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Protein

Androgen receptor

Gene

Ar

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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).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

GO - Biological processi

  • activation of prostate induction by androgen receptor signaling pathway Source: MGI
  • androgen receptor signaling pathway Source: MGI
  • cellular process Source: MGI
  • epithelial cell differentiation involved in prostate gland development Source: MGI
  • epithelial cell morphogenesis Source: MGI
  • fertilization Source: MGI
  • intracellular receptor signaling pathway Source: BHF-UCL
  • in utero embryonic development Source: MGI
  • lateral sprouting involved in mammary gland duct morphogenesis Source: MGI
  • Leydig cell differentiation Source: MGI
  • male genitalia morphogenesis Source: MGI
  • male gonad development Source: MGI
  • male somatic sex determination Source: MGI
  • mammary gland alveolus development Source: MGI
  • morphogenesis of an epithelial fold Source: MGI
  • multicellular organism growth Source: MGI
  • negative regulation of epithelial cell proliferation Source: MGI
  • negative regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
  • negative regulation of integrin biosynthetic process Source: UniProtKB
  • organ formation Source: MGI
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of insulin-like growth factor receptor signaling pathway Source: MGI
  • positive regulation of integrin biosynthetic process Source: MGI
  • positive regulation of intracellular estrogen receptor signaling pathway Source: MGI
  • positive regulation of MAPK cascade Source: MGI
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • positive regulation of phosphorylation Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase III promoter Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • prostate gland epithelium morphogenesis Source: MGI
  • prostate gland growth Source: MGI
  • protein oligomerization Source: MGI
  • regulation of catalytic activity Source: MGI
  • regulation of developmental growth Source: MGI
  • regulation of establishment of protein localization to plasma membrane Source: UniProtKB
  • regulation of gene expression Source: MGI
  • regulation of prostatic bud formation Source: MGI
  • regulation of systemic arterial blood pressure Source: MGI
  • regulation of transcription, DNA-templated Source: MGI
  • regulation of transcription from RNA polymerase II promoter Source: MGI
  • reproductive structure development Source: MGI
  • reproductive system development Source: MGI
  • response to insulin Source: Ensembl
  • seminiferous tubule development Source: MGI
  • single fertilization Source: MGI
  • spermatogenesis Source: MGI
  • tertiary branching involved in mammary gland duct morphogenesis Source: MGI
  • 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

Enzyme and pathway databases

ReactomeiREACT_276696. Nuclear Receptor transcription pathway.
REACT_358787. Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.

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 Componenti: 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

  • axon Source: Ensembl
  • cytoplasm Source: UniProtKB
  • dendrite Source: Ensembl
  • nuclear chromatin Source: UniProtKB
  • nucleus Source: UniProtKB
  • plasma membrane Source: MGI
  • protein complex Source: MGI
Complete GO annotation...

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 residuei251 – 2511PhosphoserineBy 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.
GenevisibleiP19091. MM.

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. Interacts with CCAR1 and GATA2 (By similarity).By similarity6 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi198179. 16 interactions.
DIPiDIP-41803N.
IntActiP19091. 2 interactions.
MINTiMINT-151935.
STRINGi10090.ENSMUSP00000052648.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QPYX-ray2.50A649-899[»]
ProteinModelPortaliP19091.
SMRiP19091. Positions 535-898.
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
Regioni571 – 899329Interaction with CCAR1By 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.
GeneTreeiENSGT00760000118887.
HOGENOMiHOG000254783.
HOVERGENiHBG007583.
InParanoidiP19091.
KOiK08557.
OMAiMENYSGP.
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

        10         20         30         40         50
MEVQLGLGRV YPRPPSKTYR GAFQNLFQSV REAIQNPGPR HPEAANIAPP
60 70 80 90 100
GACLQQRQET SPRRRRRQQH TEDGSPQAHI RGPTGYLALE EEQQPSQQQA
110 120 130 140 150
ASEGHPESSC LPEPGAATAP GKGLPQQPPA PPDQDDSAAP STLSLLGPTF
160 170 180 190 200
PGLSSCSADI KDILNEAGTM QLLQQQQQQQ QHQQQHQQHQ QQQEVISEGS
210 220 230 240 250
SARAREATGA PSSSKDSYLG GNSTISDSAK ELCKAVSVSM GLGVEALEHL
260 270 280 290 300
SPGEQLRGDC MYASLLGGPP AVRPTPCAPL PECKGLPLDE GPGKSTEETA
310 320 330 340 350
EYSSFKGGYA KGLEGESLGC SGSSEAGSSG TLEIPSSLSL YKSGALDEAA
360 370 380 390 400
AYQNRDYYNF PLALSGPPHP PPPTHPHARI KLENPLDYGS AWAAAAAQCR
410 420 430 440 450
YGDLGSLHGG SVAGPSTGSP PATTSSSWHT LFTAEEGQLY GPGGGGGSSS
460 470 480 490 500
PSDAGPVAPY GYTRPPQGLT SQESDYSASE VWYPGGVVNR VPYPSPNCVK
510 520 530 540 550
SEMGPWMENY SGPYGDMRLD STRDHVLPID YYFPPQKTCL ICGDEASGCH
560 570 580 590 600
YGALTCGSCK VFFKRAAEGK QKYLCASRND CTIDKFRRKN CPSCRLRKCY
610 620 630 640 650
EAGMTLGARK LKKLGNLKLQ EEGENSNAGS PTEDPSQKMT VSHIEGYECQ
660 670 680 690 700
PIFLNVLEAI EPGVVCAGHD NNQPDSFAAL LSSLNELGER QLVHVVKWAK
710 720 730 740 750
ALPGFRNLHV DDQMAVIQYS WMGLMVFAMG WRSFTNVNSR MLYFAPDLVF
760 770 780 790 800
NEYRMHKSRM YSQCVRMRHL SQEFGWLQIT PQEFLCMKAL LLFSIIPVDG
810 820 830 840 850
LKNQKFFDEL RMNYIKELDR IIACKRKNPT SCSRRFYQLT KLLDSVQPIA
860 870 880 890
RELHQFTFDL LIKSHMVSVD FPEMMAEIIS VQVPKILSGK VKPIYFHTQ
Length:899
Mass (Da):98,194
Last modified:November 1, 1990 - v1
Checksum:iFD9EE07C07F7A568
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QPYX-ray2.50A649-899[»]
ProteinModelPortaliP19091.
SMRiP19091. Positions 535-898.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198179. 16 interactions.
DIPiDIP-41803N.
IntActiP19091. 2 interactions.
MINTiMINT-151935.
STRINGi10090.ENSMUSP00000052648.

Chemistry

BindingDBiP19091.
ChEMBLiCHEMBL3056.
GuidetoPHARMACOLOGYi628.

PTM databases

PhosphoSiteiP19091.

Proteomic databases

PRIDEiP19091.

Protocols and materials databases

DNASUi11835.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi367.
MGIiMGI:88064. Ar.

Phylogenomic databases

eggNOGiNOG245477.
GeneTreeiENSGT00760000118887.
HOGENOMiHOG000254783.
HOVERGENiHBG007583.
InParanoidiP19091.
KOiK08557.
OMAiMENYSGP.
OrthoDBiEOG7J17Z7.
PhylomeDBiP19091.
TreeFamiTF350286.

Enzyme and pathway databases

ReactomeiREACT_276696. Nuclear Receptor transcription pathway.
REACT_358787. Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.

Miscellaneous databases

EvolutionaryTraceiP19091.
NextBioi279763.
PROiP19091.
SOURCEiSearch...

Gene expression databases

BgeeiP19091.
CleanExiMM_AR.
GenevisibleiP19091. MM.

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]
ProtoNetiSearch...

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: June 24, 2015
This is version 171 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.