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Androgen receptor (Dihydrotestosterone receptor) (Nuclear receptor subfamily 3 group C member 4)

 ANDR_MOUSE              Reviewed;         899 AA.
P19091;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 1.
17-JUN-2020, entry version 214.
RecName: Full=Androgen receptor;
AltName: Full=Dihydrotestosterone receptor;
AltName: Full=Nuclear receptor subfamily 3 group C member 4;
Name=Ar; Synonyms=Nr3c4;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ;
PubMed=2403358; DOI=10.1016/0006-291x(90)91202-4;
He W.W., Fischer L.M., Sun S., Bilhartz D.L., Zhu X., Young C.Y.F.,
Kelley D.B., Tindall D.J.;
"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.";
Biochem. Biophys. Res. Commun. 171:697-704(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2178222; DOI=10.1210/mend-4-10-1600;
Gaspar M.L., Meo T., Tosi M.;
"Structure and size distribution of the androgen receptor mRNA in wild-type
and Tfm/Y mutant mice.";
Mol. Endocrinol. 4:1600-1610(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1883336; DOI=10.1042/bj2780269;
Faber P.W., King A., van Rooij H.C.J., Brinkmann A.O., de Both N.J.,
Trapman J.;
"The mouse androgen receptor. Functional analysis of the protein and
characterization of the gene.";
Biochem. J. 278:269-278(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1681426; DOI=10.1210/mend-5-4-573;
Charest N.J., Zhou Z., Lubahn D.B., Olsen K.L., Wilson E.M., French F.S.;
"A frameshift mutation destabilizes androgen receptor messenger RNA in the
Tfm mouse.";
Mol. Endocrinol. 5:573-581(1991).
[5]
INTERACTION WITH RAD54L2.
STRAIN=Swiss Webster; TISSUE=Embryo;
PubMed=12058073; DOI=10.1091/mbc.01-10-0484.;
Rouleau N., Domans'kyi A., Reeben M., Moilanen A.-M., Havas K., Kang Z.,
Owen-Hughes T., Palvimo J.J., Jaenne O.A.;
"Novel ATPase of SNF2-like protein family interacts with androgen receptor
and modulates androgen-dependent transcription.";
Mol. Biol. Cell 13:2106-2119(2002).
[6]
INTERACTION WITH RAD54L2.
PubMed=15199138; DOI=10.1128/mcb.24.13.5821-5834.2004;
Sitz J.H., Tigges M., Baumgaertel K., Khaspekov L.G., Lutz B.;
"Dyrk1A potentiates steroid hormone-induced transcription via the chromatin
remodeling factor Arip4.";
Mol. Cell. Biol. 24:5821-5834(2004).
[7]
INTERACTION WITH ZNF318.
PubMed=15882980; DOI=10.1016/j.bbrc.2005.04.024;
Ishizuka M., Kawate H., Takayanagi R., Ohshima H., Tao R.-H., Hagiwara H.;
"A zinc finger protein TZF is a novel corepressor of androgen receptor.";
Biochem. Biophys. Res. Commun. 331:1025-1031(2005).
[8]
INTERACTION WITH SLC30A9.
PubMed=15988012; DOI=10.1128/mcb.25.14.5965-5972.2005;
Chen Y.-H., Kim J.H., Stallcup M.R.;
"GAC63, a GRIP1-dependent nuclear receptor coactivator.";
Mol. Cell. Biol. 25:5965-5972(2005).
[9]
INTERACTION WITH ZNF318.
PubMed=16446156; DOI=10.1016/j.bbrc.2005.12.213;
Tao R.H., Kawate H., Ohnaka K., Ishizuka M., Hagiwara H., Takayanagi R.;
"Opposite effects of alternative TZF spliced variants on androgen
receptor.";
Biochem. Biophys. Res. Commun. 341:515-521(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-630, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
[11]
INTERACTION WITH CRY1.
PubMed=22170608; DOI=10.1038/nature10700;
Lamia K.A., Papp S.J., Yu R.T., Barish G.D., Uhlenhaut N.H., Jonker J.W.,
Downes M., Evans R.M.;
"Cryptochromes mediate rhythmic repression of the glucocorticoid
receptor.";
Nature 480:552-556(2011).
[12]
INTERACTION WITH ARID4A AND ARID4B.
PubMed=23487765; DOI=10.1073/pnas.1218318110;
Wu R.C., Jiang M., Beaudet A.L., Wu M.Y.;
"ARID4A and ARID4B regulate male fertility, a functional link to the AR and
RB pathways.";
Proc. Natl. Acad. Sci. U.S.A. 110:4616-4621(2013).
[13]
INTERACTION WITH CRY1 AND CRY2.
PubMed=28751364; DOI=10.1073/pnas.1704955114;
Kriebs A., Jordan S.D., Soto E., Henriksson E., Sandate C.R., Vaughan M.E.,
Chan A.B., Duglan D., Papp S.J., Huber A.L., Afetian M.E., Yu R.T.,
Zhao X., Downes M., Evans R.M., Lamia K.A.;
"Circadian repressors CRY1 and CRY2 broadly interact with nuclear receptors
and modulate transcriptional activity.";
Proc. Natl. Acad. Sci. U.S.A. 114:8776-8781(2017).
[14]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 649-899 IN COMPLEX WITH NCOA2 AND
DIHYDROTESTOSTERONE.
PubMed=17911242; DOI=10.1073/pnas.0708036104;
Estebanez-Perpina E., Arnold L.A., Nguyen P., Rodrigues E.D., Mar E.,
Bateman R., Pallai P., Shokat K.M., Baxter J.D., Guy R.K., Webb P.,
Fletterick R.J.;
"A surface on the androgen receptor that allosterically regulates
coactivator binding.";
Proc. Natl. Acad. Sci. U.S.A. 104:16074-16079(2007).
-!- FUNCTION: 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 like ZBTB7A that recruits NCOR1 and NCOR2 to the androgen
response elements/ARE on target genes, negatively regulating androgen
receptor signaling and androgen-induced cell proliferation.
Transcription activation is also down-regulated by NR0B2. Activated,
but not phosphorylated, by HIPK3 and ZIPK/DAPK3.
{ECO:0000250|UniProtKB:P10275, ECO:0000250|UniProtKB:P15207}.
-!- SUBUNIT: 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 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
(PubMed:22170608, PubMed:28751364). Interacts with CCAR1 and GATA2 (By
similarity). Interacts with BUD31 (By similarity). Interacts with
ARID4A (PubMed:23487765). Interacts with ARID4B (PubMed:23487765).
Interacts (via NR LBD domain) with ZBTB7A; the interaction is direct
and androgen-dependent (By similarity). Interacts with NCOR1 (By
similarity). Interacts with NCOR2 (By similarity). Interacts with CRY2
in a ligand-dependent manner (PubMed:28751364).
{ECO:0000250|UniProtKB:P10275, ECO:0000250|UniProtKB:P15207,
ECO:0000269|PubMed:12058073, ECO:0000269|PubMed:15199138,
ECO:0000269|PubMed:15882980, ECO:0000269|PubMed:15988012,
ECO:0000269|PubMed:16446156, ECO:0000269|PubMed:17911242,
ECO:0000269|PubMed:22170608, ECO:0000269|PubMed:23487765,
ECO:0000269|PubMed:28751364}.
-!- INTERACTION:
P19091; O89110: Casp8; NbExp=2; IntAct=EBI-1776062, EBI-851690;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10275}. Cytoplasm
{ECO:0000250|UniProtKB:P10275}. Note=Detected at the promoter of target
genes. 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 RACK1.
{ECO:0000250|UniProtKB:P10275}.
-!- DOMAIN: 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). {ECO:0000250}.
-!- PTM: 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). {ECO:0000250|UniProtKB:P10275}.
-!- PTM: 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).
{ECO:0000250|UniProtKB:P10275}.
-!- PTM: 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).
{ECO:0000250|UniProtKB:P10275}.
-!- 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.
-!- MISCELLANEOUS: Transcriptional activity is enhanced by binding to
RANBP9.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
subfamily. {ECO:0000305}.
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EMBL; S56585; AAB19916.1; -; mRNA.
EMBL; X53779; CAA37795.1; -; mRNA.
EMBL; M37890; AAA37234.1; -; mRNA.
EMBL; X59592; CAA42160.1; -; mRNA.
CCDS; CCDS30294.1; -.
PIR; A35895; A35895.
RefSeq; NP_038504.1; NM_013476.4.
PDB; 2QPY; X-ray; 2.50 A; A=649-899.
PDBsum; 2QPY; -.
SMR; P19091; -.
BioGRID; 198179; 23.
DIP; DIP-41803N; -.
IntAct; P19091; 9.
MINT; P19091; -.
STRING; 10090.ENSMUSP00000052648; -.
BindingDB; P19091; -.
ChEMBL; CHEMBL3056; -.
DrugCentral; P19091; -.
iPTMnet; P19091; -.
PhosphoSitePlus; P19091; -.
EPD; P19091; -.
PaxDb; P19091; -.
PRIDE; P19091; -.
Antibodypedia; 3489; 2370 antibodies.
DNASU; 11835; -.
Ensembl; ENSMUST00000052837; ENSMUSP00000052648; ENSMUSG00000046532.
GeneID; 11835; -.
KEGG; mmu:11835; -.
UCSC; uc009tuv.1; mouse.
CTD; 367; -.
MGI; MGI:88064; Ar.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
GeneTree; ENSGT00940000155516; -.
HOGENOM; CLU_016847_0_0_1; -.
InParanoid; P19091; -.
KO; K08557; -.
OMA; GPWMENY; -.
OrthoDB; 615449at2759; -.
PhylomeDB; P19091; -.
TreeFam; TF350286; -.
Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
Reactome; R-MMU-4090294; SUMOylation of intracellular receptors.
Reactome; R-MMU-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
Reactome; R-MMU-8940973; RUNX2 regulates osteoblast differentiation.
BioGRID-ORCS; 11835; 1 hit in 15 CRISPR screens.
ChiTaRS; Ar; mouse.
EvolutionaryTrace; P19091; -.
PRO; PR:P19091; -.
Proteomes; UP000000589; Chromosome X.
RNAct; P19091; protein.
Bgee; ENSMUSG00000046532; Expressed in lacrimal gland and 210 other tissues.
Genevisible; P19091; MM.
GO; GO:0030424; C:axon; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:CAFA.
GO; GO:0030425; C:dendrite; ISO:MGI.
GO; GO:0042025; C:host cell nucleus; IEA:InterPro.
GO; GO:0000790; C:nuclear chromatin; ISS:UniProtKB.
GO; GO:0016607; C:nuclear speck; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:CAFA.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0005497; F:androgen binding; ISS:UniProtKB.
GO; GO:0050681; F:androgen receptor binding; ISO:MGI.
GO; GO:0051117; F:ATPase binding; ISO:MGI.
GO; GO:0008013; F:beta-catenin binding; ISS:UniProtKB.
GO; GO:0003682; F:chromatin binding; ISO:MGI.
GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0004879; F:nuclear receptor activity; IDA:CAFA.
GO; GO:0070974; F:POU domain binding; IDA:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0032553; F:ribonucleotide binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0001091; F:RNA polymerase II general transcription initiation factor binding; ISO:MGI.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; ISO:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0060520; P:activation of prostate induction by androgen receptor signaling pathway; IMP:MGI.
GO; GO:0030521; P:androgen receptor signaling pathway; IDA:CAFA.
GO; GO:0048645; P:animal organ formation; IMP:MGI.
GO; GO:0009987; P:cellular process; IDA:MGI.
GO; GO:0071383; P:cellular response to steroid hormone stimulus; ISO:MGI.
GO; GO:0071394; P:cellular response to testosterone stimulus; IDA:CAFA.
GO; GO:0007620; P:copulation; ISO:MGI.
GO; GO:0060742; P:epithelial cell differentiation involved in prostate gland development; IMP:MGI.
GO; GO:0003382; P:epithelial cell morphogenesis; IGI:MGI.
GO; GO:0009566; P:fertilization; IMP:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0030522; P:intracellular receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0060599; P:lateral sprouting involved in mammary gland duct morphogenesis; IMP:MGI.
GO; GO:0033327; P:Leydig cell differentiation; IMP:MGI.
GO; GO:0008049; P:male courtship behavior; ISO:MGI.
GO; GO:0048808; P:male genitalia morphogenesis; IMP:MGI.
GO; GO:0008584; P:male gonad development; IMP:MGI.
GO; GO:0046661; P:male sex differentiation; ISO:MGI.
GO; GO:0019102; P:male somatic sex determination; IMP:MGI.
GO; GO:0060749; P:mammary gland alveolus development; IMP:MGI.
GO; GO:0060571; P:morphogenesis of an epithelial fold; IMP:MGI.
GO; GO:0035264; P:multicellular organism growth; IGI:MGI.
GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISS:BHF-UCL.
GO; GO:0045720; P:negative regulation of integrin biosynthetic process; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0045597; P:positive regulation of cell differentiation; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
GO; GO:0060769; P:positive regulation of epithelial cell proliferation involved in prostate gland development; IDA:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; IMP:MGI.
GO; GO:0045726; P:positive regulation of integrin biosynthetic process; ISO:MGI.
GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IMP:MGI.
GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:MGI.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
GO; GO:0060406; P:positive regulation of penile erection; ISO:MGI.
GO; GO:0042327; P:positive regulation of phosphorylation; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0060740; P:prostate gland epithelium morphogenesis; IMP:MGI.
GO; GO:0060736; P:prostate gland growth; IMP:MGI.
GO; GO:0048638; P:regulation of developmental growth; IMP:MGI.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0060685; P:regulation of prostatic bud formation; IGI:MGI.
GO; GO:1903076; P:regulation of protein localization to plasma membrane; ISS:UniProtKB.
GO; GO:0003073; P:regulation of systemic arterial blood pressure; IGI:MGI.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0019098; P:reproductive behavior; ISO:MGI.
GO; GO:0048608; P:reproductive structure development; IMP:MGI.
GO; GO:0061458; P:reproductive system development; IGI:MGI.
GO; GO:0072520; P:seminiferous tubule development; IMP:MGI.
GO; GO:0007338; P:single fertilization; IGI:MGI.
GO; GO:0014734; P:skeletal muscle hypertrophy; ISO:MGI.
GO; GO:0007283; P:spermatogenesis; IMP:MGI.
GO; GO:0060748; P:tertiary branching involved in mammary gland duct morphogenesis; IMP:MGI.
GO; GO:0006351; P:transcription, DNA-templated; ISS:UniProtKB.
Gene3D; 1.10.565.10; -; 1.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR001103; Andrgn_rcpt.
InterPro; IPR035500; NHR-like_dom_sf.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF02166; Androgen_recep; 1.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR00521; ANDROGENR.
PRINTS; PR00047; STROIDFINGER.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 1.
PROSITE; PS51843; NR_LBD; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
3D-structure; Cytoplasm; DNA-binding; Isopeptide bond; Lipid-binding;
Lipoprotein; Metal-binding; Nucleus; Palmitate; Phosphoprotein; Receptor;
Reference proteome; Steroid-binding; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1..899
/note="Androgen receptor"
/id="PRO_0000053707"
DOMAIN 648..879
/note="NR LBD"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
DNA_BIND 538..611
/note="Nuclear receptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
ZN_FING 539..559
/note="NR C4-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
ZN_FING 575..599
/note="NR C4-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
REGION 1..566
/note="Interaction with ZNF318"
/evidence="ECO:0000269|PubMed:15882980"
REGION 1..537
/note="Modulating"
/evidence="ECO:0000250"
REGION 531..898
/note="Interaction with LPXN"
/evidence="ECO:0000250|UniProtKB:P10275"
REGION 551..641
/note="Interaction with HIPK3"
/evidence="ECO:0000250|UniProtKB:P15207"
REGION 571..898
/note="Interaction with CCAR1"
/evidence="ECO:0000250|UniProtKB:P10275"
REGION 604..898
/note="Interaction with KAT7"
/evidence="ECO:0000250|UniProtKB:P10275"
COMPBIAS 63..67
/note="Poly-Arg"
COMPBIAS 174..193
/note="Poly-Gln"
COMPBIAS 367..373
/note="Poly-Pro"
COMPBIAS 391..397
/note="Poly-Ala"
COMPBIAS 441..447
/note="Poly-Gly"
BINDING 685
/note="Androgen"
/evidence="ECO:0000244|PDB:2QPY,
ECO:0000269|PubMed:17911242"
BINDING 732
/note="Androgen"
/evidence="ECO:0000244|PDB:2QPY,
ECO:0000269|PubMed:17911242"
BINDING 857
/note="Androgen"
/evidence="ECO:0000244|PDB:2QPY,
ECO:0000269|PubMed:17911242"
SITE 700
/note="Interaction with coactivator LXXL and FXXFY motifs"
/evidence="ECO:0000250|UniProtKB:P10275"
SITE 877
/note="Interaction with coactivator FXXLF and FXXFY motifs"
/evidence="ECO:0000250|UniProtKB:P10275"
MOD_RES 61
/note="Phosphoserine; by CDK9"
/evidence="ECO:0000250|UniProtKB:P10275"
MOD_RES 75
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10275"
MOD_RES 218
/note="Phosphotyrosine; by CSK"
/evidence="ECO:0000250|UniProtKB:P10275"
MOD_RES 251
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10275"
MOD_RES 262
/note="Phosphotyrosine; by CSK and TNK2"
/evidence="ECO:0000250|UniProtKB:P10275"
MOD_RES 302
/note="Phosphotyrosine; by CSK"
/evidence="ECO:0000250|UniProtKB:P10275"
MOD_RES 341
/note="Phosphotyrosine; by CSK"
/evidence="ECO:0000250|UniProtKB:P10275"
MOD_RES 352
/note="Phosphotyrosine; by CSK"
/evidence="ECO:0000250|UniProtKB:P10275"
MOD_RES 357
/note="Phosphotyrosine; by CSK"
/evidence="ECO:0000250|UniProtKB:P10275"
MOD_RES 358
/note="Phosphotyrosine; by CSK and TNK2"
/evidence="ECO:0000250|UniProtKB:P10275"
MOD_RES 388
/note="Phosphotyrosine; by CSK"
/evidence="ECO:0000250|UniProtKB:P10275"
MOD_RES 514
/note="Phosphotyrosine; by CSK"
/evidence="ECO:0000250|UniProtKB:P10275"
MOD_RES 531
/note="Phosphotyrosine; by CSK"
/evidence="ECO:0000250|UniProtKB:P10275"
MOD_RES 630
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:21183079"
MOD_RES 895
/note="Phosphotyrosine; by CSK"
/evidence="ECO:0000250|UniProtKB:P10275"
CROSSLNK 381
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO)"
/evidence="ECO:0000250"
CROSSLNK 500
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO)"
/evidence="ECO:0000250"
CROSSLNK 825
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:P10275"
CROSSLNK 827
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:P10275"
HELIX 652..659
/evidence="ECO:0000244|PDB:2QPY"
HELIX 677..701
/evidence="ECO:0000244|PDB:2QPY"
HELIX 705..707
/evidence="ECO:0000244|PDB:2QPY"
HELIX 710..736
/evidence="ECO:0000244|PDB:2QPY"
STRAND 740..745
/evidence="ECO:0000244|PDB:2QPY"
STRAND 748..750
/evidence="ECO:0000244|PDB:2QPY"
HELIX 752..757
/evidence="ECO:0000244|PDB:2QPY"
HELIX 761..776
/evidence="ECO:0000244|PDB:2QPY"
HELIX 781..792
/evidence="ECO:0000244|PDB:2QPY"
STRAND 794..799
/evidence="ECO:0000244|PDB:2QPY"
HELIX 804..823
/evidence="ECO:0000244|PDB:2QPY"
HELIX 831..844
/evidence="ECO:0000244|PDB:2QPY"
HELIX 846..862
/evidence="ECO:0000244|PDB:2QPY"
TURN 863..868
/evidence="ECO:0000244|PDB:2QPY"
HELIX 873..887
/evidence="ECO:0000244|PDB:2QPY"
STRAND 890..893
/evidence="ECO:0000244|PDB:2QPY"
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


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WP783: Androgen Receptor Signaling Pathway
WP1133: Androgen receptor signaling pathway
WP1348: Androgen Receptor Signaling Pathway
WP138: Androgen receptor signaling pathway
WP68: Androgen Receptor Signaling Pathway
WP1014: Androgen receptor signaling pathway
WP252: Androgen Receptor Signaling Pathway
WP897: Androgen receptor signaling pathway
WP1965: VEGF-receptor Signal Transduction
WP1004: Kit Receptor Signaling Pathway
WP1384: Toll-like receptor signaling pathway
WP878: EPO Receptor Signaling
WP1183: Toll-like receptor signaling pathway
WP352: T Cell Receptor Signaling Pathway
WP894: T Cell Receptor Signaling Pathway
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP2140: MaxYvesSuperCombo
WP734: Serotonin Receptor 4/6/7 and NR3C Signaling
WP1025: B Cell Receptor Signaling Pathway
WP1449: Regulation of toll-like receptor signaling pathway
WP768: EPO Receptor Signaling
WP1067: Toll-like receptor signaling pathway
WP926: TGF-beta Receptor Signaling Pathway
WP1284: EPO Receptor Signaling
WP2272: Pathogenic Escherichia coli infection

Related Genes :
[AR DHTR NR3C4] Androgen receptor (Dihydrotestosterone receptor) (Nuclear receptor subfamily 3 group C member 4)
[Nr2c1 Tr2 Tr2-11] Nuclear receptor subfamily 2 group C member 1 (Orphan nuclear receptor TR2) (Testicular receptor 2) (mTR2)
[Nr2c2 Mtr2r1 Tak1 Tr4] Nuclear receptor subfamily 2 group C member 2 (Orphan nuclear receptor TAK1) (Orphan nuclear receptor TR4) (Testicular receptor 4)
[Rorc Nr1f3 Rorg Thor] Nuclear receptor ROR-gamma (Nuclear receptor RZR-gamma) (Nuclear receptor subfamily 1 group F member 3) (RAR-related orphan receptor C) (Retinoid-related orphan receptor-gamma) (Thymus orphan receptor) (TOR)
[NR4A1 GFRP1 HMR NAK1] Nuclear receptor subfamily 4 group A member 1 (Early response protein NAK1) (Nuclear hormone receptor NUR/77) (Nur77) (Orphan nuclear receptor HMR) (Orphan nuclear receptor TR3) (ST-59) (Testicular receptor 3)
[NR2C2 TAK1 TR4] Nuclear receptor subfamily 2 group C member 2 (Orphan nuclear receptor TAK1) (Orphan nuclear receptor TR4) (Testicular receptor 4)
[Esr1 Esr Estr Estra Nr3a1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[Nr1h2 Lxrb] Oxysterols receptor LXR-beta (Liver X receptor beta) (Nuclear receptor subfamily 1 group H member 2) (Orphan nuclear receptor OR-1) (Ubiquitously-expressed nuclear receptor) (UR)
[Esr2 Estrb Nr3a2] Estrogen receptor beta (ER-beta) (Nuclear receptor subfamily 3 group A member 2)
[RORC NR1F3 RORG RZRG] Nuclear receptor ROR-gamma (Nuclear receptor RZR-gamma) (Nuclear receptor subfamily 1 group F member 3) (RAR-related orphan receptor C) (Retinoid-related orphan receptor-gamma)
[Thra C-erba-alpha Nr1a1] Thyroid hormone receptor alpha (Nuclear receptor subfamily 1 group A member 1) (c-erbA-1) (c-erbA-alpha)
[nhr-6 cnr-8 nr4a5 C48D5.1] Nuclear hormone receptor family member nhr-6 (Nuclear receptor subfamily 4 group A member 5) (Steroid hormone receptor family member cnr8)
[Esrrb Err-2 Err2 Nr3b2] Steroid hormone receptor ERR2 (Estrogen receptor-like 2) (Estrogen-related receptor beta) (ERR-beta) (Nuclear receptor subfamily 3 group B member 2)
[Nr3c1 Grl] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[Nr4a1 Gfrp Hmr N10 Nur77] Nuclear receptor subfamily 4 group A member 1 (Nuclear hormone receptor NUR/77) (Nuclear protein N10) (Orphan nuclear receptor HMR)
[Nr1d2] Nuclear receptor subfamily 1 group D member 2 (Orphan nuclear receptor RVR) (Rev-erb-beta)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[Nr3c2 Mlr] Mineralocorticoid receptor (MR) (Nuclear receptor subfamily 3 group C member 2)
[Esrrg Err3 Kiaa0832 Nr3b3] Estrogen-related receptor gamma (Estrogen receptor-related protein 3) (Nuclear receptor subfamily 3 group B member 3)
[Pgr Nr3c3 Pr] Progesterone receptor (PR) (Nuclear receptor subfamily 3 group C member 3)
[Esr1 Esr Estr Nr3a1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[Nr2f6 Ear-2 Ear2 Erbal2] Nuclear receptor subfamily 2 group F member 6 (COUP transcription factor 3) (COUP-TF3) (V-erbA-related protein 2) (EAR-2)
[Nr1h4 Bar Fxr Rip14] Bile acid receptor (Farnesoid X-activated receptor) (Farnesol receptor HRR-1) (Nuclear receptor subfamily 1 group H member 4) (Retinoid X receptor-interacting protein 14) (RXR-interacting protein 14)
[Nr2e3 Pnr Rnr] Photoreceptor-specific nuclear receptor (Nuclear receptor subfamily 2 group E member 3) (Retina-specific nuclear receptor)
[Rora Nr1f1 Rzra] Nuclear receptor ROR-alpha (Nuclear receptor RZR-alpha) (Nuclear receptor subfamily 1 group F member 1) (RAR-related orphan receptor A) (Retinoid-related orphan receptor-alpha)
[Nr4a1 Hmr Ngfib] Nuclear receptor subfamily 4 group A member 1 (NUR77) (Nerve growth factor-induced protein I-B) (NGFI-B) (Orphan nuclear receptor HMR)
[Rxrg Nr2b3] Retinoic acid receptor RXR-gamma (Nuclear receptor subfamily 2 group B member 3) (Retinoid X receptor gamma)
[NR1H4 BAR FXR HRR1 RIP14] Bile acid receptor (Farnesoid X-activated receptor) (Farnesol receptor HRR-1) (Nuclear receptor subfamily 1 group H member 4) (Retinoid X receptor-interacting protein 14) (RXR-interacting protein 14)

Bibliography :