarg, but not Rara and Rarb, double knockout mice exhibit growth retardation after 3 weeks. 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.3 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi74 – 741S → A: No effect on phosphorylation, no effect on transcriptional activity. 1 Publication
    Mutagenesisi77 – 771S → A: Decreases phosphorylation and no effect on interaction with CDK7. Strongly reduces transcriptional activity. 2 Publications
    Mutagenesisi347 – 3471K → A or Q: Greatly reduced interaction with RXRA and NCOR1 and transcriptional activation. 1 Publication
    Mutagenesisi347 – 3471K → F: Reduced methylation levels. Little effect on interaction with RXRA or NCOR1. Small loss in transcriptional activation. 1 Publication
    Mutagenesisi369 – 3691S → A: Abolishes phosphorylation and prevents phosphorylation of S-77. 1 Publication
    Mutagenesisi449 – 4491S → A: No change in phosphorylation levels and no effect on transcriptional activity. 1 Publication
    Mutagenesisi456 – 4561S → A: No change in phosphorylation levels and no effect on transcriptional activity. 1 Publication
    Mutagenesisi461 – 4611S → A: No change in phosphorylation levels and no effect on transcriptional activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 462462Retinoic acid receptor alphaPRO_0000053462Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei77 – 771Phosphoserine; by CDK73 Publications
    Modified residuei96 – 961Phosphoserine; by PKB/AKT1By similarity
    Cross-linki166 – 166Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Cross-linki171 – 171Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Modified residuei219 – 2191Phosphoserine; by PKABy similarity
    Modified residuei347 – 3471N6,N6,N6-trimethyllysine1 Publication
    Modified residuei369 – 3691Phosphoserine; by PKA and RPS6KA52 Publications
    Cross-linki399 – 399Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

    Post-translational modificationi

    Phosphorylated on serine and threonine residues. Phosphorylation does not change during cell cycle. Phosphorylation on Ser-77 is crucial for the N-terminal AF1 transcriptional activity. Under stress conditions, MAPK8 enhances phosphorylation on Thr-181, Ser-445 and Ser-461 leading to RARA ubiquitination and degradation. Phosphorylation by AKT1 inhibits the transactivation activity. On retinoic acid stimulation, phosphorylation on Ser-369 by RPS6KA5 promotes interaction with GTF2H3 and the CDK7-mediated phosphorylation of Ser-77.3 Publications
    Sumoylated with SUMO2, mainly on Lys-399 which is also required for SENP6 binding. On all-trans retinoic acid (ATRA) binding, a confromational change may occur that allows sumoylation on two additional site, Lys-166 and Lys-171. Probably desumoylated by SENP6. Sumoylation levels determine nuclear localization and regulate ATRA-mediated transcriptional activity By similarity.By similarity

    Keywords - PTMi

    Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiP11416.

    PTM databases

    PhosphoSiteiP11416.

    Expressioni

    Tissue specificityi

    Expressed in Sertoli cells and germ cells.1 Publication

    Inductioni

    By retinoic acid.1 Publication

    Gene expression databases

    ArrayExpressiP11416.
    BgeeiP11416.
    CleanExiMM_RARA.
    GenevestigatoriP11416.

    Interactioni

    Subunit structurei

    Interacts with PRMT2 By similarity. Interacts with LRIF1 By similarity. Interacts with NCOA7 in a ligand-inducible manner. Interacts with KMT2E/MLL5. Interacts (via the ligand-binding domain) with PRAME; interaction is direct and ligand (retinoic acid)-dependent. Interacts with PRKAR1A; the interaction negatively. regulates RARA transcriptional activity. Interacts with NCOR1 and NCOR2; the interaction occurs in the absence of ligand and represses transciptional activity. Interacts with NCOA3 and NCOA6 coactivators, leading to a strong increase of transcription of target genes. Interacts with CDK7; the interaction is enhanced by interaction with GTF2H3. Interacts with GTF2H3; the interaction requires prior phosphorylation on Ser-369 which then enhances interaction with CDK7. Interacts with ASXL1 and NCOA1 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Rps6ka5Q8C0502EBI-346736,EBI-8391218

    Protein-protein interaction databases

    BioGridi202586. 70 interactions.
    DIPiDIP-31480N.
    IntActiP11416. 11 interactions.
    MINTiMINT-5210296.

    Structurei

    3D structure databases

    ProteinModelPortaliP11416.
    SMRiP11416. Positions 87-415.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 8787ModulatingAdd
    BLAST
    Regioni154 – 19946HingeAdd
    BLAST
    Regioni200 – 419220Ligand-bindingAdd
    BLAST
    Regioni404 – 41916Required for binding corepressor NCOR1Add
    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 fingeri88 – 10821NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri124 – 14825NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG297448.
    GeneTreeiENSGT00740000114969.
    HOGENOMiHOG000010312.
    HOVERGENiHBG005606.
    InParanoidiP11416.
    KOiK08527.
    OMAiNNSSDQR.
    OrthoDBiEOG738053.
    PhylomeDBiP11416.
    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. 2 hits.
    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 Alpha-1 (identifier: P11416-1) [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

    MASNSSSCPT PGGGHLNGYP VPPYAFFFPP MLGGLSPPGA LTSLQHQLPV    50
    SGYSTPSPAT IETQSSSSEE IVPSPPSPPP LPRIYKPCFV CQDKSSGYHY 100
    GVSACEGCKG FFRRSIQKNM VYTCHRDKNC IINKVTRNRC QYCRLQKCFD 150
    VGMSKESVRN DRNKKKKEAP KPECSESYTL TPEVGELIEK VRKAHQETFP 200
    ALCQLGKYTT NNSSEQRVSL DIDLWDKFSE LSTKCIIKTV EFAKQLPGFT 250
    TLTIADQITL LKAACLDILI LRICTRYTPE QDTMTFSDGL TLNRTQMHNA 300
    GFGPLTDLVF AFANQLLPLE MDDAETGLLS AICLICGDRQ DLEQPDKVDM 350
    LQEPLLEALK VYVRKRRPSR PHMFPKMLMK ITDLRSISAK GAERVITLKM 400
    EIPGSMPPLI QEMLENSEGL DTLSGQSGGG TRDGGGLAPP PGSCSPSLSP 450
    SSHRSSPATQ SP 462
    Length:462
    Mass (Da):50,735
    Last modified:October 1, 1989 - v1
    Checksum:i726F7799633A85AD
    GO
    Isoform Alpha-2 (identifier: P11416-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-60: MASNSSSCPT...SGYSTPSPAT → MYESVEVGGL...TPLWNGSNHS

    Show »
    Length:459
    Mass (Da):50,935
    Checksum:i15096242FF09896E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti163 – 1631N → K in AAA40031. (PubMed:2174108)Curated
    Sequence conflicti179 – 1791T → S in AAA40031. (PubMed:2174108)Curated
    Sequence conflicti284 – 2841M → L in AAA40031. (PubMed:2174108)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti391 – 3911G → A in embryonal carcinoma cell line RAC65.
    Natural varianti392 – 46271Missing in embryonal carcinoma cell line RAC65.
    Add
    BLAST

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6060MASNS…PSPAT → MYESVEVGGLTPAPNPFLVV DFYNQNRACLLQEKGLPAPG PYSTPLRTPLWNGSNHS in isoform Alpha-2. 1 PublicationVSP_003630Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56572 mRNA. Translation: CAA39919.1.
    X56565 mRNA. Translation: CAA39917.1.
    S56656 mRNA. Translation: AAB25783.1.
    X57528 mRNA. Translation: CAA40749.1.
    M60909 mRNA. Translation: AAA40031.1.
    BC010216 mRNA. Translation: AAH10216.1.
    CCDSiCCDS36304.1. [P11416-1]
    CCDS48905.1. [P11416-2]
    PIRiS05050.
    RefSeqiNP_001169999.1. NM_001176528.1. [P11416-2]
    NP_001170773.1. NM_001177302.1. [P11416-1]
    NP_001170774.1. NM_001177303.1. [P11416-1]
    NP_033050.2. NM_009024.2. [P11416-1]
    XP_006532654.1. XM_006532591.1. [P11416-1]
    XP_006532655.1. XM_006532592.1. [P11416-1]
    XP_006532656.1. XM_006532593.1. [P11416-1]
    XP_006532657.1. XM_006532594.1. [P11416-1]
    UniGeneiMm.439744.

    Genome annotation databases

    EnsembliENSMUST00000068133; ENSMUSP00000069744; ENSMUSG00000037992. [P11416-1]
    ENSMUST00000107473; ENSMUSP00000103097; ENSMUSG00000037992. [P11416-2]
    ENSMUST00000107474; ENSMUSP00000103098; ENSMUSG00000037992. [P11416-1]
    ENSMUST00000107475; ENSMUSP00000103099; ENSMUSG00000037992. [P11416-1]
    ENSMUST00000164748; ENSMUSP00000129791; ENSMUSG00000037992. [P11416-1]
    GeneIDi19401.
    KEGGimmu:19401.
    UCSCiuc007lhx.1. mouse. [P11416-1]
    uc007lhz.2. mouse. [P11416-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56572 mRNA. Translation: CAA39919.1 .
    X56565 mRNA. Translation: CAA39917.1 .
    S56656 mRNA. Translation: AAB25783.1 .
    X57528 mRNA. Translation: CAA40749.1 .
    M60909 mRNA. Translation: AAA40031.1 .
    BC010216 mRNA. Translation: AAH10216.1 .
    CCDSi CCDS36304.1. [P11416-1 ]
    CCDS48905.1. [P11416-2 ]
    PIRi S05050.
    RefSeqi NP_001169999.1. NM_001176528.1. [P11416-2 ]
    NP_001170773.1. NM_001177302.1. [P11416-1 ]
    NP_001170774.1. NM_001177303.1. [P11416-1 ]
    NP_033050.2. NM_009024.2. [P11416-1 ]
    XP_006532654.1. XM_006532591.1. [P11416-1 ]
    XP_006532655.1. XM_006532592.1. [P11416-1 ]
    XP_006532656.1. XM_006532593.1. [P11416-1 ]
    XP_006532657.1. XM_006532594.1. [P11416-1 ]
    UniGenei Mm.439744.

    3D structure databases

    ProteinModelPortali P11416.
    SMRi P11416. Positions 87-415.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202586. 70 interactions.
    DIPi DIP-31480N.
    IntActi P11416. 11 interactions.
    MINTi MINT-5210296.

    Chemistry

    BindingDBi P11416.
    ChEMBLi CHEMBL2792.
    GuidetoPHARMACOLOGYi 590.

    PTM databases

    PhosphoSitei P11416.

    Proteomic databases

    PRIDEi P11416.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000068133 ; ENSMUSP00000069744 ; ENSMUSG00000037992 . [P11416-1 ]
    ENSMUST00000107473 ; ENSMUSP00000103097 ; ENSMUSG00000037992 . [P11416-2 ]
    ENSMUST00000107474 ; ENSMUSP00000103098 ; ENSMUSG00000037992 . [P11416-1 ]
    ENSMUST00000107475 ; ENSMUSP00000103099 ; ENSMUSG00000037992 . [P11416-1 ]
    ENSMUST00000164748 ; ENSMUSP00000129791 ; ENSMUSG00000037992 . [P11416-1 ]
    GeneIDi 19401.
    KEGGi mmu:19401.
    UCSCi uc007lhx.1. mouse. [P11416-1 ]
    uc007lhz.2. mouse. [P11416-2 ]

    Organism-specific databases

    CTDi 5914.
    MGIi MGI:97856. Rara.

    Phylogenomic databases

    eggNOGi NOG297448.
    GeneTreei ENSGT00740000114969.
    HOGENOMi HOG000010312.
    HOVERGENi HBG005606.
    InParanoidi P11416.
    KOi K08527.
    OMAi NNSSDQR.
    OrthoDBi EOG738053.
    PhylomeDBi P11416.
    TreeFami TF328382.

    Miscellaneous databases

    NextBioi 296513.
    PROi P11416.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P11416.
    Bgeei P11416.
    CleanExi MM_RARA.
    Genevestigatori P11416.

    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. 2 hits.
    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 ALPHA-1).
    2. "Cloning of several genes coding for retinoic acid nuclear receptors in the mouse embryonal carcinoma cell line PCC7-MZ1."
      Heiermann R., Rentrop M., Lang E., Maelicke A.
      J. Recept. Res. 13:693-709(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1).
    3. "Multiple isoforms of the mouse retinoic acid receptor alpha are generated by alternative splicing and differential induction by retinoic acid."
      Leroy P., Krust A., Zelent A., Mendelsohn C., Garnier J.-M., Kastner P., Dierich A., Chambon P.
      EMBO J. 10:59-69(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-1 AND ALPHA-2).
    4. "Retinoic acid resistance of the variant embryonal carcinoma cell line RAC65 is caused by expression of a truncated RAR alpha."
      Kruyt F.A.E., van der Veer L., Mader S., van den Brink C.E., Feijen A., Jonk L.J., Kruijer W., van der Saag P.T.
      Differentiation 49:27-37(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (VARIANT IN EMBRYONAL CARCINOMA CELL LINE RAC65).
    5. "A dominant negative mutation of the alpha retinoic acid receptor gene in a retinoic acid-nonresponsive embryonal carcinoma cell."
      Pratt M.A.C., Kralova J., McBurney M.W.
      Mol. Cell. Biol. 10:6445-6453(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (VARIANT IN EMBRYONAL CARCINOMA CELL LINE RAC65).
    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 ALPHA-1).
      Strain: FVB/N.
      Tissue: Mammary gland.
    7. "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: PROTEIN SEQUENCE OF 340-359, METHYLATION AT LYS-347, FUNCTION, INTERACTION WITH RXRA AND NCOR1, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF LYS-347.
    8. "Stimulation of RAR alpha activation function AF-1 through binding to the general transcription factor TFIIH and phosphorylation by CDK7."
      Rochette-Egly C., Adam S., Rossignol M., Egly J.-M., Chambon P.
      Cell 90:97-107(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDK7 AND GTF2H3, PHOSPHORYLATION AT SER-77, FUNCTION, MUTAGENESIS OF SER-74; SER-77; SER-449; SER-456 AND SER-461.
    9. "The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function."
      Torchia J., Rose D.W., Inostroza J., Kamei Y., Westin S., Glass C.K., Rosenfeld M.G.
      Nature 387:677-684(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NCOA3.
    10. "Follicle-stimulating hormone inhibits all-trans-retinoic acid-induced retinoic acid receptor alpha nuclear localization and transcriptional activation in mouse Sertoli cell lines."
      Braun K.W., Tribley W.A., Griswold M.D., Kim K.H.
      J. Biol. Chem. 275:4145-4151(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    11. "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.
    12. "Positive regulation of retinoic acid receptor alpha by protein kinase C and mitogen-activated protein kinase in sertoli cells."
      Braun K.W., Vo M.N., Kim K.H.
      Biol. Reprod. 67:29-37(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION.
    13. "Male sterility in mice lacking retinoic acid receptor alpha involves specific abnormalities in spermiogenesis."
      Chung S.S., Wang X., Wolgemuth D.J.
      Differentiation 73:188-198(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION.
    14. "Potential functions of retinoic acid receptor A in Sertoli cells and germ cells during spermatogenesis."
      Doyle T.J., Braun K.W., McLean D.J., Wright R.W., Griswold M.D., Kim K.H.
      Ann. N. Y. Acad. Sci. 1120:114-130(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, INDUCTION.
    15. "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.
    16. "A coordinated phosphorylation cascade initiated by p38MAPK/MSK1 directs RARalpha to target promoters."
      Bruck N., Vitoux D., Ferry C., Duong V., Bauer A., de The H., Rochette-Egly C.
      EMBO J. 28:34-47(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-77 AND SER-369, FUNCTION, INTERACTION WITH GTF2H3, MUTAGENESIS OF SER-77 AND SER-369.

    Entry informationi

    Entry nameiRARA_MOUSE
    AccessioniPrimary (citable) accession number: P11416
    Secondary accession number(s): P22603
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 166 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

    Complete proteome, Direct protein sequencing, 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