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P15207

- ANDR_RAT

UniProt

P15207 - ANDR_RAT

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Protein

Androgen receptor

Gene
Ar, Nr3c4
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei688 – 6881Androgen
Sitei703 – 7031Interaction with coactivator LXXL motif By similarity
Binding sitei735 – 7351Androgen
Binding sitei860 – 8601Androgen
Sitei880 – 8801Interaction with coactivator FXXLF motif By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi541 – 61474Nuclear receptorAdd
BLAST
Zinc fingeri542 – 56221NR C4-typeAdd
BLAST
Zinc fingeri578 – 60225NR C4-typeAdd
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
Complete GO annotation...

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. 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.1 Publication

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
Complete GO annotation...

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).1 Publication

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 CDK9 By similarity
Modified residuei75 – 751Phosphoserine By similarity
Modified residuei221 – 2211Phosphotyrosine; by CSK By similarity
Modified residuei265 – 2651Phosphotyrosine; by CSK and TNK2 By similarity
Modified residuei305 – 3051Phosphotyrosine; by CSK By similarity
Modified residuei344 – 3441Phosphotyrosine; by CSK By similarity
Modified residuei355 – 3551Phosphotyrosine; by CSK By similarity
Modified residuei360 – 3601Phosphotyrosine; by CSK By similarity
Modified residuei361 – 3611Phosphotyrosine; by CSK and TNK2 By similarity
Cross-linki384 – 384Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Modified residuei391 – 3911Phosphotyrosine; by CSK By similarity
Cross-linki503 – 503Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Modified residuei517 – 5171Phosphotyrosine; by CSK By similarity
Modified residuei534 – 5341Phosphotyrosine; by CSK By similarity
Modified residuei633 – 6331Phosphoserine; by STK4/MST1 By 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 CSK By 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.
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.
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.

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 CRY1.3 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.

Miscellaneous databases

EvolutionaryTraceiP15207.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 540540ModulatingAdd
BLAST
Regioni534 – 902369Interaction with LPXN By similarityAdd
BLAST
Regioni554 – 64491Interaction with HIPK3Add
BLAST
Regioni607 – 902296Interaction with KAT7 By 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.

Sequence similaritiesi

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti195 – 1951Missing in AAA40734. 1 Publication
Sequence conflicti389 – 3891S → L in AAA40759. 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: July 9, 2014
This is version 161 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

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