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P19091

- ANDR_MOUSE

UniProt

P19091 - ANDR_MOUSE

Protein

Androgen receptor

Gene

Ar

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      Previous versions | rss
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    Functioni

    Steroid hormone receptors are ligand-activated transcription factors that regulate eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcription factor activity is modulated by bound coactivator and corepressor proteins. Transcription activation is down-regulated by NR0B2. Activated, but not phosphorylated, by HIPK3 and ZIPK/DAPK3 By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei685 – 6851Androgen
    Sitei700 – 7001Interaction with coactivator LXXL motifBy similarity
    Binding sitei732 – 7321Androgen
    Binding sitei857 – 8571Androgen
    Sitei877 – 8771Interaction with coactivator FXXLF motifBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi538 – 61174Nuclear receptorPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri539 – 55921NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri575 – 59925NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. androgen binding Source: Ensembl
    2. androgen receptor activity Source: UniProtKB
    3. beta-catenin binding Source: UniProtKB
    4. enzyme binding Source: BHF-UCL
    5. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: BHF-UCL
    6. POU domain binding Source: UniProtKB
    7. protein binding Source: UniProtKB
    8. sequence-specific DNA binding Source: MGI
    9. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    10. transcription regulatory region DNA binding Source: UniProtKB
    11. zinc ion binding Source: InterPro

    GO - Biological processi

    1. activation of prostate induction by androgen receptor signaling pathway Source: MGI
    2. androgen receptor signaling pathway Source: MGI
    3. cellular process Source: MGI
    4. epithelial cell differentiation involved in prostate gland development Source: MGI
    5. epithelial cell morphogenesis Source: MGI
    6. fertilization Source: MGI
    7. intracellular receptor signaling pathway Source: BHF-UCL
    8. in utero embryonic development Source: MGI
    9. lateral sprouting involved in mammary gland duct morphogenesis Source: MGI
    10. Leydig cell differentiation Source: MGI
    11. male genitalia morphogenesis Source: MGI
    12. male gonad development Source: MGI
    13. male somatic sex determination Source: MGI
    14. mammary gland alveolus development Source: MGI
    15. morphogenesis of an epithelial fold Source: MGI
    16. multicellular organism growth Source: MGI
    17. negative regulation of epithelial cell proliferation Source: MGI
    18. negative regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
    19. negative regulation of integrin biosynthetic process Source: UniProtKB
    20. organ formation Source: MGI
    21. positive regulation of cell proliferation Source: UniProtKB
    22. positive regulation of insulin-like growth factor receptor signaling pathway Source: MGI
    23. positive regulation of intracellular estrogen receptor signaling pathway Source: MGI
    24. positive regulation of MAPK cascade Source: MGI
    25. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    26. positive regulation of phosphorylation Source: UniProtKB
    27. positive regulation of transcription, DNA-templated Source: UniProtKB
    28. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    29. prostate gland epithelium morphogenesis Source: MGI
    30. prostate gland growth Source: MGI
    31. protein oligomerization Source: MGI
    32. regulation of catalytic activity Source: MGI
    33. regulation of developmental growth Source: MGI
    34. regulation of establishment of protein localization to plasma membrane Source: UniProtKB
    35. regulation of gene expression Source: MGI
    36. regulation of prostatic bud formation Source: MGI
    37. regulation of systemic arterial blood pressure Source: MGI
    38. regulation of transcription, DNA-templated Source: MGI
    39. regulation of transcription from RNA polymerase II promoter Source: MGI
    40. reproductive structure development Source: MGI
    41. reproductive system development Source: MGI
    42. response to insulin Source: Ensembl
    43. seminiferous tubule development Source: MGI
    44. single fertilization Source: MGI
    45. spermatogenesis Source: MGI
    46. tertiary branching involved in mammary gland duct morphogenesis Source: MGI
    47. transcription, DNA-templated Source: UniProtKB

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Lipid-binding, Metal-binding, Steroid-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Androgen receptor
    Alternative name(s):
    Dihydrotestosterone receptor
    Nuclear receptor subfamily 3 group C member 4
    Gene namesi
    Name:Ar
    Synonyms:Nr3c4
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:88064. Ar.

    Subcellular locationi

    Nucleus. Cytoplasm By similarity
    Note: Predominantly cytoplasmic in unligated form but translocates to the nucleus upon ligand-binding. Can also translocate to the nucleus in unligated form in the presence of GNB2L1 By similarity.By similarity

    GO - Cellular componenti

    1. axon Source: Ensembl
    2. cytoplasm Source: UniProtKB
    3. dendrite Source: Ensembl
    4. nuclear chromatin Source: UniProtKB
    5. nucleus Source: UniProtKB
    6. plasma membrane Source: MGI
    7. protein complex Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 899899Androgen receptorPRO_0000053707Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei61 – 611Phosphoserine; by CDK9By similarity
    Modified residuei75 – 751PhosphoserineBy similarity
    Modified residuei218 – 2181Phosphotyrosine; by CSKBy similarity
    Modified residuei262 – 2621Phosphotyrosine; by CSK and TNK2By similarity
    Modified residuei302 – 3021Phosphotyrosine; by CSKBy similarity
    Modified residuei341 – 3411Phosphotyrosine; by CSKBy similarity
    Modified residuei352 – 3521Phosphotyrosine; by CSKBy similarity
    Modified residuei357 – 3571Phosphotyrosine; by CSKBy similarity
    Modified residuei358 – 3581Phosphotyrosine; by CSK and TNK2By similarity
    Cross-linki381 – 381Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Modified residuei388 – 3881Phosphotyrosine; by CSKBy similarity
    Cross-linki500 – 500Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Modified residuei514 – 5141Phosphotyrosine; by CSKBy similarity
    Modified residuei531 – 5311Phosphotyrosine; by CSKBy similarity
    Modified residuei630 – 6301Phosphoserine; by STK4/MST1By similarity
    Cross-linki825 – 825Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki827 – 827Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei895 – 8951Phosphotyrosine; by CSKBy similarity

    Post-translational modificationi

    Phosphorylated in prostate cancer cells in response to several growth factors including EGF. Phosphorylation is induced by c-Src kinase (CSK). Tyr-514 is one of the major phosphorylation sites and an increase in phosphorylation and Src kinase activity is associated with prostate cancer progression By similarity. Phosphorylation by TNK2 enhances the DNA-binding and transcriptional activity. Phosphorylation at Ser-61 by CDK9 regulates AR promoter selectivity and cell growth. Phosphorylation by PAK6 leads to AR-mediated transcription inhibition By similarity.By similarity
    Sumoylated on Lys-381 (major) and Lys-500 By similarity. Ubiquitinated. Deubiquitinated by USP26 By similarity. 'Lys-6' and 'Lys-27'-linked polyubiquitination by RNF6 modulates AR transcriptional activity and specificity By similarity.By similarity
    Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is required for plasma membrane targeting and for rapid intracellular signaling via ERK and AKT kinases and cAMP generation By similarity.By similarity

    Keywords - PTMi

    Isopeptide bond, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiP19091.

    PTM databases

    PhosphoSiteiP19091.

    Expressioni

    Gene expression databases

    BgeeiP19091.
    CleanExiMM_AR.
    GenevestigatoriP19091.

    Interactioni

    Subunit structurei

    Binds DNA as a homodimer. Part of a ternary complex containing AR, EFCAB6/DJBP and PARK7. Interacts with HIPK3 and NR0B2 in the presence of androgen. The ligand binding domain interacts with KAT7/HBO1 in the presence of dihydrotestosterone. Interacts with EFCAB6/DJBP, PELP1, PQBP1, RANBP9, SPDEF, SRA1, TGFB1I1, ZNF318 and RREB1. The AR N-terminal poly-Gln region binds Ran resulting in enhancement of AR-mediated transactivation. Ran-binding decreases as the poly-Gln length increases. Interacts with ZMIZ1/ZIMP10 and ZMIZ2/ZMIP7 which both enhance its transactivation activity. Interacts with RBAK. Interacts via the ligand-binding domain with LXXLL and FXXLF motifs from NCOA1, NCOA2, NCOA3, NCOA4 and MAGEA11. Interacts with HIP1 (via coiled coil domain). Interacts with SLC30A9 and RAD54L2/ARIP4. Interacts with MACROD1. Interacts (via ligand-binding domain) with TRIM68. Interacts with TNK2. Interacts with USP26. Interacts with RNF6. Interacts (regulated by RNF6 probably through polyubiquitination) with RNF14; regulates AR transcriptional activity. Interacts with PRMT2 and TRIM24. Interacts with GNB2L1/RACK1. Interacts with RANBP10; this interaction enhances hormone-induced AR transcriptional activity. Interacts with PRPF6 in a hormone-independent way; this interaction enhances hormone-induced AR transcriptional activity. Interacts with STK4/MST1. Interacts with ZIPK/DAPK3. Interacts with LPXN. Interacts with MAK. Part of a complex containing AR, MAK and NCOA3. Interacts with CRY1.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Casp8O891102EBI-1776062,EBI-851690

    Protein-protein interaction databases

    BioGridi198179. 16 interactions.
    DIPiDIP-41803N.
    IntActiP19091. 2 interactions.
    MINTiMINT-151935.

    Structurei

    Secondary structure

    1
    899
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi652 – 6598
    Helixi677 – 70125
    Helixi705 – 7073
    Helixi710 – 73627
    Beta strandi740 – 7456
    Beta strandi748 – 7503
    Helixi752 – 7576
    Helixi761 – 77616
    Helixi781 – 79212
    Beta strandi794 – 7996
    Helixi804 – 82320
    Helixi831 – 84414
    Helixi846 – 86217
    Turni863 – 8686
    Helixi873 – 88715
    Beta strandi890 – 8934

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2QPYX-ray2.50A649-899[»]
    ProteinModelPortaliP19091.
    SMRiP19091. Positions 534-898.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19091.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 537537ModulatingBy similarityAdd
    BLAST
    Regioni531 – 899369Interaction with LPXNBy similarityAdd
    BLAST
    Regioni551 – 64191Interaction with HIPK3By similarityAdd
    BLAST
    Regioni604 – 899296Interaction with KAT7By similarityAdd
    BLAST
    Regioni670 – 899230Ligand-bindingAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi63 – 675Poly-Arg
    Compositional biasi174 – 19320Poly-GlnAdd
    BLAST
    Compositional biasi367 – 3737Poly-Pro
    Compositional biasi391 – 3977Poly-Ala
    Compositional biasi441 – 4477Poly-Gly

    Domaini

    Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. In the presence of bound steroid the ligand-binding domain interacts with the N-terminal modulating domain, and thereby activates AR transcription factor activity. Agonist binding is required for dimerization and binding to target DNA. The transcription factor activity of the complex formed by ligand-activated AR and DNA is modulated by interactions with coactivator and corepressor proteins. Interaction with RANBP9 is mediated by both the N-terminal domain and the DNA-binding domain. Interaction with EFCAB6/DJBP is mediated by the DNA-binding domain By similarity.By similarity

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri539 – 55921NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri575 – 59925NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG245477.
    GeneTreeiENSGT00730000110451.
    HOGENOMiHOG000254783.
    HOVERGENiHBG007583.
    InParanoidiP19091.
    KOiK08557.
    OMAiCSTDLKD.
    OrthoDBiEOG7J17Z7.
    PhylomeDBiP19091.
    TreeFamiTF350286.

    Family and domain databases

    Gene3Di1.10.565.10. 2 hits.
    3.30.50.10. 1 hit.
    InterProiIPR001103. Andrgn_rcpt.
    IPR008946. Nucl_hormone_rcpt_ligand-bd.
    IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
    IPR001628. Znf_hrmn_rcpt.
    IPR013088. Znf_NHR/GATA.
    [Graphical view]
    PfamiPF02166. Androgen_recep. 1 hit.
    PF00104. Hormone_recep. 1 hit.
    PF00105. zf-C4. 1 hit.
    [Graphical view]
    PRINTSiPR00521. ANDROGENR.
    PR00047. STROIDFINGER.
    SMARTiSM00430. HOLI. 1 hit.
    SM00399. ZnF_C4. 1 hit.
    [Graphical view]
    SUPFAMiSSF48508. SSF48508. 1 hit.
    PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
    PS51030. NUCLEAR_REC_DBD_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P19091-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEVQLGLGRV YPRPPSKTYR GAFQNLFQSV REAIQNPGPR HPEAANIAPP    50
    GACLQQRQET SPRRRRRQQH TEDGSPQAHI RGPTGYLALE EEQQPSQQQA 100
    ASEGHPESSC LPEPGAATAP GKGLPQQPPA PPDQDDSAAP STLSLLGPTF 150
    PGLSSCSADI KDILNEAGTM QLLQQQQQQQ QHQQQHQQHQ QQQEVISEGS 200
    SARAREATGA PSSSKDSYLG GNSTISDSAK ELCKAVSVSM GLGVEALEHL 250
    SPGEQLRGDC MYASLLGGPP AVRPTPCAPL PECKGLPLDE GPGKSTEETA 300
    EYSSFKGGYA KGLEGESLGC SGSSEAGSSG TLEIPSSLSL YKSGALDEAA 350
    AYQNRDYYNF PLALSGPPHP PPPTHPHARI KLENPLDYGS AWAAAAAQCR 400
    YGDLGSLHGG SVAGPSTGSP PATTSSSWHT LFTAEEGQLY GPGGGGGSSS 450
    PSDAGPVAPY GYTRPPQGLT SQESDYSASE VWYPGGVVNR VPYPSPNCVK 500
    SEMGPWMENY SGPYGDMRLD STRDHVLPID YYFPPQKTCL ICGDEASGCH 550
    YGALTCGSCK VFFKRAAEGK QKYLCASRND CTIDKFRRKN CPSCRLRKCY 600
    EAGMTLGARK LKKLGNLKLQ EEGENSNAGS PTEDPSQKMT VSHIEGYECQ 650
    PIFLNVLEAI EPGVVCAGHD NNQPDSFAAL LSSLNELGER QLVHVVKWAK 700
    ALPGFRNLHV DDQMAVIQYS WMGLMVFAMG WRSFTNVNSR MLYFAPDLVF 750
    NEYRMHKSRM YSQCVRMRHL SQEFGWLQIT PQEFLCMKAL LLFSIIPVDG 800
    LKNQKFFDEL RMNYIKELDR IIACKRKNPT SCSRRFYQLT KLLDSVQPIA 850
    RELHQFTFDL LIKSHMVSVD FPEMMAEIIS VQVPKILSGK VKPIYFHTQ 899
    Length:899
    Mass (Da):98,194
    Last modified:November 1, 1990 - v1
    Checksum:iFD9EE07C07F7A568
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S56585 mRNA. Translation: AAB19916.1.
    X53779 mRNA. Translation: CAA37795.1.
    M37890 mRNA. Translation: AAA37234.1.
    X59592 mRNA. Translation: CAA42160.1.
    CCDSiCCDS30294.1.
    PIRiA35895.
    RefSeqiNP_038504.1. NM_013476.3.
    UniGeneiMm.39005.
    Mm.394224.
    Mm.439657.

    Genome annotation databases

    EnsembliENSMUST00000052837; ENSMUSP00000052648; ENSMUSG00000046532.
    GeneIDi11835.
    KEGGimmu:11835.
    UCSCiuc009tuv.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S56585 mRNA. Translation: AAB19916.1 .
    X53779 mRNA. Translation: CAA37795.1 .
    M37890 mRNA. Translation: AAA37234.1 .
    X59592 mRNA. Translation: CAA42160.1 .
    CCDSi CCDS30294.1.
    PIRi A35895.
    RefSeqi NP_038504.1. NM_013476.3.
    UniGenei Mm.39005.
    Mm.394224.
    Mm.439657.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2QPY X-ray 2.50 A 649-899 [» ]
    ProteinModelPortali P19091.
    SMRi P19091. Positions 534-898.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198179. 16 interactions.
    DIPi DIP-41803N.
    IntActi P19091. 2 interactions.
    MINTi MINT-151935.

    Chemistry

    BindingDBi P19091.
    ChEMBLi CHEMBL3056.
    GuidetoPHARMACOLOGYi 628.

    PTM databases

    PhosphoSitei P19091.

    Proteomic databases

    PRIDEi P19091.

    Protocols and materials databases

    DNASUi 11835.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000052837 ; ENSMUSP00000052648 ; ENSMUSG00000046532 .
    GeneIDi 11835.
    KEGGi mmu:11835.
    UCSCi uc009tuv.1. mouse.

    Organism-specific databases

    CTDi 367.
    MGIi MGI:88064. Ar.

    Phylogenomic databases

    eggNOGi NOG245477.
    GeneTreei ENSGT00730000110451.
    HOGENOMi HOG000254783.
    HOVERGENi HBG007583.
    InParanoidi P19091.
    KOi K08557.
    OMAi CSTDLKD.
    OrthoDBi EOG7J17Z7.
    PhylomeDBi P19091.
    TreeFami TF350286.

    Miscellaneous databases

    EvolutionaryTracei P19091.
    NextBioi 279763.
    PROi P19091.
    SOURCEi Search...

    Gene expression databases

    Bgeei P19091.
    CleanExi MM_AR.
    Genevestigatori P19091.

    Family and domain databases

    Gene3Di 1.10.565.10. 2 hits.
    3.30.50.10. 1 hit.
    InterProi IPR001103. Andrgn_rcpt.
    IPR008946. Nucl_hormone_rcpt_ligand-bd.
    IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
    IPR001628. Znf_hrmn_rcpt.
    IPR013088. Znf_NHR/GATA.
    [Graphical view ]
    Pfami PF02166. Androgen_recep. 1 hit.
    PF00104. Hormone_recep. 1 hit.
    PF00105. zf-C4. 1 hit.
    [Graphical view ]
    PRINTSi PR00521. ANDROGENR.
    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. "Molecular cloning of androgen receptors from divergent species with a polymerase chain reaction technique: complete cDNA sequence of the mouse androgen receptor and isolation of androgen receptor cDNA probes from dog, guinea pig and clawed frog."
      He W.W., Fischer L.M., Sun S., Bilhartz D.L., Zhu X., Young C.Y.F., Kelley D.B., Tindall D.J.
      Biochem. Biophys. Res. Commun. 171:697-704(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
    2. "Structure and size distribution of the androgen receptor mRNA in wild-type and Tfm/Y mutant mice."
      Gaspar M.L., Meo T., Tosi M.
      Mol. Endocrinol. 4:1600-1610(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The mouse androgen receptor. Functional analysis of the protein and characterization of the gene."
      Faber P.W., King A., van Rooij H.C.J., Brinkmann A.O., de Both N.J., Trapman J.
      Biochem. J. 278:269-278(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "A frameshift mutation destabilizes androgen receptor messenger RNA in the Tfm mouse."
      Charest N.J., Zhou Z., Lubahn D.B., Olsen K.L., Wilson E.M., French F.S.
      Mol. Endocrinol. 5:573-581(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "Novel ATPase of SNF2-like protein family interacts with androgen receptor and modulates androgen-dependent transcription."
      Rouleau N., Domans'kyi A., Reeben M., Moilanen A.-M., Havas K., Kang Z., Owen-Hughes T., Palvimo J.J., Jaenne O.A.
      Mol. Biol. Cell 13:2106-2119(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAD54L2.
      Strain: Swiss Webster.
      Tissue: Embryo.
    6. "Dyrk1A potentiates steroid hormone-induced transcription via the chromatin remodeling factor Arip4."
      Sitz J.H., Tigges M., Baumgaertel K., Khaspekov L.G., Lutz B.
      Mol. Cell. Biol. 24:5821-5834(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAD54L2.
    7. Cited for: INTERACTION WITH ZNF318.
    8. "GAC63, a GRIP1-dependent nuclear receptor coactivator."
      Chen Y.-H., Kim J.H., Stallcup M.R.
      Mol. Cell. Biol. 25:5965-5972(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLC30A9.
    9. "Cryptochromes mediate rhythmic repression of the glucocorticoid receptor."
      Lamia K.A., Papp S.J., Yu R.T., Barish G.D., Uhlenhaut N.H., Jonker J.W., Downes M., Evans R.M.
      Nature 480:552-556(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CRY1.
    10. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 649-899 IN COMPLEX WITH NCOA2 AND DIHYDROTESTOSTERONE.

    Entry informationi

    Entry nameiANDR_MOUSE
    AccessioniPrimary (citable) accession number: P19091
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 163 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    In the absence of ligand, steroid hormone receptors are thought to be weakly associated with nuclear components; hormone binding greatly increases receptor affinity. The hormone-receptor complex appears to recognize discrete DNA sequences upstream of transcriptional start sites.
    Transcriptional activity is enhanced by binding to RANBP9.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3