Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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

 ANDR_HUMAN              Reviewed;         920 AA.
P10275; A0A0B4J1T2; A2RUN2; B1AKD7; C0JKD3; C0JKD4; E7EVX6; Q9UD95;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
16-MAR-2016, sequence version 3.
22-NOV-2017, entry version 256.
RecName: Full=Androgen receptor;
AltName: Full=Dihydrotestosterone receptor;
AltName: Full=Nuclear receptor subfamily 3 group C member 4;
Name=AR; Synonyms=DHTR, NR3C4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3216866; DOI=10.1210/mend-2-12-1265;
Lubahn D.B., Joseph D.R., Sar M., Tan J., Higgs H.N., Larson R.E.,
French F.S., Wilson E.M.;
"The human androgen receptor: complementary deoxyribonucleic acid
cloning, sequence analysis and gene expression in prostate.";
Mol. Endocrinol. 2:1265-1275(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Prostate;
PubMed=3174628; DOI=10.1073/pnas.85.19.7211;
Chang C., Kokontis J., Liao S.;
"Structural analysis of complementary DNA and amino acid sequences of
human and rat androgen receptors.";
Proc. Natl. Acad. Sci. U.S.A. 85:7211-7215(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Prostate;
PubMed=2911578; DOI=10.1073/pnas.86.1.327;
Tilley W.D., Marcelli M., Wilson J.D., McPhaul M.J.;
"Characterization and expression of a cDNA encoding the human androgen
receptor.";
Proc. Natl. Acad. Sci. U.S.A. 86:327-331(1989).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT AIS MET-867.
PubMed=2594783; DOI=10.1073/pnas.86.23.9534;
Lubahn D.B., Brown T.R., Simental J.A., Higgs H.N., Migeon C.J.,
Wilson E.M., French F.S.;
"Sequence of the intron/exon junctions of the coding region of the
human androgen receptor gene and identification of a point mutation in
a family with complete androgen insensitivity.";
Proc. Natl. Acad. Sci. U.S.A. 86:9534-9538(1989).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2342476; DOI=10.1210/mend-4-3-417;
Govindan M.V.;
"Specific region in hormone binding domain is essential for hormone
binding and trans-activation by human androgen receptor.";
Mol. Endocrinol. 4:417-427(1990).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND NUCLEOTIDE SEQUENCE [MRNA]
(ISOFORM 1).
TISSUE=Prostate;
PubMed=2293020; DOI=10.1210/mend-4-8-1105;
Marcelli M., Tilley W.D., Wilson C.M., Griffin J.E., Wilson J.D.,
McPhaul M.J.;
"Definition of the human androgen receptor gene structure permits the
identification of mutations that cause androgen resistance: premature
termination of the receptor protein at amino acid residue 588 causes
complete androgen resistance.";
Mol. Endocrinol. 4:1105-1116(1990).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2),
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=15634333; DOI=10.1111/j.1432-1033.2004.04395.x;
Ahrens-Fath I., Politz O., Geserick C., Haendler B.;
"Androgen receptor function is modulated by the tissue-specific AR45
variant.";
FEBS J. 272:74-84(2005).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), VARIANT GLN-57,
FUNCTION (ISOFORMS 3 AND 4), AND SUBCELLULAR LOCATION (ISOFORM 3).
PubMed=19244107; DOI=10.1158/0008-5472.CAN-08-3795;
Guo Z., Yang X., Sun F., Jiang R., Linn D.E., Chen H., Chen H.,
Kong X., Melamed J., Tepper C.G., Kung H.J., Brodie A.M., Edwards J.,
Qiu Y.;
"A novel androgen receptor splice variant is up-regulated during
prostate cancer progression and promotes androgen depletion-resistant
growth.";
Cancer Res. 69:2305-2313(2009).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-539.
PubMed=2917688; DOI=10.1016/0303-7207(89)90137-8;
Faber P.W., Kuiper G.G.J.M., van Rooij H.C.J.,
van der Korput J.A.G.M., Brinkmann A.O., Trapman J.;
"The N-terminal domain of the human androgen receptor is encoded by
one, large exon.";
Mol. Cell. Endocrinol. 61:257-262(1989).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 191-920 (ISOFORM 1).
PubMed=3353726; DOI=10.1126/science.3353726;
Chang C., Kokontis J., Liao S.;
"Molecular cloning of human and rat complementary DNA encoding
androgen receptors.";
Science 240:324-326(1988).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 448-476.
TISSUE=Blood;
Lu J., Danielsen M.;
Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 470-920 (ISOFORM 1).
PubMed=3377788; DOI=10.1016/S0006-291X(88)81214-2;
Trapman J., Klaassen P., Kuiper G.G.J.M., van der Korput J.A.G.M.,
Faber P.W., van Rooij H.C.J., Geurts van Kessel A., Voorhorst M.M.,
Mulder E., Brinkmann A.O.;
"Cloning, structure and expression of a cDNA encoding the human
androgen receptor.";
Biochem. Biophys. Res. Commun. 153:241-248(1988).
[16]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 537-541; 587-591; 626-630;
722-726; 770-774; 814-817 AND 866-870.
PubMed=2546571; DOI=10.1677/jme.0.002R001;
Kuiper G.G., Faber P.W., van Rooij H.C., van der Korput J.A.,
Ris-Stalpers C., Klaassen P., Trapman J., Brinkmann A.O.;
"Structural organization of the human androgen receptor gene.";
J. Mol. Endocrinol. 2:R1-R4(1989).
[17]
NUCLEOTIDE SEQUENCE [MRNA] OF 558-625 (ISOFORMS 1/2), AND VARIANT AIS
HIS-616.
TISSUE=Fibroblast;
PubMed=8413310; DOI=10.1210/mend.7.7.8413310;
Mowszowicz I., Lee H.-J., Chen H.-T., Mestayer C., Portois M.-C.,
Cabrol S., Mauvais-Jarvis P., Chang C.;
"A point mutation in the second zinc finger of the DNA-binding domain
of the androgen receptor gene causes complete androgen insensitivity
in two siblings with receptor-positive androgen resistance.";
Mol. Endocrinol. 7:861-869(1993).
[18]
NUCLEOTIDE SEQUENCE [MRNA] OF 560-625 (ISOFORMS 1/2).
PubMed=3353727; DOI=10.1126/science.3353727;
Lubahn D.B., Joseph D.R., Sullivan P.M., Willard H.F., French F.S.,
Wilson E.M.;
"Cloning of human androgen receptor complementary DNA and localization
to the X chromosome.";
Science 240:327-330(1988).
[19]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 630-724, AND VARIANTS AIS ASN-696
AND HIS-696.
PubMed=1775137; DOI=10.1210/mend-5-10-1562;
Ris-Stalpers C., Trifiro M.A., Kuiper G.G.J.M., Jenster G., Romalo G.,
Sai T., van Rooij H.C.J., Kaufman M., Rosenfield R.L., Liao S.,
Schweikert H.-U., Trapman J., Pinsky L., Brinkmann A.O.;
"Substitution of aspartic acid-686 by histidine or asparagine in the
human androgen receptor leads to a functionally inactive protein with
altered hormone-binding characteristics.";
Mol. Endocrinol. 5:1562-1569(1991).
[20]
POLYMORPHISM OF POLY-GLN REGION.
PubMed=1561105; DOI=10.1093/nar/20.6.1427-a;
Sleddens H.F.B.M., Oostra B.A., Brinkmann A.O., Trapman J.;
"Trinucleotide repeat polymorphism in the androgen receptor gene
(AR).";
Nucleic Acids Res. 20:1427-1427(1992).
[21]
POLYMORPHISM OF POLY-GLN REGION.
PubMed=9096391; DOI=10.1073/pnas.94.7.3320;
Giovannucci E., Stampfer M.J., Krithivas K., Brown M., Dahl D.,
Brufsky A., Talcott J., Hennekens C.H., Kantoff P.W.;
"The CAG repeat within the androgen receptor gene and its relationship
to prostate cancer.";
Proc. Natl. Acad. Sci. U.S.A. 94:3320-3323(1997).
[22]
ERRATUM.
Giovannucci E., Stampfer M.J., Krithivas K., Brown M., Dahl D.,
Brufsky A., Talcott J., Hennekens C.H., Kantoff P.W.;
Proc. Natl. Acad. Sci. U.S.A. 94:8272-8272(1997).
[23]
INTERACTION WITH PQBP1.
TISSUE=Brain;
PubMed=10332029; DOI=10.1093/hmg/8.6.977;
Waragai M., Lammers C.-H., Takeuchi S., Imafuku I., Udagawa Y.,
Kanazawa I., Kawabata M., Mouradian M.M., Okazawa H.;
"PQBP-1, a novel polyglutamine tract binding protein, inhibits
transcription activation by Brn-2 and affects cell survival.";
Hum. Mol. Genet. 8:977-987(1999).
[24]
INTERACTION WITH TGFB1I1.
PubMed=10075738; DOI=10.1074/jbc.274.12.8316;
Fujimoto N., Yeh S., Kang H.-Y., Inui S., Chang H.-C., Mizokami A.,
Chang C.;
"Cloning and characterization of androgen receptor coactivator, ARA55,
in human prostate.";
J. Biol. Chem. 274:8316-8321(1999).
[25]
INTERACTION WITH UBE2I.
PubMed=10383460; DOI=10.1074/jbc.274.27.19441;
Poukka H., Aarnisalo P., Karvonen U., Palvimo J.J., Jaenne O.A.;
"Ubc9 interacts with the androgen receptor and activates receptor-
dependent transcription.";
J. Biol. Chem. 274:19441-19446(1999).
[26]
INTERACTION WITH RAN.
PubMed=10400640; DOI=10.1074/jbc.274.29.20229;
Hsiao P.-W., Lin D.-L., Nakao R., Chang C.;
"The linkage of Kennedy's neuron disease to ARA24, the first
identified androgen receptor polyglutamine region-associated
coactivator.";
J. Biol. Chem. 274:20229-20234(1999).
[27]
INTERACTION WITH SPDEF.
PubMed=10625666; DOI=10.1074/jbc.275.2.1216;
Oettgen P., Finger E., Sun Z., Akbarali Y., Thamrongsak U., Boltax J.,
Grall F., Dube A., Weiss A., Brown L., Quinn G., Kas K., Endress G.,
Kunsch C., Libermann T.A.;
"PDEF, a novel prostate epithelium-specific ets transcription factor,
interacts with the androgen receptor and activates prostate-specific
antigen gene expression.";
J. Biol. Chem. 275:1216-1225(2000).
[28]
INTERACTION WITH KAT7.
PubMed=10930412; DOI=10.1074/jbc.M004838200;
Sharma M., Zarnegar M., Li X., Lim B., Sun Z.;
"Androgen receptor interacts with a novel MYST protein, HBO1.";
J. Biol. Chem. 275:35200-35208(2000).
[29]
SUMOYLATION AT LYS-388 AND LYS-521.
PubMed=11121022; DOI=10.1073/pnas.97.26.14145;
Poukka H., Karvonen U., Jaenne O.A., Palvimo J.J.;
"Covalent modification of the androgen receptor by small ubiquitin-
like modifier 1 (SUMO-1).";
Proc. Natl. Acad. Sci. U.S.A. 97:14145-14150(2000).
[30]
INTERACTION WITH RANBP9.
PubMed=12361945; DOI=10.1074/jbc.M209741200;
Rao M.A., Cheng H., Quayle A.N., Nishitani H., Nelson C.C.,
Rennie P.S.;
"RanBPM, a nuclear protein that interacts with and regulates
transcriptional activity of androgen receptor and glucocorticoid
receptor.";
J. Biol. Chem. 277:48020-48027(2002).
[31]
INTERACTION WITH PRPF6.
PubMed=12039962; DOI=10.1074/jbc.M203811200;
Zhao Y., Goto K., Saitoh M., Yanase T., Nomura M., Okabe T.,
Takayanagi R., Nawata H.;
"Activation function-1 domain of androgen receptor contributes to the
interaction between subnuclear splicing factor compartment and nuclear
receptor compartment. Identification of the p102 U5 small nuclear
ribonucleoprotein particle-binding protein as a coactivator for the
receptor.";
J. Biol. Chem. 277:30031-30039(2002).
[32]
INTERACTION WITH PELP1.
PubMed=12415108; DOI=10.1073/pnas.192569699;
Wong C.-W., McNally C., Nickbarg E., Komm B.S., Cheskis B.J.;
"Estrogen receptor-interacting protein that modulates its nongenomic
activity-crosstalk with Src/Erk phosphorylation cascade.";
Proc. Natl. Acad. Sci. U.S.A. 99:14783-14788(2002).
[33]
INTERACTION WITH ZMIZ1.
PubMed=14609956; DOI=10.1093/emboj/cdg585;
Sharma M., Li X., Wang Y., Zarnegar M., Huang C.-Y., Palvimo J.J.,
Lim B., Sun Z.;
"hZimp10 is an androgen receptor co-activator and forms a complex with
SUMO-1 at replication foci.";
EMBO J. 22:6101-6114(2003).
[34]
INTERACTION WITH RACK1, AND SUBCELLULAR LOCATION.
PubMed=12958311; DOI=10.1074/jbc.M306219200;
Rigas A.C., Ozanne D.M., Neal D.E., Robson C.N.;
"The scaffolding protein RACK1 interacts with androgen receptor and
promotes cross-talk through a protein kinase C signaling pathway.";
J. Biol. Chem. 278:46087-46093(2003).
[35]
FUNCTION, AND INTERACTION WITH RBAK.
PubMed=14664718; DOI=10.1677/jme.0.0310583;
Hofman K., Swinnen J.V., Claessens F., Verhoeven G., Heyns W.;
"The retinoblastoma protein-associated transcription repressor RBaK
interacts with the androgen receptor and enhances its transcriptional
activity.";
J. Mol. Endocrinol. 31:583-596(2003).
[36]
INTERACTION WITH EFCAB6.
PubMed=12612053;
Niki T., Takahashi-Niki K., Taira T., Iguchi-Ariga S.M.M., Ariga H.;
"DJBP: a novel DJ-1-binding protein, negatively regulates the androgen
receptor by recruiting histone deacetylase complex, and DJ-1
antagonizes this inhibition by abrogation of this complex.";
Mol. Cancer Res. 1:247-261(2003).
[37]
PHOSPHORYLATION BY PAK6.
PubMed=14573606; DOI=10.1074/jbc.M311145200;
Schrantz N., da Silva Correia J., Fowler B., Ge Q., Sun Z.,
Bokoch G.M.;
"Mechanism of p21-activated kinase 6-mediated inhibition of androgen
receptor signaling.";
J. Biol. Chem. 279:1922-1931(2004).
[38]
INTERACTION WITH HIP1.
PubMed=16027218; DOI=10.1083/jcb.200503106;
Mills I.G., Gaughan L., Robson C., Ross T., McCracken S., Kelly J.,
Neal D.E.;
"Huntingtin interacting protein 1 modulates the transcriptional
activity of nuclear hormone receptors.";
J. Cell Biol. 170:191-200(2005).
[39]
INTERACTION WITH ZMIZ2.
PubMed=16051670; DOI=10.1210/me.2005-0097;
Huang C.-Y., Beliakoff J., Li X., Lee J., Li X., Sharma M., Lim B.,
Sun Z.;
"hZimp7, a novel PIAS-like protein, enhances androgen receptor-
mediated transcription and interacts with SWI/SNF-like BAF
complexes.";
Mol. Endocrinol. 19:2915-2929(2005).
[40]
PHOSPHORYLATION AT TYR-225; TYR-269; TYR-309; TYR-348; TYR-359;
TYR-364; TYR-365; TYR-395; TYR-535; TYR-552 AND TYR-916, MUTAGENESIS
OF TYR-225; TYR-269; TYR-309; TYR-348; TYR-359; TYR-364; TYR-365;
TYR-395; TYR-535; TYR-552 AND TYR-916, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=17045208; DOI=10.1016/j.ccr.2006.08.021;
Guo Z., Dai B., Jiang T., Xu K., Xie Y., Kim O., Nesheiwat I.,
Kong X., Melamed J., Handratta V.D., Njar V.C., Brodie A.M., Yu L.-R.,
Veenstra T.D., Chen H., Qiu Y.;
"Regulation of androgen receptor activity by tyrosine
phosphorylation.";
Cancer Cell 10:309-319(2006).
[41]
ERRATUM.
Guo Z., Dai B., Jiang T., Xu K., Xie Y., Kim O., Nesheiwat I.,
Kong X., Melamed J., Handratta V.D., Njar V.C., Brodie A.M., Yu L.-R.,
Veenstra T.D., Chen H., Qiu Y.;
Cancer Cell 11:97-97(2007).
[42]
INTERACTION WITH MAK, AND SUBUNIT.
PubMed=16951154; DOI=10.1158/0008-5472.CAN-06-1636;
Ma A.H., Xia L., Desai S.J., Boucher D.L., Guan Y., Shih H.M.,
Shi X.B., deVere White R.W., Chen H.W., Tepper C.G., Kung H.J.;
"Male germ cell-associated kinase, a male-specific kinase regulated by
androgen, is a coactivator of androgen receptor in prostate cancer
cells.";
Cancer Res. 66:8439-8447(2006).
[43]
INTERACTION WITH PRMT2, AND SUBCELLULAR LOCATION.
PubMed=17587566; DOI=10.1016/j.jsbmb.2007.05.006;
Meyer R., Wolf S.S., Obendorf M.;
"PRMT2, a member of the protein arginine methyltransferase family, is
a coactivator of the androgen receptor.";
J. Steroid Biochem. Mol. Biol. 107:1-14(2007).
[44]
INTERACTION WITH RREB1.
PubMed=17550981; DOI=10.1210/me.2006-0503;
Mukhopadhyay N.K., Cinar B., Mukhopadhyay L., Lutchman M.,
Ferdinand A.S., Kim J., Chung L.W.K., Adam R.M., Ray S.K.,
Leiter A.B., Richie J.P., Liu B.C.-S., Freeman M.R.;
"The zinc finger protein Ras-responsive element binding protein-1 is a
coregulator of the androgen receptor: implications for the role of the
Ras pathway in enhancing androgenic signaling in prostate cancer.";
Mol. Endocrinol. 21:2056-2070(2007).
[45]
INTERACTION WITH RANBP10.
PubMed=18222118; DOI=10.1016/j.bbrc.2008.01.072;
Harada N., Yokoyama T., Yamaji R., Nakano Y., Inui H.;
"RanBP10 acts as a novel coactivator for the androgen receptor.";
Biochem. Biophys. Res. Commun. 368:121-125(2008).
[46]
INTERACTION WITH TNK2, PHOSPHORYLATION AT TYR-269 AND TYR-365 BY TNK2,
AND MUTAGENESIS OF TYR-269 AND TYR-365.
PubMed=17494760; DOI=10.1073/pnas.0700420104;
Mahajan N.P., Liu Y., Majumder S., Warren M.R., Parker C.E.,
Mohler J.L., Earp H.S., Whang Y.E.;
"Activated Cdc42-associated kinase Ack1 promotes prostate cancer
progression via androgen receptor tyrosine phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 104:8438-8443(2007).
[47]
INTERACTION WITH TRIM68.
PubMed=18451177; DOI=10.1158/0008-5472.CAN-07-6059;
Miyajima N., Maruyama S., Bohgaki M., Kano S., Shigemura M.,
Shinohara N., Nonomura K., Hatakeyama S.;
"TRIM68 regulates ligand-dependent transcription of androgen receptor
in prostate cancer cells.";
Cancer Res. 68:3486-3494(2008).
[48]
INTERACTION WITH LPXN.
PubMed=18451096; DOI=10.1210/me.2006-0546;
Kaulfuss S., Grzmil M., Hemmerlein B., Thelen P., Schweyer S.,
Neesen J., Bubendorf L., Glass A.G., Jarry H., Auber B., Burfeind P.;
"Leupaxin, a novel coactivator of the androgen receptor, is expressed
in prostate cancer and plays a role in adhesion and invasion of
prostate carcinoma cells.";
Mol. Endocrinol. 22:1606-1621(2008).
[49]
FUNCTION, AND INTERACTION WITH ZIPK/DAPK3.
PubMed=18084323; DOI=10.1038/sj.onc.1210995;
Leister P., Felten A., Chasan A.I., Scheidtmann K.H.;
"ZIP kinase plays a crucial role in androgen receptor-mediated
transcription.";
Oncogene 27:3292-3300(2008).
[50]
INTERACTION WITH TRIM24.
PubMed=19909775; DOI=10.1016/j.bbamcr.2009.11.001;
Kikuchi M., Okumura F., Tsukiyama T., Watanabe M., Miyajima N.,
Tanaka J., Imamura M., Hatakeyama S.;
"TRIM24 mediates ligand-dependent activation of androgen receptor and
is repressed by a bromodomain-containing protein, BRD7, in prostate
cancer cells.";
Biochim. Biophys. Acta 1793:1828-1836(2009).
[51]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, POLYUBIQUITINATION AT
LYS-846 AND LYS-848 BY RNF6, MUTAGENESIS OF LYS-846 AND LYS-848,
INTERACTION WITH RNF14 AND RNF6, AND SUBCELLULAR LOCATION.
PubMed=19345326; DOI=10.1016/j.ccr.2009.02.021;
Xu K., Shimelis H., Linn D.E., Jiang R., Yang X., Sun F., Guo Z.,
Chen H., Li W., Chen H., Kong X., Melamed J., Fang S., Xiao Z.,
Veenstra T.D., Qiu Y.;
"Regulation of androgen receptor transcriptional activity and
specificity by RNF6-induced ubiquitination.";
Cancer Cell 15:270-282(2009).
[52]
FUNCTION IN AR KINASE, PHOSPHORYLATION AT SER-83 BY CDK9, MUTAGENESIS
OF SER-83, AND INTERACTION WITH CDK9.
PubMed=20980437; DOI=10.1210/me.2010-0238;
Gordon V., Bhadel S., Wunderlich W., Zhang J., Ficarro S.B.,
Mollah S.A., Shabanowitz J., Hunt D.F., Xenarios I., Hahn W.C.,
Conaway M., Carey M.F., Gioeli D.;
"CDK9 regulates AR promoter selectivity and cell growth through serine
81 phosphorylation.";
Mol. Endocrinol. 24:2267-2280(2010).
[53]
UBIQUITINATION, DEUBIQUITINATION, AND INTERACTION WITH USP26.
PubMed=20501646; DOI=10.1158/1541-7786.MCR-09-0424;
Dirac A.M., Bernards R.;
"The deubiquitinating enzyme USP26 is a regulator of androgen receptor
signaling.";
Mol. Cancer Res. 8:844-854(2010).
[54]
PHOSPHORYLATION AT TYR-269, AND ENZYME REGULATION.
PubMed=20623637; DOI=10.1002/pros.21163;
Mahajan K., Challa S., Coppola D., Lawrence H., Luo Y., Gevariya H.,
Zhu W., Chen Y.A., Lawrence N.J., Mahajan N.P.;
"Effect of Ack1 tyrosine kinase inhibitor on ligand-independent
androgen receptor activity.";
Prostate 70:1274-1285(2010).
[55]
PHOSPHORYLATION AT SER-651, AND INTERACTION WITH STK4/MST1.
PubMed=21512132; DOI=10.1158/0008-5472.CAN-10-4532;
Cinar B., Collak F.K., Lopez D., Akgul S., Mukhopadhyay N.K.,
Kilicarslan M., Gioeli D.G., Freeman M.R.;
"MST1 is a multifunctional caspase-independent inhibitor of androgenic
signaling.";
Cancer Res. 71:4303-4313(2011).
[56]
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).
[57]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[58]
PALMITOYLATION.
PubMed=22031296; DOI=10.1091/mbc.E11-07-0638;
Pedram A., Razandi M., Deschenes R.J., Levin E.R.;
"DHHC-7 and -21 are palmitoylacyltransferases for sex steroid
receptors.";
Mol. Biol. Cell 23:188-199(2012).
[59]
INTERACTION WITH CCAR1 AND GATA2.
PubMed=23887938; DOI=10.1093/nar/gkt644;
Seo W.Y., Jeong B.C., Yu E.J., Kim H.J., Kim S.H., Lim J.E.,
Kwon G.Y., Lee H.M., Kim J.H.;
"CCAR1 promotes chromatin loading of androgen receptor (AR)
transcription complex by stabilizing the association between AR and
GATA2.";
Nucleic Acids Res. 41:8526-8536(2013).
[60]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND SER-258, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[61]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 658-920.
PubMed=10840043; DOI=10.1074/jbc.M004571200;
Matias P.M., Donner P., Coelho R., Thomaz M., Peixoto C., Macedo S.,
Otto N., Joschko S., Scholz P., Wegg A., Baesler S., Schaefer M.,
Egner U., Carrondo M.A.;
"Structural evidence for ligand specificity in the binding domain of
the human androgen receptor. Implications for pathogenic gene
mutations.";
J. Biol. Chem. 275:26164-26171(2000).
[62]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 671-918.
PubMed=11906285; DOI=10.1021/jm011072j;
Matias P.M., Carrondo M.A., Coelho R., Thomaz M., Zhao X.Y., Wegg A.,
Crusius K., Egner U., Donner P.;
"Structural basis for the glucocorticoid response in a mutant human
androgen receptor (AR(ccr)) derived from an androgen-independent
prostate cancer.";
J. Med. Chem. 45:1439-1446(2002).
[63]
X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 672-920 IN COMPLEXES WITH
N-TERMINAL MODULATING DOMAIN AND NCOA2, INTERACTION WITH NCOA1, AND
CHARACTERIZATION OF VARIANT PROSTATE CANCER MET-731.
PubMed=15525515; DOI=10.1016/j.molcel.2004.09.036;
He B., Gampe R.T. Jr., Kole A.J., Hnat A.T., Stanley T.B., An G.,
Stewart E.L., Kalman R.I., Minges J.T., Wilson E.M.;
"Structural basis for androgen receptor interdomain and coactivator
interactions suggests a transition in nuclear receptor activation
function dominance.";
Mol. Cell 16:425-438(2004).
[64]
X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 670-920 IN COMPLEXES WITH
DIHYDROTESTOSTERONE AND NCOA1; NCOA2; NCOA3 AND NCOA4, FUNCTION,
INTERACTION WITH NCOA1; NCOA2; NCOA3 AND NCOA4, AND MUTAGENESIS OF
LYS-721 AND GLU-898.
PubMed=15563469; DOI=10.1074/jbc.M407046200;
Estebanez-Perpina E., Moore J.M.R., Mar E., Delgado-Rodrigues E.,
Nguyen P., Baxter J.D., Buehrer B.M., Webb P., Fletterick R.J.,
Guy R.K.;
"The molecular mechanisms of coactivator utilization in ligand-
dependent transactivation by the androgen receptor.";
J. Biol. Chem. 280:8060-8068(2005).
[65]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 665-920 IN COMPLEXES WITH
NONSTEROIDAL LIGANDS, MUTAGENESIS OF TRP-742, CHARACTERIZATION OF
VARIANT PROSTATE CANCER ALA-878, AND CHARACTERIZATION OF VARIANT AIS
THR-896.
PubMed=16129672; DOI=10.1074/jbc.M507464200;
Bohl C.E., Miller D.D., Chen J., Bell C.E., Dalton J.T.;
"Structural basis for accommodation of nonsteroidal ligands in the
androgen receptor.";
J. Biol. Chem. 280:37747-37754(2005).
[66]
X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 655-920 IN COMPLEXES WITH
TESTOSTERONE; DIHYDROTESTOSTERONE AND TETRAHYDROGESTRINONE.
PubMed=16641486; DOI=10.1110/ps.051905906;
Pereira de Jesus-Tran K., Cote P.-L., Cantin L., Blanchet J.,
Labrie F., Breton R.;
"Comparison of crystal structures of human androgen receptor ligand-
binding domain complexed with various agonists reveals molecular
determinants responsible for binding affinity.";
Protein Sci. 15:987-999(2006).
[67]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 672-919 IN COMPLEX WITH
NR0B2.
PubMed=18007036; DOI=10.1107/S0907444907045702;
Jouravel N., Sablin E., Arnold L.A., Guy R.K., Fletterick R.J.;
"Interaction between the androgen receptor and a segment of its
corepressor SHP.";
Acta Crystallogr. D 63:1198-1200(2007).
[68]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 671-919 OF MUTANT ALA-878 IN
COMPLEX WITH THE ANTIANDROGEN CYPROTERONE ACETATE, CHARACTERIZATION OF
VARIANT PROSTATE CANCER ALA-878, AND MUTAGENESIS OF LEU-702.
PubMed=17311914; DOI=10.1074/jbc.M611711200;
Bohl C.E., Wu Z., Miller D.D., Bell C.E., Dalton J.T.;
"Crystal structure of the T877A human androgen receptor ligand-binding
domain complexed to cyproterone acetate provides insight for ligand-
induced conformational changes and structure-based drug design.";
J. Biol. Chem. 282:13648-13655(2007).
[69]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 663-919 OF WILD-TYPE AND
MUTANT TYR-875 IN COMPLEX WITH TESTOSTERONE AND NCOA2, ACTIVATION BY
THE N-TERMINAL MODULATING DOMAIN, INTERACTION WITH NCOA2 AND MAGEA11,
FUNCTION, MUTAGENESIS OF LYS-721 AND GLU-898, AND CHARACTERIZATION OF
VARIANT PROSTATE CANCER TYR-875.
PubMed=17591767; DOI=10.1074/jbc.M703268200;
Askew E.B., Gampe R.T. Jr., Stanley T.B., Faggart J.L., Wilson E.M.;
"Modulation of androgen receptor activation function 2 by testosterone
and dihydrotestosterone.";
J. Biol. Chem. 282:25801-25816(2007).
[70]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 655-920 IN COMPLEX WITH
EM5744.
PubMed=17711855; DOI=10.1074/jbc.M705524200;
Cantin L., Faucher F., Couture J.-F., de Jesus-Tran K.P., Legrand P.,
Ciobanu L.C., Frechette Y., Labrecque R., Singh S.M., Labrie F.,
Breton R.;
"Structural characterization of the human androgen receptor ligand-
binding domain complexed with EM5744, a rationally designed steroidal
ligand bearing a bulky chain directed toward helix 12.";
J. Biol. Chem. 282:30910-30919(2007).
[71]
X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 670-920 IN COMPLEXES WITH
SYNTHETIC LIGANDS, FUNCTION, AND INTERACTION WITH NCOA2.
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).
[72]
REVIEW ON VARIANTS.
PubMed=1458719;
Pinsky L., Trifiro M.A., Kaufman M., Beitel L.K., Mhatre A.,
Kazemi-Esfarjani P., Sabbaghian N., Lumbroso R., Alvarado C.,
Vasiliou M., Gottlieb B.;
"Androgen resistance due to mutation of the androgen receptor.";
Clin. Invest. Med. 15:456-472(1992).
[73]
REVIEW ON VARIANTS AIS.
PubMed=8339746; DOI=10.1007/BF02125442;
Brown T.R., Scherer P.A., Chang Y.-T., Migeon C.J., Ghirri P.,
Murono K., Zhou Z.;
"Molecular genetics of human androgen insensitivity.";
Eur. J. Pediatr. 152 Suppl. 2:S62-S69(1993).
[74]
REVIEW ON VARIANTS.
PubMed=8240973; DOI=10.1016/0960-0760(93)90178-Y;
Sultan C., Lumbroso S., Poujol N., Belon C., Boudon C.,
Lobaccaro J.-M.;
"Mutations of androgen receptor gene in androgen insensitivity
syndromes.";
J. Steroid Biochem. Mol. Biol. 46:519-530(1993).
[75]
REVIEW ON VARIANTS.
PubMed=7937057;
Patterson M.N., Hughes I.A., Gottlieb B., Pinsky L.;
"The androgen receptor gene mutations database.";
Nucleic Acids Res. 22:3560-3562(1994).
[76]
REVIEW ON VARIANTS.
PubMed=7626493; DOI=10.1016/0960-0760(95)00090-M;
Brinkmann A.O., Jenster G., Ris-Stalpers C., van der Korput J.A.G.M.,
Bruggenwirth H.T., Boehmer A.L.M., Trapman J.;
"Androgen receptor mutations.";
J. Steroid Biochem. Mol. Biol. 53:443-448(1995).
[77]
REVIEW ON VARIANTS.
PubMed=9016528; DOI=10.1093/nar/25.1.158;
Gottlieb B., Trifiro M.A., Lumbroso R., Vasiliou D.M., Pinsky L.;
"The androgen receptor gene mutations database.";
Nucleic Acids Res. 25:158-162(1997).
[78]
REVIEW ON VARIANTS.
PubMed=22334387; DOI=10.1002/humu.22046;
Gottlieb B., Beitel L.K., Nadarajah A., Paliouras M., Trifiro M.;
"The androgen receptor gene mutations database: 2012 update.";
Hum. Mutat. 33:887-894(2012).
[79]
VARIANT LNCAP ALA-878.
PubMed=2260966; DOI=10.1016/S0006-291X(05)80067-1;
Veldscholte J., Ris-Stalpers C., Kuiper G.G.J.M., Jenster G.,
Berrevoets C.A., Claassen E., van Rooij H.C.J., Trapman J.,
Brinkmann A.O., Mulder E.;
"A mutation in the ligand binding domain of the androgen receptor of
human LNCaP cells affects steroid binding characteristics and response
to anti-androgens.";
Biochem. Biophys. Res. Commun. 173:534-540(1990).
[80]
VARIANTS AIS CYS-775; GLN-832 AND MET-867.
PubMed=2082179; DOI=10.1210/mend-4-12-1759;
Brown T.R., Lubahn D.B., Wilson E.M., French F.S., Migeon C.J.,
Corfen J.L.;
"Functional characterization of naturally occurring mutant androgen
receptors from subjects with complete androgen insensitivity.";
Mol. Endocrinol. 4:1759-1772(1990).
[81]
VARIANT CYS-775.
PubMed=1856263; DOI=10.1210/jcem-73-2-318;
Marcelli M., Tilley W.D., Zoppi S., Griffin J.E., Wilson J.D.,
McPhaul M.J.;
"Androgen resistance associated with a mutation of the androgen
receptor at amino acid 772 (Arg-->Cys) results from a combination of
decreased messenger ribonucleic acid levels and impairment of receptor
function.";
J. Clin. Endocrinol. Metab. 73:318-325(1991).
[82]
VARIANT AIS PRO-618.
PubMed=1999491; DOI=10.1172/JCI115076;
Marcelli M., Zoppi S., Grino P.B., Griffin J.E., Wilson J.D.,
McPhaul M.J.;
"A mutation in the DNA-binding domain of the androgen receptor gene
causes complete testicular feminization in a patient with receptor-
positive androgen resistance.";
J. Clin. Invest. 87:1123-1126(1991).
[83]
VARIANT PAIS CYS-764.
PubMed=2010552; DOI=10.1172/JCI115147;
McPhaul M.J., Marcelli M., Tilley W.D., Griffin J.E.,
Isidro-Gutierrez R.F., Wilson J.D.;
"Molecular basis of androgen resistance in a family with a qualitative
abnormality of the androgen receptor and responsive to high-dose
androgen therapy.";
J. Clin. Invest. 87:1413-1421(1991).
[84]
POLY-GLN REGION EXPANSION, AND INVOLVEMENT IN SPINAL AND BULBAR
MUSCULAR ATROPHY.
PubMed=2062380; DOI=10.1038/352077a0;
la Spada A.R., Wilson E.M., Lubahn D.B., Harding A.E., Fischbeck K.H.;
"Androgen receptor gene mutations in X-linked spinal and bulbar
muscular atrophy.";
Nature 352:77-79(1991).
[85]
VARIANTS AIS CYS-775 AND HIS-775.
PubMed=1609793;
Prior L., Bordet S., Trifiro M.A., Mhatre A., Kaufman M., Pinsky L.,
Wrogemann K., Belsham D.D., Pereira F., Greenberg C.R., Trapman J.,
Brinkmann A.O., Chang C., Liao S.;
"Replacement of arginine 773 by cysteine or histidine in the human
androgen receptor causes complete androgen insensitivity with
different receptor phenotypes.";
Am. J. Hum. Genet. 51:143-155(1992).
[86]
VARIANTS PAIS LYS-609 AND LEU-867.
PubMed=1424203; DOI=10.1111/j.1365-2265.1992.tb02313.x;
Saunders P.T., Padayachi T., Tincello D.G., Shalet S.M., Wu F.C.;
"Point mutations detected in the androgen receptor gene of three men
with partial androgen insensitivity syndrome.";
Clin. Endocrinol. (Oxf.) 37:214-220(1992).
[87]
VARIANT AIS THR-766.
PubMed=1426313;
Sweet C.R., Behzadian M.A., McDonough P.G.;
"A unique point mutation in the androgen receptor gene in a family
with complete androgen insensitivity syndrome.";
Fertil. Steril. 58:703-707(1992).
[88]
VARIANT AIS VAL-750.
PubMed=1487249; DOI=10.1007/BF00220088;
Jakubiczka S., Werder E.A., Wieacker P.;
"Point mutation in the steroid-binding domain of the androgen receptor
gene in a family with complete androgen insensitivity syndrome
(CAIS).";
Hum. Genet. 90:311-312(1992).
[89]
VARIANTS AIS, AND VARIANTS PAIS.
PubMed=1307250; DOI=10.1093/hmg/1.7.497;
Batch J.A., Williams D.M., Davies H.R., Brown B.D., Evans B.A.J.,
Hughes I.A., Patterson M.N.;
"Androgen receptor gene mutations identified by SSCP in fourteen
subjects with androgen insensitivity syndrome.";
Hum. Mol. Genet. 1:497-503(1992).
[90]
VARIANT AIS VAL-788.
PubMed=1569163; DOI=10.1210/jcem.74.5.1569163;
Nakao R., Haji M., Yanase T., Ogo A., Takayanagi R., Katsube T.,
Fukumaki Y., Nawata H.;
"A single amino acid substitution (Met-786-->Val) in the steroid-
binding domain of human androgen receptor leads to complete androgen
insensitivity syndrome.";
J. Clin. Endocrinol. Metab. 74:1152-1157(1992).
[91]
VARIANTS AIS ARG-742 AND CYS-835.
PubMed=1464650; DOI=10.1210/jcem.75.6.1464650;
Wilson C.M., Griffin J.E., Wilson J.D., Marcelli M., Zoppi S.,
McPhaul M.J.;
"Immunoreactive androgen receptor expression in subjects with androgen
resistance.";
J. Clin. Endocrinol. Metab. 75:1474-1478(1992).
[92]
VARIANTS AIS, AND VARIANTS PAIS.
PubMed=1430233; DOI=10.1172/JCI116093;
McPhaul M.J., Marcelli M., Zoppi S., Wilson C.M., Griffin J.E.,
Wilson J.D.;
"Mutations in the ligand-binding domain of the androgen receptor gene
cluster in two regions of the gene.";
J. Clin. Invest. 90:2097-2101(1992).
[93]
VARIANT PROSTATE CANCER ALA-878.
PubMed=1562539; DOI=10.1016/0960-0760(92)90401-4;
Veldscholte J., Berrevoets C.A., Ris-Stalpers C., Kuiper G.G.J.M.,
Jenster G., Trapman J., Brinkmann A.O., Mulder E.;
"The androgen receptor in LNCaP cells contains a mutation in the
ligand binding domain which affects steroid binding characteristics
and response to antiandrogens.";
J. Steroid Biochem. Mol. Biol. 41:665-669(1992).
[94]
VARIANTS AIS TYR-560 AND ARG-577, AND VARIANTS PAIS GLY-598 AND
PRO-618.
PubMed=1316540; DOI=10.1210/mend.6.3.1316540;
Zoppi S., Marcelli M., Deslypere J.-P., Griffin J.E., Wilson J.D.,
McPhaul M.J.;
"Amino acid substitutions in the DNA-binding domain of the human
androgen receptor are a frequent cause of receptor-binding positive
androgen resistance.";
Mol. Endocrinol. 6:409-415(1992).
[95]
VARIANTS AIS SER-706; VAL-750; PHE-760; HIS-775; CYS-856 AND GLY-865.
PubMed=1480178; DOI=10.1210/me.6.11.1909;
De Bellis A., Quigley C.A., Cariello N.F., el-Awady M.K., Sar M.,
Lane M.V., Wilson E.M., French F.S.;
"Single base mutations in the human androgen receptor gene causing
complete androgen insensitivity: rapid detection by a modified
denaturing gradient gel electrophoresis technique.";
Mol. Endocrinol. 6:1909-1920(1992).
[96]
VARIANT PAIS/BREAST CANCER GLN-608.
PubMed=1303262; DOI=10.1038/ng1092-132;
Wooster R., Mangion J., Eeles R., Smith S., Dowsett M., Averill D.,
Barrett-Lee P., Easton D.F., Ponder B.A., Stratton M.R.;
"A germline mutation in the androgen receptor gene in two brothers
with breast cancer and Reifenstein syndrome.";
Nat. Genet. 2:132-134(1992).
[97]
VARIANT MET-731.
PubMed=1631125; DOI=10.1073/pnas.89.14.6319;
Newmark J.R., Hardy D.O., Tonb D.C., Carter B.S., Epstein J.I.,
Isaacs W.B., Brown T.R., Barrack E.R.;
"Androgen receptor gene mutations in human prostate cancer.";
Proc. Natl. Acad. Sci. U.S.A. 89:6319-6323(1992).
[98]
VARIANTS ARG-207 AND ASP-794.
PubMed=8213813;
Macke J.P., Hu N., Hu S., Bailey M., King V.L., Brown T., Hamer D.,
Nathans J.;
"Sequence variation in the androgen receptor gene is not a common
determinant of male sexual orientation.";
Am. J. Hum. Genet. 53:844-852(1993).
[99]
VARIANT AIS PHE-582.
PubMed=8224266;
Lumbroso S., Lobaccaro J.-M., Belon C., Martin D., Chaussain J.-L.,
Sultan C.;
"A new mutation within the deoxyribonucleic acid-binding domain of the
androgen receptor gene in a family with complete androgen
insensitivity syndrome.";
Fertil. Steril. 60:814-819(1993).
[100]
VARIANT AIS VAL-755.
PubMed=8103398; DOI=10.1093/hmg/2.7.1041;
Lobaccaro J.-M., Lumbroso S., Ktari R., Dumas R., Sultan C.;
"An exonic point mutation creates a MaeIII site in the androgen
receptor gene of a family with complete androgen insensitivity
syndrome.";
Hum. Mol. Genet. 2:1041-1043(1993).
[101]
VARIANT PAIS/BREAST CANCER LYS-609.
PubMed=8281139; DOI=10.1093/hmg/2.11.1799;
Lobaccaro J.-M., Lumbroso S., Belon C., Galtier-Dereure F.,
Bringer J., Lesimple T., Namer M., Cutuli B.F., Pujol H., Sultan C.;
"Androgen receptor gene mutation in male breast cancer.";
Hum. Mol. Genet. 2:1799-1802(1993).
[102]
VARIANT AIS ARG-808.
PubMed=8281140; DOI=10.1093/hmg/2.11.1809;
Adeyemo O., Kallio P.J., Palvimo J.J., Kontula K., Jaenne O.A.;
"A single-base substitution in exon 6 of the androgen receptor gene
causing complete androgen insensitivity: the mutated receptor fails to
transactivate but binds to DNA in vitro.";
Hum. Mol. Genet. 2:1809-1812(1993).
[103]
VARIANT PAIS VAL-744.
PubMed=8325932; DOI=10.1210/jcem.77.1.8325932;
Nakao R., Yanase T., Sakai Y., Haji M., Nawata H.;
"A single amino acid substitution (Gly743 --> Val) in the steroid-
binding domain of the human androgen receptor leads to Reifenstein
syndrome.";
J. Clin. Endocrinol. Metab. 77:103-107(1993).
[104]
VARIANTS AIS LYS-682 AND THR-843, AND VARIANTS PAIS HIS-841 AND
LEU-867.
PubMed=8325950; DOI=10.1210/jcem.77.1.8325950;
Hiort O., Huang Q., Sinnecker G.H., Sadeghi-Nejad A., Kruse K.,
Wolfe H.J., Yandell D.W.;
"Single strand conformation polymorphism analysis of androgen receptor
gene mutations in patients with androgen insensitivity syndromes:
application for diagnosis, genetic counseling, and therapy.";
J. Clin. Endocrinol. Metab. 77:262-266(1993).
[105]
VARIANTS PAIS HIS-856 AND MET-870.
PubMed=8097257; DOI=10.1136/jmg.30.3.198;
Batch J.A., Evans B.A.J., Hughes I.A., Patterson M.N.;
"Mutations of the androgen receptor gene identified in perineal
hypospadias.";
J. Med. Genet. 30:198-201(1993).
[106]
VARIANT AIS VAL-744.
PubMed=8096390; DOI=10.1016/0960-0760(93)90081-7;
Lobaccaro J.-M., Lumbroso S., Berta P., Chaussain J.-L., Sultan C.;
"Complete androgen insensitivity syndrome associated with a de novo
mutation of the androgen receptor gene detected by single strand
conformation polymorphism.";
J. Steroid Biochem. Mol. Biol. 44:211-216(1993).
[107]
VARIANTS PROSTATE CANCER HIS-702 AND ALA-878.
PubMed=8274409; DOI=10.1016/0960-0760(93)90316-O;
Suzuki H., Sato N., Watabe Y., Masai M., Seino S., Shimazaki J.;
"Androgen receptor gene mutations in human prostate cancer.";
J. Steroid Biochem. Mol. Biol. 46:759-765(1993).
[108]
VARIANT AIS MET-867, AND VARIANT PAIS LEU-867.
PubMed=8446106; DOI=10.1210/mend.7.1.8446106;
Kazemi-Esfarjani P., Beitel L.K., Trifiro M.A., Kaufman M., Rennie P.,
Sheppard P., Matusik R., Pinsky L.;
"Substitution of valine-865 by methionine or leucine in the human
androgen receptor causes complete or partial androgen insensitivity,
respectively with distinct androgen receptor phenotypes.";
Mol. Endocrinol. 7:37-46(1993).
[109]
VARIANT PROSTATE CANCER MET-716.
PubMed=8145761; DOI=10.1210/mend.7.12.8145761;
Culig Z., Hobisch A., Cronauer M.V., Cato A.C.B., Hittmair A.,
Radmayr C., Eberle J., Bartsch G., Klocker H.;
"Mutant androgen receptor detected in an advanced-stage prostatic
carcinoma is activated by adrenal androgens and progesterone.";
Mol. Endocrinol. 7:1541-1550(1993).
[110]
VARIANTS AIS PHE-582; VAL-744; VAL-755; GLU-768 AND CYS-856.
Lobaccaro J.-M., Lumbroso S., Belon C., Chaussain J.L., Toublanc J.E.,
Leheup B., Sultan C.;
"Androgen receptor (AR) gene mutations in 6 families with androgen
insensitivity syndrome (Abstract #114).";
Pediatr. Res. Suppl. 33:S22-S22(1993).
[111]
VARIANTS PROSTATE CANCER LEU-342 AND GLU-799.
PubMed=7511268;
Castagnaro M., Yandell D.W., Dockhorn-Dworniczak B., Wolfe H.J.,
Poremba C.;
"Androgen receptor gene mutations and p53 gene analysis in advanced
prostate cancer.";
Verh. Dtsch. Ges. Pathol. 77:119-123(1993).
[112]
POLY-GLN REGION CONTRACTION, AND INVOLVEMENT IN PROSTATE CANCER.
PubMed=8292051; DOI=10.1006/bbrc.1994.1011;
Schoenberg M.P., Hakimi J.M., Wang S., Bova G.S., Epstein J.I.,
Fischbeck K.H., Isaacs W.B., Walsh P.C., Barrack E.R.;
"Microsatellite mutation (CAG24-->18) in the androgen receptor gene in
human prostate cancer.";
Biochem. Biophys. Res. Commun. 198:74-80(1994).
[113]
VARIANT PROSTATE CANCER ALA-878.
PubMed=8187068;
Gaddipati J.P., McLeod D.G., Heidenberg H.B., Sesterhenn I.A.,
Finger M.J., Moul J.W., Srivastava S.;
"Frequent detection of codon 877 mutation in the androgen receptor
gene in advanced prostate cancers.";
Cancer Res. 54:2861-2864(1994).
[114]
VARIANT PAIS TRP-569.
PubMed=7910529;
Lobaccaro J.-M., Belon C., Lumbroso S., Olewniczack G.,
Carre-Pigeon F., Job J.C., Chaussain J.L., Toublanc J.E., Sultan C.;
"Molecular prenatal diagnosis of partial androgen insensitivity
syndrome based on the Hind III polymorphism of the androgen receptor
gene.";
Clin. Endocrinol. (Oxf.) 40:297-302(1994).
[115]
VARIANT PAIS HIS-841.
PubMed=7909256; DOI=10.1530/eje.0.1300327;
Lumbroso S., Lobaccaro J.-M., Belon C., Amram S., Bachelard B.,
Garandeau P., Sultan C.;
"Molecular prenatal exclusion of familial partial androgen
insensitivity (Reifenstein syndrome).";
Eur. J. Endocrinol. 130:327-332(1994).
[116]
VARIANT PAIS HIS-841.
PubMed=8205256; DOI=10.1530/eje.0.1300569;
Imasaki K., Hasegawa T., Okabe T., Sakai Y., Haji M., Takayanagi R.,
Nawata H.;
"Single amino acid substitution (840Arg-->His) in the hormone-binding
domain of the androgen receptor leads to incomplete androgen
insensitivity syndrome associated with a thermolabile androgen
receptor.";
Eur. J. Endocrinol. 130:569-574(1994).
[117]
VARIANT PAIS VAL-871.
PubMed=8033918; DOI=10.1007/BF01956409;
Hiort O., Klauber G., Cendron M., Sinnecker G.H., Keim L.,
Schwinger E., Wolfe H.J., Yandell D.W.;
"Molecular characterization of the androgen receptor gene in boys with
hypospadias.";
Eur. J. Pediatr. 153:317-321(1994).
[118]
VARIANT PAIS ASP-691 DEL.
Schwartz M., Skovby F., Mueller J., Nielsen O., Skakkebaek N.E.;
"Partial androgen insensitivity (PAIS) in a large eskimo kindred
caused by a delD690 mutation in the androgen receptor (AR) gene
(Abstract #244).";
Horm. Res. 41:117-117(1994).
[119]
VARIANTS AIS PHE-583 DEL; ARG-616 DEL AND HIS-616.
PubMed=8162033; DOI=10.1093/hmg/3.1.21;
Beitel L.K., Prior L., Vasiliou D.M., Gottlieb B., Kaufman M.,
Lumbroso R., Alvarado C., McGillivray B., Trifiro M.A., Pinsky L.;
"Complete androgen insensitivity due to mutations in the probable
alpha-helical segments of the DNA-binding domain in the human androgen
receptor.";
Hum. Mol. Genet. 3:21-27(1994).
[120]
VARIANTS PAIS SER-583; TYR-605; ALA-709; LEU-755 AND HIS-772, AND
VARIANT AIS TRP-780.
PubMed=7981687; DOI=10.1093/hmg/3.7.1163;
Hiort O., Wodtke A., Struve D., Zoellner A., Sinnecker G.H.;
"Detection of point mutations in the androgen receptor gene using non-
isotopic single strand conformation polymorphism analysis.";
Hum. Mol. Genet. 3:1163-1166(1994).
[121]
VARIANT AIS PHE-602.
PubMed=7981689; DOI=10.1093/hmg/3.7.1169;
Baldazzi L., Baroncini C., Pirazzoli P., Balsamo A., Capelli M.,
Marchetti G., Bernardi F., Cacciari E.;
"Two mutations causing complete androgen insensitivity: a frame-shift
in the steroid binding domain and a Cys-->Phe substitution in the
second zinc finger of the androgen receptor.";
Hum. Mol. Genet. 3:1169-1170(1994).
[122]
VARIANTS PAIS ARG-617; HIS-841 AND MET-890.
PubMed=8126121; DOI=10.1210/jc.78.3.513;
De Bellis A., Quigley C.A., Marschke K.B., el-Awady M.K., Lane M.V.,
Smith E.P., Sar M., Wilson E.M., French F.S.;
"Characterization of mutant androgen receptors causing partial
androgen insensitivity syndrome.";
J. Clin. Endocrinol. Metab. 78:513-522(1994).
[123]
VARIANT AIS PHE-791.
PubMed=7962294; DOI=10.1210/jcem.79.4.7962294;
Tsukada T., Inoue M., Tachibana S., Nakai Y., Takebe H.;
"An androgen receptor mutation causing androgen resistance in
undervirilized male syndrome.";
J. Clin. Endocrinol. Metab. 79:1202-1207(1994).
[124]
VARIANTS AIS CYS-841 AND HIS-841.
PubMed=8040309; DOI=10.1172/JCI117368;
Beitel L.K., Kazemi-Esfarjani P., Kaufman M., Lumbroso R.,
DiGeorge A.M., Killinger D.W., Trifiro M.A., Pinsky L.;
"Substitution of arginine-839 by cysteine or histidine in the androgen
receptor causes different receptor phenotypes in cultured cells and
coordinate degrees of clinical androgen resistance.";
J. Clin. Invest. 94:546-554(1994).
[125]
VARIANTS AIS, AND VARIANTS PAIS.
PubMed=7929841; DOI=10.1172/JCI117507;
Marcelli M., Zoppi S., Wilson C.M., Griffin J.E., McPhaul M.J.;
"Amino acid substitutions in the hormone-binding domain of the human
androgen receptor alter the stability of the hormone receptor
complex.";
J. Clin. Invest. 94:1642-1650(1994).
[126]
VARIANT AIS LYS-728.
PubMed=7993455; DOI=10.1016/S0140-6736(94)92385-X;
Yong E.L., Ng S.C., Roy A.C., Yun G., Ratnam S.S.;
"Pregnancy after hormonal correction of severe spermatogenic defect
due to mutation in androgen receptor gene.";
Lancet 344:826-827(1994).
[127]
VARIANTS AIS HIS-616 AND LEU-765, AND VARIANTS PAIS VAL-743 AND
THR-746.
PubMed=7970939; DOI=10.1203/00006450-199408000-00015;
Ris-Stalpers C., Hoogenboezem T., Sleddens H.F.B.M.,
Verleun-Mooijman M.C.T., Degenhart H.J., Drop S.L.S., Halley D.J.J.,
Oosterwijk J.C., Hodgins M.B., Trapman J., Brinkmann A.O.;
"A practical approach to the detection of androgen receptor gene
mutations and pedigree analysis in families with X-linked androgen
insensitivity.";
Pediatr. Res. 36:227-234(1994).
[128]
VARIANT AIS HIS-841.
PubMed=8830623;
Imai A., Ohno T., Iida K., Ohsuye K., Okano Y., Tamaya T.;
"A frame-shift mutation of the androgen receptor gene in a patient
with receptor-negative complete testicular feminization: comparison
with a single base substitution in a receptor-reduced incomplete
form.";
Ann. Clin. Biochem. 32:482-486(1995).
[129]
VARIANTS PROSTATE CANCER.
PubMed=7712463;
Takahashi H., Furusato M., Allsbrook W.C. Jr., Nishii H., Wakui S.,
Barrett J.C., Boyd J.;
"Prevalence of androgen receptor gene mutations in latent prostatic
carcinomas from Japanese men.";
Cancer Res. 55:1621-1624(1995).
[130]
VARIANT AIS VAL-882.
PubMed=7641413; DOI=10.1111/j.1365-2265.1995.tb01895.x;
Davies H.R., Hughes I.A., Patterson M.N.;
"Genetic counselling in complete androgen insensitivity syndrome:
trinucleotide repeat polymorphisms, single-strand conformation
polymorphism and direct detection of two novel mutations in the
androgen receptor gene.";
Clin. Endocrinol. (Oxf.) 43:69-77(1995).
[131]
VARIANTS AIS SER-706 AND HIS-764, AND VARIANTS PAIS LEU-726; THR-738;
HIS-775 AND GLU-799.
PubMed=7671849; DOI=10.1210/edrv-16-3-271;
Quigley C.A., De Bellis A., Marschke K.B., el-Awady M.K., Wilson E.M.,
French F.S.;
"Androgen receptor defects: historical, clinical, and molecular
perspectives.";
Endocr. Rev. 16:271-321(1995).
[132]
ERRATUM.
Quigley C.A., De Bellis A., Marschke K.B., el-Awady M.K., Wilson E.M.,
French F.S.;
Endocr. Rev. 16:546-546(1995).
[133]
VARIANTS AIS LEU-832 AND GLN-832.
PubMed=7633398; DOI=10.1093/hmg/4.4.515;
Shkolny D.L., Brown T.R., Punnett H.H., Kaufman M., Trifiro M.A.,
Pinsky L.;
"Characterization of alternative amino acid substitutions at arginine
830 of the androgen receptor that cause complete androgen
insensitivity in three families.";
Hum. Mol. Genet. 4:515-521(1995).
[134]
VARIANT AIS PRO-678.
PubMed=7537149; DOI=10.1002/humu.1380050104;
Belsham D.D., Pereira F., Greenberg C.R., Liao S., Wrogemann K.;
"Leu-676-Pro mutation of the androgen receptor causes complete
androgen insensitivity syndrome in a large Hutterite kindred.";
Hum. Mutat. 5:28-33(1995).
[135]
VARIANT PAIS CYS-764, AND VARIANTS AIS TRP-780; VAL-808 AND CYS-856.
PubMed=7581399; DOI=10.1002/humu.1380060208;
Murono K., Mendonca B.B., Arnhold I.J.P., Rigon A.C.M.M., Migeon C.J.,
Brown T.R.;
"Human androgen insensitivity due to point mutations encoding amino
acid substitutions in the androgen receptor steroid-binding domain.";
Hum. Mutat. 6:152-162(1995).
[136]
VARIANT PROSTATE CANCER MET-731.
PubMed=7591265; DOI=10.1002/ijc.2910630415;
Peterziel H., Culig Z., Stober J., Hobisch A., Radmayr C., Bartsch G.,
Klocker H., Cato A.C.B.;
"Mutant androgen receptors in prostatic tumors distinguish between
amino-acid-sequence requirements for transactivation and ligand
binding.";
Int. J. Cancer 63:544-550(1995).
[137]
VARIANT VAL-569.
PubMed=7673412; DOI=10.1210/jcem.80.9.7673412;
Allera A., Herbst M.A., Griffin J.E., Wilson J.D., Schweikert H.-U.,
McPhaul M.J.;
"Mutations of the androgen receptor coding sequence are infrequent in
patients with isolated hypospadias.";
J. Clin. Endocrinol. Metab. 80:2697-2699(1995).
[138]
VARIANT PROSTATE CANCER LEU-727.
PubMed=8530589; DOI=10.1210/jcem.80.12.8530589;
Elo J.P., Kvist L., Leinonen K., Isomaa V., Henttu P., Lukkarinen O.,
Vihko P.;
"Mutated human androgen receptor gene detected in a prostatic cancer
patient is also activated by estradiol.";
J. Clin. Endocrinol. Metab. 80:3494-3500(1995).
[139]
VARIANT PAIS THR-597.
PubMed=7649358; DOI=10.1016/0303-7207(95)03554-K;
Gast A., Neuschmid-Kaspar F., Klocker H., Cato A.C.B.;
"A single amino acid exchange abolishes dimerization of the androgen
receptor and causes Reifenstein syndrome.";
Mol. Cell. Endocrinol. 111:93-98(1995).
[140]
VARIANTS PROSTATE CANCER.
PubMed=7723794; DOI=10.1056/NEJM199505253322101;
Taplin M.-E., Bubley G.J., Shuster T.D., Frantz M.E., Spooner A.E.,
Ogata G.K., Keer H.N., Balk S.P.;
"Mutation of the androgen-receptor gene in metastatic androgen-
independent prostate cancer.";
N. Engl. J. Med. 332:1393-1398(1995).
[141]
VARIANTS AIS AND PAIS.
PubMed=8723113;
DOI=10.1002/(SICI)1096-8628(19960503)63:1<218::AID-AJMG38>3.0.CO;2-P;
Hiort O., Sinnecker G.H., Holterhus P.M., Nitsche E.M., Kruse K.;
"The clinical and molecular spectrum of androgen insensitivity
syndromes.";
Am. J. Med. Genet. 63:218-222(1996).
[142]
VARIANTS PROSTATE CANCER.
PubMed=9816170;
Tilley W.D., Buchanan G., Hickey T.E., Bentel J.M.;
"Mutations in the androgen receptor gene are associated with
progression of human prostate cancer to androgen independence.";
Clin. Cancer Res. 2:277-285(1996).
[143]
VARIANTS PAIS GLN-608; THR-611; LEU-755; HIS-841; THR-843 AND HIS-856,
AND VARIANT AIS MET-867.
PubMed=9039340; DOI=10.1046/j.1365-2265.1996.8600869.x;
Weidemann W., Linck B., Haupt H., Mentrup B., Romalo G.,
Stockklauser K., Brinkmann A.O., Schweikert H.-U., Spindler K.D.;
"Clinical and biochemical investigations and molecular analysis of
subjects with mutations in the androgen receptor gene.";
Clin. Endocrinol. (Oxf.) 45:733-739(1996).
[144]
VARIANT AIS CYS-856.
PubMed=9001799;
Malmgren H., Gustavsson J., Tuvemo T., Dahl N.;
"Rapid detection of a mutation hot-spot in the human androgen
receptor.";
Clin. Genet. 50:202-205(1996).
[145]
VARIANTS PAIS ILE-743; ILE-781; GLU-799; CYS-841; HIS-856 AND MET-870.
PubMed=8824883; DOI=10.1093/hmg/5.2.265;
Bevan C.L., Brown B.B., Davies H.R., Evans B.A.J., Hughes I.A.,
Patterson M.N.;
"Functional analysis of six androgen receptor mutations identified in
patients with partial androgen insensitivity syndrome.";
Hum. Mol. Genet. 5:265-273(1996).
[146]
VARIANT PAIS ARG-910.
PubMed=8550758; DOI=10.1210/jcem.81.1.8550758;
Choong C.S., Sturm M.J., Strophair J.A., McCulloch R.K., Tilley W.D.,
Leedman P.J., Hurley D.M.;
"Partial androgen insensitivity caused by an androgen receptor
mutation at amino acid 907 (Gly-->Arg) that results in decreased
ligand binding affinity and reduced androgen receptor messenger
ribonucleic acid levels.";
J. Clin. Endocrinol. Metab. 81:236-243(1996).
[147]
VARIANT AIS ARG-708.
PubMed=8626869; DOI=10.1210/jcem.81.5.8626869;
Lumbroso S., Lobaccaro J.-M., Georget V., Leger J., Poujol N.,
Terouanne B., Evain-Brion D., Czernichow P., Sultan C.;
"A novel substitution (Leu707Arg) in exon 4 of the androgen receptor
gene causes complete androgen resistance.";
J. Clin. Endocrinol. Metab. 81:1984-1988(1996).
[148]
VARIANT AIS ILE-781.
PubMed=8768864; DOI=10.1210/jcem.81.8.8768864;
Rodien P., Mebarki F., Mowszowicz I., Chaussain J.L., Young J.,
Morel Y., Schaison G.;
"Different phenotypes in a family with androgen insensitivity caused
by the same M780I point mutation in the androgen receptor gene.";
J. Clin. Endocrinol. Metab. 81:2994-2998(1996).
[149]
VARIANT PAIS LYS-2.
PubMed=8823308; DOI=10.1172/JCI118930;
Choong C.S., Quigley C.A., French F.S., Wilson E.M.;
"A novel missense mutation in the amino-terminal domain of the human
androgen receptor gene in a family with partial androgen insensitivity
syndrome causes reduced efficiency of protein translation.";
J. Clin. Invest. 98:1423-1431(1996).
[150]
VARIANT AIS ASP-574.
PubMed=8918984; DOI=10.1016/0960-0760(96)00095-7;
Bruggenwirth H.T., Boehmer A.L.M., Verleun-Mooijman M.C.T.,
Hoogenboezem T., Kleijer W.J., Otten B.J., Trapman J., Brinkmann A.O.;
"Molecular basis of androgen insensitivity.";
J. Steroid Biochem. Mol. Biol. 58:569-575(1996).
[151]
VARIANT AIS SER-549.
PubMed=8683794; DOI=10.1097/00005392-199608001-00077;
Sutherland R.W., Wiener J.S., Hicks J.P., Marcelli M.,
Gonzales E.T. Jr., Roth D.R., Lamb D.J.;
"Androgen receptor gene mutations are rarely associated with isolated
penile hypospadias.";
J. Urol. 156:828-831(1996).
[152]
VARIANT AIS PRO-617.
PubMed=8647313; DOI=10.1016/0303-7207(95)03709-8;
Lobaccaro J.-M., Poujol N., Chiche L., Lumbroso S., Brown T.R.,
Sultan C.;
"Molecular modeling and in vitro investigations of the human androgen
receptor DNA-binding domain: application for the study of two
mutations.";
Mol. Cell. Endocrinol. 116:137-147(1996).
[153]
VARIANT AIS PHE-580, AND VARIANT PAIS TYR-583.
PubMed=8809734; DOI=10.1016/0303-7207(96)03812-9;
Imasaki K., Okabe T., Murakami H., Tanaka Y., Haji M., Takayanagi R.,
Nawata H.;
"Androgen insensitivity syndrome due to new mutations in the DNA-
binding domain of the androgen receptor.";
Mol. Cell. Endocrinol. 120:15-24(1996).
[154]
VARIANT PROSTATE CANCER GLU-799.
PubMed=8628719;
DOI=10.1002/(SICI)1097-0045(199603)28:3<162::AID-PROS3>3.0.CO;2-H;
Evans B.A.J., Harper M.E., Daniells C.E., Watts C.E., Matenhelia S.,
Green J., Griffiths K.;
"Low incidence of androgen receptor gene mutations in human prostatic
tumors using single strand conformation polymorphism analysis.";
Prostate 28:162-171(1996).
[155]
VARIANT PROSTATE CANCER ALA-878.
PubMed=8827083;
DOI=10.1002/1097-0045(199609)29:3<153::AID-PROS2990290303>3.0.CO;2-5;
Suzuki H., Akakura K., Komiya A., Aida S., Akimoto S., Shimazaki J.;
"Codon 877 mutation in the androgen receptor gene in advanced prostate
cancer: relation to antiandrogen withdrawal syndrome.";
Prostate 29:153-158(1996).
[156]
VARIANT AIS HIS-856.
PubMed=9106550;
Boehmer A.L.M., Brinkmann A.O., Niermeijer M.F., Bakker L.,
Halley D.J.J., Drop S.L.S.;
"Germ-line and somatic mosaicism in the androgen insensitivity
syndrome: implications for genetic counseling.";
Am. J. Hum. Genet. 60:1003-1006(1997).
[157]
VARIANT PROSTATE CANCER ALA-684.
PubMed=9000575;
Koivisto P., Kononen J., Palmberg C., Tammela T., Hyytinen E.,
Isola J., Trapman J., Cleutjens K., Noordzij A., Visakorpi T.,
Kallioniemi O.-P.;
"Androgen receptor gene amplification: a possible molecular mechanism
for androgen deprivation therapy failure in prostate cancer.";
Cancer Res. 57:314-319(1997).
[158]
VARIANTS PAIS LYS-609 AND GLY-773.
PubMed=9196614; DOI=10.1046/j.1365-2265.1997.1140927.x;
Tincello D.G., Saunders P.T., Hodgins M.B., Simpson N.B.,
Edwards C.R., Hargreaves T.B., Wu F.C.;
"Correlation of clinical, endocrine and molecular abnormalities with
in vivo responses to high-dose testosterone in patients with partial
androgen insensitivity syndrome.";
Clin. Endocrinol. (Oxf.) 46:497-506(1997).
[159]
VARIANT AIS MET-890.
PubMed=9160185;
Essawi M., Gad Y.Z., el-Rouby O., Temtamy S.A., Sabour Y.A.,
el-Awady M.K.;
"Molecular analysis of androgen resistance syndromes in Egyptian
patients.";
Dis. Markers 13:99-105(1997).
[160]
VARIANT AIS TRP-780.
PubMed=9007482; DOI=10.1007/s004310050542;
Sinnecker G.H., Hiort O., Nitsche E.M., Holterhus P.M., Kruse K.;
"Functional assessment and clinical classification of androgen
sensitivity in patients with mutations of the androgen receptor
gene.";
Eur. J. Pediatr. 156:7-14(1997).
[161]
VARIANTS AIS VAL-750; CYS-775; ILE-781 AND SER-795.
PubMed=8990010;
DOI=10.1002/(SICI)1098-1004(1997)9:1<57::AID-HUMU10>3.3.CO;2-0;
Jakubiczka S., Nedel S., Werder E.A., Schleiermacher E., Theile U.,
Wolff G., Wieacker P.;
"Mutations of the androgen receptor gene in patients with complete
androgen insensitivity.";
Hum. Mutat. 9:57-61(1997).
[162]
VARIANTS PROSTATE CANCER IN POLY-GLN REGION; HIS-702 AND ARG-911.
PubMed=9438000; DOI=10.1093/jjco/27.6.389;
Watanabe M., Ushijima T., Shiraishi T., Yatani R., Shimazaki J.,
Kotake T., Sugimura T., Nagao M.;
"Genetic alterations of androgen receptor gene in Japanese human
prostate cancer.";
Jpn. J. Clin. Oncol. 27:389-393(1997).
[163]
VARIANT PROSTATE CANCER GLN-630.
PubMed=9184448; DOI=10.5980/jpnjurol1989.88.550;
Wang C., Uchida T.;
"Androgen receptor gene mutations in prostate cancer.";
Nihon Hinyokika Gakkai Zasshi 88:550-556(1997).
[164]
VARIANTS AIS ARG-196 AND CYS-856.
PubMed=9255042; DOI=10.1111/j.1447-0756.1997.tb00845.x;
Komori S., Sakata K., Tanaka H., Shima H., Koyama K.;
"DNA analysis of the androgen receptor gene in two cases with complete
androgen insensitivity syndrome.";
J. Obstet. Gynaecol. Res. 23:277-281(1997).
[165]
VARIANTS PAIS ALA-709 AND GLY-871.
PubMed=9329414; DOI=10.1016/S0022-3476(97)80063-7;
Albers N., Ulrichs C., Gluer S., Hiort O., Sinnecker G.H.,
Mildenberger H., Brodehl J.;
"Etiologic classification of severe hypospadias: implications for
prognosis and management.";
J. Pediatr. 131:386-392(1997).
[166]
VARIANTS AIS ASN-733 AND THR-766.
PubMed=9252933;
Ko T.M., Yang Y.S., Wu M.Y., Kao C.H., Hsu P.M., Chuang S.M.,
Lee T.Y.;
"Complete androgen insensitivity syndrome. Molecular characterization
in two Chinese women.";
J. Reprod. Med. 42:424-428(1997).
[167]
VARIANTS AIS ASP-751; PHE-763; THR-766; ASN-865 AND PHE-908.
PubMed=9328206; DOI=10.1016/S0960-0760(97)00001-0;
Bevan C.L., Hughes I.A., Patterson M.N.;
"Wide variation in androgen receptor dysfunction in complete androgen
insensitivity syndrome.";
J. Steroid Biochem. Mol. Biol. 61:19-26(1997).
[168]
VARIANT PAIS GLY-704, AND VARIANT AIS LEU-917.
PubMed=9302173; DOI=10.1016/S0022-5347(01)64279-4;
Radmayr C., Culig Z., Glatzl J., Neuschmid-Kaspar F., Bartsch G.,
Klocker H.;
"Androgen receptor point mutations as the underlying molecular defect
in 2 patients with androgen insensitivity syndrome.";
J. Urol. 158:1553-1556(1997).
[169]
VARIANTS AIS CYS-572; GLN-753 AND CYS-775.
PubMed=9544375; DOI=10.1007/s004040050206;
Komori S., Kasumi H., Sakata K., Tanaka H., Hamada K., Koyama K.;
"Molecular analysis of the androgen receptor gene in 4 patients with
complete androgen insensitivity.";
Arch. Gynecol. Obstet. 261:95-100(1998).
[170]
VARIANTS AIS HIS-616 AND GLN-753.
PubMed=9698822; DOI=10.1590/S0100-879X1998000600008;
Cabral D.F., Maciel-Guerra A.T., Hackel C.;
"Mutations of androgen receptor gene in Brazilian patients with male
pseudohermaphroditism.";
Braz. J. Med. Biol. Res. 31:775-778(1998).
[171]
VARIANT ARG-216, AND CHARACTERIZATION OF VARIANT ARG-216.
PubMed=9788719;
Wang Q., Ghadessy F.J., Yong E.L.;
"Analysis of the transactivation domain of the androgen receptor in
patients with male infertility.";
Clin. Genet. 54:185-192(1998).
[172]
VARIANTS AIS PRO-257 AND ALA-821.
PubMed=9610419; DOI=10.3109/09513599809024954;
Tanaka H., Komori S., Sakata K., Shima H., Koyama K.;
"One additional mutation at exon A amplifies thermolability of
androgen receptor in a case with complete androgen insensitivity
syndrome.";
Gynecol. Endocrinol. 12:75-82(1998).
[173]
VARIANTS AIS THR-766; TYR-785 AND THR-896, AND VARIANT PAIS GLY-841.
PubMed=9856504; DOI=10.1007/s004390050864;
Lundberg Giwercman Y., Nikoshkov A., Lindsten K., Bystroem B.,
Pousette A., Chibalin A.V., Arvidsson S., Tiulpakov A.,
Semitcheva T.V., Peterkova V., Hagenfeldt K., Ritzen E.M., Wedell A.;
"Functional characterisation of mutations in the ligand-binding domain
of the androgen receptor gene in patients with androgen insensitivity
syndrome.";
Hum. Genet. 103:529-531(1998).
[174]
VARIANT AIS VAL-696.
PubMed=9554754;
Doerk T., Schnieders F., Jakubiczka S., Wieacker P.,
Schroeder-Kurth T., Schmidtke J.;
"A new missense substitution at a mutational hot spot of the androgen
receptor in siblings with complete androgen insensitivity syndrome.";
Hum. Mutat. 11:337-339(1998).
[175]
VARIANT ASP-646.
PubMed=9554755;
Nordenskjoeld A., Soederhaell S.;
"An androgen receptor gene mutation (A645D) in a boy with a normal
phenotype.";
Hum. Mutat. 11:339-339(1998).
[176]
VARIANT AIS LEU-893.
Knoke I., Jakubiczka S., Rohrer T., Hanimann B., Werder E.A.,
Wieacker P.;
"Single amino acid substitution in the hormone-binding domain of the
androgen receptor in a family with complete androgen insensitivity
syndrome (CAIS).";
Hum. Mutat. 12:220-220(1998).
[177]
VARIANT PAIS GLN-608.
PubMed=9543136; DOI=10.1210/jcem.83.4.4704;
Weidemann W., Peters B., Romalo G., Spindler K.D., Schweikert H.-U.;
"Response to androgen treatment in a patient with partial androgen
insensitivity and a mutation in the deoxyribonucleic acid-binding
domain of the androgen receptor.";
J. Clin. Endocrinol. Metab. 83:1173-1176(1998).
[178]
VARIANTS PAIS VAL-744 AND CYS-841.
PubMed=9768671; DOI=10.1210/jcem.83.10.5201;
Georget V., Terouanne B., Lumbroso S., Nicolas J.C., Sultan C.;
"Trafficking of androgen receptor mutants fused to green fluorescent
protein: a new investigation of partial androgen insensitivity
syndrome.";
J. Clin. Endocrinol. Metab. 83:3597-3603(1998).
[179]
VARIANT AIS GLU-799.
PubMed=9851768; DOI=10.1210/jcem.83.12.5358;
Wang Q., Ghadessy F.J., Trounson A., de Kretser D., McLachlan R.,
Ng S.C., Yong E.L.;
"Azoospermia associated with a mutation in the ligand-binding domain
of an androgen receptor displaying normal ligand binding, but
defective trans-activation.";
J. Clin. Endocrinol. Metab. 83:4303-4309(1998).
[180]
VARIANTS AIS.
PubMed=9627582; DOI=10.1016/S0022-3476(98)70387-7;
Hiort O., Sinnecker G.H., Holterhus P.M., Nitsche E.M., Kruse K.;
"Inherited and de novo androgen receptor gene mutations: investigation
of single-case families.";
J. Pediatr. 132:939-943(1998).
[181]
VARIANT PAIS THR-759.
PubMed=9607727; DOI=10.1016/S0303-7207(97)00229-3;
Yong E.L., Tut T.G., Ghadessy F.J., Prins G., Ratnam S.S.;
"Partial androgen insensitivity and correlations with the predicted
three dimensional structure of the androgen receptor ligand-binding
domain.";
Mol. Cell. Endocrinol. 137:41-50(1998).
[182]
VARIANT PAIS LEU-912.
PubMed=10470409; DOI=10.1046/j.1439-0272.1999.00278.x;
Knoke I., Jakubiczka S., Lehnert H., Wieacker P.;
"A new point mutation of the androgen receptor gene in a patient with
partial androgen resistance and severe oligozoospermia.";
Andrologia 31:199-201(1999).
[183]
VARIANTS PROSTATE CANCER ALA-878 AND ASN-891.
PubMed=10363963;
Taplin M.-E., Bubley G.J., Ko Y.J., Small E.J., Upton M.,
Rajeshkumar B., Balk S.P.;
"Selection for androgen receptor mutations in prostate cancers treated
with androgen antagonist.";
Cancer Res. 59:2511-2515(1999).
[184]
VARIANT PAIS SER-841.
PubMed=10502786;
DOI=10.1002/(SICI)1098-1004(199910)14:4<353::AID-HUMU16>3.0.CO;2-7;
Melo K.F.S., Latronico A.C., Costa E.M.F., Billerbeck A.E.C.,
Mendonca B.B., Arnhold I.J.P.;
"A novel point mutation (R840S) in the androgen receptor in a
Brazilian family with partial androgen insensitivity syndrome.";
Hum. Mutat. 14:353-353(1999).
[185]
VARIANTS AIS ARG-392 AND ARG-445.
PubMed=10571951;
DOI=10.1002/(SICI)1098-1004(199912)14:6<527::AID-HUMU12>3.0.CO;2-X;
Gottlieb B., Vasiliou D.M., Lumbroso R., Beitel L.K., Pinsky L.,
Trifiro M.A.;
"Analysis of exon 1 mutations in the androgen receptor gene.";
Hum. Mutat. 14:527-539(1999).
[186]
VARIANT PAIS GLN-608, AND VARIANT AIS LYS-682.
PubMed=10221692; DOI=10.1093/humrep/14.3.664;
Chen C.P., Chern S.R., Wang T.Y., Wang W., Wang K.L., Jeng C.J.;
"Androgen receptor gene mutations in 46,XY females with germ cell
tumours.";
Hum. Reprod. 14:664-670(1999).
[187]
VARIANT AIS LEU-893.
PubMed=10404311; DOI=10.1046/j.1442-2042.1999.00065.x;
Kanayama H., Naroda T., Inoue Y., Kurokawa Y., Kagawa S.;
"A case of complete testicular feminization: laparoscopic orchiectomy
and analysis of androgen receptor gene mutation.";
Int. J. Urol. 6:327-330(1999).
[188]
VARIANT PAIS ALA-773, AND VARIANT AIS GLY-872.
PubMed=10022458; DOI=10.1210/jcem.84.2.5453;
Shkolny D.L., Beitel L.K., Ginsberg J., Pekeles G., Arbour L.,
Pinsky L., Trifiro M.A.;
"Discordant measures of androgen-binding kinetics in two mutant
androgen receptors causing mild or partial androgen insensitivity,
respectively.";
J. Clin. Endocrinol. Metab. 84:805-810(1999).
[189]
VARIANTS PROSTATE CANCER IN POLY-GLN REGION AND ALA-684.
PubMed=10629558;
DOI=10.1002/(SICI)1096-9896(199912)189:4<559::AID-PATH471>3.0.CO;2-Y;
Wallen M.J., Linja M., Kaartinen K., Schleutker J., Visakorpi T.;
"Androgen receptor gene mutations in hormone-refractory prostate
cancer.";
J. Pathol. 189:559-563(1999).
[190]
VARIANTS PROSTATE CANCER HIS-702 AND ALA-878.
PubMed=10569618; DOI=10.1016/S0022-5347(05)68158-X;
Zhao X.Y., Boyle B., Krishnan A.V., Navone N.M., Peehl D.M.,
Feldman D.;
"Two mutations identified in the androgen receptor of the new human
prostate cancer cell line MDA PCa 2a.";
J. Urol. 162:2192-2199(1999).
[191]
VARIANT PAIS THR-808.
PubMed=10543676; DOI=10.1016/S0140-6736(99)03205-5;
Ong Y.C., Wong H.B., Adaikan G., Yong E.L.;
"Directed pharmacological therapy of ambiguous genitalia due to an
androgen receptor gene mutation.";
Lancet 354:1444-1445(1999).
[192]
VARIANT AIS LEU-893.
PubMed=10221770; DOI=10.1016/S0303-7207(98)00237-8;
Peters I., Weidemann W., Romalo G., Knorr D., Schweikert H.-U.,
Spindler K.D.;
"An androgen receptor mutation in the direct vicinity of the proposed
C-terminal alpha-helix of the ligand binding domain containing the AF-
2 transcriptional activating function core is associated with complete
androgen insensitivity.";
Mol. Cell. Endocrinol. 148:47-53(1999).
[193]
VARIANT PROSTATE CANCER TYR-620.
PubMed=10598582; DOI=10.1210/mend.13.12.0382;
Nazareth L.V., Stenoien D.L., Bingman W.E. III, James A.J., Wu C.,
Zhang Y., Edwards D.P., Mancini M., Marcelli M., Lamb D.J.,
Weigel N.L.;
"A C619Y mutation in the human androgen receptor causes inactivation
and mislocalization of the receptor with concomitant sequestration of
SRC-1.";
Mol. Endocrinol. 13:2065-2075(1999).
[194]
ERRATUM.
Nazareth L.V., Stenoien D.L., Bingman W.E. III, James A.J., Wu C.,
Zhang Y., Edwards D.P., Mancini M., Marcelli M., Lamb D.J.,
Weigel N.L.;
Mol. Endocrinol. 14:544-544(2000).
[195]
VARIANT AIS THR-597.
PubMed=10590024; DOI=10.1203/00006450-199912000-00008;
Holterhus P.M., Wiebel J., Sinnecker G.H., Bruggenwirth H.T.,
Sippell W.G., Brinkmann A.O., Kruse K., Hiort O.;
"Clinical and molecular spectrum of somatic mosaicism in androgen
insensitivity syndrome.";
Pediatr. Res. 46:684-690(1999).
[196]
VARIANTS AIS PHE-813 AND GLN-832.
PubMed=10458483; DOI=10.1620/tjem.187.263;
Yaegashi N., Uehara S., Senoo M., Sato J., Fujiwara J., Funato T.,
Sasaki T., Yajima A.;
"Point mutations in the steroid-binding domain of the androgen
receptor gene of five Japanese patients with androgen insensitivity
syndrome.";
Tohoku J. Exp. Med. 187:263-272(1999).
[197]
VARIANTS THR-598 AND LEU-726.
PubMed=10092153; DOI=10.1007/s002400050088;
Nordenskjoeld A., Friedman E., Tapper-Persson M., Soederhaell C.,
Leviav A., Svensson J., Anvret M.;
"Screening for mutations in candidate genes for hypospadias.";
Urol. Res. 27:49-55(1999).
[198]
VARIANTS PROSTATE CANCER ALA-576; ARG-581; VAL-587; TYR-620; ALA-758
AND GLY-847.
PubMed=10706109;
Marcelli M., Ittmann M., Mariani S., Sutherland R.W., Nigam R.,
Murthy L., Zhao Y., DiConcini D., Puxeddu E., Esen A., Eastham J.,
Weigel N.L., Lamb D.J.;
"Androgen receptor mutations in prostate cancer.";
Cancer Res. 60:944-949(2000).
[199]
VARIANTS AIS AND PAIS.
PubMed=10690872; DOI=10.1210/jcem.85.2.6337;
Ahmed S.F., Cheng A., Dovey L., Hawkins J.R., Martin H., Rowland J.,
Shimura N., Tait A.D., Hughes I.A.;
"Phenotypic features, androgen receptor binding, and mutational
analysis in 278 clinical cases reported as androgen insensitivity
syndrome.";
J. Clin. Endocrinol. Metab. 85:658-665(2000).
[200]
VARIANTS PAIS THR-683 AND GLU-712, AND VARIANTS AIS GLU-744; VAL-828;
ARG-875 AND TYR-880.
PubMed=11587068; DOI=10.1007/s100380170021;
Chavez B., Mendez J.P., Ulloa-Aguirre A., Larrea F., Vilchis F.;
"Eight novel mutations of the androgen receptor gene in patients with
androgen insensitivity syndrome.";
J. Hum. Genet. 46:560-565(2001).
[201]
INVOLVEMENT IN ANDROGENETIC ALOPECIA, AND POLYMORPHISM OF POLY-GLY
REGION.
PubMed=11231320; DOI=10.1046/j.1523-1747.2001.01261.x;
Ellis J.A., Stebbing M., Harrap S.B.;
"Polymorphism of the androgen receptor gene is associated with male
pattern baldness.";
J. Invest. Dermatol. 116:452-455(2001).
[202]
VARIANT AIS TYR-706.
PubMed=11744994;
Sills E.S., Sholes T.E., Perloe M., Kaplan C.R., Davis J.G.,
Tucker M.J.;
"Characterization of a novel receptor mutation A->T at exon 4 in
complete androgen insensitivity syndrome and a carrier sibling via
bidirectional polymorphism sequence analysis.";
Int. J. Mol. Med. 9:45-48(2002).
[203]
INVOLVEMENT IN ANDROGENETIC ALOPECIA, AND POLYMORPHISM OF POLY-GLY
REGION.
PubMed=15902657; DOI=10.1086/431425;
Hillmer A.M., Hanneken S., Ritzmann S., Becker T., Freudenberg J.,
Brockschmidt F.F., Flaquer A., Freudenberg-Hua Y., Jamra R.A.,
Metzen C., Heyn U., Schweiger N., Betz R.C., Blaumeiser B., Hampe J.,
Schreiber S., Schulze T.G., Hennies H.C., Schumacher J., Propping P.,
Ruzicka T., Cichon S., Wienker T.F., Kruse R., Noethen M.M.;
"Genetic variation in the human androgen receptor gene is the major
determinant of common early-onset androgenetic alopecia.";
Am. J. Hum. Genet. 77:140-148(2005).
[204]
INVOLVEMENT IN SMAX1.
PubMed=15851746; DOI=10.1212/01.WNL.0000158617.41819.F3;
Echaniz-Laguna A., Rousso E., Anheim M., Cossee M., Tranchant C.;
"A family with early-onset and rapidly progressive X-linked spinal and
bulbar muscular atrophy.";
Neurology 64:1458-1460(2005).
[205]
VARIANT AIS PHE-577.
PubMed=14756668; DOI=10.1111/j.0009-9163.2004.00197.x;
Hooper H.T., Figueiredo B.C., Pavan-Senn C.C., De Lacerda L.,
Sandrini R., Mengarelli J.K., Japp K., Karaviti L.P.;
"Concordance of phenotypic expression and gender identity in a large
kindred with a mutation in the androgen receptor.";
Clin. Genet. 65:183-190(2004).
[206]
CHARACTERIZATION OF VARIANTS AIS ASN-696; CYS-764; HIS-775; GLU-799;
HIS-856 AND PHE-908.
PubMed=16595706; DOI=10.1677/jme.1.01885;
Jaeaeskelaeinen J., Deeb A., Schwabe J.W., Mongan N.P., Martin H.,
Hughes I.A.;
"Human androgen receptor gene ligand-binding-domain mutations leading
to disrupted interaction between the N- and C-terminal domains.";
J. Mol. Endocrinol. 36:361-368(2006).
[207]
VARIANT ARG-216.
PubMed=27535533; DOI=10.1038/nature19057;
Exome Aggregation Consortium;
Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E.,
Fennell T., O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B.,
Tukiainen T., Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K.,
Zhao F., Zou J., Pierce-Hoffman E., Berghout J., Cooper D.N.,
Deflaux N., DePristo M., Do R., Flannick J., Fromer M., Gauthier L.,
Goldstein J., Gupta N., Howrigan D., Kiezun A., Kurki M.I.,
Moonshine A.L., Natarajan P., Orozco L., Peloso G.M., Poplin R.,
Rivas M.A., Ruano-Rubio V., Rose S.A., Ruderfer D.M., Shakir K.,
Stenson P.D., Stevens C., Thomas B.P., Tiao G., Tusie-Luna M.T.,
Weisburd B., Won H.H., Yu D., Altshuler D.M., Ardissino D.,
Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S.,
Laakso M., McCarroll S., McCarthy M.I., McGovern D., McPherson R.,
Neale B.M., Palotie A., Purcell S.M., Saleheen D., Scharf J.M.,
Sklar P., Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C.,
Wilson J.G., Daly M.J., MacArthur D.G.;
"Analysis of protein-coding genetic variation in 60,706 humans.";
Nature 536:285-291(2016).
-!- 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. Transcription activation is
down-regulated by NR0B2. Activated, but not phosphorylated, by
HIPK3 and ZIPK/DAPK3. {ECO:0000269|PubMed:14664718,
ECO:0000269|PubMed:15563469, ECO:0000269|PubMed:17591767,
ECO:0000269|PubMed:17911242, ECO:0000269|PubMed:18084323,
ECO:0000269|PubMed:19345326, ECO:0000269|PubMed:20980437}.
-!- FUNCTION: Isoform 3 and isoform 4 lack the C-terminal ligand-
binding domain and may therefore constitutively activate the
transcription of a specific set of genes independently of steroid
hormones. {ECO:0000269|PubMed:19244107}.
-!- ENZYME REGULATION: AIM-100 (4-amino-5,6-biaryl-furo[2,3-
d]pyrimidine) suppresses TNK2-mediated phosphorylation at Tyr-269.
Inhibits the binding of the Tyr-269 phosphorylated form to
androgen-responsive enhancers (AREs) and its transcriptional
activity. {ECO:0000269|PubMed:20623637}.
-!- 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, 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 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. Interacts with CCAR1 and GATA2.
{ECO:0000269|PubMed:10075738, ECO:0000269|PubMed:10332029,
ECO:0000269|PubMed:10383460, ECO:0000269|PubMed:10400640,
ECO:0000269|PubMed:10625666, ECO:0000269|PubMed:10930412,
ECO:0000269|PubMed:12039962, ECO:0000269|PubMed:12361945,
ECO:0000269|PubMed:12415108, ECO:0000269|PubMed:12612053,
ECO:0000269|PubMed:12958311, ECO:0000269|PubMed:14609956,
ECO:0000269|PubMed:14664718, ECO:0000269|PubMed:15525515,
ECO:0000269|PubMed:15563469, ECO:0000269|PubMed:16027218,
ECO:0000269|PubMed:16051670, ECO:0000269|PubMed:16951154,
ECO:0000269|PubMed:17311914, ECO:0000269|PubMed:17494760,
ECO:0000269|PubMed:17550981, ECO:0000269|PubMed:17587566,
ECO:0000269|PubMed:17591767, ECO:0000269|PubMed:17711855,
ECO:0000269|PubMed:17911242, ECO:0000269|PubMed:18007036,
ECO:0000269|PubMed:18084323, ECO:0000269|PubMed:18222118,
ECO:0000269|PubMed:18451096, ECO:0000269|PubMed:18451177,
ECO:0000269|PubMed:19345326, ECO:0000269|PubMed:19909775,
ECO:0000269|PubMed:20501646, ECO:0000269|PubMed:20980437,
ECO:0000269|PubMed:21512132, ECO:0000269|PubMed:22170608,
ECO:0000269|PubMed:23887938}.
-!- INTERACTION:
P00519:ABL1; NbExp=2; IntAct=EBI-608057, EBI-375543;
Q9UBL3:ASH2L; NbExp=2; IntAct=EBI-608057, EBI-540797;
P51451:BLK; NbExp=3; IntAct=EBI-608057, EBI-2105445;
Q8WV28:BLNK; NbExp=2; IntAct=EBI-608057, EBI-2623522;
O60885-1:BRD4; NbExp=6; IntAct=EBI-608057, EBI-9345088;
P78543:BTG2; NbExp=4; IntAct=EBI-608057, EBI-1047576;
Q14790:CASP8; NbExp=3; IntAct=EBI-608057, EBI-78060;
P24385:CCND1; NbExp=4; IntAct=EBI-608057, EBI-375001;
Q92793:CREBBP; NbExp=2; IntAct=EBI-608057, EBI-81215;
O14595:CTDSP2; NbExp=3; IntAct=EBI-608057, EBI-2802973;
P35222:CTNNB1; NbExp=11; IntAct=EBI-608057, EBI-491549;
Q9UER7:DAXX; NbExp=5; IntAct=EBI-608057, EBI-77321;
P20711:DDC; NbExp=2; IntAct=EBI-608057, EBI-1632155;
P11308:ERG; NbExp=4; IntAct=EBI-608057, EBI-79704;
P07332:FES; NbExp=3; IntAct=EBI-608057, EBI-1055635;
P09769:FGR; NbExp=3; IntAct=EBI-608057, EBI-1383732;
Q02790:FKBP4; NbExp=2; IntAct=EBI-608057, EBI-1047444;
P55317:FOXA1; NbExp=3; IntAct=EBI-608057, EBI-3918034;
O75593:FOXH1; NbExp=3; IntAct=EBI-608057, EBI-1759806;
Q9R1E0:Foxo1 (xeno); NbExp=4; IntAct=EBI-608057, EBI-1371343;
Q14451:GRB7; NbExp=3; IntAct=EBI-608057, EBI-970191;
P06396:GSN; NbExp=2; IntAct=EBI-608057, EBI-351506;
P56524:HDAC4; NbExp=4; IntAct=EBI-608057, EBI-308629;
Q16665:HIF1A; NbExp=2; IntAct=EBI-608057, EBI-447269;
Q16666:IFI16; NbExp=3; IntAct=EBI-608057, EBI-2867186;
O15357:INPPL1; NbExp=3; IntAct=EBI-608057, EBI-1384248;
Q15652:JMJD1C; NbExp=2; IntAct=EBI-608057, EBI-1224969;
P17535:JUND; NbExp=2; IntAct=EBI-608057, EBI-2682803;
O95251:KAT7; NbExp=5; IntAct=EBI-608057, EBI-473199;
Q9BY66:KDM5D; NbExp=2; IntAct=EBI-608057, EBI-1246860;
Q9BY66-3:KDM5D; NbExp=2; IntAct=EBI-608057, EBI-12559887;
P07288:KLK3; NbExp=3; IntAct=EBI-608057, EBI-1220791;
Q03164:KMT2A; NbExp=2; IntAct=EBI-608057, EBI-591370;
O14686:KMT2D; NbExp=2; IntAct=EBI-608057, EBI-996065;
P06239:LCK; NbExp=7; IntAct=EBI-608057, EBI-1348;
P07948:LYN; NbExp=5; IntAct=EBI-608057, EBI-79452;
P20794:MAK; NbExp=5; IntAct=EBI-608057, EBI-3911321;
P42679:MATK; NbExp=4; IntAct=EBI-608057, EBI-751664;
Q00987:MDM2; NbExp=2; IntAct=EBI-608057, EBI-389668;
Q15596:NCOA2; NbExp=2; IntAct=EBI-608057, EBI-81236;
Q14686:NCOA6; NbExp=2; IntAct=EBI-608057, EBI-78670;
O96028:NSD2; NbExp=5; IntAct=EBI-608057, EBI-2693298;
Q99497:PARK7; NbExp=6; IntAct=EBI-608057, EBI-1164361;
P27986:PIK3R1; NbExp=5; IntAct=EBI-608057, EBI-79464;
O00459:PIK3R2; NbExp=14; IntAct=EBI-608057, EBI-346930;
Q92569:PIK3R3; NbExp=37; IntAct=EBI-608057, EBI-79893;
P19174:PLCG1; NbExp=22; IntAct=EBI-608057, EBI-79387;
P16885:PLCG2; NbExp=6; IntAct=EBI-608057, EBI-617403;
Q06830:PRDX1; NbExp=3; IntAct=EBI-608057, EBI-353193;
P78527:PRKDC; NbExp=3; IntAct=EBI-608057, EBI-352053;
Q06124:PTPN11; NbExp=12; IntAct=EBI-608057, EBI-297779;
P20936:RASA1; NbExp=16; IntAct=EBI-608057, EBI-1026476;
Q9UBS8:RNF14; NbExp=2; IntAct=EBI-608057, EBI-2130308;
Q9Y252:RNF6; NbExp=10; IntAct=EBI-608057, EBI-2341483;
O14796:SH2D1B; NbExp=3; IntAct=EBI-608057, EBI-3923013;
Q9NP31:SH2D2A; NbExp=6; IntAct=EBI-608057, EBI-490630;
P29353:SHC1; NbExp=14; IntAct=EBI-608057, EBI-78835;
Q6S5L8:SHC4; NbExp=3; IntAct=EBI-608057, EBI-9453524;
Q5VZ18:SHE; NbExp=3; IntAct=EBI-608057, EBI-3956977;
Q06986:Siah2 (xeno); NbExp=6; IntAct=EBI-608057, EBI-957413;
Q15797:SMAD1; NbExp=6; IntAct=EBI-608057, EBI-1567153;
O14544:SOCS6; NbExp=4; IntAct=EBI-608057, EBI-3929549;
P12931:SRC; NbExp=7; IntAct=EBI-608057, EBI-621482;
Q9ULZ2:STAP1; NbExp=2; IntAct=EBI-608057, EBI-6083058;
P63165:SUMO1; NbExp=7; IntAct=EBI-608057, EBI-80140;
Q9HBL0:TNS1; NbExp=3; IntAct=EBI-608057, EBI-3389814;
Q01534-1:TSPY1; NbExp=3; IntAct=EBI-608057, EBI-15888922;
P07947:YES1; NbExp=5; IntAct=EBI-608057, EBI-515331;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12958311,
ECO:0000269|PubMed:15634333, ECO:0000269|PubMed:17587566,
ECO:0000269|PubMed:19244107, ECO:0000269|PubMed:19345326}.
Cytoplasm {ECO:0000269|PubMed:12958311,
ECO:0000269|PubMed:17587566, ECO:0000269|PubMed:19244107}.
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 RACK1.
{ECO:0000269|PubMed:12958311, ECO:0000269|PubMed:17587566}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=AR-B;
IsoId=P10275-1; Sequence=Displayed;
Name=2; Synonyms=AR-A, Variant AR45;
IsoId=P10275-2; Sequence=VSP_036889, VSP_036890;
Name=3; Synonyms=AR3;
IsoId=P10275-3; Sequence=VSP_058166, VSP_058168;
Note=Minor isoform up-regulated in prostate cancer cells.
{ECO:0000269|PubMed:19244107};
Name=4; Synonyms=AR4;
IsoId=P10275-4; Sequence=VSP_058167, VSP_058169;
Note=Minor isoform identified in prostate cancer cells.
{ECO:0000269|PubMed:19244107};
-!- TISSUE SPECIFICITY: Isoform 2 is mainly expressed in heart and
skeletal muscle (PubMed:15634333). Isoform 3 is expressed by basal
and stromal cells of prostate (at protein level)
(PubMed:19244107). {ECO:0000269|PubMed:15634333,
ECO:0000269|PubMed:19244107}.
-!- 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.
-!- PTM: Sumoylated on Lys-388 (major) and Lys-521. Ubiquitinated.
Deubiquitinated by USP26. 'Lys-6' and 'Lys-27'-linked
polyubiquitination by RNF6 modulates AR transcriptional activity
and specificity. {ECO:0000269|PubMed:11121022,
ECO:0000269|PubMed:19345326, ECO:0000269|PubMed:20501646}.
-!- PTM: Phosphorylated in prostate cancer cells in response to
several growth factors including EGF. Phosphorylation is induced
by c-Src kinase (CSK). Tyr-535 is one of the major phosphorylation
sites and an increase in phosphorylation and Src kinase activity
is associated with prostate cancer progression. Phosphorylation by
TNK2 enhances the DNA-binding and transcriptional activity and may
be responsible for androgen-independent progression of prostate
cancer. Phosphorylation at Ser-83 by CDK9 regulates AR promoter
selectivity and cell growth. Phosphorylation by PAK6 leads to AR-
mediated transcription inhibition. {ECO:0000269|PubMed:14573606,
ECO:0000269|PubMed:17045208, ECO:0000269|PubMed:17494760,
ECO:0000269|PubMed:20623637, ECO:0000269|PubMed:20980437,
ECO:0000269|PubMed:21512132}.
-!- 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.
{ECO:0000269|PubMed:22031296}.
-!- POLYMORPHISM: The poly-Gln region of AR is highly polymorphic and
the number of Gln varies in the population (from 17 to 26). A
smaller size of the poly-Gln region may be associated with the
development of prostate cancer. {ECO:0000269|PubMed:1561105,
ECO:0000269|PubMed:2062380, ECO:0000269|PubMed:8292051,
ECO:0000269|PubMed:9096391}.
-!- POLYMORPHISM: The poly-Gly region of AR is polymorphic and ranges
from 24 to 31 Gly. A poly-Gly region shorter or equal to 23 may be
associated with the development of androgenetic alopecia.
{ECO:0000269|PubMed:11231320, ECO:0000269|PubMed:15902657}.
-!- DISEASE: Androgen insensitivity syndrome (AIS) [MIM:300068]: An X-
linked recessive form of pseudohermaphroditism due end-organ
resistance to androgen. Affected males have female external
genitalia, female breast development, blind vagina, absent uterus
and female adnexa, and abdominal or inguinal testes, despite a
normal 46,XY karyotype. {ECO:0000269|PubMed:10022458,
ECO:0000269|PubMed:10221692, ECO:0000269|PubMed:10221770,
ECO:0000269|PubMed:10404311, ECO:0000269|PubMed:10458483,
ECO:0000269|PubMed:10571951, ECO:0000269|PubMed:10590024,
ECO:0000269|PubMed:10690872, ECO:0000269|PubMed:11587068,
ECO:0000269|PubMed:11744994, ECO:0000269|PubMed:1307250,
ECO:0000269|PubMed:1316540, ECO:0000269|PubMed:1426313,
ECO:0000269|PubMed:1430233, ECO:0000269|PubMed:1464650,
ECO:0000269|PubMed:14756668, ECO:0000269|PubMed:1480178,
ECO:0000269|PubMed:1487249, ECO:0000269|PubMed:1569163,
ECO:0000269|PubMed:1609793, ECO:0000269|PubMed:16129672,
ECO:0000269|PubMed:16595706, ECO:0000269|PubMed:1775137,
ECO:0000269|PubMed:1999491, ECO:0000269|PubMed:2082179,
ECO:0000269|PubMed:2594783, ECO:0000269|PubMed:7537149,
ECO:0000269|PubMed:7581399, ECO:0000269|PubMed:7633398,
ECO:0000269|PubMed:7641413, ECO:0000269|PubMed:7671849,
ECO:0000269|PubMed:7929841, ECO:0000269|PubMed:7962294,
ECO:0000269|PubMed:7970939, ECO:0000269|PubMed:7981687,
ECO:0000269|PubMed:7981689, ECO:0000269|PubMed:7993455,
ECO:0000269|PubMed:8040309, ECO:0000269|PubMed:8096390,
ECO:0000269|PubMed:8103398, ECO:0000269|PubMed:8162033,
ECO:0000269|PubMed:8224266, ECO:0000269|PubMed:8281140,
ECO:0000269|PubMed:8325950, ECO:0000269|PubMed:8339746,
ECO:0000269|PubMed:8413310, ECO:0000269|PubMed:8446106,
ECO:0000269|PubMed:8626869, ECO:0000269|PubMed:8647313,
ECO:0000269|PubMed:8683794, ECO:0000269|PubMed:8723113,
ECO:0000269|PubMed:8768864, ECO:0000269|PubMed:8809734,
ECO:0000269|PubMed:8830623, ECO:0000269|PubMed:8918984,
ECO:0000269|PubMed:8990010, ECO:0000269|PubMed:9001799,
ECO:0000269|PubMed:9007482, ECO:0000269|PubMed:9039340,
ECO:0000269|PubMed:9106550, ECO:0000269|PubMed:9160185,
ECO:0000269|PubMed:9252933, ECO:0000269|PubMed:9255042,
ECO:0000269|PubMed:9302173, ECO:0000269|PubMed:9328206,
ECO:0000269|PubMed:9544375, ECO:0000269|PubMed:9554754,
ECO:0000269|PubMed:9610419, ECO:0000269|PubMed:9627582,
ECO:0000269|PubMed:9698822, ECO:0000269|PubMed:9851768,
ECO:0000269|PubMed:9856504, ECO:0000269|Ref.110,
ECO:0000269|Ref.176}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- DISEASE: Spinal and bulbar muscular atrophy X-linked 1 (SMAX1)
[MIM:313200]: An X-linked recessive form of spinal muscular
atrophy. Spinal muscular atrophy refers to a group of
neuromuscular disorders characterized by degeneration of the
anterior horn cells of the spinal cord, leading to symmetrical
muscle weakness and atrophy. SMAX1 occurs only in men. Age at
onset is usually in the third to fifth decade of life, but earlier
involvement has been reported. It is characterized by slowly
progressive limb and bulbar muscle weakness with fasciculations,
muscle atrophy, and gynecomastia. The disorder is clinically
similar to classic forms of autosomal spinal muscular atrophy.
{ECO:0000269|PubMed:15851746}. Note=The disease is caused by
mutations affecting the gene represented in this entry. Caused by
trinucleotide CAG repeat expansion. In SMAX1 patients the number
of Gln ranges from 38 to 62. Longer expansions result in earlier
onset and more severe clinical manifestations of the disease.
-!- DISEASE: Note=Defects in AR may play a role in metastatic prostate
cancer. The mutated receptor stimulates prostate growth and
metastases development despite of androgen ablation. This
treatment can reduce primary and metastatic lesions probably by
inducing apoptosis of tumor cells when they express the wild-type
receptor.
-!- DISEASE: Androgen insensitivity, partial (PAIS) [MIM:312300]: A
disorder that is characterized by hypospadias, hypogonadism,
gynecomastia, genital ambiguity, normal XY karyotype, and a
pedigree pattern consistent with X-linked recessive inheritance.
Some patients present azoospermia or severe oligospermia without
other clinical manifestations. {ECO:0000269|PubMed:10022458,
ECO:0000269|PubMed:10221692, ECO:0000269|PubMed:10470409,
ECO:0000269|PubMed:10502786, ECO:0000269|PubMed:10543676,
ECO:0000269|PubMed:11587068, ECO:0000269|PubMed:1303262,
ECO:0000269|PubMed:1307250, ECO:0000269|PubMed:1316540,
ECO:0000269|PubMed:1424203, ECO:0000269|PubMed:1430233,
ECO:0000269|PubMed:14756668, ECO:0000269|PubMed:2010552,
ECO:0000269|PubMed:7581399, ECO:0000269|PubMed:7649358,
ECO:0000269|PubMed:7671849, ECO:0000269|PubMed:7909256,
ECO:0000269|PubMed:7910529, ECO:0000269|PubMed:7929841,
ECO:0000269|PubMed:7970939, ECO:0000269|PubMed:7981687,
ECO:0000269|PubMed:8033918, ECO:0000269|PubMed:8097257,
ECO:0000269|PubMed:8126121, ECO:0000269|PubMed:8205256,
ECO:0000269|PubMed:8281139, ECO:0000269|PubMed:8325932,
ECO:0000269|PubMed:8325950, ECO:0000269|PubMed:8446106,
ECO:0000269|PubMed:8550758, ECO:0000269|PubMed:8809734,
ECO:0000269|PubMed:8823308, ECO:0000269|PubMed:8824883,
ECO:0000269|PubMed:9039340, ECO:0000269|PubMed:9196614,
ECO:0000269|PubMed:9302173, ECO:0000269|PubMed:9329414,
ECO:0000269|PubMed:9543136, ECO:0000269|PubMed:9607727,
ECO:0000269|PubMed:9768671, ECO:0000269|PubMed:9856504,
ECO:0000269|Ref.118}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- 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.
-!- MISCELLANEOUS: The level of tyrosine phosphorylation may serve as
a diagnostic tool to predict patient outcome in response to
hormone-ablation therapy. Inhibition of tyrosine phosphorylation
may be an effective intervention target for hormone-refractory
prostate cancer.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Androgen receptor gene mutations database;
URL="http://androgendb.mcgill.ca";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ARID685chXq12.html";
-!- WEB RESOURCE: Name=Wikipedia; Note=Androgen receptor entry;
URL="https://en.wikipedia.org/wiki/Androgen_receptor";
-!- WEB RESOURCE: Name=X-chromosome gene database, androgen receptor
(AR); Note=Leiden Open Variation Database (LOVD);
URL="http://www.lovd.nl/AR";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M20132; AAA51729.1; -; mRNA.
EMBL; M23263; AAA51775.1; -; mRNA.
EMBL; M27430; AAA51886.1; -; Genomic_DNA.
EMBL; M27423; AAA51886.1; JOINED; Genomic_DNA.
EMBL; M27424; AAA51886.1; JOINED; Genomic_DNA.
EMBL; M27425; AAA51886.1; JOINED; Genomic_DNA.
EMBL; M27426; AAA51886.1; JOINED; Genomic_DNA.
EMBL; M27427; AAA51886.1; JOINED; Genomic_DNA.
EMBL; M27428; AAA51886.1; JOINED; Genomic_DNA.
EMBL; M27429; AAA51886.1; JOINED; Genomic_DNA.
EMBL; M34233; AAA51780.1; -; mRNA.
EMBL; M21748; AAA51771.1; -; mRNA.
EMBL; M35851; AAA51772.1; -; Genomic_DNA.
EMBL; M35844; AAA51772.1; JOINED; Genomic_DNA.
EMBL; M35845; AAA51772.1; JOINED; Genomic_DNA.
EMBL; M35846; AAA51772.1; JOINED; Genomic_DNA.
EMBL; M35847; AAA51772.1; JOINED; Genomic_DNA.
EMBL; M35848; AAA51772.1; JOINED; Genomic_DNA.
EMBL; M35849; AAA51772.1; JOINED; Genomic_DNA.
EMBL; M35850; AAA51772.1; JOINED; Genomic_DNA.
EMBL; AX453758; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
EMBL; FJ235916; ACN39559.1; -; mRNA.
EMBL; FJ235917; ACN39560.1; -; mRNA.
EMBL; AL049564; CAI43080.1; -; Genomic_DNA.
EMBL; AL158016; CAI43080.1; JOINED; Genomic_DNA.
EMBL; AL356358; CAI43080.1; JOINED; Genomic_DNA.
EMBL; AL158016; CAI40853.1; -; Genomic_DNA.
EMBL; AL049564; CAI40853.1; JOINED; Genomic_DNA.
EMBL; AL356358; CAI40853.1; JOINED; Genomic_DNA.
EMBL; AL356358; CAI40496.1; -; Genomic_DNA.
EMBL; AL049564; CAI40496.1; JOINED; Genomic_DNA.
EMBL; AL158016; CAI40496.1; JOINED; Genomic_DNA.
EMBL; CH471132; EAX05380.1; -; Genomic_DNA.
EMBL; BC132975; AAI32976.1; -; mRNA.
EMBL; L29496; AAA51770.1; -; mRNA.
EMBL; U16371; AAB60346.1; -; Genomic_DNA.
EMBL; M20260; AAA51774.1; -; mRNA.
EMBL; S79366; AAB21256.2; -; Genomic_DNA.
EMBL; S79366; AAB21257.2; -; Genomic_DNA.
CCDS; CCDS14387.1; -. [P10275-1]
CCDS; CCDS43965.1; -. [P10275-2]
PIR; A39248; A39248.
RefSeq; NP_000035.2; NM_000044.4. [P10275-1]
RefSeq; NP_001011645.1; NM_001011645.3. [P10275-2]
RefSeq; NP_001334990.1; NM_001348061.1. [P10275-3]
RefSeq; NP_001334992.1; NM_001348063.1. [P10275-4]
RefSeq; NP_001334993.1; NM_001348064.1.
UniGene; Hs.76704; -.
PDB; 1E3G; X-ray; 2.40 A; A=658-920.
PDB; 1GS4; X-ray; 1.95 A; A=671-918.
PDB; 1T5Z; X-ray; 2.30 A; A=670-920.
PDB; 1T63; X-ray; 2.07 A; A=670-919.
PDB; 1T65; X-ray; 1.66 A; A=670-920.
PDB; 1XJ7; X-ray; 2.70 A; A=664-920.
PDB; 1XOW; X-ray; 1.80 A; A=672-920, B=20-30.
PDB; 1XQ3; X-ray; 2.25 A; A=672-920.
PDB; 1Z95; X-ray; 1.80 A; A=673-918.
PDB; 2AM9; X-ray; 1.64 A; A=655-920.
PDB; 2AMA; X-ray; 1.90 A; A=655-920.
PDB; 2AMB; X-ray; 1.75 A; A=655-920.
PDB; 2AO6; X-ray; 1.89 A; A=672-920.
PDB; 2AX6; X-ray; 1.50 A; A=665-920.
PDB; 2AX7; X-ray; 1.90 A; A=665-920.
PDB; 2AX8; X-ray; 1.70 A; A=665-920.
PDB; 2AX9; X-ray; 1.65 A; A=665-920.
PDB; 2AXA; X-ray; 1.80 A; A=665-920.
PDB; 2HVC; X-ray; 2.10 A; A=670-919.
PDB; 2OZ7; X-ray; 1.80 A; A=672-920.
PDB; 2PIO; X-ray; 2.03 A; A=670-920.
PDB; 2PIP; X-ray; 1.80 A; L=670-920.
PDB; 2PIQ; X-ray; 2.40 A; A=670-920.
PDB; 2PIR; X-ray; 2.10 A; A=670-920.
PDB; 2PIT; X-ray; 1.76 A; A=670-920.
PDB; 2PIU; X-ray; 2.12 A; A=670-920.
PDB; 2PIV; X-ray; 1.95 A; A=670-920.
PDB; 2PIW; X-ray; 2.58 A; A=670-920.
PDB; 2PIX; X-ray; 2.40 A; A=670-920.
PDB; 2PKL; X-ray; 2.49 A; A=670-920.
PDB; 2PNU; X-ray; 1.65 A; A=655-920.
PDB; 2Q7I; X-ray; 1.87 A; A=664-920, B=20-30.
PDB; 2Q7J; X-ray; 1.90 A; A=664-920.
PDB; 2Q7K; X-ray; 1.80 A; A=664-920, B=20-30.
PDB; 2Q7L; X-ray; 1.92 A; A=664-920.
PDB; 2YHD; X-ray; 2.20 A; A=672-920.
PDB; 2YLO; X-ray; 2.50 A; A=665-920.
PDB; 2YLP; X-ray; 2.30 A; A=665-920.
PDB; 2YLQ; X-ray; 2.40 A; A=665-920.
PDB; 2Z4J; X-ray; 2.60 A; A=672-919.
PDB; 3B5R; X-ray; 1.80 A; A=672-920.
PDB; 3B65; X-ray; 1.80 A; A=672-920.
PDB; 3B66; X-ray; 1.65 A; A=672-920.
PDB; 3B67; X-ray; 1.90 A; A=672-920.
PDB; 3B68; X-ray; 1.90 A; A=672-920.
PDB; 3BTR; X-ray; 2.60 A; B=622-636.
PDB; 3L3X; X-ray; 1.55 A; A=671-919.
PDB; 3L3Z; X-ray; 2.00 A; A=671-919.
PDB; 3RLJ; X-ray; 1.90 A; A=672-918.
PDB; 3RLL; X-ray; 1.70 A; A=672-918.
PDB; 3V49; X-ray; 1.70 A; A=655-920, B=21-31.
PDB; 3V4A; X-ray; 1.95 A; A=672-920, B=21-31.
PDB; 3ZQT; X-ray; 2.29 A; A=665-920.
PDB; 4HLW; X-ray; 2.50 A; A=665-920.
PDB; 4K7A; X-ray; 2.44 A; A=671-919.
PDB; 4OEA; X-ray; 2.12 A; A=671-920.
PDB; 4OED; X-ray; 2.79 A; A=671-920.
PDB; 4OEY; X-ray; 1.83 A; A=671-920.
PDB; 4OEZ; X-ray; 1.80 A; A=671-920.
PDB; 4OFR; X-ray; 2.26 A; A=671-920.
PDB; 4OFU; X-ray; 2.12 A; A=671-920.
PDB; 4OGH; X-ray; 2.98 A; A=671-920.
PDB; 4OH5; X-ray; 2.00 A; A=671-920.
PDB; 4OH6; X-ray; 3.56 A; A=671-920.
PDB; 4OHA; X-ray; 1.42 A; A=671-920.
PDB; 4OIL; X-ray; 2.51 A; A=671-920.
PDB; 4OIU; X-ray; 3.01 A; A=671-920.
PDB; 4OJ9; X-ray; 3.31 A; A=671-920.
PDB; 4OJB; X-ray; 2.00 A; A=671-920.
PDB; 4OK1; X-ray; 2.09 A; A=671-920.
PDB; 4OKB; X-ray; 2.95 A; A=671-920.
PDB; 4OKT; X-ray; 2.50 A; A=671-920.
PDB; 4OKW; X-ray; 2.00 A; A=671-920.
PDB; 4OKX; X-ray; 2.10 A; A=671-920.
PDB; 4OLM; X-ray; 2.80 A; A=671-920.
PDB; 4QL8; X-ray; 2.10 A; A=663-920.
PDB; 5CJ6; X-ray; 2.07 A; A=642-920, B=21-30.
PDB; 5JJM; X-ray; 2.15 A; A/B/C/D=669-920.
PDB; 5T8E; X-ray; 2.71 A; A=672-920.
PDB; 5T8J; X-ray; 2.70 A; A=672-920.
PDB; 5V8Q; X-ray; 1.44 A; A=672-920.
PDBsum; 1E3G; -.
PDBsum; 1GS4; -.
PDBsum; 1T5Z; -.
PDBsum; 1T63; -.
PDBsum; 1T65; -.
PDBsum; 1XJ7; -.
PDBsum; 1XOW; -.
PDBsum; 1XQ3; -.
PDBsum; 1Z95; -.
PDBsum; 2AM9; -.
PDBsum; 2AMA; -.
PDBsum; 2AMB; -.
PDBsum; 2AO6; -.
PDBsum; 2AX6; -.
PDBsum; 2AX7; -.
PDBsum; 2AX8; -.
PDBsum; 2AX9; -.
PDBsum; 2AXA; -.
PDBsum; 2HVC; -.
PDBsum; 2OZ7; -.
PDBsum; 2PIO; -.
PDBsum; 2PIP; -.
PDBsum; 2PIQ; -.
PDBsum; 2PIR; -.
PDBsum; 2PIT; -.
PDBsum; 2PIU; -.
PDBsum; 2PIV; -.
PDBsum; 2PIW; -.
PDBsum; 2PIX; -.
PDBsum; 2PKL; -.
PDBsum; 2PNU; -.
PDBsum; 2Q7I; -.
PDBsum; 2Q7J; -.
PDBsum; 2Q7K; -.
PDBsum; 2Q7L; -.
PDBsum; 2YHD; -.
PDBsum; 2YLO; -.
PDBsum; 2YLP; -.
PDBsum; 2YLQ; -.
PDBsum; 2Z4J; -.
PDBsum; 3B5R; -.
PDBsum; 3B65; -.
PDBsum; 3B66; -.
PDBsum; 3B67; -.
PDBsum; 3B68; -.
PDBsum; 3BTR; -.
PDBsum; 3L3X; -.
PDBsum; 3L3Z; -.
PDBsum; 3RLJ; -.
PDBsum; 3RLL; -.
PDBsum; 3V49; -.
PDBsum; 3V4A; -.
PDBsum; 3ZQT; -.
PDBsum; 4HLW; -.
PDBsum; 4K7A; -.
PDBsum; 4OEA; -.
PDBsum; 4OED; -.
PDBsum; 4OEY; -.
PDBsum; 4OEZ; -.
PDBsum; 4OFR; -.
PDBsum; 4OFU; -.
PDBsum; 4OGH; -.
PDBsum; 4OH5; -.
PDBsum; 4OH6; -.
PDBsum; 4OHA; -.
PDBsum; 4OIL; -.
PDBsum; 4OIU; -.
PDBsum; 4OJ9; -.
PDBsum; 4OJB; -.
PDBsum; 4OK1; -.
PDBsum; 4OKB; -.
PDBsum; 4OKT; -.
PDBsum; 4OKW; -.
PDBsum; 4OKX; -.
PDBsum; 4OLM; -.
PDBsum; 4QL8; -.
PDBsum; 5CJ6; -.
PDBsum; 5JJM; -.
PDBsum; 5T8E; -.
PDBsum; 5T8J; -.
PDBsum; 5V8Q; -.
DisProt; DP00492; -.
ProteinModelPortal; P10275; -.
SMR; P10275; -.
BioGrid; 106862; 265.
CORUM; P10275; -.
DIP; DIP-125N; -.
ELM; P10275; -.
IntAct; P10275; 132.
MINT; MINT-94801; -.
STRING; 9606.ENSP00000363822; -.
BindingDB; P10275; -.
ChEMBL; CHEMBL1871; -.
DrugBank; DB02932; (2r)-N-[4-Cyano-3-(Trifluoromethyl)Phenyl]-3-[(4-Fluorophenyl)Sulfonyl]-2-Hydroxy-2-Methylpropanamide.
DrugBank; DB07422; (2S)-2-hydroxy-2-methyl-N-[4-nitro-3-(trifluoromethyl)phenyl]-3-(pentafluorophenoxy)propanamide.
DrugBank; DB07419; (2S)-3-(4-chloro-3-fluorophenoxy)-N-[4-cyano-3-(trifluoromethyl)phenyl]-2-hydroxy-2-methylpropanamide.
DrugBank; DB07423; (2S)-3-[4-(acetylamino)phenoxy]-2-hydroxy-2-methyl-N-[4-nitro-3-(trifluoromethyl)phenyl]propanamide.
DrugBank; DB07039; (2S)-N-(4-cyano-3-iodophenyl)-3-(4-cyanophenoxy)-2-hydroxy-2-methylpropanamide.
DrugBank; DB07454; (R)-3-BROMO-2-HYDROXY-2-METHYL-N-[4-NITRO-3-(TRIFLUOROMETHYL)PHENYL]PROPANAMIDE.
DrugBank; DB01128; Bicalutamide.
DrugBank; DB01541; Boldenone.
DrugBank; DB01564; Calusterone.
DrugBank; DB04839; Cyproterone acetate.
DrugBank; DB01406; Danazol.
DrugBank; DB01481; Delta1-dihydrotestosterone.
DrugBank; DB02901; Dihydrotestosterone.
DrugBank; DB01395; Drospirenone.
DrugBank; DB00858; Drostanolone.
DrugBank; DB08899; Enzalutamide.
DrugBank; DB13155; Esculin.
DrugBank; DB00687; Fludrocortisone.
DrugBank; DB02266; Flufenamic Acid.
DrugBank; DB01185; Fluoxymesterone.
DrugBank; DB00499; Flutamide.
DrugBank; DB01026; Ketoconazole.
DrugBank; DB00367; Levonorgestrel.
DrugBank; DB05234; LGD2941.
DrugBank; DB05094; MDV3100.
DrugBank; DB06710; Methyltestosterone.
DrugBank; DB02998; Methyltrienolone.
DrugBank; DB08804; Nandrolone decanoate.
DrugBank; DB00984; Nandrolone phenpropionate.
DrugBank; DB00665; Nilutamide.
DrugBank; DB09389; Norgestrel.
DrugBank; DB00621; Oxandrolone.
DrugBank; DB06412; Oxymetholone.
DrugBank; DB01708; Prasterone.
DrugBank; DB07769; S-3-(4-FLUOROPHENOXY)-2-HYDROXY-2-METHYL-N-[4-NITRO-3-(TRIFLUOROMETHYL)PHENYL]PROPANAMIDE.
DrugBank; DB00421; Spironolactone.
DrugBank; DB00624; Testosterone.
DrugBank; DB01420; Testosterone Propionate.
DrugBank; DB08867; Ulipristal.
GuidetoPHARMACOLOGY; 628; -.
SwissLipids; SLP:000001553; -.
iPTMnet; P10275; -.
PhosphoSitePlus; P10275; -.
SwissPalm; P10275; -.
BioMuta; AR; -.
DMDM; 113830; -.
EPD; P10275; -.
MaxQB; P10275; -.
PaxDb; P10275; -.
PeptideAtlas; P10275; -.
PRIDE; P10275; -.
TopDownProteomics; P10275-1; -. [P10275-1]
Ensembl; ENST00000374690; ENSP00000363822; ENSG00000169083. [P10275-1]
Ensembl; ENST00000396043; ENSP00000379358; ENSG00000169083. [P10275-2]
Ensembl; ENST00000504326; ENSP00000421155; ENSG00000169083. [P10275-3]
GeneID; 367; -.
KEGG; hsa:367; -.
UCSC; uc004dwv.3; human. [P10275-1]
UCSC; uc011mpf.2; human.
CTD; 367; -.
DisGeNET; 367; -.
EuPathDB; HostDB:ENSG00000169083.15; -.
GeneCards; AR; -.
GeneReviews; AR; -.
H-InvDB; HIX0056152; -.
HGNC; HGNC:644; AR.
HPA; CAB000001; -.
HPA; CAB065764; -.
HPA; HPA065701; -.
MalaCards; AR; -.
MIM; 300068; phenotype.
MIM; 312300; phenotype.
MIM; 313200; phenotype.
MIM; 313700; gene.
neXtProt; NX_P10275; -.
OpenTargets; ENSG00000169083; -.
Orphanet; 99429; Complete androgen insensitivity syndrome.
Orphanet; 440; Familial hypospadias.
Orphanet; 481; Kennedy disease.
Orphanet; 90797; Partial androgen insensitivity syndrome.
PharmGKB; PA57; -.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
GeneTree; ENSGT00760000118887; -.
HOVERGEN; HBG007583; -.
InParanoid; P10275; -.
KO; K08557; -.
OMA; YGDMRLE; -.
OrthoDB; EOG091G032J; -.
PhylomeDB; P10275; -.
TreeFam; TF350286; -.
Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
Reactome; R-HSA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-8940973; RUNX2 regulates osteoblast differentiation.
SignaLink; P10275; -.
SIGNOR; P10275; -.
ChiTaRS; AR; human.
EvolutionaryTrace; P10275; -.
GeneWiki; Androgen_receptor; -.
GenomeRNAi; 367; -.
PMAP-CutDB; B1AKD7; -.
PRO; PR:P10275; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000169083; -.
CleanEx; HS_AR; -.
ExpressionAtlas; P10275; baseline and differential.
Genevisible; P10275; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0016607; C:nuclear speck; IDA:CAFA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0005497; F:androgen binding; IDA:UniProtKB.
GO; GO:0004882; F:androgen receptor activity; IDA:UniProtKB.
GO; GO:0051117; F:ATPase binding; IDA:MGI.
GO; GO:0008013; F:beta-catenin binding; IDA:BHF-UCL.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0004879; F:nuclear receptor activity; IDA:BHF-UCL.
GO; GO:0070974; F:POU domain binding; IEA:Ensembl.
GO; GO:0046983; F:protein dimerization activity; NAS:UniProtKB.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; IPI:BHF-UCL.
GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:BHF-UCL.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0060520; P:activation of prostate induction by androgen receptor signaling pathway; IEA:Ensembl.
GO; GO:0030521; P:androgen receptor signaling pathway; IDA:UniProtKB.
GO; GO:0048645; P:animal organ formation; IEA:Ensembl.
GO; GO:0016049; P:cell growth; NAS:UniProtKB.
GO; GO:0008283; P:cell proliferation; NAS:UniProtKB.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0071383; P:cellular response to steroid hormone stimulus; IMP:CAFA.
GO; GO:0071394; P:cellular response to testosterone stimulus; IEA:Ensembl.
GO; GO:0060742; P:epithelial cell differentiation involved in prostate gland development; IEA:Ensembl.
GO; GO:0003382; P:epithelial cell morphogenesis; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0030522; P:intracellular receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0060599; P:lateral sprouting involved in mammary gland duct morphogenesis; IEA:Ensembl.
GO; GO:0033327; P:Leydig cell differentiation; IEA:Ensembl.
GO; GO:0048808; P:male genitalia morphogenesis; IEA:Ensembl.
GO; GO:0019102; P:male somatic sex determination; IEA:Ensembl.
GO; GO:0060749; P:mammary gland alveolus development; IEA:Ensembl.
GO; GO:0060571; P:morphogenesis of an epithelial fold; IEA:Ensembl.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IDA:BHF-UCL.
GO; GO:0045720; P:negative regulation of integrin biosynthetic process; IDA:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:CAFA.
GO; GO:0045597; P:positive regulation of cell differentiation; IMP:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:BHF-UCL.
GO; GO:0060769; P:positive regulation of epithelial cell proliferation involved in prostate gland development; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0045726; P:positive regulation of integrin biosynthetic process; IDA:BHF-UCL.
GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IEA:Ensembl.
GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:BHF-UCL.
GO; GO:0042327; P:positive regulation of phosphorylation; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045945; P:positive regulation of transcription from RNA polymerase III promoter; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0030850; P:prostate gland development; NAS:UniProtKB.
GO; GO:0060740; P:prostate gland epithelium morphogenesis; IEA:Ensembl.
GO; GO:0060736; P:prostate gland growth; IEA:Ensembl.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0051259; P:protein oligomerization; IDA:MGI.
GO; GO:0050790; P:regulation of catalytic activity; IEA:Ensembl.
GO; GO:0048638; P:regulation of developmental growth; IEA:Ensembl.
GO; GO:1903076; P:regulation of protein localization to plasma membrane; IDA:BHF-UCL.
GO; GO:0003073; P:regulation of systemic arterial blood pressure; IEA:Ensembl.
GO; GO:0072520; P:seminiferous tubule development; IEA:Ensembl.
GO; GO:0007548; P:sex differentiation; NAS:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0007338; P:single fertilization; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0060748; P:tertiary branching involved in mammary gland duct morphogenesis; IEA:Ensembl.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006351; P:transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006810; P:transport; TAS:ProtInc.
Gene3D; 1.10.565.10; -; 1.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR001103; Andrgn_rcpt.
InterPro; IPR035500; NHR_like_dom_sf.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001628; Znf_hrmn_rcpt.
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; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Complete proteome;
Cytoplasm; Disease mutation; DNA-binding; Isopeptide bond;
Lipid-binding; Lipoprotein; Metal-binding; Neurodegeneration; Nucleus;
Palmitate; Phosphoprotein; Polymorphism; Pseudohermaphroditism;
Receptor; Reference proteome; Steroid-binding; Transcription;
Transcription regulation; Triplet repeat expansion; Ubl conjugation;
Zinc; Zinc-finger.
CHAIN 1 920 Androgen receptor.
/FTId=PRO_0000053704.
DNA_BIND 560 632 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 560 580 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 596 620 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 1 559 Modulating.
REGION 552 919 Interaction with LPXN.
{ECO:0000269|PubMed:18451096}.
REGION 572 662 Interaction with HIPK3. {ECO:0000250}.
REGION 592 919 Interaction with CCAR1.
{ECO:0000269|PubMed:23887938}.
REGION 625 919 Interaction with KAT7.
{ECO:0000269|PubMed:10930412}.
REGION 691 919 Ligand-binding.
COMPBIAS 58 120 Gln-rich.
COMPBIAS 58 80 Poly-Gln.
COMPBIAS 86 91 Poly-Gln.
COMPBIAS 195 199 Poly-Gln.
COMPBIAS 374 383 Poly-Pro.
COMPBIAS 398 404 Poly-Ala.
COMPBIAS 451 473 Poly-Gly.
BINDING 706 706 Androgen.
BINDING 753 753 Androgen.
BINDING 878 878 Androgen.
SITE 721 721 Interaction with coactivator LXXL motif.
SITE 898 898 Interaction with coactivator FXXLF motif.
MOD_RES 83 83 Phosphoserine; by CDK9.
{ECO:0000269|PubMed:20980437}.
MOD_RES 96 96 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 225 225 Phosphotyrosine; by CSK.
{ECO:0000269|PubMed:17045208}.
MOD_RES 258 258 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 269 269 Phosphotyrosine; by CSK and TNK2.
{ECO:0000269|PubMed:17045208,
ECO:0000269|PubMed:17494760,
ECO:0000269|PubMed:20623637}.
MOD_RES 309 309 Phosphotyrosine; by CSK.
{ECO:0000269|PubMed:17045208}.
MOD_RES 348 348 Phosphotyrosine; by CSK.
{ECO:0000269|PubMed:17045208}.
MOD_RES 359 359 Phosphotyrosine; by CSK.
{ECO:0000269|PubMed:17045208}.
MOD_RES 364 364 Phosphotyrosine; by CSK.
{ECO:0000269|PubMed:17045208}.
MOD_RES 365 365 Phosphotyrosine; by CSK and TNK2.
{ECO:0000269|PubMed:17045208,
ECO:0000269|PubMed:17494760}.
MOD_RES 395 395 Phosphotyrosine; by CSK.
{ECO:0000269|PubMed:17045208}.
MOD_RES 535 535 Phosphotyrosine; by CSK.
{ECO:0000269|PubMed:17045208}.
MOD_RES 552 552 Phosphotyrosine; by CSK.
{ECO:0000269|PubMed:17045208}.
MOD_RES 651 651 Phosphoserine; by STK4/MST1.
{ECO:0000269|PubMed:21512132}.
MOD_RES 916 916 Phosphotyrosine; by CSK.
{ECO:0000269|PubMed:17045208}.
CROSSLNK 388 388 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:11121022}.
CROSSLNK 521 521 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:11121022}.
CROSSLNK 846 846 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:19345326}.
CROSSLNK 848 848 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:19345326}.
VAR_SEQ 1 532 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_036889.
VAR_SEQ 533 539 GPYGDMR -> MILWLHS (in isoform 2).
{ECO:0000305}.
/FTId=VSP_036890.
VAR_SEQ 629 644 ARKLKKLGNLKLQEEG -> EKFRVGNCKHLKMTRP (in
isoform 3).
/FTId=VSP_058166.
VAR_SEQ 630 648 RKLKKLGNLKLQEEGEASS -> AVVVSERILRVFGVSEWL
P (in isoform 4).
/FTId=VSP_058167.
VAR_SEQ 645 920 Missing (in isoform 3).
/FTId=VSP_058168.
VAR_SEQ 649 920 Missing (in isoform 4).
/FTId=VSP_058169.
VARIANT 2 2 E -> K (in PAIS; dbSNP:rs104894742).
{ECO:0000269|PubMed:8823308}.
/FTId=VAR_004679.
VARIANT 54 54 L -> S (in prostate cancer).
/FTId=VAR_004680.
VARIANT 57 57 L -> Q (in prostate cancer;
dbSNP:rs78686797).
{ECO:0000269|PubMed:19244107}.
/FTId=VAR_004681.
VARIANT 64 64 Q -> R (in prostate cancer).
/FTId=VAR_009711.
VARIANT 114 114 Q -> H (in prostate cancer).
/FTId=VAR_009712.
VARIANT 182 182 K -> R (in prostate cancer).
/FTId=VAR_009713.
VARIANT 196 196 Q -> R (in AIS).
{ECO:0000269|PubMed:9255042}.
/FTId=VAR_009224.
VARIANT 207 207 S -> R (in dbSNP:rs374549047).
{ECO:0000269|PubMed:8213813}.
/FTId=VAR_009714.
VARIANT 216 216 G -> R (functional polymorphism; 20%
lower transactivation capacity;
dbSNP:rs199554641).
{ECO:0000269|PubMed:27535533,
ECO:0000269|PubMed:9788719}.
/FTId=VAR_009715.
VARIANT 257 257 L -> P (in AIS).
{ECO:0000269|PubMed:9610419}.
/FTId=VAR_009225.
VARIANT 268 268 M -> T (in prostate cancer).
/FTId=VAR_009716.
VARIANT 271 271 P -> S (in prostate cancer).
/FTId=VAR_009717.
VARIANT 342 342 P -> L (in prostate cancer;
dbSNP:rs138454018).
{ECO:0000269|PubMed:7511268}.
/FTId=VAR_009718.
VARIANT 392 392 P -> R (in AIS; dbSNP:rs773996740).
{ECO:0000269|PubMed:10571951}.
/FTId=VAR_009226.
VARIANT 392 392 P -> S (in AIS; dbSNP:rs201934623).
/FTId=VAR_009227.
VARIANT 445 445 Q -> R (in AIS; unknown pathological
significance).
{ECO:0000269|PubMed:10571951}.
/FTId=VAR_009228.
VARIANT 492 492 G -> S (in AIS).
/FTId=VAR_009719.
VARIANT 529 529 D -> G (in prostate cancer).
/FTId=VAR_009720.
VARIANT 548 548 L -> F (in PAIS; dbSNP:rs139524801).
/FTId=VAR_009721.
VARIANT 549 549 P -> S (in AIS; dbSNP:rs137852588).
{ECO:0000269|PubMed:8683794}.
/FTId=VAR_009722.
VARIANT 560 560 C -> Y (in AIS).
{ECO:0000269|PubMed:1316540}.
/FTId=VAR_009723.
VARIANT 569 569 G -> V (in a patient with isolated
hypospadias).
{ECO:0000269|PubMed:7673412}.
/FTId=VAR_009725.
VARIANT 569 569 G -> W (in PAIS).
{ECO:0000269|PubMed:7910529}.
/FTId=VAR_009726.
VARIANT 572 572 Y -> C (in AIS).
{ECO:0000269|PubMed:9544375}.
/FTId=VAR_009727.
VARIANT 574 574 A -> D (in AIS).
/FTId=VAR_009728.
VARIANT 575 575 L -> P (in prostate cancer).
/FTId=VAR_009729.
VARIANT 576 576 T -> A (in prostate cancer).
{ECO:0000269|PubMed:10706109}.
/FTId=VAR_009730.
VARIANT 577 577 C -> F (in AIS).
{ECO:0000269|PubMed:14756668}.
/FTId=VAR_009731.
VARIANT 577 577 C -> R (in AIS).
{ECO:0000269|PubMed:1316540}.
/FTId=VAR_009732.
VARIANT 580 580 C -> F (in AIS; reduced transcription and
DNA binding; dbSNP:rs137852586).
{ECO:0000269|PubMed:8809734}.
/FTId=VAR_009733.
VARIANT 580 580 C -> Y (in AIS).
/FTId=VAR_009734.
VARIANT 581 581 K -> R (in prostate cancer).
{ECO:0000269|PubMed:10706109}.
/FTId=VAR_009735.
VARIANT 582 582 V -> F (in AIS).
{ECO:0000269|PubMed:8224266,
ECO:0000269|Ref.110}.
/FTId=VAR_009736.
VARIANT 583 583 F -> S (in PAIS).
{ECO:0000269|PubMed:7981687}.
/FTId=VAR_009737.
VARIANT 583 583 F -> Y (in PAIS; dbSNP:rs137852587).
{ECO:0000269|PubMed:8809734}.
/FTId=VAR_009738.
VARIANT 583 583 Missing (in AIS).
{ECO:0000269|PubMed:8162033}.
/FTId=VAR_009739.
VARIANT 586 586 R -> K (in AIS).
/FTId=VAR_009740.
VARIANT 587 587 A -> V (in prostate cancer; somatic
mutation). {ECO:0000269|PubMed:10706109}.
/FTId=VAR_009741.
VARIANT 588 588 A -> S (in prostate cancer; somatic
mutation).
/FTId=VAR_009742.
VARIANT 597 597 A -> T (in AIS; abolishes dimerization;
dbSNP:rs137852569).
{ECO:0000269|PubMed:10590024,
ECO:0000269|PubMed:7649358}.
/FTId=VAR_009743.
VARIANT 598 598 S -> G (in PAIS; associated with P-618 in
a PAIS patient; normal androgen binding;
does not activate transcription; impairs
DNA binding; dbSNP:rs142280455).
{ECO:0000269|PubMed:1316540}.
/FTId=VAR_009744.
VARIANT 598 598 S -> T (in a patient with severe
hypospadias).
{ECO:0000269|PubMed:10092153}.
/FTId=VAR_009745.
VARIANT 602 602 C -> F (in AIS).
{ECO:0000269|PubMed:7981689}.
/FTId=VAR_009746.
VARIANT 605 605 D -> Y (in PAIS).
{ECO:0000269|PubMed:7981687}.
/FTId=VAR_009747.
VARIANT 608 608 R -> Q (in PAIS and breast cancer;
dbSNP:rs137852573).
{ECO:0000269|PubMed:10221692,
ECO:0000269|PubMed:1303262,
ECO:0000269|PubMed:9039340,
ECO:0000269|PubMed:9543136}.
/FTId=VAR_004684.
VARIANT 609 609 R -> K (in PAIS and breast cancer;
defective nuclear localization;
dbSNP:rs137852576).
{ECO:0000269|PubMed:1424203,
ECO:0000269|PubMed:8281139,
ECO:0000269|PubMed:9196614}.
/FTId=VAR_004685.
VARIANT 611 611 N -> T (in PAIS).
{ECO:0000269|PubMed:9039340}.
/FTId=VAR_009748.
VARIANT 612 612 C -> Y (in AIS).
/FTId=VAR_009749.
VARIANT 616 616 R -> H (in AIS and PAIS;
dbSNP:rs754201976).
{ECO:0000269|PubMed:7970939,
ECO:0000269|PubMed:8162033,
ECO:0000269|PubMed:8413310,
ECO:0000269|PubMed:9698822}.
/FTId=VAR_009751.
VARIANT 616 616 R -> P (in AIS).
/FTId=VAR_009752.
VARIANT 616 616 Missing (in AIS).
{ECO:0000269|PubMed:8162033}.
/FTId=VAR_009750.
VARIANT 617 617 L -> P (in AIS).
{ECO:0000269|PubMed:8647313}.
/FTId=VAR_009753.
VARIANT 617 617 L -> R (in PAIS).
{ECO:0000269|PubMed:8126121}.
/FTId=VAR_009754.
VARIANT 618 618 R -> P (in AIS and PAIS; associated with
G-598 in a PAIS patient; loss of DNA-
binding activity).
{ECO:0000269|PubMed:1316540,
ECO:0000269|PubMed:1999491}.
/FTId=VAR_009755.
VARIANT 620 620 C -> Y (in prostate cancer; loss of DNA
binding; somatic mutation).
{ECO:0000269|PubMed:10598582,
ECO:0000269|PubMed:10706109}.
/FTId=VAR_009756.
VARIANT 630 630 R -> Q (in prostate cancer).
{ECO:0000269|PubMed:9184448}.
/FTId=VAR_009757.
VARIANT 631 631 K -> T (in prostate cancer).
/FTId=VAR_009758.
VARIANT 646 646 A -> D (in dbSNP:rs1800053).
{ECO:0000269|PubMed:9554755}.
/FTId=VAR_004686.
VARIANT 648 648 S -> N (in prostate cancer;
dbSNP:rs137852584).
/FTId=VAR_009760.
VARIANT 665 665 I -> N (in AIS and PAIS).
/FTId=VAR_004687.
VARIANT 671 671 Q -> R (in prostate cancer).
/FTId=VAR_009761.
VARIANT 672 672 P -> H (in PAIS).
/FTId=VAR_009762.
VARIANT 673 673 I -> T (in prostate cancer).
/FTId=VAR_009763.
VARIANT 678 678 L -> P (in AIS; dbSNP:rs137852579).
{ECO:0000269|PubMed:7537149}.
/FTId=VAR_004688.
VARIANT 682 682 E -> K (in AIS).
{ECO:0000269|PubMed:10221692,
ECO:0000269|PubMed:8325950}.
/FTId=VAR_009764.
VARIANT 683 683 P -> T (in PAIS).
{ECO:0000269|PubMed:11587068}.
/FTId=VAR_013474.
VARIANT 684 684 G -> A (in prostate cancer).
{ECO:0000269|PubMed:10629558,
ECO:0000269|PubMed:9000575}.
/FTId=VAR_009765.
VARIANT 685 685 V -> I (in AIS).
/FTId=VAR_009766.
VARIANT 687 687 C -> R (in PAIS).
/FTId=VAR_009767.
VARIANT 688 688 A -> V (in PAIS).
/FTId=VAR_009768.
VARIANT 689 689 G -> E (in AIS).
/FTId=VAR_009769.
VARIANT 691 691 Missing (in PAIS). {ECO:0000269|Ref.118}.
/FTId=VAR_009770.
VARIANT 693 693 Missing (in AIS).
/FTId=VAR_004689.
VARIANT 696 696 D -> H (in AIS).
{ECO:0000269|PubMed:1775137}.
/FTId=VAR_004690.
VARIANT 696 696 D -> N (in AIS; almost complete loss of
androgen binding and transcription
activation).
{ECO:0000269|PubMed:16595706,
ECO:0000269|PubMed:1775137}.
/FTId=VAR_004691.
VARIANT 696 696 D -> V (in AIS).
{ECO:0000269|PubMed:9554754}.
/FTId=VAR_004692.
VARIANT 701 701 L -> M (in AIS).
/FTId=VAR_009771.
VARIANT 702 702 L -> F (in AIS).
/FTId=VAR_009772.
VARIANT 702 702 L -> H (in AIS and prostate cancer;
dbSNP:rs864622007).
{ECO:0000269|PubMed:10569618,
ECO:0000269|PubMed:8274409,
ECO:0000269|PubMed:9438000}.
/FTId=VAR_009773.
VARIANT 703 703 S -> A (in AIS).
/FTId=VAR_009774.
VARIANT 704 704 S -> C (in AIS).
/FTId=VAR_009775.
VARIANT 704 704 S -> G (in PAIS and AIS).
{ECO:0000269|PubMed:9302173}.
/FTId=VAR_004693.
VARIANT 706 706 N -> S (in AIS).
{ECO:0000269|PubMed:1480178,
ECO:0000269|PubMed:7671849}.
/FTId=VAR_009776.
VARIANT 706 706 N -> Y (in AIS).
{ECO:0000269|PubMed:11744994}.
/FTId=VAR_013475.
VARIANT 708 708 L -> R (in AIS; dbSNP:rs137852585).
{ECO:0000269|PubMed:8626869}.
/FTId=VAR_004694.
VARIANT 709 709 G -> A (in PAIS).
{ECO:0000269|PubMed:7981687,
ECO:0000269|PubMed:9329414}.
/FTId=VAR_009777.
VARIANT 709 709 G -> V (in AIS).
/FTId=VAR_009778.
VARIANT 711 711 R -> T (in AIS).
/FTId=VAR_009779.
VARIANT 712 712 Q -> E (in PAIS).
{ECO:0000269|PubMed:11587068}.
/FTId=VAR_013476.
VARIANT 713 713 L -> F (in PAIS; dbSNP:rs137852595).
/FTId=VAR_009780.
VARIANT 716 716 V -> M (in prostate cancer; gain in
function). {ECO:0000269|PubMed:8145761}.
/FTId=VAR_009781.
VARIANT 718 718 K -> E (in prostate cancer).
/FTId=VAR_009782.
VARIANT 721 721 K -> E (in prostate cancer; found in bone
metastases).
/FTId=VAR_009783.
VARIANT 722 722 A -> T (in prostate cancer; somatic
mutation; dbSNP:rs137852583).
/FTId=VAR_009784.
VARIANT 723 723 L -> F (in AIS).
/FTId=VAR_009785.
VARIANT 724 724 P -> S (in AIS).
/FTId=VAR_009786.
VARIANT 725 725 G -> D (in AIS and prostate cancer).
/FTId=VAR_009787.
VARIANT 726 726 F -> L (in a patient with severe
hypospadias).
{ECO:0000269|PubMed:10092153,
ECO:0000269|PubMed:7671849}.
/FTId=VAR_009788.
VARIANT 727 727 R -> L (in prostate cancer;
dbSNP:rs137852593).
{ECO:0000269|PubMed:8530589}.
/FTId=VAR_009789.
VARIANT 728 728 N -> K (in AIS; dbSNP:rs768869912).
{ECO:0000269|PubMed:7993455}.
/FTId=VAR_009790.
VARIANT 729 729 L -> S (in PAIS).
/FTId=VAR_009791.
VARIANT 731 731 V -> M (in prostate cancer; increases
transcription activation;
dbSNP:rs137852571).
{ECO:0000269|PubMed:15525515,
ECO:0000269|PubMed:1631125,
ECO:0000269|PubMed:7591265}.
/FTId=VAR_004695.
VARIANT 733 733 D -> N (in AIS).
{ECO:0000269|PubMed:9252933}.
/FTId=VAR_004696.
VARIANT 733 733 D -> Y (in AIS).
/FTId=VAR_004697.
VARIANT 734 734 Q -> H (in PAIS).
/FTId=VAR_009792.
VARIANT 738 738 I -> T (in PAIS).
{ECO:0000269|PubMed:7671849}.
/FTId=VAR_009793.
VARIANT 742 742 W -> R (in AIS).
{ECO:0000269|PubMed:1464650}.
/FTId=VAR_009794.
VARIANT 743 743 M -> I (in PAIS).
{ECO:0000269|PubMed:8824883}.
/FTId=VAR_004698.
VARIANT 743 743 M -> V (in PAIS).
{ECO:0000269|PubMed:7970939}.
/FTId=VAR_009795.
VARIANT 744 744 G -> E (in AIS; dbSNP:rs137852600).
{ECO:0000269|PubMed:11587068}.
/FTId=VAR_013477.
VARIANT 744 744 G -> V (in PAIS and AIS;
dbSNP:rs137852600).
{ECO:0000269|PubMed:8096390,
ECO:0000269|PubMed:8325932,
ECO:0000269|PubMed:9768671,
ECO:0000269|Ref.110}.
/FTId=VAR_004699.
VARIANT 745 745 L -> F (in AIS and prostate cancer).
/FTId=VAR_009796.
VARIANT 746 746 M -> T (in PAIS).
{ECO:0000269|PubMed:7970939}.
/FTId=VAR_009797.
VARIANT 747 747 V -> M (in PAIS).
/FTId=VAR_009798.
VARIANT 749 749 A -> D (in PAIS).
/FTId=VAR_009799.
VARIANT 749 749 A -> T (in prostate cancer).
/FTId=VAR_009800.
VARIANT 749 749 A -> V (in prostate cancer).
/FTId=VAR_009801.
VARIANT 750 750 M -> I (in prostate cancer).
/FTId=VAR_009802.
VARIANT 750 750 M -> V (in PAIS and AIS).
{ECO:0000269|PubMed:1480178,
ECO:0000269|PubMed:1487249,
ECO:0000269|PubMed:8990010}.
/FTId=VAR_004700.
VARIANT 751 751 G -> D (in AIS; loss of androgen
binding). {ECO:0000269|PubMed:9328206}.
/FTId=VAR_004701.
VARIANT 751 751 G -> S (in prostate cancer).
/FTId=VAR_009803.
VARIANT 752 752 W -> R (in AIS).
/FTId=VAR_009804.
VARIANT 753 753 R -> Q (in AIS).
{ECO:0000269|PubMed:9544375,
ECO:0000269|PubMed:9698822}.
/FTId=VAR_004702.
VARIANT 755 755 F -> L (in PAIS and prostate cancer).
{ECO:0000269|PubMed:7981687,
ECO:0000269|PubMed:9039340}.
/FTId=VAR_009805.
VARIANT 755 755 F -> V (in AIS).
{ECO:0000269|PubMed:8103398,
ECO:0000269|Ref.110}.
/FTId=VAR_004703.
VARIANT 756 756 T -> A (in prostate cancer).
/FTId=VAR_009806.
VARIANT 757 757 N -> S (in PAIS; dbSNP:rs141425171).
/FTId=VAR_009807.
VARIANT 758 758 V -> A (in prostate cancer).
{ECO:0000269|PubMed:10706109}.
/FTId=VAR_009808.
VARIANT 759 759 N -> T (in PAIS; 50% reduction in
transactivation).
{ECO:0000269|PubMed:9607727}.
/FTId=VAR_009809.
VARIANT 760 760 S -> F (in AIS).
{ECO:0000269|PubMed:1480178}.
/FTId=VAR_009810.
VARIANT 760 760 S -> P (in prostate cancer).
/FTId=VAR_009811.
VARIANT 763 763 L -> F (in AIS; loss of androgen
binding). {ECO:0000269|PubMed:9328206}.
/FTId=VAR_004704.
VARIANT 764 764 Y -> C (in PAIS and prostate cancer;
partial loss of androgen binding;
dbSNP:rs137852567).
{ECO:0000269|PubMed:16595706,
ECO:0000269|PubMed:2010552,
ECO:0000269|PubMed:7581399}.
/FTId=VAR_004705.
VARIANT 764 764 Y -> H (in AIS).
{ECO:0000269|PubMed:7671849}.
/FTId=VAR_009812.
VARIANT 765 765 F -> L (in AIS).
{ECO:0000269|PubMed:7970939}.
/FTId=VAR_009813.
VARIANT 766 766 A -> T (in AIS; loss of androgen
binding). {ECO:0000269|PubMed:1426313,
ECO:0000269|PubMed:9252933,
ECO:0000269|PubMed:9328206,
ECO:0000269|PubMed:9856504}.
/FTId=VAR_004707.
VARIANT 766 766 A -> V (in AIS).
/FTId=VAR_009814.
VARIANT 767 767 P -> S (in AIS).
/FTId=VAR_009815.
VARIANT 768 768 D -> E (in AIS). {ECO:0000269|Ref.110}.
/FTId=VAR_009816.
VARIANT 769 769 L -> P (in AIS).
/FTId=VAR_009817.
VARIANT 772 772 N -> H (in PAIS).
{ECO:0000269|PubMed:7981687}.
/FTId=VAR_009818.
VARIANT 773 773 E -> A (in PAIS).
{ECO:0000269|PubMed:10022458}.
/FTId=VAR_009819.
VARIANT 773 773 E -> G (in PAIS).
{ECO:0000269|PubMed:9196614}.
/FTId=VAR_009820.
VARIANT 775 775 R -> C (in AIS; frequent mutation; loss
of androgen binding; dbSNP:rs137852562).
{ECO:0000269|PubMed:1609793,
ECO:0000269|PubMed:1856263,
ECO:0000269|PubMed:2082179,
ECO:0000269|PubMed:8990010,
ECO:0000269|PubMed:9544375}.
/FTId=VAR_004709.
VARIANT 775 775 R -> H (in AIS and PAIS; almost complete
loss of androgen binding;
dbSNP:rs137852572).
{ECO:0000269|PubMed:1480178,
ECO:0000269|PubMed:1609793,
ECO:0000269|PubMed:16595706,
ECO:0000269|PubMed:7671849}.
/FTId=VAR_004708.
VARIANT 780 780 R -> W (in AIS).
{ECO:0000269|PubMed:7581399,
ECO:0000269|PubMed:7981687,
ECO:0000269|PubMed:9007482}.
/FTId=VAR_004710.
VARIANT 781 781 M -> I (in PAIS and AIS;
dbSNP:rs137852589).
{ECO:0000269|PubMed:8768864,
ECO:0000269|PubMed:8824883,
ECO:0000269|PubMed:8990010}.
/FTId=VAR_004711.
VARIANT 783 783 S -> N (in prostate cancer; somatic
mutation).
/FTId=VAR_009821.
VARIANT 785 785 C -> Y (in AIS; loss of androgen binding
and of transactivation).
{ECO:0000269|PubMed:9856504}.
/FTId=VAR_004712.
VARIANT 788 788 M -> V (in AIS; dbSNP:rs137852570).
{ECO:0000269|PubMed:1569163}.
/FTId=VAR_004713.
VARIANT 789 789 R -> S (in AIS).
/FTId=VAR_009822.
VARIANT 791 791 L -> F (in AIS).
{ECO:0000269|PubMed:7962294}.
/FTId=VAR_009823.
VARIANT 792 792 S -> P (in prostate cancer).
/FTId=VAR_009824.
VARIANT 794 794 E -> D. {ECO:0000269|PubMed:8213813}.
/FTId=VAR_009825.
VARIANT 795 795 F -> S (in AIS).
{ECO:0000269|PubMed:8990010}.
/FTId=VAR_004714.
VARIANT 799 799 Q -> E (in PAIS, AIS and prostate cancer;
reduced transcription activation;
dbSNP:rs137852591).
{ECO:0000269|PubMed:16595706,
ECO:0000269|PubMed:7511268,
ECO:0000269|PubMed:7671849,
ECO:0000269|PubMed:8628719,
ECO:0000269|PubMed:8824883,
ECO:0000269|PubMed:9851768}.
/FTId=VAR_004715.
VARIANT 807 807 C -> Y (in PAIS).
/FTId=VAR_009826.
VARIANT 808 808 M -> R (in AIS; loss of transactivation).
{ECO:0000269|PubMed:8281140}.
/FTId=VAR_004716.
VARIANT 808 808 M -> T (in PAIS; dbSNP:rs137852592).
{ECO:0000269|PubMed:10543676}.
/FTId=VAR_009827.
VARIANT 808 808 M -> V (in AIS; 25% androgen binding).
{ECO:0000269|PubMed:7581399}.
/FTId=VAR_004717.
VARIANT 813 813 L -> F (in AIS).
{ECO:0000269|PubMed:10458483}.
/FTId=VAR_009828.
VARIANT 815 815 S -> N (in AIS and PAIS).
/FTId=VAR_004718.
VARIANT 821 821 G -> A (in AIS).
{ECO:0000269|PubMed:9610419}.
/FTId=VAR_009829.
VARIANT 822 822 L -> V (in PAIS).
/FTId=VAR_009830.
VARIANT 828 828 F -> V (in PAIS).
{ECO:0000269|PubMed:11587068}.
/FTId=VAR_013478.
VARIANT 831 831 L -> P (in prostate cancer).
/FTId=VAR_009831.
VARIANT 832 832 R -> L (in AIS).
{ECO:0000269|PubMed:7633398}.
/FTId=VAR_004719.
VARIANT 832 832 R -> Q (in AIS; loss of androgen
binding). {ECO:0000269|PubMed:10458483,
ECO:0000269|PubMed:2082179,
ECO:0000269|PubMed:7633398}.
/FTId=VAR_004720.
VARIANT 835 835 Y -> C (in AIS; loss of androgen
binding). {ECO:0000269|PubMed:1464650}.
/FTId=VAR_009832.
VARIANT 841 841 R -> C (in AIS; dbSNP:rs137852577).
{ECO:0000269|PubMed:8040309,
ECO:0000269|PubMed:8824883,
ECO:0000269|PubMed:9768671}.
/FTId=VAR_004721.
VARIANT 841 841 R -> G (in PAIS).
{ECO:0000269|PubMed:9856504}.
/FTId=VAR_004722.
VARIANT 841 841 R -> H (in AIS; dbSNP:rs9332969).
{ECO:0000269|PubMed:7909256,
ECO:0000269|PubMed:8040309,
ECO:0000269|PubMed:8126121,
ECO:0000269|PubMed:8205256,
ECO:0000269|PubMed:8325950,
ECO:0000269|PubMed:8830623,
ECO:0000269|PubMed:9039340}.
/FTId=VAR_004723.
VARIANT 841 841 R -> S (in PAIS).
{ECO:0000269|PubMed:10502786}.
/FTId=VAR_009229.
VARIANT 842 842 I -> S (in PAIS).
/FTId=VAR_009833.
VARIANT 843 843 I -> T (in AIS; dbSNP:rs9332970).
{ECO:0000269|PubMed:8325950,
ECO:0000269|PubMed:9039340}.
/FTId=VAR_004724.
VARIANT 847 847 R -> G (in prostate cancer).
{ECO:0000269|PubMed:10706109}.
/FTId=VAR_009834.
VARIANT 855 855 R -> K (in PAIS).
/FTId=VAR_009835.
VARIANT 856 856 R -> C (in AIS).
{ECO:0000269|PubMed:1480178,
ECO:0000269|PubMed:7581399,
ECO:0000269|PubMed:9001799,
ECO:0000269|PubMed:9255042,
ECO:0000269|Ref.110}.
/FTId=VAR_004725.
VARIANT 856 856 R -> H (in AIS; strongly reduced
transcription activation;
dbSNP:rs9332971).
{ECO:0000269|PubMed:16595706,
ECO:0000269|PubMed:8097257,
ECO:0000269|PubMed:8824883,
ECO:0000269|PubMed:9039340,
ECO:0000269|PubMed:9106550}.
/FTId=VAR_004726.
VARIANT 857 857 F -> L (in AIS; dbSNP:rs137852598).
/FTId=VAR_009836.
VARIANT 864 864 L -> R (in AIS).
/FTId=VAR_009837.
VARIANT 865 865 D -> G (in AIS).
{ECO:0000269|PubMed:1480178}.
/FTId=VAR_009838.
VARIANT 865 865 D -> N (in AIS; loss of androgen
binding). {ECO:0000269|PubMed:9328206}.
/FTId=VAR_004727.
VARIANT 866 866 S -> P (in AIS; dbSNP:rs137852597).
/FTId=VAR_009839.
VARIANT 867 867 V -> E (in AIS).
/FTId=VAR_004728.
VARIANT 867 867 V -> L (in PAIS; dbSNP:rs137852564).
{ECO:0000269|PubMed:1424203,
ECO:0000269|PubMed:8325950,
ECO:0000269|PubMed:8446106}.
/FTId=VAR_004729.
VARIANT 867 867 V -> M (in AIS and prostate cancer;
dbSNP:rs137852564).
{ECO:0000269|PubMed:2082179,
ECO:0000269|PubMed:2594783,
ECO:0000269|PubMed:8446106,
ECO:0000269|PubMed:9039340}.
/FTId=VAR_004730.
VARIANT 870 870 I -> M (in PAIS; dbSNP:rs137852574).
{ECO:0000269|PubMed:8097257,
ECO:0000269|PubMed:8824883}.
/FTId=VAR_004731.
VARIANT 871 871 A -> G (in PAIS).
{ECO:0000269|PubMed:9329414}.
/FTId=VAR_009840.
VARIANT 871 871 A -> V (in PAIS; dbSNP:rs143040492).
{ECO:0000269|PubMed:8033918}.
/FTId=VAR_009841.
VARIANT 872 872 R -> G (in AIS).
{ECO:0000269|PubMed:10022458}.
/FTId=VAR_009842.
VARIANT 875 875 H -> R (in AIS).
{ECO:0000269|PubMed:11587068}.
/FTId=VAR_013479.
VARIANT 875 875 H -> Y (in prostate cancer; increases
affinity for testosterone and androgen
sensitivity; increased transcription
activation; dbSNP:rs137852581).
{ECO:0000269|PubMed:17591767}.
/FTId=VAR_009843.
VARIANT 878 878 T -> A (in prostate cancer; found in bone
metastases; alters receptor specificity
so that transcription is activated by
antiandrogens such as cyproterone
acetate; dbSNP:rs137852578).
{ECO:0000269|PubMed:10363963,
ECO:0000269|PubMed:10569618,
ECO:0000269|PubMed:1562539,
ECO:0000269|PubMed:16129672,
ECO:0000269|PubMed:17311914,
ECO:0000269|PubMed:2260966,
ECO:0000269|PubMed:8187068,
ECO:0000269|PubMed:8274409,
ECO:0000269|PubMed:8827083}.
/FTId=VAR_004732.
VARIANT 878 878 T -> S (in prostate cancer;
dbSNP:rs137852580).
/FTId=VAR_009844.
VARIANT 880 880 D -> Y (in AIS).
{ECO:0000269|PubMed:11587068}.
/FTId=VAR_013480.
VARIANT 881 881 L -> Q (in prostate cancer).
/FTId=VAR_009845.
VARIANT 882 882 L -> V (in AIS).
{ECO:0000269|PubMed:7641413}.
/FTId=VAR_009846.
VARIANT 887 887 M -> V (in AIS; dbSNP:rs755226547).
/FTId=VAR_009847.
VARIANT 890 890 V -> M (in AIS and PAIS).
{ECO:0000269|PubMed:8126121,
ECO:0000269|PubMed:9160185}.
/FTId=VAR_009848.
VARIANT 891 891 D -> N (in prostate cancer).
{ECO:0000269|PubMed:10363963}.
/FTId=VAR_009849.
VARIANT 892 892 F -> L (in prostate cancer).
/FTId=VAR_009850.
VARIANT 893 893 P -> L (in AIS).
{ECO:0000269|PubMed:10221770,
ECO:0000269|PubMed:10404311,
ECO:0000269|Ref.176}.
/FTId=VAR_004733.
VARIANT 896 896 M -> T (in AIS; low androgen binding and
transactivation).
{ECO:0000269|PubMed:16129672,
ECO:0000269|PubMed:9856504}.
/FTId=VAR_004734.
VARIANT 897 897 A -> T (in prostate cancer).
/FTId=VAR_009851.
VARIANT 899 899 I -> T (in AIS).
/FTId=VAR_009852.
VARIANT 903 903 Q -> R (in prostate cancer;
dbSNP:rs137852582).
/FTId=VAR_009853.
VARIANT 904 904 V -> M (in PAIS).
/FTId=VAR_009854.
VARIANT 905 905 P -> H (in AIS).
/FTId=VAR_009855.
VARIANT 905 905 P -> S (in AIS).
/FTId=VAR_009856.
VARIANT 908 908 L -> F (in AIS; almost complete loss of
transcription activation).
{ECO:0000269|PubMed:16595706,
ECO:0000269|PubMed:9328206}.
/FTId=VAR_004735.
VARIANT 910 910 G -> E (in prostate cancer).
/FTId=VAR_009857.
VARIANT 910 910 G -> R (in PAIS).
{ECO:0000269|PubMed:8550758}.
/FTId=VAR_009858.
VARIANT 911 911 K -> R (in prostate cancer).
{ECO:0000269|PubMed:9438000}.
/FTId=VAR_009859.
VARIANT 912 912 V -> L (in PAIS).
{ECO:0000269|PubMed:10470409}.
/FTId=VAR_009860.
VARIANT 914 914 P -> S (in PAIS).
/FTId=VAR_004736.
VARIANT 917 917 F -> L (in AIS).
{ECO:0000269|PubMed:9302173}.
/FTId=VAR_009861.
VARIANT 918 918 H -> R (in AIS).
/FTId=VAR_009862.
VARIANT 920 920 Q -> R (in prostate cancer).
/FTId=VAR_009863.
MUTAGEN 83 83 S->A: Reduced cell growth.
{ECO:0000269|PubMed:20980437}.
MUTAGEN 225 225 Y->F: Decrease of CSK-induced
phosphorylation.
{ECO:0000269|PubMed:17045208}.
MUTAGEN 269 269 Y->F: Decrease of CSK-induced
phosphorylation and phosphorylation by
TNK2. Complete loss of TNK2-dependent
phosphorylation; when associated with F-
365. {ECO:0000269|PubMed:17045208,
ECO:0000269|PubMed:17494760}.
MUTAGEN 309 309 Y->F: Decrease of CSK-induced
phosphorylation.
{ECO:0000269|PubMed:17045208}.
MUTAGEN 348 348 Y->F: Decrease of CSK-induced
phosphorylation.
{ECO:0000269|PubMed:17045208}.
MUTAGEN 359 359 Y->F: Decrease of CSK-induced
phosphorylation.
{ECO:0000269|PubMed:17045208}.
MUTAGEN 364 364 Y->F: Decrease of CSK-induced
phosphorylation.
{ECO:0000269|PubMed:17045208}.
MUTAGEN 365 365 Y->F: Decrease of CSK-induced
phosphorylation and phosphorylation by
TNK2. Complete loss of TNK2-dependent
phosphorylation; when associated with F-
269. {ECO:0000269|PubMed:17045208,
ECO:0000269|PubMed:17494760}.
MUTAGEN 395 395 Y->F: Decrease of CSK-induced
phosphorylation.
{ECO:0000269|PubMed:17045208}.
MUTAGEN 535 535 Y->F: Greatest decrease of CSK-induced
phosphorylation and inhibition of
transcriptional activity induced by EGF.
{ECO:0000269|PubMed:17045208}.
MUTAGEN 552 552 Y->F: Decrease in CSK-induced
phosphorylation.
{ECO:0000269|PubMed:17045208}.
MUTAGEN 702 702 L->A: Alters receptor specificity, so
that transcription is activated by the
antiandrogen cyproterone acetate.
{ECO:0000269|PubMed:17311914}.
MUTAGEN 721 721 K->A: Loss of transcription activation in
the presence of androgen and of
interaction with NCOA2.
{ECO:0000269|PubMed:15563469,
ECO:0000269|PubMed:17591767}.
MUTAGEN 742 742 W->L: Strongly decreased transcription
activation in the presence of androgen.
{ECO:0000269|PubMed:16129672}.
MUTAGEN 846 846 K->R: Prevents ubiquitination by RNF6.
Prevents AR transcriptional activation by
RNF14 in absence of hormone.
{ECO:0000269|PubMed:19345326}.
MUTAGEN 848 848 K->R: Partially prevents ubiquitination
by RNF6. {ECO:0000269|PubMed:19345326}.
MUTAGEN 898 898 E->A,Q: Reduced transcription activation
in the presence of androgen.
{ECO:0000269|PubMed:15563469,
ECO:0000269|PubMed:17591767}.
MUTAGEN 898 898 E->K,R: Loss of transcription activation
in the presence of androgen.
{ECO:0000269|PubMed:15563469,
ECO:0000269|PubMed:17591767}.
MUTAGEN 916 916 Y->F: Decrease in CSK-induced
phosphorylation.
{ECO:0000269|PubMed:17045208}.
CONFLICT 168 168 G -> A (in Ref. 5; AAA51780).
{ECO:0000305}.
CONFLICT 214 214 A -> R (in Ref. 3 and 6; AAA51771/
AAA51772). {ECO:0000305}.
CONFLICT 476 476 G -> E (in Ref. 2; AAA51775 and 13;
AAA51770). {ECO:0000305}.
CONFLICT 566 566 E -> K (in Ref. 15; AAA51774).
{ECO:0000305}.
CONFLICT 635 635 L -> P (in Ref. 19; AAB21256/AAB21257).
{ECO:0000305}.
CONFLICT 676 676 N -> I (in Ref. 19; AAB21256/AAB21257).
{ECO:0000305}.
CONFLICT 811 811 L -> M (in Ref. 5; AAA51780).
{ECO:0000305}.
HELIX 22 29 {ECO:0000244|PDB:3V49}.
STRAND 667 669 {ECO:0000244|PDB:1XJ7}.
HELIX 673 681 {ECO:0000244|PDB:4OHA}.
STRAND 692 694 {ECO:0000244|PDB:1XJ7}.
HELIX 698 721 {ECO:0000244|PDB:4OHA}.
HELIX 726 728 {ECO:0000244|PDB:4OHA}.
HELIX 731 758 {ECO:0000244|PDB:4OHA}.
STRAND 761 766 {ECO:0000244|PDB:4OHA}.
STRAND 769 771 {ECO:0000244|PDB:4OHA}.
HELIX 773 778 {ECO:0000244|PDB:4OHA}.
HELIX 782 797 {ECO:0000244|PDB:4OHA}.
HELIX 802 812 {ECO:0000244|PDB:4OHA}.
STRAND 815 818 {ECO:0000244|PDB:4OHA}.
HELIX 825 843 {ECO:0000244|PDB:4OHA}.
TURN 844 846 {ECO:0000244|PDB:2PKL}.
TURN 850 852 {ECO:0000244|PDB:2PIV}.
HELIX 853 883 {ECO:0000244|PDB:4OHA}.
HELIX 885 888 {ECO:0000244|PDB:4OHA}.
HELIX 894 902 {ECO:0000244|PDB:4OHA}.
HELIX 904 908 {ECO:0000244|PDB:4OHA}.
STRAND 911 914 {ECO:0000244|PDB:4OHA}.
SEQUENCE 920 AA; 99188 MW; A73432C55D39AE06 CRC64;
MEVQLGLGRV YPRPPSKTYR GAFQNLFQSV REVIQNPGPR HPEAASAAPP GASLLLLQQQ
QQQQQQQQQQ QQQQQQQQQQ ETSPRQQQQQ QGEDGSPQAH RRGPTGYLVL DEEQQPSQPQ
SALECHPERG CVPEPGAAVA ASKGLPQQLP APPDEDDSAA PSTLSLLGPT FPGLSSCSAD
LKDILSEAST MQLLQQQQQE AVSEGSSSGR AREASGAPTS SKDNYLGGTS TISDNAKELC
KAVSVSMGLG VEALEHLSPG EQLRGDCMYA PLLGVPPAVR PTPCAPLAEC KGSLLDDSAG
KSTEDTAEYS PFKGGYTKGL EGESLGCSGS AAAGSSGTLE LPSTLSLYKS GALDEAAAYQ
SRDYYNFPLA LAGPPPPPPP PHPHARIKLE NPLDYGSAWA AAAAQCRYGD LASLHGAGAA
GPGSGSPSAA ASSSWHTLFT AEEGQLYGPC GGGGGGGGGG GGGGGGGGGG GGGEAGAVAP
YGYTRPPQGL AGQESDFTAP DVWYPGGMVS RVPYPSPTCV KSEMGPWMDS YSGPYGDMRL
ETARDHVLPI DYYFPPQKTC LICGDEASGC HYGALTCGSC KVFFKRAAEG KQKYLCASRN
DCTIDKFRRK NCPSCRLRKC YEAGMTLGAR KLKKLGNLKL QEEGEASSTT SPTEETTQKL
TVSHIEGYEC QPIFLNVLEA IEPGVVCAGH DNNQPDSFAA LLSSLNELGE RQLVHVVKWA
KALPGFRNLH VDDQMAVIQY SWMGLMVFAM GWRSFTNVNS RMLYFAPDLV FNEYRMHKSR
MYSQCVRMRH LSQEFGWLQI TPQEFLCMKA LLLFSIIPVD GLKNQKFFDE LRMNYIKELD
RIIACKRKNP TSCSRRFYQL TKLLDSVQPI ARELHQFTFD LLIKSHMVSV DFPEMMAEII
SVQVPKILSG KVKPIYFHTQ


Related products :

Catalog number Product name Quantity
E1252p ELISA kit Androgen receptor,AR,Dihydrotestosterone receptor,NR3C4,Nuclear receptor subfamily 3 group C member 4,Pig,Sus scrofa 96T
U1252p CLIA Androgen receptor,AR,Dihydrotestosterone receptor,NR3C4,Nuclear receptor subfamily 3 group C member 4,Pig,Sus scrofa 96T
18-783-77237 RABBIT ANTI ANDROGEN RECEPTOR - Dihydrotestosterone receptor; Nuclear receptor subfamily 3 group C member 4 Polyclonal 1 ml
18-783-77236 RABBIT ANTI ANDROGEN RECEPTOR - Dihydrotestosterone receptor; Nuclear receptor subfamily 3 group C member 4 Polyclonal 1 ml
E1252p ELISA Androgen receptor,AR,Dihydrotestosterone receptor,NR3C4,Nuclear receptor subfamily 3 group C member 4,Pig,Sus scrofa 96T
E1252r ELISA kit Androgen receptor,Ar,Dihydrotestosterone receptor,Nr3c4,Nuclear receptor subfamily 3 group C member 4,Rat,Rattus norvegicus 96T
E1252m ELISA kit Androgen receptor,Ar,Dihydrotestosterone receptor,Mouse,Mus musculus,Nr3c4,Nuclear receptor subfamily 3 group C member 4 96T
U1252r CLIA Androgen receptor,Ar,Dihydrotestosterone receptor,Nr3c4,Nuclear receptor subfamily 3 group C member 4,Rat,Rattus norvegicus 96T
E1252m ELISA Androgen receptor,Ar,Dihydrotestosterone receptor,Mouse,Mus musculus,Nr3c4,Nuclear receptor subfamily 3 group C member 4 96T
E1252r ELISA Androgen receptor,Ar,Dihydrotestosterone receptor,Nr3c4,Nuclear receptor subfamily 3 group C member 4,Rat,Rattus norvegicus 96T
U1252m CLIA Androgen receptor,Ar,Dihydrotestosterone receptor,Mouse,Mus musculus,Nr3c4,Nuclear receptor subfamily 3 group C member 4 96T
U1252Rb CLIA Androgen receptor,AR,Dihydrotestosterone receptor,NR3C4,Nuclear receptor subfamily 3 group C member 4,Oryctolagus cuniculus,Rabbit 96T
E1252Rb ELISA Androgen receptor,AR,Dihydrotestosterone receptor,NR3C4,Nuclear receptor subfamily 3 group C member 4,Oryctolagus cuniculus,Rabbit 96T
E1252Rb ELISA kit Androgen receptor,AR,Dihydrotestosterone receptor,NR3C4,Nuclear receptor subfamily 3 group C member 4,Oryctolagus cuniculus,Rabbit 96T
E1252h ELISA Androgen receptor,AR,DHTR,Dihydrotestosterone receptor,Homo sapiens,Human,NR3C4,Nuclear receptor subfamily 3 group C member 4 96T
E1252h ELISA kit Androgen receptor,AR,DHTR,Dihydrotestosterone receptor,Homo sapiens,Human,NR3C4,Nuclear receptor subfamily 3 group C member 4 96T
U1252h CLIA Androgen receptor,AR,DHTR,Dihydrotestosterone receptor,Homo sapiens,Human,NR3C4,Nuclear receptor subfamily 3 group C member 4 96T
E1252c ELISA Androgen receptor,AR,Canis familiaris,Canis lupus familiaris,Dihydrotestosterone receptor,Dog,NR3C4,Nuclear receptor subfamily 3 group C member 4 96T
U1252c CLIA Androgen receptor,AR,Canis familiaris,Canis lupus familiaris,Dihydrotestosterone receptor,Dog,NR3C4,Nuclear receptor subfamily 3 group C member 4 96T
E1252c ELISA kit Androgen receptor,AR,Canis familiaris,Canis lupus familiaris,Dihydrotestosterone receptor,Dog,NR3C4,Nuclear receptor subfamily 3 group C member 4 96T
EIAAB27783 Homo sapiens,Human,Liver X receptor beta,LXRB,NER,NR1H2,Nuclear receptor NER,Nuclear receptor subfamily 1 group H member 2,Oxysterols receptor LXR-beta,Ubiquitously-expressed nuclear receptor,UNR
EIAAB27782 Liver X receptor beta,Lxrb,Nr1h2,Nuclear receptor subfamily 1 group H member 2,Orphan nuclear receptor OR-1,Oxysterols receptor LXR-beta,Rat,Rattus norvegicus,Ubiquitously-expressed nuclear receptor,U
EIAAB27785 Homo sapiens,Human,NR1I2,Nuclear receptor subfamily 1 group I member 2,Orphan nuclear receptor PAR1,Orphan nuclear receptor PXR,Pregnane X receptor,PXR,Steroid and xenobiotic receptor,SXR
EIAAB27810 Gfrp,Hmr,Mouse,Mus musculus,N10,Nr4a1,Nuclear hormone receptor NUR_77,Nuclear protein N10,Nuclear receptor subfamily 4 group A member 1,Nur77,Orphan nuclear receptor HMR
U2042r CLIA kit Bar,Bile acid receptor,Farnesoid X-activated receptor,Farnesol receptor HRR-1,Fxr,Nr1h4,Nuclear receptor subfamily 1 group H member 4,Rat,Rattus norvegicus,Retinoid X receptor-interacting pr 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur