ANDR_MOUSE
ID ANDR_MOUSE Reviewed; 899 AA.
AC P19091;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 224.
DE RecName: Full=Androgen receptor;
DE AltName: Full=Dihydrotestosterone receptor;
DE AltName: Full=Nuclear receptor subfamily 3 group C member 4;
GN Name=Ar; Synonyms=Nr3c4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=2403358; DOI=10.1016/0006-291x(90)91202-4;
RA He W.W., Fischer L.M., Sun S., Bilhartz D.L., Zhu X., Young C.Y.F.,
RA Kelley D.B., Tindall D.J.;
RT "Molecular cloning of androgen receptors from divergent species with a
RT polymerase chain reaction technique: complete cDNA sequence of the mouse
RT androgen receptor and isolation of androgen receptor cDNA probes from dog,
RT guinea pig and clawed frog.";
RL Biochem. Biophys. Res. Commun. 171:697-704(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2178222; DOI=10.1210/mend-4-10-1600;
RA Gaspar M.L., Meo T., Tosi M.;
RT "Structure and size distribution of the androgen receptor mRNA in wild-type
RT and Tfm/Y mutant mice.";
RL Mol. Endocrinol. 4:1600-1610(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1883336; DOI=10.1042/bj2780269;
RA Faber P.W., King A., van Rooij H.C.J., Brinkmann A.O., de Both N.J.,
RA Trapman J.;
RT "The mouse androgen receptor. Functional analysis of the protein and
RT characterization of the gene.";
RL Biochem. J. 278:269-278(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1681426; DOI=10.1210/mend-5-4-573;
RA Charest N.J., Zhou Z., Lubahn D.B., Olsen K.L., Wilson E.M., French F.S.;
RT "A frameshift mutation destabilizes androgen receptor messenger RNA in the
RT Tfm mouse.";
RL Mol. Endocrinol. 5:573-581(1991).
RN [5]
RP INTERACTION WITH RAD54L2.
RC STRAIN=Swiss Webster; TISSUE=Embryo;
RX PubMed=12058073; DOI=10.1091/mbc.01-10-0484.;
RA Rouleau N., Domans'kyi A., Reeben M., Moilanen A.-M., Havas K., Kang Z.,
RA Owen-Hughes T., Palvimo J.J., Jaenne O.A.;
RT "Novel ATPase of SNF2-like protein family interacts with androgen receptor
RT and modulates androgen-dependent transcription.";
RL Mol. Biol. Cell 13:2106-2119(2002).
RN [6]
RP INTERACTION WITH RAD54L2.
RX PubMed=15199138; DOI=10.1128/mcb.24.13.5821-5834.2004;
RA Sitz J.H., Tigges M., Baumgaertel K., Khaspekov L.G., Lutz B.;
RT "Dyrk1A potentiates steroid hormone-induced transcription via the chromatin
RT remodeling factor Arip4.";
RL Mol. Cell. Biol. 24:5821-5834(2004).
RN [7]
RP INTERACTION WITH ZNF318.
RX PubMed=15882980; DOI=10.1016/j.bbrc.2005.04.024;
RA Ishizuka M., Kawate H., Takayanagi R., Ohshima H., Tao R.-H., Hagiwara H.;
RT "A zinc finger protein TZF is a novel corepressor of androgen receptor.";
RL Biochem. Biophys. Res. Commun. 331:1025-1031(2005).
RN [8]
RP INTERACTION WITH SLC30A9.
RX PubMed=15988012; DOI=10.1128/mcb.25.14.5965-5972.2005;
RA Chen Y.-H., Kim J.H., Stallcup M.R.;
RT "GAC63, a GRIP1-dependent nuclear receptor coactivator.";
RL Mol. Cell. Biol. 25:5965-5972(2005).
RN [9]
RP INTERACTION WITH ZNF318.
RX PubMed=16446156; DOI=10.1016/j.bbrc.2005.12.213;
RA Tao R.H., Kawate H., Ohnaka K., Ishizuka M., Hagiwara H., Takayanagi R.;
RT "Opposite effects of alternative TZF spliced variants on androgen
RT receptor.";
RL Biochem. Biophys. Res. Commun. 341:515-521(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-630, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP INTERACTION WITH CRY1.
RX PubMed=22170608; DOI=10.1038/nature10700;
RA Lamia K.A., Papp S.J., Yu R.T., Barish G.D., Uhlenhaut N.H., Jonker J.W.,
RA Downes M., Evans R.M.;
RT "Cryptochromes mediate rhythmic repression of the glucocorticoid
RT receptor.";
RL Nature 480:552-556(2011).
RN [12]
RP INTERACTION WITH ARID4A AND ARID4B.
RX PubMed=23487765; DOI=10.1073/pnas.1218318110;
RA Wu R.C., Jiang M., Beaudet A.L., Wu M.Y.;
RT "ARID4A and ARID4B regulate male fertility, a functional link to the AR and
RT RB pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:4616-4621(2013).
RN [13]
RP INTERACTION WITH CRY1 AND CRY2.
RX PubMed=28751364; DOI=10.1073/pnas.1704955114;
RA Kriebs A., Jordan S.D., Soto E., Henriksson E., Sandate C.R., Vaughan M.E.,
RA Chan A.B., Duglan D., Papp S.J., Huber A.L., Afetian M.E., Yu R.T.,
RA Zhao X., Downes M., Evans R.M., Lamia K.A.;
RT "Circadian repressors CRY1 and CRY2 broadly interact with nuclear receptors
RT and modulate transcriptional activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:8776-8781(2017).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 649-899 IN COMPLEX WITH NCOA2 AND
RP DIHYDROTESTOSTERONE.
RX PubMed=17911242; DOI=10.1073/pnas.0708036104;
RA Estebanez-Perpina E., Arnold L.A., Nguyen P., Rodrigues E.D., Mar E.,
RA Bateman R., Pallai P., Shokat K.M., Baxter J.D., Guy R.K., Webb P.,
RA Fletterick R.J.;
RT "A surface on the androgen receptor that allosterically regulates
RT coactivator binding.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:16074-16079(2007).
CC -!- FUNCTION: Steroid hormone receptors are ligand-activated transcription
CC factors that regulate eukaryotic gene expression and affect cellular
CC proliferation and differentiation in target tissues. Transcription
CC factor activity is modulated by bound coactivator and corepressor
CC proteins like ZBTB7A that recruits NCOR1 and NCOR2 to the androgen
CC response elements/ARE on target genes, negatively regulating androgen
CC receptor signaling and androgen-induced cell proliferation.
CC Transcription activation is also down-regulated by NR0B2. Activated,
CC but not phosphorylated, by HIPK3 and ZIPK/DAPK3.
CC {ECO:0000250|UniProtKB:P10275, ECO:0000250|UniProtKB:P15207}.
CC -!- SUBUNIT: Binds DNA as a homodimer. Part of a ternary complex containing
CC AR, EFCAB6/DJBP and PARK7. Interacts with HIPK3 and NR0B2 in the
CC presence of androgen. The ligand binding domain interacts with
CC KAT7/HBO1 in the presence of dihydrotestosterone. Interacts with
CC EFCAB6/DJBP, PQBP1, RANBP9, SPDEF, SRA1, TGFB1I1, ZNF318 and RREB1. The
CC AR N-terminal poly-Gln region binds Ran resulting in enhancement of AR-
CC mediated transactivation. Ran-binding decreases as the poly-Gln length
CC increases. Interacts with ZMIZ1/ZIMP10 and ZMIZ2/ZMIP7 which both
CC enhance its transactivation activity. Interacts with RBAK. Interacts
CC via the ligand-binding domain with LXXLL and FXXLF motifs from NCOA1,
CC NCOA2, NCOA3, NCOA4 and MAGEA11. Interacts with HIP1 (via coiled coil
CC domain). Interacts with SLC30A9 and RAD54L2/ARIP4. Interacts with
CC MACROD1 (via macro domain) (By similarity). Interacts (via ligand-
CC binding domain) with TRIM68. Interacts with TNK2. Interacts with USP26.
CC Interacts with RNF6. Interacts (regulated by RNF6 probably through
CC polyubiquitination) with RNF14; regulates AR transcriptional activity.
CC Interacts with PRMT2 and TRIM24. Interacts with RACK1. Interacts with
CC RANBP10; this interaction enhances hormone-induced AR transcriptional
CC activity. Interacts with PRPF6 in a hormone-independent way; this
CC interaction enhances hormone-induced AR transcriptional activity.
CC Interacts with STK4/MST1. Interacts with ZIPK/DAPK3. Interacts with
CC LPXN. Interacts with MAK. Part of a complex containing AR, MAK and
CC NCOA3. Interacts with CRY1 (PubMed:22170608, PubMed:28751364).
CC Interacts with CCAR1 and GATA2 (By similarity). Interacts with BUD31
CC (By similarity). Interacts with ARID4A (PubMed:23487765). Interacts
CC with ARID4B (PubMed:23487765). Interacts (via NR LBD domain) with
CC ZBTB7A; the interaction is direct and androgen-dependent (By
CC similarity). Interacts with NCOR1 (By similarity). Interacts with NCOR2
CC (By similarity). Interacts with CRY2 in a ligand-dependent manner
CC (PubMed:28751364). {ECO:0000250|UniProtKB:P10275,
CC ECO:0000250|UniProtKB:P15207, ECO:0000269|PubMed:12058073,
CC ECO:0000269|PubMed:15199138, ECO:0000269|PubMed:15882980,
CC ECO:0000269|PubMed:15988012, ECO:0000269|PubMed:16446156,
CC ECO:0000269|PubMed:17911242, ECO:0000269|PubMed:22170608,
CC ECO:0000269|PubMed:23487765, ECO:0000269|PubMed:28751364}.
CC -!- INTERACTION:
CC P19091; O89110: Casp8; NbExp=2; IntAct=EBI-1776062, EBI-851690;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10275}. Cytoplasm
CC {ECO:0000250|UniProtKB:P10275}. Note=Detected at the promoter of target
CC genes. Predominantly cytoplasmic in unligated form but translocates to
CC the nucleus upon ligand-binding. Can also translocate to the nucleus in
CC unligated form in the presence of RACK1.
CC {ECO:0000250|UniProtKB:P10275}.
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC DNA-binding domain and a C-terminal ligand-binding domain. In the
CC presence of bound steroid the ligand-binding domain interacts with the
CC N-terminal modulating domain, and thereby activates AR transcription
CC factor activity. Agonist binding is required for dimerization and
CC binding to target DNA. The transcription factor activity of the complex
CC formed by ligand-activated AR and DNA is modulated by interactions with
CC coactivator and corepressor proteins. Interaction with RANBP9 is
CC mediated by both the N-terminal domain and the DNA-binding domain.
CC Interaction with EFCAB6/DJBP is mediated by the DNA-binding domain (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated in prostate cancer cells in response to several
CC growth factors including EGF. Phosphorylation is induced by c-Src
CC kinase (CSK). Tyr-514 is one of the major phosphorylation sites and an
CC increase in phosphorylation and Src kinase activity is associated with
CC prostate cancer progression (By similarity). Phosphorylation by TNK2
CC enhances the DNA-binding and transcriptional activity. Phosphorylation
CC at Ser-61 by CDK9 regulates AR promoter selectivity and cell growth.
CC Phosphorylation by PAK6 leads to AR-mediated transcription inhibition
CC (By similarity). {ECO:0000250|UniProtKB:P10275}.
CC -!- PTM: Sumoylated on Lys-381 (major) and Lys-500 (By similarity).
CC Ubiquitinated. Deubiquitinated by USP26 (By similarity). 'Lys-6' and
CC 'Lys-27'-linked polyubiquitination by RNF6 modulates AR transcriptional
CC activity and specificity (By similarity).
CC {ECO:0000250|UniProtKB:P10275}.
CC -!- PTM: Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is required
CC for plasma membrane targeting and for rapid intracellular signaling via
CC ERK and AKT kinases and cAMP generation (By similarity).
CC {ECO:0000250|UniProtKB:P10275}.
CC -!- MISCELLANEOUS: In the absence of ligand, steroid hormone receptors are
CC thought to be weakly associated with nuclear components; hormone
CC binding greatly increases receptor affinity. The hormone-receptor
CC complex appears to recognize discrete DNA sequences upstream of
CC transcriptional start sites.
CC -!- MISCELLANEOUS: Transcriptional activity is enhanced by binding to
CC RANBP9.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC subfamily. {ECO:0000305}.
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DR EMBL; S56585; AAB19916.1; -; mRNA.
DR EMBL; X53779; CAA37795.1; -; mRNA.
DR EMBL; M37890; AAA37234.1; -; mRNA.
DR EMBL; X59592; CAA42160.1; -; mRNA.
DR CCDS; CCDS30294.1; -.
DR PIR; A35895; A35895.
DR RefSeq; NP_038504.1; NM_013476.4.
DR PDB; 2QPY; X-ray; 2.50 A; A=649-899.
DR PDBsum; 2QPY; -.
DR AlphaFoldDB; P19091; -.
DR SMR; P19091; -.
DR BioGRID; 198179; 26.
DR DIP; DIP-41803N; -.
DR IntAct; P19091; 10.
DR MINT; P19091; -.
DR STRING; 10090.ENSMUSP00000052648; -.
DR BindingDB; P19091; -.
DR ChEMBL; CHEMBL3056; -.
DR DrugCentral; P19091; -.
DR iPTMnet; P19091; -.
DR PhosphoSitePlus; P19091; -.
DR EPD; P19091; -.
DR PaxDb; P19091; -.
DR PRIDE; P19091; -.
DR ProteomicsDB; 281823; -.
DR Antibodypedia; 3489; 2550 antibodies from 51 providers.
DR DNASU; 11835; -.
DR Ensembl; ENSMUST00000052837; ENSMUSP00000052648; ENSMUSG00000046532.
DR GeneID; 11835; -.
DR KEGG; mmu:11835; -.
DR UCSC; uc009tuv.1; mouse.
DR CTD; 367; -.
DR MGI; MGI:88064; Ar.
DR VEuPathDB; HostDB:ENSMUSG00000046532; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000155516; -.
DR HOGENOM; CLU_016847_0_0_1; -.
DR InParanoid; P19091; -.
DR OMA; GHPESSC; -.
DR OrthoDB; 615449at2759; -.
DR PhylomeDB; P19091; -.
DR TreeFam; TF350286; -.
DR Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-MMU-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-MMU-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-8940973; RUNX2 regulates osteoblast differentiation.
DR BioGRID-ORCS; 11835; 2 hits in 79 CRISPR screens.
DR ChiTaRS; Ar; mouse.
DR EvolutionaryTrace; P19091; -.
DR PRO; PR:P19091; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P19091; protein.
DR Bgee; ENSMUSG00000046532; Expressed in lacrimal gland and 173 other tissues.
DR Genevisible; P19091; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:CAFA.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005497; F:androgen binding; ISS:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0008013; F:beta-catenin binding; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0050681; F:nuclear androgen receptor binding; ISO:MGI.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:CAFA.
DR GO; GO:0070974; F:POU domain binding; IDA:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0032553; F:ribonucleotide binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0001091; F:RNA polymerase II general transcription initiation factor binding; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0001223; F:transcription coactivator binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0060520; P:activation of prostate induction by androgen receptor signaling pathway; IMP:MGI.
DR GO; GO:0030521; P:androgen receptor signaling pathway; IDA:CAFA.
DR GO; GO:0048645; P:animal organ formation; IMP:MGI.
DR GO; GO:0071391; P:cellular response to estrogen stimulus; ISO:MGI.
DR GO; GO:0071383; P:cellular response to steroid hormone stimulus; ISO:MGI.
DR GO; GO:0071394; P:cellular response to testosterone stimulus; IDA:CAFA.
DR GO; GO:0007620; P:copulation; ISO:MGI.
DR GO; GO:0060742; P:epithelial cell differentiation involved in prostate gland development; IMP:MGI.
DR GO; GO:0003382; P:epithelial cell morphogenesis; IGI:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI.
DR GO; GO:0009566; P:fertilization; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IMP:MGI.
DR GO; GO:0030522; P:intracellular receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0060599; P:lateral sprouting involved in mammary gland duct morphogenesis; IMP:MGI.
DR GO; GO:0033327; P:Leydig cell differentiation; IMP:MGI.
DR GO; GO:0008049; P:male courtship behavior; ISO:MGI.
DR GO; GO:0048808; P:male genitalia morphogenesis; IMP:MGI.
DR GO; GO:0008584; P:male gonad development; IMP:MGI.
DR GO; GO:0046661; P:male sex differentiation; ISO:MGI.
DR GO; GO:0019102; P:male somatic sex determination; IMP:MGI.
DR GO; GO:0060749; P:mammary gland alveolus development; IMP:MGI.
DR GO; GO:0000165; P:MAPK cascade; IMP:MGI.
DR GO; GO:0060571; P:morphogenesis of an epithelial fold; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IGI:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0045720; P:negative regulation of integrin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0045597; P:positive regulation of cell differentiation; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0060769; P:positive regulation of epithelial cell proliferation involved in prostate gland development; IDA:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0045726; P:positive regulation of integrin biosynthetic process; ISO:MGI.
DR GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IMP:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0060406; P:positive regulation of penile erection; ISO:MGI.
DR GO; GO:0042327; P:positive regulation of phosphorylation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0060740; P:prostate gland epithelium morphogenesis; IMP:MGI.
DR GO; GO:0060736; P:prostate gland growth; IMP:MGI.
DR GO; GO:0048638; P:regulation of developmental growth; IMP:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0060685; P:regulation of prostatic bud formation; IGI:MGI.
DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0003073; P:regulation of systemic arterial blood pressure; IGI:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0019098; P:reproductive behavior; ISO:MGI.
DR GO; GO:0048608; P:reproductive structure development; IMP:MGI.
DR GO; GO:0061458; P:reproductive system development; IGI:MGI.
DR GO; GO:0072520; P:seminiferous tubule development; IMP:MGI.
DR GO; GO:0007338; P:single fertilization; IGI:MGI.
DR GO; GO:0014734; P:skeletal muscle hypertrophy; ISO:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:0060748; P:tertiary branching involved in mammary gland duct morphogenesis; IMP:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR001103; Andrgn_rcpt.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF02166; Androgen_recep; 1.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00521; ANDROGENR.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; Isopeptide bond; Lipid-binding;
KW Lipoprotein; Metal-binding; Nucleus; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Steroid-binding; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..899
FT /note="Androgen receptor"
FT /id="PRO_0000053707"
FT DOMAIN 648..879
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 538..611
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 539..559
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 575..599
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..566
FT /note="Interaction with ZNF318"
FT /evidence="ECO:0000269|PubMed:15882980"
FT REGION 1..537
FT /note="Modulating"
FT /evidence="ECO:0000250"
FT REGION 35..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..898
FT /note="Interaction with LPXN"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT REGION 551..641
FT /note="Interaction with HIPK3"
FT /evidence="ECO:0000250|UniProtKB:P15207"
FT REGION 571..898
FT /note="Interaction with CCAR1"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT REGION 604..898
FT /note="Interaction with KAT7"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT COMPBIAS 59..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 685
FT /ligand="17beta-hydroxy-5alpha-androstan-3-one"
FT /ligand_id="ChEBI:CHEBI:16330"
FT /evidence="ECO:0000269|PubMed:17911242,
FT ECO:0007744|PDB:2QPY"
FT BINDING 732
FT /ligand="17beta-hydroxy-5alpha-androstan-3-one"
FT /ligand_id="ChEBI:CHEBI:16330"
FT /evidence="ECO:0000269|PubMed:17911242,
FT ECO:0007744|PDB:2QPY"
FT BINDING 857
FT /ligand="17beta-hydroxy-5alpha-androstan-3-one"
FT /ligand_id="ChEBI:CHEBI:16330"
FT /evidence="ECO:0000269|PubMed:17911242,
FT ECO:0007744|PDB:2QPY"
FT SITE 700
FT /note="Interaction with coactivator LXXL and FXXFY motifs"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT SITE 877
FT /note="Interaction with coactivator FXXLF and FXXFY motifs"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT MOD_RES 61
FT /note="Phosphoserine; by CDK9"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT MOD_RES 218
FT /note="Phosphotyrosine; by CSK"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT MOD_RES 262
FT /note="Phosphotyrosine; by CSK and TNK2"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT MOD_RES 302
FT /note="Phosphotyrosine; by CSK"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT MOD_RES 341
FT /note="Phosphotyrosine; by CSK"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT MOD_RES 352
FT /note="Phosphotyrosine; by CSK"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT MOD_RES 357
FT /note="Phosphotyrosine; by CSK"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT MOD_RES 358
FT /note="Phosphotyrosine; by CSK and TNK2"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT MOD_RES 388
FT /note="Phosphotyrosine; by CSK"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT MOD_RES 514
FT /note="Phosphotyrosine; by CSK"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT MOD_RES 531
FT /note="Phosphotyrosine; by CSK"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 895
FT /note="Phosphotyrosine; by CSK"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT CROSSLNK 381
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 500
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 825
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT CROSSLNK 827
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P10275"
FT HELIX 652..659
FT /evidence="ECO:0007829|PDB:2QPY"
FT HELIX 677..701
FT /evidence="ECO:0007829|PDB:2QPY"
FT HELIX 705..707
FT /evidence="ECO:0007829|PDB:2QPY"
FT HELIX 710..736
FT /evidence="ECO:0007829|PDB:2QPY"
FT STRAND 740..745
FT /evidence="ECO:0007829|PDB:2QPY"
FT STRAND 748..750
FT /evidence="ECO:0007829|PDB:2QPY"
FT HELIX 752..757
FT /evidence="ECO:0007829|PDB:2QPY"
FT HELIX 761..776
FT /evidence="ECO:0007829|PDB:2QPY"
FT HELIX 781..792
FT /evidence="ECO:0007829|PDB:2QPY"
FT STRAND 794..799
FT /evidence="ECO:0007829|PDB:2QPY"
FT HELIX 804..823
FT /evidence="ECO:0007829|PDB:2QPY"
FT HELIX 831..844
FT /evidence="ECO:0007829|PDB:2QPY"
FT HELIX 846..862
FT /evidence="ECO:0007829|PDB:2QPY"
FT TURN 863..868
FT /evidence="ECO:0007829|PDB:2QPY"
FT HELIX 873..887
FT /evidence="ECO:0007829|PDB:2QPY"
FT STRAND 890..893
FT /evidence="ECO:0007829|PDB:2QPY"
SQ SEQUENCE 899 AA; 98194 MW; FD9EE07C07F7A568 CRC64;
MEVQLGLGRV YPRPPSKTYR GAFQNLFQSV REAIQNPGPR HPEAANIAPP GACLQQRQET
SPRRRRRQQH TEDGSPQAHI RGPTGYLALE EEQQPSQQQA ASEGHPESSC LPEPGAATAP
GKGLPQQPPA PPDQDDSAAP STLSLLGPTF PGLSSCSADI KDILNEAGTM QLLQQQQQQQ
QHQQQHQQHQ QQQEVISEGS SARAREATGA PSSSKDSYLG GNSTISDSAK ELCKAVSVSM
GLGVEALEHL SPGEQLRGDC MYASLLGGPP AVRPTPCAPL PECKGLPLDE GPGKSTEETA
EYSSFKGGYA KGLEGESLGC SGSSEAGSSG TLEIPSSLSL YKSGALDEAA AYQNRDYYNF
PLALSGPPHP PPPTHPHARI KLENPLDYGS AWAAAAAQCR YGDLGSLHGG SVAGPSTGSP
PATTSSSWHT LFTAEEGQLY GPGGGGGSSS PSDAGPVAPY GYTRPPQGLT SQESDYSASE
VWYPGGVVNR VPYPSPNCVK SEMGPWMENY SGPYGDMRLD STRDHVLPID YYFPPQKTCL
ICGDEASGCH YGALTCGSCK VFFKRAAEGK QKYLCASRND CTIDKFRRKN CPSCRLRKCY
EAGMTLGARK LKKLGNLKLQ EEGENSNAGS PTEDPSQKMT VSHIEGYECQ PIFLNVLEAI
EPGVVCAGHD NNQPDSFAAL LSSLNELGER QLVHVVKWAK ALPGFRNLHV DDQMAVIQYS
WMGLMVFAMG WRSFTNVNSR MLYFAPDLVF NEYRMHKSRM YSQCVRMRHL SQEFGWLQIT
PQEFLCMKAL LLFSIIPVDG LKNQKFFDEL RMNYIKELDR IIACKRKNPT SCSRRFYQLT
KLLDSVQPIA RELHQFTFDL LIKSHMVSVD FPEMMAEIIS VQVPKILSGK VKPIYFHTQ
