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P15207

- ANDR_RAT

UniProt

P15207 - ANDR_RAT

Protein

Androgen receptor

Gene

Ar

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 162 (01 Oct 2014)
      Sequence version 1 (01 Apr 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 sitei688 – 6881Androgen
    Sitei703 – 7031Interaction with coactivator LXXL motifBy similarity
    Binding sitei735 – 7351Androgen
    Binding sitei860 – 8601Androgen
    Sitei880 – 8801Interaction with coactivator FXXLF motifBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi541 – 61474Nuclear receptorPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri542 – 56221NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri578 – 60225NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. activation of prostate induction by androgen receptor signaling pathway Source: Ensembl
    2. androgen receptor signaling pathway Source: RGD
    3. cellular response to steroid hormone stimulus Source: RGD
    4. epithelial cell differentiation involved in prostate gland development Source: Ensembl
    5. intracellular receptor signaling pathway Source: BHF-UCL
    6. in utero embryonic development Source: Ensembl
    7. lateral sprouting involved in mammary gland duct morphogenesis Source: Ensembl
    8. male genitalia morphogenesis Source: Ensembl
    9. male gonad development Source: Ensembl
    10. male sex differentiation Source: RGD
    11. male somatic sex determination Source: Ensembl
    12. mammary gland alveolus development Source: Ensembl
    13. morphogenesis of an epithelial fold Source: Ensembl
    14. negative regulation of epithelial cell proliferation Source: Ensembl
    15. negative regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
    16. negative regulation of integrin biosynthetic process Source: UniProtKB
    17. organ formation Source: Ensembl
    18. positive regulation of cell proliferation Source: UniProtKB
    19. positive regulation of insulin-like growth factor receptor signaling pathway Source: Ensembl
    20. positive regulation of intracellular estrogen receptor signaling pathway Source: Ensembl
    21. positive regulation of MAPK cascade Source: Ensembl
    22. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    23. positive regulation of phosphorylation Source: UniProtKB
    24. positive regulation of transcription, DNA-templated Source: UniProtKB
    25. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    26. prostate gland epithelium morphogenesis Source: Ensembl
    27. prostate gland growth Source: Ensembl
    28. regulation of catalytic activity Source: Ensembl
    29. regulation of developmental growth Source: Ensembl
    30. regulation of establishment of protein localization to plasma membrane Source: UniProtKB
    31. regulation of prostatic bud formation Source: Ensembl
    32. regulation of systemic arterial blood pressure Source: Ensembl
    33. response to insulin Source: RGD
    34. spermatogenesis Source: Ensembl
    35. tertiary branching involved in mammary gland duct morphogenesis Source: Ensembl
    36. 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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome X

    Organism-specific databases

    RGDi2147. Ar.

    Subcellular locationi

    Nucleus 1 PublicationPROSITE-ProRule annotation. 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: RGD
    2. cytoplasm Source: UniProtKB
    3. dendrite Source: RGD
    4. nuclear chromatin Source: UniProtKB
    5. nucleus Source: UniProtKB
    6. plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Defects in Ar are a cause of androgen insensitivity. Rats with this syndrome are called testicular feminized (TFM).

    Keywords - Diseasei

    Disease mutation

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 902902Androgen receptorPRO_0000053712Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei61 – 611Phosphoserine; by CDK9By similarity
    Modified residuei75 – 751PhosphoserineBy similarity
    Modified residuei221 – 2211Phosphotyrosine; by CSKBy similarity
    Modified residuei265 – 2651Phosphotyrosine; by CSK and TNK2By similarity
    Modified residuei305 – 3051Phosphotyrosine; by CSKBy similarity
    Modified residuei344 – 3441Phosphotyrosine; by CSKBy similarity
    Modified residuei355 – 3551Phosphotyrosine; by CSKBy similarity
    Modified residuei360 – 3601Phosphotyrosine; by CSKBy similarity
    Modified residuei361 – 3611Phosphotyrosine; by CSK and TNK2By similarity
    Cross-linki384 – 384Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Modified residuei391 – 3911Phosphotyrosine; by CSKBy similarity
    Cross-linki503 – 503Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Modified residuei517 – 5171Phosphotyrosine; by CSKBy similarity
    Modified residuei534 – 5341Phosphotyrosine; by CSKBy similarity
    Modified residuei633 – 6331Phosphoserine; by STK4/MST1By similarity
    Cross-linki828 – 828Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki830 – 830Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei898 – 8981Phosphotyrosine; 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-517 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-384 (major) and Lys-503 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

    PaxDbiP15207.
    PRIDEiP15207.

    PTM databases

    PhosphoSiteiP15207.

    Expressioni

    Tissue specificityi

    Highest levels in the seminal vesicle, ventral prostate and coagulating gland with lower levels in the kidney and levator ani muscle.

    Gene expression databases

    GenevestigatoriP15207.

    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, RBAK, SPDEF, SRA1, TGFB1I1, ZNF318 and RREB1. Interacts with ZMIZ1/ZIMP10 and ZMIZ2/ZMIP7 which both enhance its transactivation activity. Interacts with SLC30A9 and RAD54L2/ARIP4. Interacts via the ligand-binding domain with LXXLL and FXXLF motifs from NCOA1, NCOA2, NCOA3, NCOA4 and MAGEA11. 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 HIP1 (via coiled coil domain). 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 dihydrotestosterone-induced AR transcriptional activity. Interacts with PRPF6 in a hormone-independent way; this interaction enhances dihydrotestosterone-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 CRY1.7 Publications

    Protein-protein interaction databases

    BioGridi246396. 2 interactions.
    DIPiDIP-5963N.
    IntActiP15207. 1 interaction.
    STRINGi10116.ENSRNOP00000009129.

    Structurei

    Secondary structure

    1
    902
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi543 – 5453
    Beta strandi551 – 5533
    Beta strandi556 – 5583
    Helixi560 – 57011
    Beta strandi579 – 5824
    Turni588 – 5936
    Helixi595 – 60511
    Helixi655 – 6639
    Beta strandi674 – 6763
    Helixi680 – 70324
    Helixi708 – 7103
    Helixi713 – 74028
    Beta strandi743 – 7486
    Beta strandi751 – 7533
    Helixi755 – 7606
    Helixi764 – 77916
    Helixi784 – 79512
    Beta strandi797 – 8004
    Helixi807 – 82620
    Beta strandi827 – 8293
    Helixi833 – 86634
    Helixi867 – 8693
    Helixi876 – 8849
    Helixi886 – 8905
    Beta strandi893 – 8964

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1I37X-ray2.00A647-902[»]
    1I38X-ray2.00A647-902[»]
    1R4IX-ray3.10A/B533-637[»]
    1XNNX-ray2.20A647-902[»]
    2IHQX-ray2.00A647-902[»]
    2NW4X-ray3.00A647-902[»]
    3G0WX-ray1.95A647-902[»]
    ProteinModelPortaliP15207.
    SMRiP15207. Positions 538-611, 646-901.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15207.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 540540ModulatingAdd
    BLAST
    Regioni534 – 902369Interaction with LPXNBy similarityAdd
    BLAST
    Regioni554 – 64491Interaction with HIPK3Add
    BLAST
    Regioni607 – 902296Interaction with KAT7By similarityAdd
    BLAST
    Regioni673 – 902230Ligand-bindingAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi63 – 675Poly-Arg
    Compositional biasi174 – 19522Poly-GlnAdd
    BLAST
    Compositional biasi370 – 3767Poly-Pro
    Compositional biasi394 – 4007Poly-Ala
    Compositional biasi444 – 4507Poly-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 fingeri542 – 56221NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri578 – 60225NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG245477.
    GeneTreeiENSGT00730000110451.
    HOGENOMiHOG000254783.
    HOVERGENiHBG007583.
    InParanoidiP15207.
    KOiK08557.
    OrthoDBiEOG7J17Z7.
    PhylomeDBiP15207.
    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.

    P15207-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEVQLGLGRV YPRPPSKTYR GAFQNLFQSV REAIQNPGPR HPEAASIAPP    50
    GACLQQRQET SPRRRRRQQH PEDGSPQAHI RGTTGYLALE EEQQPSQQQS 100
    ASEGHPESGC LPEPGAATAP GKGLPQQPPA PPDQDDSAAP STLSLLGPTF 150
    PGLSSCSADI KDILSEAGTM QLLQQQQQQQ QQQQQQQQQQ QQQQQEVISE 200
    GSSSVRAREA TGAPSSSKDS YLGGNSTISD SAKELCKAVS VSMGLGVEAL 250
    EHLSPGEQLR GDCMYASLLG GPPAVRPTPC APLAECKGLS LDEGPGKGTE 300
    ETAEYSSFKG GYAKGLEGES LGCSGSSEAG SSGTLEIPSS LSLYKSGAVD 350
    EAAAYQNRDY YNFPLALSGP PHPPPPTHPH ARIKLENPSD YGSAWAAAAA 400
    QCRYGDLASL HGGSVAGPST GSPPATASSS WHTLFTAEEG QLYGPGGGGG 450
    SSSPSDAGPV APYGYTRPPQ GLASQEGDFS ASEVWYPGGV VNRVPYPSPS 500
    CVKSEMGPWM ENYSGPYGDM RLDSTRDHVL PIDYYFPPQK TCLICGDEAS 550
    GCHYGALTCG SCKVFFKRAA EGKQKYLCAS RNDCTIDKFR RKNCPSCRLR 600
    KCYEAGMTLG ARKLKKLGNL KLQEEGENSS AGSPTEDPSQ KMTVSHIEGY 650
    ECQPIFLNVL EAIEPGVVCA GHDNNQPDSF AALLSSLNEL GERQLVHVVK 700
    WAKALPGFRN LHVDDQMAVI QYSWMGLMVF AMGWRSFTNV NSRMLYFAPD 750
    LVFNEYRMHK SRMYSQCVRM RHLSQEFGWL QITPQEFLCM KALLLFSIIP 800
    VDGLKNQKFF DELRMNYIKE LDRIIACKRK NPTSCSRRFY QLTKLLDSVQ 850
    PIARELHQFT FDLLIKSHMV SVDFPEMMAE IISVQVPKIL SGKVKPIYFH 900
    TQ 902
    Length:902
    Mass (Da):98,218
    Last modified:April 1, 1990 - v1
    Checksum:i43F4064759FDCBED
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti195 – 1951Missing in AAA40734. (PubMed:2341409)Curated
    Sequence conflicti389 – 3891S → L in AAA40759. (PubMed:3174628)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti735 – 7351R → Q in TFM; has only 10-15% of the androgen-binding capacity of wild-type AR. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20133 mRNA. Translation: AAA40733.1.
    M23264 mRNA. Translation: AAA40759.1.
    J05454 Genomic DNA. Translation: AAA40734.1.
    PIRiB40494.
    RefSeqiNP_036634.1. NM_012502.1.
    UniGeneiRn.9813.

    Genome annotation databases

    EnsembliENSRNOT00000009129; ENSRNOP00000009129; ENSRNOG00000005639.
    GeneIDi24208.
    KEGGirno:24208.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20133 mRNA. Translation: AAA40733.1 .
    M23264 mRNA. Translation: AAA40759.1 .
    J05454 Genomic DNA. Translation: AAA40734.1 .
    PIRi B40494.
    RefSeqi NP_036634.1. NM_012502.1.
    UniGenei Rn.9813.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1I37 X-ray 2.00 A 647-902 [» ]
    1I38 X-ray 2.00 A 647-902 [» ]
    1R4I X-ray 3.10 A/B 533-637 [» ]
    1XNN X-ray 2.20 A 647-902 [» ]
    2IHQ X-ray 2.00 A 647-902 [» ]
    2NW4 X-ray 3.00 A 647-902 [» ]
    3G0W X-ray 1.95 A 647-902 [» ]
    ProteinModelPortali P15207.
    SMRi P15207. Positions 538-611, 646-901.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 246396. 2 interactions.
    DIPi DIP-5963N.
    IntActi P15207. 1 interaction.
    STRINGi 10116.ENSRNOP00000009129.

    Chemistry

    BindingDBi P15207.
    ChEMBLi CHEMBL3072.
    GuidetoPHARMACOLOGYi 628.

    PTM databases

    PhosphoSitei P15207.

    Proteomic databases

    PaxDbi P15207.
    PRIDEi P15207.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000009129 ; ENSRNOP00000009129 ; ENSRNOG00000005639 .
    GeneIDi 24208.
    KEGGi rno:24208.

    Organism-specific databases

    CTDi 367.
    RGDi 2147. Ar.

    Phylogenomic databases

    eggNOGi NOG245477.
    GeneTreei ENSGT00730000110451.
    HOGENOMi HOG000254783.
    HOVERGENi HBG007583.
    InParanoidi P15207.
    KOi K08557.
    OrthoDBi EOG7J17Z7.
    PhylomeDBi P15207.
    TreeFami TF350286.

    Miscellaneous databases

    EvolutionaryTracei P15207.
    NextBioi 602605.
    PROi P15207.

    Gene expression databases

    Genevestigatori P15207.

    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. "The rat androgen receptor: primary structure, autoregulation of its messenger ribonucleic acid, and immunocytochemical localization of the receptor protein."
      Tan J., Joseph D.R., Quarmby V.E., Lubahn D.B., Sar M., French F.S., Wilson E.M.
      Mol. Endocrinol. 2:1276-1285(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Structural analysis of complementary DNA and amino acid sequences of human and rat androgen receptors."
      Chang C., Kokontis J., Liao S.
      Proc. Natl. Acad. Sci. U.S.A. 85:7211-7215(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Prostate.
    3. "A single base mutation in the androgen receptor gene causes androgen insensitivity in the testicular feminized rat."
      Yarbrough W.G., Quarmby V.E., Simental J.A., Joseph D.R., Sar M., Lubahn D.B., Olsen K.L., French F.S., Wilson E.M.
      J. Biol. Chem. 265:8893-8900(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TFM GLN-735.
    4. "Activation of androgen receptor function by a novel nuclear protein kinase."
      Moilanen A.-M., Karvonen U., Poukka H., Jaenne O.A., Palvimo J.J.
      Mol. Biol. Cell 9:2527-2543(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIPK3, SUBCELLULAR LOCATION.
      Tissue: Testis.
    5. "A novel steroid receptor co-activator protein (SRAP) as an alternative form of steroid receptor RNA-activator gene: expression in prostate cancer cells and enhancement of androgen receptor activity."
      Kawashima H., Takano H., Sugita S., Takahara Y., Sugimura K., Nakatani T.
      Biochem. J. 369:163-171(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SRA1.
    6. "Crystallographic structures of the ligand-binding domains of the androgen receptor and its T877A mutant complexed with the natural agonist dihydrotestosterone."
      Sack J.S., Kish K.F., Wang C., Attar R.M., Kiefer S.E., An Y., Wu G.Y., Scheffler J.E., Salvati M.E., Krystek S.R. Jr., Weinmann R., Einspahr H.M.
      Proc. Natl. Acad. Sci. U.S.A. 98:4904-4909(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 647-902 OF MUTANT ALA-860 IN COMPLEX WITH DIHYDROTESTOSTERONE.
    7. "Structural basis of androgen receptor binding to selective androgen response elements."
      Shaffer P.L., Jivan A., Dollins D.E., Claessens F., Gewirth D.T.
      Proc. Natl. Acad. Sci. U.S.A. 101:4758-4763(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 533-637 IN COMPLEX WITH DNA AND ZINC IONS, SUBUNIT.
    8. "Structure based approach to the design of bicyclic-1H-isoindole-1,3(2H)-dione based androgen receptor antagonists."
      Salvati M.E., Balog A., Shan W., Wei D.D., Pickering D., Attar R.M., Geng J., Rizzo C.A., Gottardis M.M., Weinmann R., Krystek S.R., Sack J., An Y., Kish K.
      Bioorg. Med. Chem. Lett. 15:271-276(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 647-902 OF MUTANT ALA-860 IN COMPLEX WITH SYNTHETIC ANTAGONIST.
    9. "Discovery of potent, orally-active, and muscle-selective androgen receptor modulators based on an N-aryl-hydroxybicyclohydantoin scaffold."
      Sun C., Robl J.A., Wang T.C., Huang Y., Kuhns J.E., Lupisella J.A., Beehler B.C., Golla R., Sleph P.G., Seethala R., Fura A., Krystek S.R. Jr., An Y., Malley M.F., Sack J.S., Salvati M.E., Grover G.J., Ostrowski J., Hamann L.G.
      J. Med. Chem. 49:7596-7599(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 647-902 IN COMPLEX WITH SYNTHETIC ANDROGEN ANTAGONIST, FUNCTION.
    10. "Pharmacological and X-ray structural characterization of a novel selective androgen receptor modulator: potent hyperanabolic stimulation of skeletal muscle with hypostimulation of prostate in rats."
      Ostrowski J., Kuhns J.E., Lupisella J.A., Manfredi M.C., Beehler B.C., Krystek S.R. Jr., Bi Y., Sun C., Seethala R., Golla R., Sleph P.G., Fura A., An Y., Kish K.F., Sack J.S., Mookhtiar K.A., Grover G.J., Hamann L.G.
      Endocrinology 148:4-12(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 647-902 IN COMPLEX WITH THE SYNTHETIC AGONIST MBS-564929, FUNCTION.

    Entry informationi

    Entry nameiANDR_RAT
    AccessioniPrimary (citable) accession number: P15207
    Secondary accession number(s): Q63049
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 162 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3