ID   ANDR_HUMAN              Reviewed;         919 AA.
AC   P10275; A2RUN2; B1AKD7; Q9UD95;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 2.
DT   11-NOV-2015, entry version 233.
DE   RecName: Full=Androgen receptor;
DE   AltName: Full=Dihydrotestosterone receptor;
DE   AltName: Full=Nuclear receptor subfamily 3 group C member 4;
GN   Name=AR; Synonyms=DHTR, NR3C4;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=3216866; DOI=10.1210/mend-2-12-1265;
RA   Lubahn D.B., Joseph D.R., Sar M., Tan J., Higgs H.N., Larson R.E.,
RA   French F.S., Wilson E.M.;
RT   "The human androgen receptor: complementary deoxyribonucleic acid
RT   cloning, sequence analysis and gene expression in prostate.";
RL   Mol. Endocrinol. 2:1265-1275(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Prostate;
RX   PubMed=3174628; DOI=10.1073/pnas.85.19.7211;
RA   Chang C., Kokontis J., Liao S.;
RT   "Structural analysis of complementary DNA and amino acid sequences of
RT   human and rat androgen receptors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:7211-7215(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Prostate;
RX   PubMed=2911578; DOI=10.1073/pnas.86.1.327;
RA   Tilley W.D., Marcelli M., Wilson J.D., McPhaul M.J.;
RT   "Characterization and expression of a cDNA encoding the human androgen
RT   receptor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:327-331(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT AIS MET-866.
RX   PubMed=2594783; DOI=10.1073/pnas.86.23.9534;
RA   Lubahn D.B., Brown T.R., Simental J.A., Higgs H.N., Migeon C.J.,
RA   Wilson E.M., French F.S.;
RT   "Sequence of the intron/exon junctions of the coding region of the
RT   human androgen receptor gene and identification of a point mutation in
RT   a family with complete androgen insensitivity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:9534-9538(1989).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT DEL
RP   GLY-465--472-GLY.
RX   PubMed=2342476; DOI=10.1210/mend-4-3-417;
RA   Govindan M.V.;
RT   "Specific region in hormone binding domain is essential for hormone
RT   binding and trans-activation by human androgen receptor.";
RL   Mol. Endocrinol. 4:417-427(1990).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND NUCLEOTIDE SEQUENCE [MRNA]
RP   (ISOFORM 1).
RC   TISSUE=Prostate;
RX   PubMed=2293020; DOI=10.1210/mend-4-8-1105;
RA   Marcelli M., Tilley W.D., Wilson C.M., Griffin J.E., Wilson J.D.,
RA   McPhaul M.J.;
RT   "Definition of the human androgen receptor gene structure permits the
RT   identification of mutations that cause androgen resistance: premature
RT   termination of the receptor protein at amino acid residue 588 causes
RT   complete androgen resistance.";
RL   Mol. Endocrinol. 4:1105-1116(1990).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2),
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=15634333; DOI=10.1111/j.1432-1033.2004.04395.x;
RA   Ahrens-Fath I., Politz O., Geserick C., Haendler B.;
RT   "Androgen receptor function is modulated by the tissue-specific AR45
RT   variant.";
RL   FEBS J. 272:74-84(2005).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA   Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA   Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA   Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA   Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA   Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA   Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA   Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA   Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA   Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA   Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA   Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA   Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA   Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA   Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA   Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA   Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA   Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA   Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA   Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA   Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA   Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA   Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA   Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA   de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA   Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA   Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA   Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA   Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA   Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA   Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA   Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA   Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA   Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA   Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA   Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA   Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA   Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA   Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA   Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA   Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA   Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA   Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA   Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND POLYMORPHISM
RP   OF POLY-GLY REGION.
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-538.
RX   PubMed=2917688; DOI=10.1016/0303-7207(89)90137-8;
RA   Faber P.W., Kuiper G.G.J.M., van Rooij H.C.J.,
RA   van der Korput J.A.G.M., Brinkmann A.O., Trapman J.;
RT   "The N-terminal domain of the human androgen receptor is encoded by
RT   one, large exon.";
RL   Mol. Cell. Endocrinol. 61:257-262(1989).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 189-919 (ISOFORM 1).
RX   PubMed=3353726; DOI=10.1126/science.3353726;
RA   Chang C., Kokontis J., Liao S.;
RT   "Molecular cloning of human and rat complementary DNA encoding
RT   androgen receptors.";
RL   Science 240:324-326(1988).
RN   [13]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 446-475, AND POLYMORPHISM OF
RP   POLY-GLY REGION.
RC   TISSUE=Blood;
RA   Lu J., Danielsen M.;
RL   Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
RN   [14]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 468-919 (ISOFORM 1).
RX   PubMed=3377788; DOI=10.1016/S0006-291X(88)81214-2;
RA   Trapman J., Klaassen P., Kuiper G.G.J.M., van der Korput J.A.G.M.,
RA   Faber P.W., van Rooij H.C.J., Geurts van Kessel A., Voorhorst M.M.,
RA   Mulder E., Brinkmann A.O.;
RT   "Cloning, structure and expression of a cDNA encoding the human
RT   androgen receptor.";
RL   Biochem. Biophys. Res. Commun. 153:241-248(1988).
RN   [15]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 536-540; 587-591; 626-630;
RP   722-726; 770-774; 814-817 AND 866-870.
RX   PubMed=2546571; DOI=10.1677/jme.0.002R001;
RA   Kuiper G.G., Faber P.W., van Rooij H.C., van der Korput J.A.,
RA   Ris-Stalpers C., Klaassen P., Trapman J., Brinkmann A.O.;
RT   "Structural organization of the human androgen receptor gene.";
RL   J. Mol. Endocrinol. 2:R1-R4(1989).
RN   [16]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 557-624 (ISOFORMS 1/2), AND VARIANT AIS
RP   HIS-615.
RC   TISSUE=Fibroblast;
RX   PubMed=8413310; DOI=10.1210/mend.7.7.8413310;
RA   Mowszowicz I., Lee H.-J., Chen H.-T., Mestayer C., Portois M.-C.,
RA   Cabrol S., Mauvais-Jarvis P., Chang C.;
RT   "A point mutation in the second zinc finger of the DNA-binding domain
RT   of the androgen receptor gene causes complete androgen insensitivity
RT   in two siblings with receptor-positive androgen resistance.";
RL   Mol. Endocrinol. 7:861-869(1993).
RN   [17]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 559-624 (ISOFORMS 1/2).
RX   PubMed=3353727; DOI=10.1126/science.3353727;
RA   Lubahn D.B., Joseph D.R., Sullivan P.M., Willard H.F., French F.S.,
RA   Wilson E.M.;
RT   "Cloning of human androgen receptor complementary DNA and localization
RT   to the X chromosome.";
RL   Science 240:327-330(1988).
RN   [18]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 629-723, AND VARIANTS AIS ASN-695
RP   AND HIS-695.
RX   PubMed=1775137; DOI=10.1210/mend-5-10-1562;
RA   Ris-Stalpers C., Trifiro M.A., Kuiper G.G.J.M., Jenster G., Romalo G.,
RA   Sai T., van Rooij H.C.J., Kaufman M., Rosenfield R.L., Liao S.,
RA   Schweikert H.-U., Trapman J., Pinsky L., Brinkmann A.O.;
RT   "Substitution of aspartic acid-686 by histidine or asparagine in the
RT   human androgen receptor leads to a functionally inactive protein with
RT   altered hormone-binding characteristics.";
RL   Mol. Endocrinol. 5:1562-1569(1991).
RN   [19]
RP   POLYMORPHISM OF POLY-GLN REGION.
RX   PubMed=1561105; DOI=10.1093/nar/20.6.1427-a;
RA   Sleddens H.F.B.M., Oostra B.A., Brinkmann A.O., Trapman J.;
RT   "Trinucleotide repeat polymorphism in the androgen receptor gene
RT   (AR).";
RL   Nucleic Acids Res. 20:1427-1427(1992).
RN   [20]
RP   POLYMORPHISM OF POLY-GLN REGION.
RX   PubMed=9096391; DOI=10.1073/pnas.94.7.3320;
RA   Giovannucci E., Stampfer M.J., Krithivas K., Brown M., Dahl D.,
RA   Brufsky A., Talcott J., Hennekens C.H., Kantoff P.W.;
RT   "The CAG repeat within the androgen receptor gene and its relationship
RT   to prostate cancer.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:3320-3323(1997).
RN   [21]
RP   ERRATUM.
RA   Giovannucci E., Stampfer M.J., Krithivas K., Brown M., Dahl D.,
RA   Brufsky A., Talcott J., Hennekens C.H., Kantoff P.W.;
RL   Proc. Natl. Acad. Sci. U.S.A. 94:8272-8272(1997).
RN   [22]
RP   INTERACTION WITH PQBP1.
RC   TISSUE=Brain;
RX   PubMed=10332029; DOI=10.1093/hmg/8.6.977;
RA   Waragai M., Lammers C.-H., Takeuchi S., Imafuku I., Udagawa Y.,
RA   Kanazawa I., Kawabata M., Mouradian M.M., Okazawa H.;
RT   "PQBP-1, a novel polyglutamine tract binding protein, inhibits
RT   transcription activation by Brn-2 and affects cell survival.";
RL   Hum. Mol. Genet. 8:977-987(1999).
RN   [23]
RP   INTERACTION WITH TGFB1I1.
RX   PubMed=10075738; DOI=10.1074/jbc.274.12.8316;
RA   Fujimoto N., Yeh S., Kang H.-Y., Inui S., Chang H.-C., Mizokami A.,
RA   Chang C.;
RT   "Cloning and characterization of androgen receptor coactivator, ARA55,
RT   in human prostate.";
RL   J. Biol. Chem. 274:8316-8321(1999).
RN   [24]
RP   INTERACTION WITH UBE2I.
RX   PubMed=10383460; DOI=10.1074/jbc.274.27.19441;
RA   Poukka H., Aarnisalo P., Karvonen U., Palvimo J.J., Jaenne O.A.;
RT   "Ubc9 interacts with the androgen receptor and activates receptor-
RT   dependent transcription.";
RL   J. Biol. Chem. 274:19441-19446(1999).
RN   [25]
RP   INTERACTION WITH RAN.
RX   PubMed=10400640; DOI=10.1074/jbc.274.29.20229;
RA   Hsiao P.-W., Lin D.-L., Nakao R., Chang C.;
RT   "The linkage of Kennedy's neuron disease to ARA24, the first
RT   identified androgen receptor polyglutamine region-associated
RT   coactivator.";
RL   J. Biol. Chem. 274:20229-20234(1999).
RN   [26]
RP   INTERACTION WITH SPDEF.
RX   PubMed=10625666; DOI=10.1074/jbc.275.2.1216;
RA   Oettgen P., Finger E., Sun Z., Akbarali Y., Thamrongsak U., Boltax J.,
RA   Grall F., Dube A., Weiss A., Brown L., Quinn G., Kas K., Endress G.,
RA   Kunsch C., Libermann T.A.;
RT   "PDEF, a novel prostate epithelium-specific ets transcription factor,
RT   interacts with the androgen receptor and activates prostate-specific
RT   antigen gene expression.";
RL   J. Biol. Chem. 275:1216-1225(2000).
RN   [27]
RP   INTERACTION WITH KAT7.
RX   PubMed=10930412; DOI=10.1074/jbc.M004838200;
RA   Sharma M., Zarnegar M., Li X., Lim B., Sun Z.;
RT   "Androgen receptor interacts with a novel MYST protein, HBO1.";
RL   J. Biol. Chem. 275:35200-35208(2000).
RN   [28]
RP   SUMOYLATION AT LYS-386 AND LYS-520.
RX   PubMed=11121022; DOI=10.1073/pnas.97.26.14145;
RA   Poukka H., Karvonen U., Jaenne O.A., Palvimo J.J.;
RT   "Covalent modification of the androgen receptor by small ubiquitin-
RT   like modifier 1 (SUMO-1).";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14145-14150(2000).
RN   [29]
RP   INTERACTION WITH RANBP9.
RX   PubMed=12361945; DOI=10.1074/jbc.M209741200;
RA   Rao M.A., Cheng H., Quayle A.N., Nishitani H., Nelson C.C.,
RA   Rennie P.S.;
RT   "RanBPM, a nuclear protein that interacts with and regulates
RT   transcriptional activity of androgen receptor and glucocorticoid
RT   receptor.";
RL   J. Biol. Chem. 277:48020-48027(2002).
RN   [30]
RP   INTERACTION WITH PRPF6.
RX   PubMed=12039962; DOI=10.1074/jbc.M203811200;
RA   Zhao Y., Goto K., Saitoh M., Yanase T., Nomura M., Okabe T.,
RA   Takayanagi R., Nawata H.;
RT   "Activation function-1 domain of androgen receptor contributes to the
RT   interaction between subnuclear splicing factor compartment and nuclear
RT   receptor compartment. Identification of the p102 U5 small nuclear
RT   ribonucleoprotein particle-binding protein as a coactivator for the
RT   receptor.";
RL   J. Biol. Chem. 277:30031-30039(2002).
RN   [31]
RP   INTERACTION WITH PELP1.
RX   PubMed=12415108; DOI=10.1073/pnas.192569699;
RA   Wong C.-W., McNally C., Nickbarg E., Komm B.S., Cheskis B.J.;
RT   "Estrogen receptor-interacting protein that modulates its nongenomic
RT   activity-crosstalk with Src/Erk phosphorylation cascade.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14783-14788(2002).
RN   [32]
RP   INTERACTION WITH ZMIZ1.
RX   PubMed=14609956; DOI=10.1093/emboj/cdg585;
RA   Sharma M., Li X., Wang Y., Zarnegar M., Huang C.-Y., Palvimo J.J.,
RA   Lim B., Sun Z.;
RT   "hZimp10 is an androgen receptor co-activator and forms a complex with
RT   SUMO-1 at replication foci.";
RL   EMBO J. 22:6101-6114(2003).
RN   [33]
RP   INTERACTION WITH GNB2L1, AND SUBCELLULAR LOCATION.
RX   PubMed=12958311; DOI=10.1074/jbc.M306219200;
RA   Rigas A.C., Ozanne D.M., Neal D.E., Robson C.N.;
RT   "The scaffolding protein RACK1 interacts with androgen receptor and
RT   promotes cross-talk through a protein kinase C signaling pathway.";
RL   J. Biol. Chem. 278:46087-46093(2003).
RN   [34]
RP   FUNCTION, AND INTERACTION WITH RBAK.
RX   PubMed=14664718; DOI=10.1677/jme.0.0310583;
RA   Hofman K., Swinnen J.V., Claessens F., Verhoeven G., Heyns W.;
RT   "The retinoblastoma protein-associated transcription repressor RBaK
RT   interacts with the androgen receptor and enhances its transcriptional
RT   activity.";
RL   J. Mol. Endocrinol. 31:583-596(2003).
RN   [35]
RP   INTERACTION WITH EFCAB6.
RX   PubMed=12612053;
RA   Niki T., Takahashi-Niki K., Taira T., Iguchi-Ariga S.M.M., Ariga H.;
RT   "DJBP: a novel DJ-1-binding protein, negatively regulates the androgen
RT   receptor by recruiting histone deacetylase complex, and DJ-1
RT   antagonizes this inhibition by abrogation of this complex.";
RL   Mol. Cancer Res. 1:247-261(2003).
RN   [36]
RP   PHOSPHORYLATION BY PAK6.
RX   PubMed=14573606; DOI=10.1074/jbc.M311145200;
RA   Schrantz N., da Silva Correia J., Fowler B., Ge Q., Sun Z.,
RA   Bokoch G.M.;
RT   "Mechanism of p21-activated kinase 6-mediated inhibition of androgen
RT   receptor signaling.";
RL   J. Biol. Chem. 279:1922-1931(2004).
RN   [37]
RP   INTERACTION WITH HIP1.
RX   PubMed=16027218; DOI=10.1083/jcb.200503106;
RA   Mills I.G., Gaughan L., Robson C., Ross T., McCracken S., Kelly J.,
RA   Neal D.E.;
RT   "Huntingtin interacting protein 1 modulates the transcriptional
RT   activity of nuclear hormone receptors.";
RL   J. Cell Biol. 170:191-200(2005).
RN   [38]
RP   INTERACTION WITH ZMIZ2.
RX   PubMed=16051670; DOI=10.1210/me.2005-0097;
RA   Huang C.-Y., Beliakoff J., Li X., Lee J., Li X., Sharma M., Lim B.,
RA   Sun Z.;
RT   "hZimp7, a novel PIAS-like protein, enhances androgen receptor-
RT   mediated transcription and interacts with SWI/SNF-like BAF
RT   complexes.";
RL   Mol. Endocrinol. 19:2915-2929(2005).
RN   [39]
RP   PHOSPHORYLATION AT TYR-223; TYR-267; TYR-307; TYR-346; TYR-357;
RP   TYR-362; TYR-363; TYR-393; TYR-534; TYR-551 AND TYR-915, MUTAGENESIS
RP   OF TYR-223; TYR-267; TYR-307; TYR-346; TYR-357; TYR-362; TYR-363;
RP   TYR-393; TYR-534; TYR-551 AND TYR-915, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=17045208; DOI=10.1016/j.ccr.2006.08.021;
RA   Guo Z., Dai B., Jiang T., Xu K., Xie Y., Kim O., Nesheiwat I.,
RA   Kong X., Melamed J., Handratta V.D., Njar V.C., Brodie A.M., Yu L.-R.,
RA   Veenstra T.D., Chen H., Qiu Y.;
RT   "Regulation of androgen receptor activity by tyrosine
RT   phosphorylation.";
RL   Cancer Cell 10:309-319(2006).
RN   [40]
RP   ERRATUM.
RA   Guo Z., Dai B., Jiang T., Xu K., Xie Y., Kim O., Nesheiwat I.,
RA   Kong X., Melamed J., Handratta V.D., Njar V.C., Brodie A.M., Yu L.-R.,
RA   Veenstra T.D., Chen H., Qiu Y.;
RL   Cancer Cell 11:97-97(2007).
RN   [41]
RP   INTERACTION WITH MAK, AND SUBUNIT.
RX   PubMed=16951154; DOI=10.1158/0008-5472.CAN-06-1636;
RA   Ma A.H., Xia L., Desai S.J., Boucher D.L., Guan Y., Shih H.M.,
RA   Shi X.B., deVere White R.W., Chen H.W., Tepper C.G., Kung H.J.;
RT   "Male germ cell-associated kinase, a male-specific kinase regulated by
RT   androgen, is a coactivator of androgen receptor in prostate cancer
RT   cells.";
RL   Cancer Res. 66:8439-8447(2006).
RN   [42]
RP   INTERACTION WITH PRMT2, AND SUBCELLULAR LOCATION.
RX   PubMed=17587566; DOI=10.1016/j.jsbmb.2007.05.006;
RA   Meyer R., Wolf S.S., Obendorf M.;
RT   "PRMT2, a member of the protein arginine methyltransferase family, is
RT   a coactivator of the androgen receptor.";
RL   J. Steroid Biochem. Mol. Biol. 107:1-14(2007).
RN   [43]
RP   INTERACTION WITH RREB1.
RX   PubMed=17550981; DOI=10.1210/me.2006-0503;
RA   Mukhopadhyay N.K., Cinar B., Mukhopadhyay L., Lutchman M.,
RA   Ferdinand A.S., Kim J., Chung L.W.K., Adam R.M., Ray S.K.,
RA   Leiter A.B., Richie J.P., Liu B.C.-S., Freeman M.R.;
RT   "The zinc finger protein Ras-responsive element binding protein-1 is a
RT   coregulator of the androgen receptor: implications for the role of the
RT   Ras pathway in enhancing androgenic signaling in prostate cancer.";
RL   Mol. Endocrinol. 21:2056-2070(2007).
RN   [44]
RP   INTERACTION WITH RANBP10.
RX   PubMed=18222118; DOI=10.1016/j.bbrc.2008.01.072;
RA   Harada N., Yokoyama T., Yamaji R., Nakano Y., Inui H.;
RT   "RanBP10 acts as a novel coactivator for the androgen receptor.";
RL   Biochem. Biophys. Res. Commun. 368:121-125(2008).
RN   [45]
RP   INTERACTION WITH TNK2, PHOSPHORYLATION AT TYR-267 AND TYR-363 BY TNK2,
RP   AND MUTAGENESIS OF TYR-267 AND TYR-363.
RX   PubMed=17494760; DOI=10.1073/pnas.0700420104;
RA   Mahajan N.P., Liu Y., Majumder S., Warren M.R., Parker C.E.,
RA   Mohler J.L., Earp H.S., Whang Y.E.;
RT   "Activated Cdc42-associated kinase Ack1 promotes prostate cancer
RT   progression via androgen receptor tyrosine phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8438-8443(2007).
RN   [46]
RP   INTERACTION WITH TRIM68.
RX   PubMed=18451177; DOI=10.1158/0008-5472.CAN-07-6059;
RA   Miyajima N., Maruyama S., Bohgaki M., Kano S., Shigemura M.,
RA   Shinohara N., Nonomura K., Hatakeyama S.;
RT   "TRIM68 regulates ligand-dependent transcription of androgen receptor
RT   in prostate cancer cells.";
RL   Cancer Res. 68:3486-3494(2008).
RN   [47]
RP   INTERACTION WITH LPXN.
RX   PubMed=18451096; DOI=10.1210/me.2006-0546;
RA   Kaulfuss S., Grzmil M., Hemmerlein B., Thelen P., Schweyer S.,
RA   Neesen J., Bubendorf L., Glass A.G., Jarry H., Auber B., Burfeind P.;
RT   "Leupaxin, a novel coactivator of the androgen receptor, is expressed
RT   in prostate cancer and plays a role in adhesion and invasion of
RT   prostate carcinoma cells.";
RL   Mol. Endocrinol. 22:1606-1621(2008).
RN   [48]
RP   FUNCTION, AND INTERACTION WITH ZIPK/DAPK3.
RX   PubMed=18084323; DOI=10.1038/sj.onc.1210995;
RA   Leister P., Felten A., Chasan A.I., Scheidtmann K.H.;
RT   "ZIP kinase plays a crucial role in androgen receptor-mediated
RT   transcription.";
RL   Oncogene 27:3292-3300(2008).
RN   [49]
RP   INTERACTION WITH TRIM24.
RX   PubMed=19909775; DOI=10.1016/j.bbamcr.2009.11.001;
RA   Kikuchi M., Okumura F., Tsukiyama T., Watanabe M., Miyajima N.,
RA   Tanaka J., Imamura M., Hatakeyama S.;
RT   "TRIM24 mediates ligand-dependent activation of androgen receptor and
RT   is repressed by a bromodomain-containing protein, BRD7, in prostate
RT   cancer cells.";
RL   Biochim. Biophys. Acta 1793:1828-1836(2009).
RN   [50]
RP   FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, POLYUBIQUITINATION AT
RP   LYS-845 AND LYS-847 BY RNF6, MUTAGENESIS OF LYS-845 AND LYS-847,
RP   INTERACTION WITH RNF14 AND RNF6, AND SUBCELLULAR LOCATION.
RX   PubMed=19345326; DOI=10.1016/j.ccr.2009.02.021;
RA   Xu K., Shimelis H., Linn D.E., Jiang R., Yang X., Sun F., Guo Z.,
RA   Chen H., Li W., Chen H., Kong X., Melamed J., Fang S., Xiao Z.,
RA   Veenstra T.D., Qiu Y.;
RT   "Regulation of androgen receptor transcriptional activity and
RT   specificity by RNF6-induced ubiquitination.";
RL   Cancer Cell 15:270-282(2009).
RN   [51]
RP   FUNCTION IN AR KINASE, PHOSPHORYLATION AT SER-81 BY CDK9, MUTAGENESIS
RP   OF SER-81, AND INTERACTION WITH CDK9.
RX   PubMed=20980437; DOI=10.1210/me.2010-0238;
RA   Gordon V., Bhadel S., Wunderlich W., Zhang J., Ficarro S.B.,
RA   Mollah S.A., Shabanowitz J., Hunt D.F., Xenarios I., Hahn W.C.,
RA   Conaway M., Carey M.F., Gioeli D.;
RT   "CDK9 regulates AR promoter selectivity and cell growth through serine
RT   81 phosphorylation.";
RL   Mol. Endocrinol. 24:2267-2280(2010).
RN   [52]
RP   UBIQUITINATION, DEUBIQUITINATION, AND INTERACTION WITH USP26.
RX   PubMed=20501646; DOI=10.1158/1541-7786.MCR-09-0424;
RA   Dirac A.M., Bernards R.;
RT   "The deubiquitinating enzyme USP26 is a regulator of androgen receptor
RT   signaling.";
RL   Mol. Cancer Res. 8:844-854(2010).
RN   [53]
RP   PHOSPHORYLATION AT TYR-267, AND ENZYME REGULATION.
RX   PubMed=20623637; DOI=10.1002/pros.21163;
RA   Mahajan K., Challa S., Coppola D., Lawrence H., Luo Y., Gevariya H.,
RA   Zhu W., Chen Y.A., Lawrence N.J., Mahajan N.P.;
RT   "Effect of Ack1 tyrosine kinase inhibitor on ligand-independent
RT   androgen receptor activity.";
RL   Prostate 70:1274-1285(2010).
RN   [54]
RP   PHOSPHORYLATION AT SER-650, AND INTERACTION WITH STK4/MST1.
RX   PubMed=21512132; DOI=10.1158/0008-5472.CAN-10-4532;
RA   Cinar B., Collak F.K., Lopez D., Akgul S., Mukhopadhyay N.K.,
RA   Kilicarslan M., Gioeli D.G., Freeman M.R.;
RT   "MST1 is a multifunctional caspase-independent inhibitor of androgenic
RT   signaling.";
RL   Cancer Res. 71:4303-4313(2011).
RN   [55]
RP   INTERACTION WITH CRY1.
RX   PubMed=22170608; DOI=10.1038/nature10700;
RA   Lamia K.A., Papp S.J., Yu R.T., Barish G.D., Uhlenhaut N.H.,
RA   Jonker J.W., Downes M., Evans R.M.;
RT   "Cryptochromes mediate rhythmic repression of the glucocorticoid
RT   receptor.";
RL   Nature 480:552-556(2011).
RN   [56]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [57]
RP   PALMITOYLATION.
RX   PubMed=22031296; DOI=10.1091/mbc.E11-07-0638;
RA   Pedram A., Razandi M., Deschenes R.J., Levin E.R.;
RT   "DHHC-7 and -21 are palmitoylacyltransferases for sex steroid
RT   receptors.";
RL   Mol. Biol. Cell 23:188-199(2012).
RN   [58]
RP   INTERACTION WITH CCAR1 AND GATA2.
RX   PubMed=23887938; DOI=10.1093/nar/gkt644;
RA   Seo W.Y., Jeong B.C., Yu E.J., Kim H.J., Kim S.H., Lim J.E.,
RA   Kwon G.Y., Lee H.M., Kim J.H.;
RT   "CCAR1 promotes chromatin loading of androgen receptor (AR)
RT   transcription complex by stabilizing the association between AR and
RT   GATA2.";
RL   Nucleic Acids Res. 41:8526-8536(2013).
RN   [59]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94 AND SER-256, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [60]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 657-919.
RX   PubMed=10840043; DOI=10.1074/jbc.M004571200;
RA   Matias P.M., Donner P., Coelho R., Thomaz M., Peixoto C., Macedo S.,
RA   Otto N., Joschko S., Scholz P., Wegg A., Baesler S., Schaefer M.,
RA   Egner U., Carrondo M.A.;
RT   "Structural evidence for ligand specificity in the binding domain of
RT   the human androgen receptor. Implications for pathogenic gene
RT   mutations.";
RL   J. Biol. Chem. 275:26164-26171(2000).
RN   [61]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 670-917.
RX   PubMed=11906285; DOI=10.1021/jm011072j;
RA   Matias P.M., Carrondo M.A., Coelho R., Thomaz M., Zhao X.Y., Wegg A.,
RA   Crusius K., Egner U., Donner P.;
RT   "Structural basis for the glucocorticoid response in a mutant human
RT   androgen receptor (AR(ccr)) derived from an androgen-independent
RT   prostate cancer.";
RL   J. Med. Chem. 45:1439-1446(2002).
RN   [62]
RP   X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 671-919 IN COMPLEXES WITH
RP   N-TERMINAL MODULATING DOMAIN AND NCOA2, INTERACTION WITH NCOA1, AND
RP   CHARACTERIZATION OF VARIANT PROSTATE CANCER M-730.
RX   PubMed=15525515; DOI=10.1016/j.molcel.2004.09.036;
RA   He B., Gampe R.T. Jr., Kole A.J., Hnat A.T., Stanley T.B., An G.,
RA   Stewart E.L., Kalman R.I., Minges J.T., Wilson E.M.;
RT   "Structural basis for androgen receptor interdomain and coactivator
RT   interactions suggests a transition in nuclear receptor activation
RT   function dominance.";
RL   Mol. Cell 16:425-438(2004).
RN   [63]
RP   X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 669-919 IN COMPLEXES WITH
RP   DIHYDROTESTOSTERONE AND NCOA1; NCOA2; NCOA3 AND NCOA4, FUNCTION,
RP   INTERACTION WITH NCOA1; NCOA2; NCOA3 AND NCOA4, AND MUTAGENESIS OF
RP   LYS-720 AND GLU-897.
RX   PubMed=15563469; DOI=10.1074/jbc.M407046200;
RA   Estebanez-Perpina E., Moore J.M.R., Mar E., Delgado-Rodrigues E.,
RA   Nguyen P., Baxter J.D., Buehrer B.M., Webb P., Fletterick R.J.,
RA   Guy R.K.;
RT   "The molecular mechanisms of coactivator utilization in ligand-
RT   dependent transactivation by the androgen receptor.";
RL   J. Biol. Chem. 280:8060-8068(2005).
RN   [64]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 664-919 IN COMPLEXES WITH
RP   NONSTEROIDAL LIGANDS, MUTAGENESIS OF TRP-741, CHARACTERIZATION OF
RP   VARIANT PROSTATE CANCER ALA-877, AND CHARACTERIZATION OF VARIANT AIS
RP   THR-895.
RX   PubMed=16129672; DOI=10.1074/jbc.M507464200;
RA   Bohl C.E., Miller D.D., Chen J., Bell C.E., Dalton J.T.;
RT   "Structural basis for accommodation of nonsteroidal ligands in the
RT   androgen receptor.";
RL   J. Biol. Chem. 280:37747-37754(2005).
RN   [65]
RP   X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 654-919 IN COMPLEXES WITH
RP   TESTOSTERONE; DIHYDROTESTOSTERONE AND TETRAHYDROGESTRINONE.
RX   PubMed=16641486; DOI=10.1110/ps.051905906;
RA   Pereira de Jesus-Tran K., Cote P.-L., Cantin L., Blanchet J.,
RA   Labrie F., Breton R.;
RT   "Comparison of crystal structures of human androgen receptor ligand-
RT   binding domain complexed with various agonists reveals molecular
RT   determinants responsible for binding affinity.";
RL   Protein Sci. 15:987-999(2006).
RN   [66]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 671-918 IN COMPLEX WITH
RP   NR0B2.
RX   PubMed=18007036; DOI=10.1107/S0907444907045702;
RA   Jouravel N., Sablin E., Arnold L.A., Guy R.K., Fletterick R.J.;
RT   "Interaction between the androgen receptor and a segment of its
RT   corepressor SHP.";
RL   Acta Crystallogr. D 63:1198-1200(2007).
RN   [67]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 671-919 OF MUTANT ALA-877 IN
RP   COMPLEX WITH THE ANTIANDROGEN CYPROTERONE ACETATE, CHARACTERIZATION OF
RP   VARIANT PROSTATE CANCER ALA-877, AND MUTAGENESIS OF LEU-701.
RX   PubMed=17311914; DOI=10.1074/jbc.M611711200;
RA   Bohl C.E., Wu Z., Miller D.D., Bell C.E., Dalton J.T.;
RT   "Crystal structure of the T877A human androgen receptor ligand-binding
RT   domain complexed to cyproterone acetate provides insight for ligand-
RT   induced conformational changes and structure-based drug design.";
RL   J. Biol. Chem. 282:13648-13655(2007).
RN   [68]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 663-919 OF WILD-TYPE AND
RP   MUTANT TYR-874 IN COMPLEX WITH TESTOSTERONE AND NCOA2, ACTIVATION BY
RP   THE N-TERMINAL MODULATING DOMAIN, INTERACTION WITH NCOA2 AND MAGEA11,
RP   FUNCTION, MUTAGENESIS OF LYS-720 AND GLU-897, AND CHARACTERIZATION OF
RP   VARIANT PROSTATE CANCER TYR-874.
RX   PubMed=17591767; DOI=10.1074/jbc.M703268200;
RA   Askew E.B., Gampe R.T. Jr., Stanley T.B., Faggart J.L., Wilson E.M.;
RT   "Modulation of androgen receptor activation function 2 by testosterone
RT   and dihydrotestosterone.";
RL   J. Biol. Chem. 282:25801-25816(2007).
RN   [69]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 654-919 IN COMPLEX WITH
RP   EM5744.
RX   PubMed=17711855; DOI=10.1074/jbc.M705524200;
RA   Cantin L., Faucher F., Couture J.-F., de Jesus-Tran K.P., Legrand P.,
RA   Ciobanu L.C., Frechette Y., Labrecque R., Singh S.M., Labrie F.,
RA   Breton R.;
RT   "Structural characterization of the human androgen receptor ligand-
RT   binding domain complexed with EM5744, a rationally designed steroidal
RT   ligand bearing a bulky chain directed toward helix 12.";
RL   J. Biol. Chem. 282:30910-30919(2007).
RN   [70]
RP   X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 669-919 IN COMPLEXES WITH
RP   SYNTHETIC LIGANDS, FUNCTION, AND INTERACTION WITH NCOA2.
RX   PubMed=17911242; DOI=10.1073/pnas.0708036104;
RA   Estebanez-Perpina E., Arnold L.A., Nguyen P., Rodrigues E.D., Mar E.,
RA   Bateman R., Pallai P., Shokat K.M., Baxter J.D., Guy R.K., Webb P.,
RA   Fletterick R.J.;
RT   "A surface on the androgen receptor that allosterically regulates
RT   coactivator binding.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:16074-16079(2007).
RN   [71]
RP   REVIEW ON VARIANTS.
RX   PubMed=1458719;
RA   Pinsky L., Trifiro M.A., Kaufman M., Beitel L.K., Mhatre A.,
RA   Kazemi-Esfarjani P., Sabbaghian N., Lumbroso R., Alvarado C.,
RA   Vasiliou M., Gottlieb B.;
RT   "Androgen resistance due to mutation of the androgen receptor.";
RL   Clin. Invest. Med. 15:456-472(1992).
RN   [72]
RP   REVIEW ON VARIANTS AIS.
RX   PubMed=8339746; DOI=10.1007/BF02125442;
RA   Brown T.R., Scherer P.A., Chang Y.-T., Migeon C.J., Ghirri P.,
RA   Murono K., Zhou Z.;
RT   "Molecular genetics of human androgen insensitivity.";
RL   Eur. J. Pediatr. 152 Suppl. 2:S62-S69(1993).
RN   [73]
RP   REVIEW ON VARIANTS.
RX   PubMed=8240973; DOI=10.1016/0960-0760(93)90178-Y;
RA   Sultan C., Lumbroso S., Poujol N., Belon C., Boudon C.,
RA   Lobaccaro J.-M.;
RT   "Mutations of androgen receptor gene in androgen insensitivity
RT   syndromes.";
RL   J. Steroid Biochem. Mol. Biol. 46:519-530(1993).
RN   [74]
RP   REVIEW ON VARIANTS.
RX   PubMed=7937057;
RA   Patterson M.N., Hughes I.A., Gottlieb B., Pinsky L.;
RT   "The androgen receptor gene mutations database.";
RL   Nucleic Acids Res. 22:3560-3562(1994).
RN   [75]
RP   REVIEW ON VARIANTS.
RX   PubMed=7626493; DOI=10.1016/0960-0760(95)00090-M;
RA   Brinkmann A.O., Jenster G., Ris-Stalpers C., van der Korput J.A.G.M.,
RA   Bruggenwirth H.T., Boehmer A.L.M., Trapman J.;
RT   "Androgen receptor mutations.";
RL   J. Steroid Biochem. Mol. Biol. 53:443-448(1995).
RN   [76]
RP   REVIEW ON VARIANTS.
RX   PubMed=9016528; DOI=10.1093/nar/25.1.158;
RA   Gottlieb B., Trifiro M.A., Lumbroso R., Vasiliou D.M., Pinsky L.;
RT   "The androgen receptor gene mutations database.";
RL   Nucleic Acids Res. 25:158-162(1997).
RN   [77]
RP   REVIEW ON VARIANTS.
RX   PubMed=22334387; DOI=10.1002/humu.22046;
RA   Gottlieb B., Beitel L.K., Nadarajah A., Paliouras M., Trifiro M.;
RT   "The androgen receptor gene mutations database: 2012 update.";
RL   Hum. Mutat. 33:887-894(2012).
RN   [78]
RP   VARIANT LNCAP ALA-877.
RX   PubMed=2260966; DOI=10.1016/S0006-291X(05)80067-1;
RA   Veldscholte J., Ris-Stalpers C., Kuiper G.G.J.M., Jenster G.,
RA   Berrevoets C.A., Claassen E., van Rooij H.C.J., Trapman J.,
RA   Brinkmann A.O., Mulder E.;
RT   "A mutation in the ligand binding domain of the androgen receptor of
RT   human LNCaP cells affects steroid binding characteristics and response
RT   to anti-androgens.";
RL   Biochem. Biophys. Res. Commun. 173:534-540(1990).
RN   [79]
RP   VARIANTS AIS CYS-774; GLN-831 AND MET-866.
RX   PubMed=2082179; DOI=10.1210/mend-4-12-1759;
RA   Brown T.R., Lubahn D.B., Wilson E.M., French F.S., Migeon C.J.,
RA   Corfen J.L.;
RT   "Functional characterization of naturally occurring mutant androgen
RT   receptors from subjects with complete androgen insensitivity.";
RL   Mol. Endocrinol. 4:1759-1772(1990).
RN   [80]
RP   VARIANT CYS-774.
RX   PubMed=1856263; DOI=10.1210/jcem-73-2-318;
RA   Marcelli M., Tilley W.D., Zoppi S., Griffin J.E., Wilson J.D.,
RA   McPhaul M.J.;
RT   "Androgen resistance associated with a mutation of the androgen
RT   receptor at amino acid 772 (Arg-->Cys) results from a combination of
RT   decreased messenger ribonucleic acid levels and impairment of receptor
RT   function.";
RL   J. Clin. Endocrinol. Metab. 73:318-325(1991).
RN   [81]
RP   VARIANT AIS PRO-617.
RX   PubMed=1999491; DOI=10.1172/JCI115076;
RA   Marcelli M., Zoppi S., Grino P.B., Griffin J.E., Wilson J.D.,
RA   McPhaul M.J.;
RT   "A mutation in the DNA-binding domain of the androgen receptor gene
RT   causes complete testicular feminization in a patient with receptor-
RT   positive androgen resistance.";
RL   J. Clin. Invest. 87:1123-1126(1991).
RN   [82]
RP   VARIANT PAIS CYS-763.
RX   PubMed=2010552; DOI=10.1172/JCI115147;
RA   McPhaul M.J., Marcelli M., Tilley W.D., Griffin J.E.,
RA   Isidro-Gutierrez R.F., Wilson J.D.;
RT   "Molecular basis of androgen resistance in a family with a qualitative
RT   abnormality of the androgen receptor and responsive to high-dose
RT   androgen therapy.";
RL   J. Clin. Invest. 87:1413-1421(1991).
RN   [83]
RP   POLY-GLN REGION EXPANSION, AND INVOLVEMENT IN SPINAL AND BULBAR
RP   MUSCULAR ATROPHY.
RX   PubMed=2062380; DOI=10.1038/352077a0;
RA   la Spada A.R., Wilson E.M., Lubahn D.B., Harding A.E., Fischbeck K.H.;
RT   "Androgen receptor gene mutations in X-linked spinal and bulbar
RT   muscular atrophy.";
RL   Nature 352:77-79(1991).
RN   [84]
RP   VARIANTS AIS CYS-774 AND HIS-774.
RX   PubMed=1609793;
RA   Prior L., Bordet S., Trifiro M.A., Mhatre A., Kaufman M., Pinsky L.,
RA   Wrogemann K., Belsham D.D., Pereira F., Greenberg C.R., Trapman J.,
RA   Brinkmann A.O., Chang C., Liao S.;
RT   "Replacement of arginine 773 by cysteine or histidine in the human
RT   androgen receptor causes complete androgen insensitivity with
RT   different receptor phenotypes.";
RL   Am. J. Hum. Genet. 51:143-155(1992).
RN   [85]
RP   VARIANTS PAIS LYS-608 AND LEU-866.
RX   PubMed=1424203; DOI=10.1111/j.1365-2265.1992.tb02313.x;
RA   Saunders P.T., Padayachi T., Tincello D.G., Shalet S.M., Wu F.C.;
RT   "Point mutations detected in the androgen receptor gene of three men
RT   with partial androgen insensitivity syndrome.";
RL   Clin. Endocrinol. (Oxf.) 37:214-220(1992).
RN   [86]
RP   VARIANT AIS THR-765.
RX   PubMed=1426313;
RA   Sweet C.R., Behzadian M.A., McDonough P.G.;
RT   "A unique point mutation in the androgen receptor gene in a family
RT   with complete androgen insensitivity syndrome.";
RL   Fertil. Steril. 58:703-707(1992).
RN   [87]
RP   VARIANT AIS VAL-749.
RX   PubMed=1487249; DOI=10.1007/BF00220088;
RA   Jakubiczka S., Werder E.A., Wieacker P.;
RT   "Point mutation in the steroid-binding domain of the androgen receptor
RT   gene in a family with complete androgen insensitivity syndrome
RT   (CAIS).";
RL   Hum. Genet. 90:311-312(1992).
RN   [88]
RP   VARIANTS AIS, AND VARIANTS PAIS.
RX   PubMed=1307250; DOI=10.1093/hmg/1.7.497;
RA   Batch J.A., Williams D.M., Davies H.R., Brown B.D., Evans B.A.J.,
RA   Hughes I.A., Patterson M.N.;
RT   "Androgen receptor gene mutations identified by SSCP in fourteen
RT   subjects with androgen insensitivity syndrome.";
RL   Hum. Mol. Genet. 1:497-503(1992).
RN   [89]
RP   VARIANT AIS VAL-787.
RX   PubMed=1569163; DOI=10.1210/jc.74.5.1152;
RA   Nakao R., Haji M., Yanase T., Ogo A., Takayanagi R., Katsube T.,
RA   Fukumaki Y., Nawata H.;
RT   "A single amino acid substitution (Met-786-->Val) in the steroid-
RT   binding domain of human androgen receptor leads to complete androgen
RT   insensitivity syndrome.";
RL   J. Clin. Endocrinol. Metab. 74:1152-1157(1992).
RN   [90]
RP   VARIANTS AIS ARG-741 AND CYS-834.
RX   PubMed=1464650; DOI=10.1210/jc.75.6.1474;
RA   Wilson C.M., Griffin J.E., Wilson J.D., Marcelli M., Zoppi S.,
RA   McPhaul M.J.;
RT   "Immunoreactive androgen receptor expression in subjects with androgen
RT   resistance.";
RL   J. Clin. Endocrinol. Metab. 75:1474-1478(1992).
RN   [91]
RP   VARIANTS AIS, AND VARIANTS PAIS.
RX   PubMed=1430233; DOI=10.1172/JCI116093;
RA   McPhaul M.J., Marcelli M., Zoppi S., Wilson C.M., Griffin J.E.,
RA   Wilson J.D.;
RT   "Mutations in the ligand-binding domain of the androgen receptor gene
RT   cluster in two regions of the gene.";
RL   J. Clin. Invest. 90:2097-2101(1992).
RN   [92]
RP   VARIANT PROSTATE CANCER ALA-877.
RX   PubMed=1562539; DOI=10.1016/0960-0760(92)90401-4;
RA   Veldscholte J., Berrevoets C.A., Ris-Stalpers C., Kuiper G.G.J.M.,
RA   Jenster G., Trapman J., Brinkmann A.O., Mulder E.;
RT   "The androgen receptor in LNCaP cells contains a mutation in the
RT   ligand binding domain which affects steroid binding characteristics
RT   and response to antiandrogens.";
RL   J. Steroid Biochem. Mol. Biol. 41:665-669(1992).
RN   [93]
RP   VARIANTS AIS TYR-559 AND ARG-576, AND VARIANTS PAIS GLY-597 AND
RP   PRO-617.
RX   PubMed=1316540; DOI=10.1210/me.6.3.409;
RA   Zoppi S., Marcelli M., Deslypere J.-P., Griffin J.E., Wilson J.D.,
RA   McPhaul M.J.;
RT   "Amino acid substitutions in the DNA-binding domain of the human
RT   androgen receptor are a frequent cause of receptor-binding positive
RT   androgen resistance.";
RL   Mol. Endocrinol. 6:409-415(1992).
RN   [94]
RP   VARIANTS AIS SER-705; VAL-749; PHE-759; HIS-774; CYS-855 AND GLY-864.
RX   PubMed=1480178; DOI=10.1210/me.6.11.1909;
RA   De Bellis A., Quigley C.A., Cariello N.F., el-Awady M.K., Sar M.,
RA   Lane M.V., Wilson E.M., French F.S.;
RT   "Single base mutations in the human androgen receptor gene causing
RT   complete androgen insensitivity: rapid detection by a modified
RT   denaturing gradient gel electrophoresis technique.";
RL   Mol. Endocrinol. 6:1909-1920(1992).
RN   [95]
RP   VARIANT PAIS/BREAST CANCER GLN-607.
RX   PubMed=1303262; DOI=10.1038/ng1092-132;
RA   Wooster R., Mangion J., Eeles R., Smith S., Dowsett M., Averill D.,
RA   Barrett-Lee P., Easton D.F., Ponder B.A., Stratton M.R.;
RT   "A germline mutation in the androgen receptor gene in two brothers
RT   with breast cancer and Reifenstein syndrome.";
RL   Nat. Genet. 2:132-134(1992).
RN   [96]
RP   VARIANT MET-730.
RX   PubMed=1631125; DOI=10.1073/pnas.89.14.6319;
RA   Newmark J.R., Hardy D.O., Tonb D.C., Carter B.S., Epstein J.I.,
RA   Isaacs W.B., Brown T.R., Barrack E.R.;
RT   "Androgen receptor gene mutations in human prostate cancer.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:6319-6323(1992).
RN   [97]
RP   VARIANTS ARG-205 AND ASP-793.
RX   PubMed=8213813;
RA   Macke J.P., Hu N., Hu S., Bailey M., King V.L., Brown T., Hamer D.,
RA   Nathans J.;
RT   "Sequence variation in the androgen receptor gene is not a common
RT   determinant of male sexual orientation.";
RL   Am. J. Hum. Genet. 53:844-852(1993).
RN   [98]
RP   VARIANT AIS PHE-581.
RX   PubMed=8224266;
RA   Lumbroso S., Lobaccaro J.-M., Belon C., Martin D., Chaussain J.-L.,
RA   Sultan C.;
RT   "A new mutation within the deoxyribonucleic acid-binding domain of the
RT   androgen receptor gene in a family with complete androgen
RT   insensitivity syndrome.";
RL   Fertil. Steril. 60:814-819(1993).
RN   [99]
RP   VARIANT AIS VAL-754.
RX   PubMed=8103398; DOI=10.1093/hmg/2.7.1041;
RA   Lobaccaro J.-M., Lumbroso S., Ktari R., Dumas R., Sultan C.;
RT   "An exonic point mutation creates a MaeIII site in the androgen
RT   receptor gene of a family with complete androgen insensitivity
RT   syndrome.";
RL   Hum. Mol. Genet. 2:1041-1043(1993).
RN   [100]
RP   VARIANT PAIS/BREAST CANCER LYS-608.
RX   PubMed=8281139; DOI=10.1093/hmg/2.11.1799;
RA   Lobaccaro J.-M., Lumbroso S., Belon C., Galtier-Dereure F.,
RA   Bringer J., Lesimple T., Namer M., Cutuli B.F., Pujol H., Sultan C.;
RT   "Androgen receptor gene mutation in male breast cancer.";
RL   Hum. Mol. Genet. 2:1799-1802(1993).
RN   [101]
RP   VARIANT AIS ARG-807.
RX   PubMed=8281140; DOI=10.1093/hmg/2.11.1809;
RA   Adeyemo O., Kallio P.J., Palvimo J.J., Kontula K., Jaenne O.A.;
RT   "A single-base substitution in exon 6 of the androgen receptor gene
RT   causing complete androgen insensitivity: the mutated receptor fails to
RT   transactivate but binds to DNA in vitro.";
RL   Hum. Mol. Genet. 2:1809-1812(1993).
RN   [102]
RP   VARIANT PAIS VAL-743.
RX   PubMed=8325932; DOI=10.1210/jcem.77.1.8325932;
RA   Nakao R., Yanase T., Sakai Y., Haji M., Nawata H.;
RT   "A single amino acid substitution (Gly743 --> Val) in the steroid-
RT   binding domain of the human androgen receptor leads to Reifenstein
RT   syndrome.";
RL   J. Clin. Endocrinol. Metab. 77:103-107(1993).
RN   [103]
RP   VARIANTS AIS LYS-681 AND THR-842, AND VARIANTS PAIS HIS-840 AND
RP   LEU-866.
RX   PubMed=8325950; DOI=10.1210/jc.77.1.262;
RA   Hiort O., Huang Q., Sinnecker G.H., Sadeghi-Nejad A., Kruse K.,
RA   Wolfe H.J., Yandell D.W.;
RT   "Single strand conformation polymorphism analysis of androgen receptor
RT   gene mutations in patients with androgen insensitivity syndromes:
RT   application for diagnosis, genetic counseling, and therapy.";
RL   J. Clin. Endocrinol. Metab. 77:262-266(1993).
RN   [104]
RP   VARIANTS PAIS HIS-855 AND MET-869.
RX   PubMed=8097257; DOI=10.1136/jmg.30.3.198;
RA   Batch J.A., Evans B.A.J., Hughes I.A., Patterson M.N.;
RT   "Mutations of the androgen receptor gene identified in perineal
RT   hypospadias.";
RL   J. Med. Genet. 30:198-201(1993).
RN   [105]
RP   VARIANT AIS VAL-743.
RX   PubMed=8096390; DOI=10.1016/0960-0760(93)90081-7;
RA   Lobaccaro J.-M., Lumbroso S., Berta P., Chaussain J.-L., Sultan C.;
RT   "Complete androgen insensitivity syndrome associated with a de novo
RT   mutation of the androgen receptor gene detected by single strand
RT   conformation polymorphism.";
RL   J. Steroid Biochem. Mol. Biol. 44:211-216(1993).
RN   [106]
RP   VARIANTS PROSTATE CANCER HIS-701 AND ALA-877.
RX   PubMed=8274409; DOI=10.1016/0960-0760(93)90316-O;
RA   Suzuki H., Sato N., Watabe Y., Masai M., Seino S., Shimazaki J.;
RT   "Androgen receptor gene mutations in human prostate cancer.";
RL   J. Steroid Biochem. Mol. Biol. 46:759-765(1993).
RN   [107]
RP   VARIANT AIS MET-866, AND VARIANT PAIS LEU-866.
RX   PubMed=8446106; DOI=10.1210/me.7.1.37;
RA   Kazemi-Esfarjani P., Beitel L.K., Trifiro M.A., Kaufman M., Rennie P.,
RA   Sheppard P., Matusik R., Pinsky L.;
RT   "Substitution of valine-865 by methionine or leucine in the human
RT   androgen receptor causes complete or partial androgen insensitivity,
RT   respectively with distinct androgen receptor phenotypes.";
RL   Mol. Endocrinol. 7:37-46(1993).
RN   [108]
RP   VARIANT PROSTATE CANCER MET-715.
RX   PubMed=8145761; DOI=10.1210/me.7.12.1541;
RA   Culig Z., Hobisch A., Cronauer M.V., Cato A.C.B., Hittmair A.,
RA   Radmayr C., Eberle J., Bartsch G., Klocker H.;
RT   "Mutant androgen receptor detected in an advanced-stage prostatic
RT   carcinoma is activated by adrenal androgens and progesterone.";
RL   Mol. Endocrinol. 7:1541-1550(1993).
RN   [109]
RP   VARIANTS AIS PHE-581; VAL-743; VAL-754; GLU-767 AND CYS-855.
RA   Lobaccaro J.-M., Lumbroso S., Belon C., Chaussain J.L., Toublanc J.E.,
RA   Leheup B., Sultan C.;
RT   "Androgen receptor (AR) gene mutations in 6 families with androgen
RT   insensitivity syndrome (Abstract #114).";
RL   Pediatr. Res. Suppl. 33:S22-S22(1993).
RN   [110]
RP   VARIANTS PROSTATE CANCER LEU-340 AND GLU-798.
RX   PubMed=7511268;
RA   Castagnaro M., Yandell D.W., Dockhorn-Dworniczak B., Wolfe H.J.,
RA   Poremba C.;
RT   "Androgen receptor gene mutations and p53 gene analysis in advanced
RT   prostate cancer.";
RL   Verh. Dtsch. Ges. Pathol. 77:119-123(1993).
RN   [111]
RP   POLY-GLN REGION CONTRACTION, AND INVOLVEMENT IN PROSTATE CANCER.
RX   PubMed=8292051; DOI=10.1006/bbrc.1994.1011;
RA   Schoenberg M.P., Hakimi J.M., Wang S., Bova G.S., Epstein J.I.,
RA   Fischbeck K.H., Isaacs W.B., Walsh P.C., Barrack E.R.;
RT   "Microsatellite mutation (CAG24-->18) in the androgen receptor gene in
RT   human prostate cancer.";
RL   Biochem. Biophys. Res. Commun. 198:74-80(1994).
RN   [112]
RP   VARIANT PROSTATE CANCER ALA-877.
RX   PubMed=8187068;
RA   Gaddipati J.P., McLeod D.G., Heidenberg H.B., Sesterhenn I.A.,
RA   Finger M.J., Moul J.W., Srivastava S.;
RT   "Frequent detection of codon 877 mutation in the androgen receptor
RT   gene in advanced prostate cancers.";
RL   Cancer Res. 54:2861-2864(1994).
RN   [113]
RP   VARIANT PAIS TRP-568.
RX   PubMed=7910529;
RA   Lobaccaro J.-M., Belon C., Lumbroso S., Olewniczack G.,
RA   Carre-Pigeon F., Job J.C., Chaussain J.L., Toublanc J.E., Sultan C.;
RT   "Molecular prenatal diagnosis of partial androgen insensitivity
RT   syndrome based on the Hind III polymorphism of the androgen receptor
RT   gene.";
RL   Clin. Endocrinol. (Oxf.) 40:297-302(1994).
RN   [114]
RP   VARIANT PAIS HIS-840.
RX   PubMed=7909256; DOI=10.1530/eje.0.1300327;
RA   Lumbroso S., Lobaccaro J.-M., Belon C., Amram S., Bachelard B.,
RA   Garandeau P., Sultan C.;
RT   "Molecular prenatal exclusion of familial partial androgen
RT   insensitivity (Reifenstein syndrome).";
RL   Eur. J. Endocrinol. 130:327-332(1994).
RN   [115]
RP   VARIANT PAIS HIS-840.
RX   PubMed=8205256; DOI=10.1530/eje.0.1300569;
RA   Imasaki K., Hasegawa T., Okabe T., Sakai Y., Haji M., Takayanagi R.,
RA   Nawata H.;
RT   "Single amino acid substitution (840Arg-->His) in the hormone-binding
RT   domain of the androgen receptor leads to incomplete androgen
RT   insensitivity syndrome associated with a thermolabile androgen
RT   receptor.";
RL   Eur. J. Endocrinol. 130:569-574(1994).
RN   [116]
RP   VARIANT PAIS VAL-870.
RX   PubMed=8033918; DOI=10.1007/BF01956409;
RA   Hiort O., Klauber G., Cendron M., Sinnecker G.H., Keim L.,
RA   Schwinger E., Wolfe H.J., Yandell D.W.;
RT   "Molecular characterization of the androgen receptor gene in boys with
RT   hypospadias.";
RL   Eur. J. Pediatr. 153:317-321(1994).
RN   [117]
RP   VARIANT PAIS ASP-690 DEL.
RA   Schwartz M., Skovby F., Mueller J., Nielsen O., Skakkebaek N.E.;
RT   "Partial androgen insensitivity (PAIS) in a large eskimo kindred
RT   caused by a delD690 mutation in the androgen receptor (AR) gene
RT   (Abstract #244).";
RL   Horm. Res. 41:117-117(1994).
RN   [118]
RP   VARIANTS AIS PHE-582 DEL; ARG-615 DEL AND HIS-615.
RX   PubMed=8162033; DOI=10.1093/hmg/3.1.21;
RA   Beitel L.K., Prior L., Vasiliou D.M., Gottlieb B., Kaufman M.,
RA   Lumbroso R., Alvarado C., McGillivray B., Trifiro M.A., Pinsky L.;
RT   "Complete androgen insensitivity due to mutations in the probable
RT   alpha-helical segments of the DNA-binding domain in the human androgen
RT   receptor.";
RL   Hum. Mol. Genet. 3:21-27(1994).
RN   [119]
RP   VARIANTS PAIS SER-582; TYR-604; ALA-708; LEU-754 AND HIS-771, AND
RP   VARIANT AIS TRP-779.
RX   PubMed=7981687; DOI=10.1093/hmg/3.7.1163;
RA   Hiort O., Wodtke A., Struve D., Zoellner A., Sinnecker G.H.;
RT   "Detection of point mutations in the androgen receptor gene using non-
RT   isotopic single strand conformation polymorphism analysis.";
RL   Hum. Mol. Genet. 3:1163-1166(1994).
RN   [120]
RP   VARIANT AIS PHE-601.
RX   PubMed=7981689; DOI=10.1093/hmg/3.7.1169;
RA   Baldazzi L., Baroncini C., Pirazzoli P., Balsamo A., Capelli M.,
RA   Marchetti G., Bernardi F., Cacciari E.;
RT   "Two mutations causing complete androgen insensitivity: a frame-shift
RT   in the steroid binding domain and a Cys-->Phe substitution in the
RT   second zinc finger of the androgen receptor.";
RL   Hum. Mol. Genet. 3:1169-1170(1994).
RN   [121]
RP   VARIANTS PAIS ARG-616; HIS-840 AND MET-889.
RX   PubMed=8126121; DOI=10.1210/jc.78.3.513;
RA   De Bellis A., Quigley C.A., Marschke K.B., el-Awady M.K., Lane M.V.,
RA   Smith E.P., Sar M., Wilson E.M., French F.S.;
RT   "Characterization of mutant androgen receptors causing partial
RT   androgen insensitivity syndrome.";
RL   J. Clin. Endocrinol. Metab. 78:513-522(1994).
RN   [122]
RP   VARIANT AIS PHE-790.
RX   PubMed=7962294; DOI=10.1210/jc.79.4.1202;
RA   Tsukada T., Inoue M., Tachibana S., Nakai Y., Takebe H.;
RT   "An androgen receptor mutation causing androgen resistance in
RT   undervirilized male syndrome.";
RL   J. Clin. Endocrinol. Metab. 79:1202-1207(1994).
RN   [123]
RP   VARIANTS AIS CYS-840 AND HIS-840.
RX   PubMed=8040309; DOI=10.1172/JCI117368;
RA   Beitel L.K., Kazemi-Esfarjani P., Kaufman M., Lumbroso R.,
RA   DiGeorge A.M., Killinger D.W., Trifiro M.A., Pinsky L.;
RT   "Substitution of arginine-839 by cysteine or histidine in the androgen
RT   receptor causes different receptor phenotypes in cultured cells and
RT   coordinate degrees of clinical androgen resistance.";
RL   J. Clin. Invest. 94:546-554(1994).
RN   [124]
RP   VARIANTS AIS, AND VARIANTS PAIS.
RX   PubMed=7929841; DOI=10.1172/JCI117507;
RA   Marcelli M., Zoppi S., Wilson C.M., Griffin J.E., McPhaul M.J.;
RT   "Amino acid substitutions in the hormone-binding domain of the human
RT   androgen receptor alter the stability of the hormone receptor
RT   complex.";
RL   J. Clin. Invest. 94:1642-1650(1994).
RN   [125]
RP   VARIANT AIS LYS-727.
RX   PubMed=7993455; DOI=10.1016/S0140-6736(94)92385-X;
RA   Yong E.L., Ng S.C., Roy A.C., Yun G., Ratnam S.S.;
RT   "Pregnancy after hormonal correction of severe spermatogenic defect
RT   due to mutation in androgen receptor gene.";
RL   Lancet 344:826-827(1994).
RN   [126]
RP   VARIANTS AIS HIS-615 AND LEU-764, AND VARIANTS PAIS VAL-742 AND
RP   THR-745.
RX   PubMed=7970939; DOI=10.1203/00006450-199408000-00015;
RA   Ris-Stalpers C., Hoogenboezem T., Sleddens H.F.B.M.,
RA   Verleun-Mooijman M.C.T., Degenhart H.J., Drop S.L.S., Halley D.J.J.,
RA   Oosterwijk J.C., Hodgins M.B., Trapman J., Brinkmann A.O.;
RT   "A practical approach to the detection of androgen receptor gene
RT   mutations and pedigree analysis in families with X-linked androgen
RT   insensitivity.";
RL   Pediatr. Res. 36:227-234(1994).
RN   [127]
RP   VARIANT AIS HIS-840.
RX   PubMed=8830623;
RA   Imai A., Ohno T., Iida K., Ohsuye K., Okano Y., Tamaya T.;
RT   "A frame-shift mutation of the androgen receptor gene in a patient
RT   with receptor-negative complete testicular feminization: comparison
RT   with a single base substitution in a receptor-reduced incomplete
RT   form.";
RL   Ann. Clin. Biochem. 32:482-486(1995).
RN   [128]
RP   VARIANTS PROSTATE CANCER.
RX   PubMed=7712463;
RA   Takahashi H., Furusato M., Allsbrook W.C. Jr., Nishii H., Wakui S.,
RA   Barrett J.C., Boyd J.;
RT   "Prevalence of androgen receptor gene mutations in latent prostatic
RT   carcinomas from Japanese men.";
RL   Cancer Res. 55:1621-1624(1995).
RN   [129]
RP   VARIANT AIS VAL-881.
RX   PubMed=7641413; DOI=10.1111/j.1365-2265.1995.tb01895.x;
RA   Davies H.R., Hughes I.A., Patterson M.N.;
RT   "Genetic counselling in complete androgen insensitivity syndrome:
RT   trinucleotide repeat polymorphisms, single-strand conformation
RT   polymorphism and direct detection of two novel mutations in the
RT   androgen receptor gene.";
RL   Clin. Endocrinol. (Oxf.) 43:69-77(1995).
RN   [130]
RP   VARIANTS AIS SER-705 AND HIS-763, AND VARIANTS PAIS LEU-725; THR-737;
RP   HIS-774 AND GLU-798.
RX   PubMed=7671849; DOI=10.1210/er.16.3.271;
RA   Quigley C.A., De Bellis A., Marschke K.B., el-Awady M.K., Wilson E.M.,
RA   French F.S.;
RT   "Androgen receptor defects: historical, clinical, and molecular
RT   perspectives.";
RL   Endocr. Rev. 16:271-321(1995).
RN   [131]
RP   ERRATUM.
RA   Quigley C.A., De Bellis A., Marschke K.B., el-Awady M.K., Wilson E.M.,
RA   French F.S.;
RL   Endocr. Rev. 16:546-546(1995).
RN   [132]
RP   VARIANTS AIS LEU-831 AND GLN-831.
RX   PubMed=7633398; DOI=10.1093/hmg/4.4.515;
RA   Shkolny D.L., Brown T.R., Punnett H.H., Kaufman M., Trifiro M.A.,
RA   Pinsky L.;
RT   "Characterization of alternative amino acid substitutions at arginine
RT   830 of the androgen receptor that cause complete androgen
RT   insensitivity in three families.";
RL   Hum. Mol. Genet. 4:515-521(1995).
RN   [133]
RP   VARIANT AIS PRO-677.
RX   PubMed=7537149; DOI=10.1002/humu.1380050104;
RA   Belsham D.D., Pereira F., Greenberg C.R., Liao S., Wrogemann K.;
RT   "Leu-676-Pro mutation of the androgen receptor causes complete
RT   androgen insensitivity syndrome in a large Hutterite kindred.";
RL   Hum. Mutat. 5:28-33(1995).
RN   [134]
RP   VARIANT PAIS CYS-763, AND VARIANTS AIS TRP-779; VAL-807 AND CYS-855.
RX   PubMed=7581399; DOI=10.1002/humu.1380060208;
RA   Murono K., Mendonca B.B., Arnhold I.J.P., Rigon A.C.M.M., Migeon C.J.,
RA   Brown T.R.;
RT   "Human androgen insensitivity due to point mutations encoding amino
RT   acid substitutions in the androgen receptor steroid-binding domain.";
RL   Hum. Mutat. 6:152-162(1995).
RN   [135]
RP   VARIANT PROSTATE CANCER MET-730.
RX   PubMed=7591265; DOI=10.1002/ijc.2910630415;
RA   Peterziel H., Culig Z., Stober J., Hobisch A., Radmayr C., Bartsch G.,
RA   Klocker H., Cato A.C.B.;
RT   "Mutant androgen receptors in prostatic tumors distinguish between
RT   amino-acid-sequence requirements for transactivation and ligand
RT   binding.";
RL   Int. J. Cancer 63:544-550(1995).
RN   [136]
RP   VARIANT VAL-568.
RX   PubMed=7673412; DOI=10.1210/jc.80.9.2697;
RA   Allera A., Herbst M.A., Griffin J.E., Wilson J.D., Schweikert H.-U.,
RA   McPhaul M.J.;
RT   "Mutations of the androgen receptor coding sequence are infrequent in
RT   patients with isolated hypospadias.";
RL   J. Clin. Endocrinol. Metab. 80:2697-2699(1995).
RN   [137]
RP   VARIANT PROSTATE CANCER LEU-726.
RX   PubMed=8530589; DOI=10.1210/jc.80.12.3494;
RA   Elo J.P., Kvist L., Leinonen K., Isomaa V., Henttu P., Lukkarinen O.,
RA   Vihko P.;
RT   "Mutated human androgen receptor gene detected in a prostatic cancer
RT   patient is also activated by estradiol.";
RL   J. Clin. Endocrinol. Metab. 80:3494-3500(1995).
RN   [138]
RP   VARIANT PAIS THR-596.
RX   PubMed=7649358; DOI=10.1016/0303-7207(95)03554-K;
RA   Gast A., Neuschmid-Kaspar F., Klocker H., Cato A.C.B.;
RT   "A single amino acid exchange abolishes dimerization of the androgen
RT   receptor and causes Reifenstein syndrome.";
RL   Mol. Cell. Endocrinol. 111:93-98(1995).
RN   [139]
RP   VARIANTS PROSTATE CANCER.
RX   PubMed=7723794; DOI=10.1056/NEJM199505253322101;
RA   Taplin M.-E., Bubley G.J., Shuster T.D., Frantz M.E., Spooner A.E.,
RA   Ogata G.K., Keer H.N., Balk S.P.;
RT   "Mutation of the androgen-receptor gene in metastatic androgen-
RT   independent prostate cancer.";
RL   N. Engl. J. Med. 332:1393-1398(1995).
RN   [140]
RP   VARIANTS AIS AND PAIS.
RX   PubMed=8723113;
RX   DOI=10.1002/(SICI)1096-8628(19960503)63:1<218::AID-AJMG38>3.0.CO;2-P;
RA   Hiort O., Sinnecker G.H., Holterhus P.M., Nitsche E.M., Kruse K.;
RT   "The clinical and molecular spectrum of androgen insensitivity
RT   syndromes.";
RL   Am. J. Med. Genet. 63:218-222(1996).
RN   [141]
RP   VARIANTS PROSTATE CANCER.
RX   PubMed=9816170;
RA   Tilley W.D., Buchanan G., Hickey T.E., Bentel J.M.;
RT   "Mutations in the androgen receptor gene are associated with
RT   progression of human prostate cancer to androgen independence.";
RL   Clin. Cancer Res. 2:277-285(1996).
RN   [142]
RP   VARIANTS PAIS GLN-607; THR-610; LEU-754; HIS-840; THR-842 AND HIS-855,
RP   AND VARIANT AIS MET-866.
RX   PubMed=9039340; DOI=10.1046/j.1365-2265.1996.8600869.x;
RA   Weidemann W., Linck B., Haupt H., Mentrup B., Romalo G.,
RA   Stockklauser K., Brinkmann A.O., Schweikert H.-U., Spindler K.D.;
RT   "Clinical and biochemical investigations and molecular analysis of
RT   subjects with mutations in the androgen receptor gene.";
RL   Clin. Endocrinol. (Oxf.) 45:733-739(1996).
RN   [143]
RP   VARIANT AIS CYS-855.
RX   PubMed=9001799;
RA   Malmgren H., Gustavsson J., Tuvemo T., Dahl N.;
RT   "Rapid detection of a mutation hot-spot in the human androgen
RT   receptor.";
RL   Clin. Genet. 50:202-205(1996).
RN   [144]
RP   VARIANTS PAIS ILE-742; ILE-780; GLU-798; CYS-840; HIS-855 AND MET-869.
RX   PubMed=8824883; DOI=10.1093/hmg/5.2.265;
RA   Bevan C.L., Brown B.B., Davies H.R., Evans B.A.J., Hughes I.A.,
RA   Patterson M.N.;
RT   "Functional analysis of six androgen receptor mutations identified in
RT   patients with partial androgen insensitivity syndrome.";
RL   Hum. Mol. Genet. 5:265-273(1996).
RN   [145]
RP   VARIANT PAIS ARG-909.
RX   PubMed=8550758; DOI=10.1210/jcem.81.1.8550758;
RA   Choong C.S., Sturm M.J., Strophair J.A., McCulloch R.K., Tilley W.D.,
RA   Leedman P.J., Hurley D.M.;
RT   "Partial androgen insensitivity caused by an androgen receptor
RT   mutation at amino acid 907 (Gly-->Arg) that results in decreased
RT   ligand binding affinity and reduced androgen receptor messenger
RT   ribonucleic acid levels.";
RL   J. Clin. Endocrinol. Metab. 81:236-243(1996).
RN   [146]
RP   VARIANT AIS ARG-707.
RX   PubMed=8626869; DOI=10.1210/jcem.81.5.8626869;
RA   Lumbroso S., Lobaccaro J.-M., Georget V., Leger J., Poujol N.,
RA   Terouanne B., Evain-Brion D., Czernichow P., Sultan C.;
RT   "A novel substitution (Leu707Arg) in exon 4 of the androgen receptor
RT   gene causes complete androgen resistance.";
RL   J. Clin. Endocrinol. Metab. 81:1984-1988(1996).
RN   [147]
RP   VARIANT AIS ILE-780.
RX   PubMed=8768864; DOI=10.1210/jc.81.8.2994;
RA   Rodien P., Mebarki F., Mowszowicz I., Chaussain J.L., Young J.,
RA   Morel Y., Schaison G.;
RT   "Different phenotypes in a family with androgen insensitivity caused
RT   by the same M780I point mutation in the androgen receptor gene.";
RL   J. Clin. Endocrinol. Metab. 81:2994-2998(1996).
RN   [148]
RP   VARIANT PAIS LYS-2.
RX   PubMed=8823308; DOI=10.1172/JCI118930;
RA   Choong C.S., Quigley C.A., French F.S., Wilson E.M.;
RT   "A novel missense mutation in the amino-terminal domain of the human
RT   androgen receptor gene in a family with partial androgen insensitivity
RT   syndrome causes reduced efficiency of protein translation.";
RL   J. Clin. Invest. 98:1423-1431(1996).
RN   [149]
RP   VARIANT AIS ASP-573.
RX   PubMed=8918984; DOI=10.1016/0960-0760(96)00095-7;
RA   Bruggenwirth H.T., Boehmer A.L.M., Verleun-Mooijman M.C.T.,
RA   Hoogenboezem T., Kleijer W.J., Otten B.J., Trapman J., Brinkmann A.O.;
RT   "Molecular basis of androgen insensitivity.";
RL   J. Steroid Biochem. Mol. Biol. 58:569-575(1996).
RN   [150]
RP   VARIANT AIS SER-548.
RX   PubMed=8683794; DOI=10.1097/00005392-199608001-00077;
RA   Sutherland R.W., Wiener J.S., Hicks J.P., Marcelli M.,
RA   Gonzales E.T. Jr., Roth D.R., Lamb D.J.;
RT   "Androgen receptor gene mutations are rarely associated with isolated
RT   penile hypospadias.";
RL   J. Urol. 156:828-831(1996).
RN   [151]
RP   VARIANT AIS PRO-616.
RX   PubMed=8647313; DOI=10.1016/0303-7207(95)03709-8;
RA   Lobaccaro J.-M., Poujol N., Chiche L., Lumbroso S., Brown T.R.,
RA   Sultan C.;
RT   "Molecular modeling and in vitro investigations of the human androgen
RT   receptor DNA-binding domain: application for the study of two
RT   mutations.";
RL   Mol. Cell. Endocrinol. 116:137-147(1996).
RN   [152]
RP   VARIANT AIS PHE-579, AND VARIANT PAIS TYR-582.
RX   PubMed=8809734; DOI=10.1016/0303-7207(96)03812-9;
RA   Imasaki K., Okabe T., Murakami H., Tanaka Y., Haji M., Takayanagi R.,
RA   Nawata H.;
RT   "Androgen insensitivity syndrome due to new mutations in the DNA-
RT   binding domain of the androgen receptor.";
RL   Mol. Cell. Endocrinol. 120:15-24(1996).
RN   [153]
RP   VARIANT PROSTATE CANCER GLU-798.
RX   PubMed=8628719;
RX   DOI=10.1002/(SICI)1097-0045(199603)28:3<162::AID-PROS3>3.0.CO;2-H;
RA   Evans B.A.J., Harper M.E., Daniells C.E., Watts C.E., Matenhelia S.,
RA   Green J., Griffiths K.;
RT   "Low incidence of androgen receptor gene mutations in human prostatic
RT   tumors using single strand conformation polymorphism analysis.";
RL   Prostate 28:162-171(1996).
RN   [154]
RP   VARIANT PROSTATE CANCER ALA-877.
RX   PubMed=8827083;
RX   DOI=10.1002/1097-0045(199609)29:3<153::AID-PROS2990290303>3.0.CO;2-5;
RA   Suzuki H., Akakura K., Komiya A., Aida S., Akimoto S., Shimazaki J.;
RT   "Codon 877 mutation in the androgen receptor gene in advanced prostate
RT   cancer: relation to antiandrogen withdrawal syndrome.";
RL   Prostate 29:153-158(1996).
RN   [155]
RP   VARIANT AIS HIS-855.
RX   PubMed=9106550;
RA   Boehmer A.L.M., Brinkmann A.O., Niermeijer M.F., Bakker L.,
RA   Halley D.J.J., Drop S.L.S.;
RT   "Germ-line and somatic mosaicism in the androgen insensitivity
RT   syndrome: implications for genetic counseling.";
RL   Am. J. Hum. Genet. 60:1003-1006(1997).
RN   [156]
RP   VARIANT PROSTATE CANCER ALA-683.
RX   PubMed=9000575;
RA   Koivisto P., Kononen J., Palmberg C., Tammela T., Hyytinen E.,
RA   Isola J., Trapman J., Cleutjens K., Noordzij A., Visakorpi T.,
RA   Kallioniemi O.-P.;
RT   "Androgen receptor gene amplification: a possible molecular mechanism
RT   for androgen deprivation therapy failure in prostate cancer.";
RL   Cancer Res. 57:314-319(1997).
RN   [157]
RP   VARIANTS PAIS LYS-608 AND GLY-772.
RX   PubMed=9196614; DOI=10.1046/j.1365-2265.1997.1140927.x;
RA   Tincello D.G., Saunders P.T., Hodgins M.B., Simpson N.B.,
RA   Edwards C.R., Hargreaves T.B., Wu F.C.;
RT   "Correlation of clinical, endocrine and molecular abnormalities with
RT   in vivo responses to high-dose testosterone in patients with partial
RT   androgen insensitivity syndrome.";
RL   Clin. Endocrinol. (Oxf.) 46:497-506(1997).
RN   [158]
RP   VARIANT AIS MET-889.
RX   PubMed=9160185;
RA   Essawi M., Gad Y.Z., el-Rouby O., Temtamy S.A., Sabour Y.A.,
RA   el-Awady M.K.;
RT   "Molecular analysis of androgen resistance syndromes in Egyptian
RT   patients.";
RL   Dis. Markers 13:99-105(1997).
RN   [159]
RP   VARIANT AIS TRP-779.
RX   PubMed=9007482; DOI=10.1007/s004310050542;
RA   Sinnecker G.H., Hiort O., Nitsche E.M., Holterhus P.M., Kruse K.;
RT   "Functional assessment and clinical classification of androgen
RT   sensitivity in patients with mutations of the androgen receptor
RT   gene.";
RL   Eur. J. Pediatr. 156:7-14(1997).
RN   [160]
RP   VARIANTS AIS VAL-749; CYS-774; ILE-780 AND SER-794.
RX   PubMed=8990010;
RX   DOI=10.1002/(SICI)1098-1004(1997)9:1<57::AID-HUMU10>3.3.CO;2-0;
RA   Jakubiczka S., Nedel S., Werder E.A., Schleiermacher E., Theile U.,
RA   Wolff G., Wieacker P.;
RT   "Mutations of the androgen receptor gene in patients with complete
RT   androgen insensitivity.";
RL   Hum. Mutat. 9:57-61(1997).
RN   [161]
RP   VARIANTS PROSTATE CANCER IN POLY-GLN REGION; HIS-701 AND ARG-910.
RX   PubMed=9438000; DOI=10.1093/jjco/27.6.389;
RA   Watanabe M., Ushijima T., Shiraishi T., Yatani R., Shimazaki J.,
RA   Kotake T., Sugimura T., Nagao M.;
RT   "Genetic alterations of androgen receptor gene in Japanese human
RT   prostate cancer.";
RL   Jpn. J. Clin. Oncol. 27:389-393(1997).
RN   [162]
RP   VARIANT PROSTATE CANCER GLN-629.
RX   PubMed=9184448;
RA   Wang C., Uchida T.;
RT   "Androgen receptor gene mutations in prostate cancer.";
RL   Nihon Hinyokika Gakkai Zasshi 88:550-556(1997).
RN   [163]
RP   VARIANTS AIS ARG-194 AND CYS-855.
RX   PubMed=9255042; DOI=10.1111/j.1447-0756.1997.tb00845.x;
RA   Komori S., Sakata K., Tanaka H., Shima H., Koyama K.;
RT   "DNA analysis of the androgen receptor gene in two cases with complete
RT   androgen insensitivity syndrome.";
RL   J. Obstet. Gynaecol. Res. 23:277-281(1997).
RN   [164]
RP   VARIANTS PAIS ALA-708 AND GLY-870.
RX   PubMed=9329414;
RA   Albers N., Ulrichs C., Gluer S., Hiort O., Sinnecker G.H.,
RA   Mildenberger H., Brodehl J.;
RT   "Etiologic classification of severe hypospadias: implications for
RT   prognosis and management.";
RL   J. Pediatr. 131:386-392(1997).
RN   [165]
RP   VARIANTS AIS ASN-732 AND THR-765.
RX   PubMed=9252933;
RA   Ko T.M., Yang Y.S., Wu M.Y., Kao C.H., Hsu P.M., Chuang S.M.,
RA   Lee T.Y.;
RT   "Complete androgen insensitivity syndrome. Molecular characterization
RT   in two Chinese women.";
RL   J. Reprod. Med. 42:424-428(1997).
RN   [166]
RP   VARIANTS AIS ASP-750; PHE-762; THR-765; ASN-864 AND PHE-907.
RX   PubMed=9328206; DOI=10.1016/S0960-0760(97)00001-0;
RA   Bevan C.L., Hughes I.A., Patterson M.N.;
RT   "Wide variation in androgen receptor dysfunction in complete androgen
RT   insensitivity syndrome.";
RL   J. Steroid Biochem. Mol. Biol. 61:19-26(1997).
RN   [167]
RP   VARIANT PAIS GLY-703, AND VARIANT AIS LEU-916.
RX   PubMed=9302173; DOI=10.1097/00005392-199710000-00075;
RA   Radmayr C., Culig Z., Glatzl J., Neuschmid-Kaspar F., Bartsch G.,
RA   Klocker H.;
RT   "Androgen receptor point mutations as the underlying molecular defect
RT   in 2 patients with androgen insensitivity syndrome.";
RL   J. Urol. 158:1553-1556(1997).
RN   [168]
RP   VARIANTS AIS CYS-571; GLN-752 AND CYS-774.
RX   PubMed=9544375; DOI=10.1007/s004040050206;
RA   Komori S., Kasumi H., Sakata K., Tanaka H., Hamada K., Koyama K.;
RT   "Molecular analysis of the androgen receptor gene in 4 patients with
RT   complete androgen insensitivity.";
RL   Arch. Gynecol. Obstet. 261:95-100(1998).
RN   [169]
RP   VARIANTS AIS HIS-615 AND GLN-752.
RX   PubMed=9698822; DOI=10.1590/S0100-879X1998000600008;
RA   Cabral D.F., Maciel-Guerra A.T., Hackel C.;
RT   "Mutations of androgen receptor gene in Brazilian patients with male
RT   pseudohermaphroditism.";
RL   Braz. J. Med. Biol. Res. 31:775-778(1998).
RN   [170]
RP   VARIANT AIS ARG-214.
RX   PubMed=9788719;
RA   Wang Q., Ghadessy F.J., Yong E.L.;
RT   "Analysis of the transactivation domain of the androgen receptor in
RT   patients with male infertility.";
RL   Clin. Genet. 54:185-192(1998).
RN   [171]
RP   VARIANTS AIS PRO-255 AND ALA-820.
RX   PubMed=9610419;
RA   Tanaka H., Komori S., Sakata K., Shima H., Koyama K.;
RT   "One additional mutation at exon A amplifies thermolability of
RT   androgen receptor in a case with complete androgen insensitivity
RT   syndrome.";
RL   Gynecol. Endocrinol. 12:75-82(1998).
RN   [172]
RP   VARIANTS AIS THR-765; TYR-784 AND THR-895, AND VARIANT PAIS GLY-840.
RX   PubMed=9856504; DOI=10.1007/s004390050864;
RA   Lundberg Giwercman Y., Nikoshkov A., Lindsten K., Bystroem B.,
RA   Pousette A., Chibalin A.V., Arvidsson S., Tiulpakov A.,
RA   Semitcheva T.V., Peterkova V., Hagenfeldt K., Ritzen E.M., Wedell A.;
RT   "Functional characterisation of mutations in the ligand-binding domain
RT   of the androgen receptor gene in patients with androgen insensitivity
RT   syndrome.";
RL   Hum. Genet. 103:529-531(1998).
RN   [173]
RP   VARIANT AIS VAL-695.
RX   PubMed=9554754;
RA   Doerk T., Schnieders F., Jakubiczka S., Wieacker P.,
RA   Schroeder-Kurth T., Schmidtke J.;
RT   "A new missense substitution at a mutational hot spot of the androgen
RT   receptor in siblings with complete androgen insensitivity syndrome.";
RL   Hum. Mutat. 11:337-339(1998).
RN   [174]
RP   VARIANT ASP-645.
RX   PubMed=9554755;
RA   Nordenskjoeld A., Soederhaell S.;
RT   "An androgen receptor gene mutation (A645D) in a boy with a normal
RT   phenotype.";
RL   Hum. Mutat. 11:339-339(1998).
RN   [175]
RP   VARIANT AIS LEU-892.
RA   Knoke I., Jakubiczka S., Rohrer T., Hanimann B., Werder E.A.,
RA   Wieacker P.;
RT   "Single amino acid substitution in the hormone-binding domain of the
RT   androgen receptor in a family with complete androgen insensitivity
RT   syndrome (CAIS).";
RL   Hum. Mutat. 12:220-220(1998).
RN   [176]
RP   VARIANT PAIS GLN-607.
RX   PubMed=9543136; DOI=10.1210/jc.83.4.1173;
RA   Weidemann W., Peters B., Romalo G., Spindler K.D., Schweikert H.-U.;
RT   "Response to androgen treatment in a patient with partial androgen
RT   insensitivity and a mutation in the deoxyribonucleic acid-binding
RT   domain of the androgen receptor.";
RL   J. Clin. Endocrinol. Metab. 83:1173-1176(1998).
RN   [177]
RP   VARIANTS PAIS VAL-743 AND CYS-840.
RX   PubMed=9768671; DOI=10.1210/jc.83.10.3597;
RA   Georget V., Terouanne B., Lumbroso S., Nicolas J.C., Sultan C.;
RT   "Trafficking of androgen receptor mutants fused to green fluorescent
RT   protein: a new investigation of partial androgen insensitivity
RT   syndrome.";
RL   J. Clin. Endocrinol. Metab. 83:3597-3603(1998).
RN   [178]
RP   VARIANT AIS GLU-798.
RX   PubMed=9851768; DOI=10.1210/jc.83.12.4303;
RA   Wang Q., Ghadessy F.J., Trounson A., de Kretser D., McLachlan R.,
RA   Ng S.C., Yong E.L.;
RT   "Azoospermia associated with a mutation in the ligand-binding domain
RT   of an androgen receptor displaying normal ligand binding, but
RT   defective trans-activation.";
RL   J. Clin. Endocrinol. Metab. 83:4303-4309(1998).
RN   [179]
RP   VARIANTS AIS.
RX   PubMed=9627582; DOI=10.1016/S0022-3476(98)70387-7;
RA   Hiort O., Sinnecker G.H., Holterhus P.M., Nitsche E.M., Kruse K.;
RT   "Inherited and de novo androgen receptor gene mutations: investigation
RT   of single-case families.";
RL   J. Pediatr. 132:939-943(1998).
RN   [180]
RP   VARIANT PAIS THR-758.
RX   PubMed=9607727; DOI=10.1016/S0303-7207(97)00229-3;
RA   Yong E.L., Tut T.G., Ghadessy F.J., Prins G., Ratnam S.S.;
RT   "Partial androgen insensitivity and correlations with the predicted
RT   three dimensional structure of the androgen receptor ligand-binding
RT   domain.";
RL   Mol. Cell. Endocrinol. 137:41-50(1998).
RN   [181]
RP   VARIANT PAIS LEU-911.
RX   PubMed=10470409; DOI=10.1046/j.1439-0272.1999.00278.x;
RA   Knoke I., Jakubiczka S., Lehnert H., Wieacker P.;
RT   "A new point mutation of the androgen receptor gene in a patient with
RT   partial androgen resistance and severe oligozoospermia.";
RL   Andrologia 31:199-201(1999).
RN   [182]
RP   VARIANTS PROSTATE CANCER ALA-877 AND ASN-890.
RX   PubMed=10363963;
RA   Taplin M.-E., Bubley G.J., Ko Y.J., Small E.J., Upton M.,
RA   Rajeshkumar B., Balk S.P.;
RT   "Selection for androgen receptor mutations in prostate cancers treated
RT   with androgen antagonist.";
RL   Cancer Res. 59:2511-2515(1999).
RN   [183]
RP   VARIANT PAIS SER-840.
RX   PubMed=10502786;
RX   DOI=10.1002/(SICI)1098-1004(199910)14:4<353::AID-HUMU16>3.0.CO;2-7;
RA   Melo K.F.S., Latronico A.C., Costa E.M.F., Billerbeck A.E.C.,
RA   Mendonca B.B., Arnhold I.J.P.;
RT   "A novel point mutation (R840S) in the androgen receptor in a
RT   Brazilian family with partial androgen insensitivity syndrome.";
RL   Hum. Mutat. 14:353-353(1999).
RN   [184]
RP   VARIANTS AIS ARG-390 AND ARG-443.
RX   PubMed=10571951;
RX   DOI=10.1002/(SICI)1098-1004(199912)14:6<527::AID-HUMU12>3.0.CO;2-X;
RA   Gottlieb B., Vasiliou D.M., Lumbroso R., Beitel L.K., Pinsky L.,
RA   Trifiro M.A.;
RT   "Analysis of exon 1 mutations in the androgen receptor gene.";
RL   Hum. Mutat. 14:527-539(1999).
RN   [185]
RP   VARIANT PAIS GLN-607, AND VARIANT AIS LYS-681.
RX   PubMed=10221692; DOI=10.1093/humrep/14.3.664;
RA   Chen C.P., Chern S.R., Wang T.Y., Wang W., Wang K.L., Jeng C.J.;
RT   "Androgen receptor gene mutations in 46,XY females with germ cell
RT   tumours.";
RL   Hum. Reprod. 14:664-670(1999).
RN   [186]
RP   VARIANT AIS LEU-892.
RX   PubMed=10404311; DOI=10.1046/j.1442-2042.1999.00065.x;
RA   Kanayama H., Naroda T., Inoue Y., Kurokawa Y., Kagawa S.;
RT   "A case of complete testicular feminization: laparoscopic orchiectomy
RT   and analysis of androgen receptor gene mutation.";
RL   Int. J. Urol. 6:327-330(1999).
RN   [187]
RP   VARIANT PAIS ALA-772, AND VARIANT AIS GLY-871.
RX   PubMed=10022458; DOI=10.1210/jc.84.2.805;
RA   Shkolny D.L., Beitel L.K., Ginsberg J., Pekeles G., Arbour L.,
RA   Pinsky L., Trifiro M.A.;
RT   "Discordant measures of androgen-binding kinetics in two mutant
RT   androgen receptors causing mild or partial androgen insensitivity,
RT   respectively.";
RL   J. Clin. Endocrinol. Metab. 84:805-810(1999).
RN   [188]
RP   VARIANTS PROSTATE CANCER IN POLY-GLN REGION AND ALA-683.
RX   PubMed=10629558;
RX   DOI=10.1002/(SICI)1096-9896(199912)189:4<559::AID-PATH471>3.0.CO;2-Y;
RA   Wallen M.J., Linja M., Kaartinen K., Schleutker J., Visakorpi T.;
RT   "Androgen receptor gene mutations in hormone-refractory prostate
RT   cancer.";
RL   J. Pathol. 189:559-563(1999).
RN   [189]
RP   VARIANTS PROSTATE CANCER HIS-701 AND ALA-877.
RX   PubMed=10569618; DOI=10.1016/S0022-5347(05)68158-X;
RA   Zhao X.Y., Boyle B., Krishnan A.V., Navone N.M., Peehl D.M.,
RA   Feldman D.;
RT   "Two mutations identified in the androgen receptor of the new human
RT   prostate cancer cell line MDA PCa 2a.";
RL   J. Urol. 162:2192-2199(1999).
RN   [190]
RP   VARIANT PAIS THR-807.
RX   PubMed=10543676; DOI=10.1016/S0140-6736(99)03205-5;
RA   Ong Y.C., Wong H.B., Adaikan G., Yong E.L.;
RT   "Directed pharmacological therapy of ambiguous genitalia due to an
RT   androgen receptor gene mutation.";
RL   Lancet 354:1444-1445(1999).
RN   [191]
RP   VARIANT AIS LEU-892.
RX   PubMed=10221770; DOI=10.1016/S0303-7207(98)00237-8;
RA   Peters I., Weidemann W., Romalo G., Knorr D., Schweikert H.-U.,
RA   Spindler K.D.;
RT   "An androgen receptor mutation in the direct vicinity of the proposed
RT   C-terminal alpha-helix of the ligand binding domain containing the AF-
RT   2 transcriptional activating function core is associated with complete
RT   androgen insensitivity.";
RL   Mol. Cell. Endocrinol. 148:47-53(1999).
RN   [192]
RP   VARIANT PROSTATE CANCER TYR-619.
RX   PubMed=10598582; DOI=10.1210/me.13.12.2065;
RA   Nazareth L.V., Stenoien D.L., Bingman W.E. III, James A.J., Wu C.,
RA   Zhang Y., Edwards D.P., Mancini M., Marcelli M., Lamb D.J.,
RA   Weigel N.L.;
RT   "A C619Y mutation in the human androgen receptor causes inactivation
RT   and mislocalization of the receptor with concomitant sequestration of
RT   SRC-1.";
RL   Mol. Endocrinol. 13:2065-2075(1999).
RN   [193]
RP   ERRATUM.
RA   Nazareth L.V., Stenoien D.L., Bingman W.E. III, James A.J., Wu C.,
RA   Zhang Y., Edwards D.P., Mancini M., Marcelli M., Lamb D.J.,
RA   Weigel N.L.;
RL   Mol. Endocrinol. 14:544-544(2000).
RN   [194]
RP   VARIANT AIS THR-596.
RX   PubMed=10590024; DOI=10.1203/00006450-199912000-00008;
RA   Holterhus P.M., Wiebel J., Sinnecker G.H., Bruggenwirth H.T.,
RA   Sippell W.G., Brinkmann A.O., Kruse K., Hiort O.;
RT   "Clinical and molecular spectrum of somatic mosaicism in androgen
RT   insensitivity syndrome.";
RL   Pediatr. Res. 46:684-690(1999).
RN   [195]
RP   VARIANTS AIS PHE-812 AND GLN-831.
RX   PubMed=10458483; DOI=10.1620/tjem.187.263;
RA   Yaegashi N., Uehara S., Senoo M., Sato J., Fujiwara J., Funato T.,
RA   Sasaki T., Yajima A.;
RT   "Point mutations in the steroid-binding domain of the androgen
RT   receptor gene of five Japanese patients with androgen insensitivity
RT   syndrome.";
RL   Tohoku J. Exp. Med. 187:263-272(1999).
RN   [196]
RP   VARIANTS THR-597 AND LEU-725.
RX   PubMed=10092153; DOI=10.1007/s002400050088;
RA   Nordenskjoeld A., Friedman E., Tapper-Persson M., Soederhaell C.,
RA   Leviav A., Svensson J., Anvret M.;
RT   "Screening for mutations in candidate genes for hypospadias.";
RL   Urol. Res. 27:49-55(1999).
RN   [197]
RP   VARIANTS PROSTATE CANCER ALA-575; ARG-580; VAL-586; TYR-619; ALA-757
RP   AND GLY-846.
RX   PubMed=10706109;
RA   Marcelli M., Ittmann M., Mariani S., Sutherland R.W., Nigam R.,
RA   Murthy L., Zhao Y., DiConcini D., Puxeddu E., Esen A., Eastham J.,
RA   Weigel N.L., Lamb D.J.;
RT   "Androgen receptor mutations in prostate cancer.";
RL   Cancer Res. 60:944-949(2000).
RN   [198]
RP   VARIANTS AIS AND PAIS.
RX   PubMed=10690872; DOI=10.1210/jc.85.2.658;
RA   Ahmed S.F., Cheng A., Dovey L., Hawkins J.R., Martin H., Rowland J.,
RA   Shimura N., Tait A.D., Hughes I.A.;
RT   "Phenotypic features, androgen receptor binding, and mutational
RT   analysis in 278 clinical cases reported as androgen insensitivity
RT   syndrome.";
RL   J. Clin. Endocrinol. Metab. 85:658-665(2000).
RN   [199]
RP   VARIANTS PAIS THR-682 AND GLU-711, AND VARIANTS AIS GLU-743; VAL-827;
RP   ARG-874 AND TYR-879.
RX   PubMed=11587068; DOI=10.1007/s100380170021;
RA   Chavez B., Mendez J.P., Ulloa-Aguirre A., Larrea F., Vilchis F.;
RT   "Eight novel mutations of the androgen receptor gene in patients with
RT   androgen insensitivity syndrome.";
RL   J. Hum. Genet. 46:560-565(2001).
RN   [200]
RP   INVOLVEMENT IN AGA.
RX   PubMed=11231320; DOI=10.1046/j.1523-1747.2001.01261.x;
RA   Ellis J.A., Stebbing M., Harrap S.B.;
RT   "Polymorphism of the androgen receptor gene is associated with male
RT   pattern baldness.";
RL   J. Invest. Dermatol. 116:452-455(2001).
RN   [201]
RP   VARIANT AIS TYR-705.
RX   PubMed=11744994;
RA   Sills E.S., Sholes T.E., Perloe M., Kaplan C.R., Davis J.G.,
RA   Tucker M.J.;
RT   "Characterization of a novel receptor mutation A->T at exon 4 in
RT   complete androgen insensitivity syndrome and a carrier sibling via
RT   bidirectional polymorphism sequence analysis.";
RL   Int. J. Mol. Med. 9:45-48(2002).
RN   [202]
RP   INVOLVEMENT IN AGA.
RX   PubMed=15902657; DOI=10.1086/431425;
RA   Hillmer A.M., Hanneken S., Ritzmann S., Becker T., Freudenberg J.,
RA   Brockschmidt F.F., Flaquer A., Freudenberg-Hua Y., Jamra R.A.,
RA   Metzen C., Heyn U., Schweiger N., Betz R.C., Blaumeiser B., Hampe J.,
RA   Schreiber S., Schulze T.G., Hennies H.C., Schumacher J., Propping P.,
RA   Ruzicka T., Cichon S., Wienker T.F., Kruse R., Noethen M.M.;
RT   "Genetic variation in the human androgen receptor gene is the major
RT   determinant of common early-onset androgenetic alopecia.";
RL   Am. J. Hum. Genet. 77:140-148(2005).
RN   [203]
RP   INVOLVEMENT IN SMAX1.
RX   PubMed=15851746; DOI=10.1212/01.WNL.0000158617.41819.F3;
RA   Echaniz-Laguna A., Rousso E., Anheim M., Cossee M., Tranchant C.;
RT   "A family with early-onset and rapidly progressive X-linked spinal and
RT   bulbar muscular atrophy.";
RL   Neurology 64:1458-1460(2005).
RN   [204]
RP   CHARACTERIZATION OF VARIANTS AIS ASN-695; CYS-763; HIS-774; GLU-798;
RP   HIS-855 AND PHE-907.
RX   PubMed=16595706; DOI=10.1677/jme.1.01885;
RA   Jaeaeskelaeinen J., Deeb A., Schwabe J.W., Mongan N.P., Martin H.,
RA   Hughes I.A.;
RT   "Human androgen receptor gene ligand-binding-domain mutations leading
RT   to disrupted interaction between the N- and C-terminal domains.";
RL   J. Mol. Endocrinol. 36:361-368(2006).
CC   -!- FUNCTION: Steroid hormone receptors are ligand-activated
CC       transcription factors that regulate eukaryotic gene expression and
CC       affect cellular proliferation and differentiation in target
CC       tissues. Transcription factor activity is modulated by bound
CC       coactivator and corepressor proteins. Transcription activation is
CC       down-regulated by NR0B2. Activated, but not phosphorylated, by
CC       HIPK3 and ZIPK/DAPK3. {ECO:0000269|PubMed:14664718,
CC       ECO:0000269|PubMed:15563469, ECO:0000269|PubMed:17591767,
CC       ECO:0000269|PubMed:17911242, ECO:0000269|PubMed:18084323,
CC       ECO:0000269|PubMed:19345326, ECO:0000269|PubMed:20980437}.
CC   -!- ENZYME REGULATION: AIM-100 (4-amino-5,6-biaryl-furo[2,3-
CC       d]pyrimidine) suppresses TNK2-mediated phosphorylation at Tyr-267.
CC       Inhibits the binding of the Tyr-267 phosphorylated form to
CC       androgen-responsive enhancers (AREs) and its transcriptional
CC       activity. {ECO:0000269|PubMed:20623637}.
CC   -!- SUBUNIT: Binds DNA as a homodimer. Part of a ternary complex
CC       containing AR, EFCAB6/DJBP and PARK7. Interacts with HIPK3 and
CC       NR0B2 in the presence of androgen. The ligand binding domain
CC       interacts with KAT7/HBO1 in the presence of dihydrotestosterone.
CC       Interacts with EFCAB6/DJBP, PELP1, PQBP1, RANBP9, RBAK, SPDEF,
CC       SRA1, TGFB1I1, ZNF318 and RREB1. Interacts with ZMIZ1/ZIMP10 and
CC       ZMIZ2/ZMIP7 which both enhance its transactivation activity.
CC       Interacts with SLC30A9 and RAD54L2/ARIP4. Interacts via the
CC       ligand-binding domain with LXXLL and FXXLF motifs from NCOA1,
CC       NCOA2, NCOA3, NCOA4 and MAGEA11. The AR N-terminal poly-Gln region
CC       binds Ran resulting in enhancement of AR-mediated transactivation.
CC       Ran-binding decreases as the poly-Gln length increases. Interacts
CC       with HIP1 (via coiled coil domain). Interacts (via ligand-binding
CC       domain) with TRIM68. Interacts with TNK2. Interacts with USP26.
CC       Interacts with RNF6. Interacts (regulated by RNF6 probably through
CC       polyubiquitination) with RNF14; regulates AR transcriptional
CC       activity. Interacts with PRMT2 and TRIM24. Interacts with
CC       GNB2L1/RACK1. Interacts with RANBP10; this interaction enhances
CC       dihydrotestosterone-induced AR transcriptional activity. Interacts
CC       with PRPF6 in a hormone-independent way; this interaction enhances
CC       dihydrotestosterone-induced AR transcriptional activity. Interacts
CC       with STK4/MST1. Interacts with ZIPK/DAPK3. Interacts with LPXN.
CC       Interacts with MAK. Part of a complex containing AR, MAK and
CC       NCOA3. Interacts with CRY1. Interacts with CCAR1 and GATA2.
CC       {ECO:0000269|PubMed:10075738, ECO:0000269|PubMed:10332029,
CC       ECO:0000269|PubMed:10383460, ECO:0000269|PubMed:10400640,
CC       ECO:0000269|PubMed:10625666, ECO:0000269|PubMed:10930412,
CC       ECO:0000269|PubMed:12039962, ECO:0000269|PubMed:12361945,
CC       ECO:0000269|PubMed:12415108, ECO:0000269|PubMed:12612053,
CC       ECO:0000269|PubMed:12958311, ECO:0000269|PubMed:14609956,
CC       ECO:0000269|PubMed:14664718, ECO:0000269|PubMed:15525515,
CC       ECO:0000269|PubMed:15563469, ECO:0000269|PubMed:16027218,
CC       ECO:0000269|PubMed:16051670, ECO:0000269|PubMed:16951154,
CC       ECO:0000269|PubMed:17311914, ECO:0000269|PubMed:17494760,
CC       ECO:0000269|PubMed:17550981, ECO:0000269|PubMed:17587566,
CC       ECO:0000269|PubMed:17591767, ECO:0000269|PubMed:17711855,
CC       ECO:0000269|PubMed:17911242, ECO:0000269|PubMed:18007036,
CC       ECO:0000269|PubMed:18084323, ECO:0000269|PubMed:18222118,
CC       ECO:0000269|PubMed:18451096, ECO:0000269|PubMed:18451177,
CC       ECO:0000269|PubMed:19345326, ECO:0000269|PubMed:19909775,
CC       ECO:0000269|PubMed:20501646, ECO:0000269|PubMed:20980437,
CC       ECO:0000269|PubMed:21512132, ECO:0000269|PubMed:22170608,
CC       ECO:0000269|PubMed:23887938}.
CC   -!- INTERACTION:
CC       P00519:ABL1; NbExp=2; IntAct=EBI-608057, EBI-375543;
CC       P51451:BLK; NbExp=3; IntAct=EBI-608057, EBI-2105445;
CC       Q8WV28:BLNK; NbExp=2; IntAct=EBI-608057, EBI-2623522;
CC       P78543:BTG2; NbExp=4; IntAct=EBI-608057, EBI-1047576;
CC       O89110:Casp8 (xeno); NbExp=2; IntAct=EBI-608057, EBI-851690;
CC       Q92793:CREBBP; NbExp=2; IntAct=EBI-608057, EBI-81215;
CC       O14595:CTDSP2; NbExp=3; IntAct=EBI-608057, EBI-2802973;
CC       P35222:CTNNB1; NbExp=8; IntAct=EBI-608057, EBI-491549;
CC       Q9UER7:DAXX; NbExp=5; IntAct=EBI-608057, EBI-77321;
CC       P20711:DDC; NbExp=2; IntAct=EBI-608057, EBI-1632155;
CC       P11308:ERG; NbExp=3; IntAct=EBI-608057, EBI-79704;
CC       P07332:FES; NbExp=3; IntAct=EBI-608057, EBI-1055635;
CC       P09769:FGR; NbExp=3; IntAct=EBI-608057, EBI-1383732;
CC       O75593:FOXH1; NbExp=3; IntAct=EBI-608057, EBI-1759806;
CC       Q9R1E0:Foxo1 (xeno); NbExp=4; IntAct=EBI-608057, EBI-1371343;
CC       Q14451:GRB7; NbExp=3; IntAct=EBI-608057, EBI-970191;
CC       P56524:HDAC4; NbExp=4; IntAct=EBI-608057, EBI-308629;
CC       Q16665:HIF1A; NbExp=2; IntAct=EBI-608057, EBI-447269;
CC       Q16666:IFI16; NbExp=3; IntAct=EBI-608057, EBI-2867186;
CC       O15357:INPPL1; NbExp=3; IntAct=EBI-608057, EBI-1384248;
CC       Q15652:JMJD1C; NbExp=2; IntAct=EBI-608057, EBI-1224969;
CC       P17535:JUND; NbExp=2; IntAct=EBI-608057, EBI-2682803;
CC       O95251:KAT7; NbExp=5; IntAct=EBI-608057, EBI-473199;
CC       P07288:KLK3; NbExp=3; IntAct=EBI-608057, EBI-1220791;
CC       P06239:LCK; NbExp=7; IntAct=EBI-608057, EBI-1348;
CC       P07948:LYN; NbExp=5; IntAct=EBI-608057, EBI-79452;
CC       P20794:MAK; NbExp=5; IntAct=EBI-608057, EBI-3911321;
CC       P42679:MATK; NbExp=4; IntAct=EBI-608057, EBI-751664;
CC       Q00987:MDM2; NbExp=2; IntAct=EBI-608057, EBI-389668;
CC       Q15596:NCOA2; NbExp=2; IntAct=EBI-608057, EBI-81236;
CC       Q14686:NCOA6; NbExp=2; IntAct=EBI-608057, EBI-78670;
CC       Q99497:PARK7; NbExp=6; IntAct=EBI-608057, EBI-1164361;
CC       P27986:PIK3R1; NbExp=5; IntAct=EBI-608057, EBI-79464;
CC       O00459:PIK3R2; NbExp=14; IntAct=EBI-608057, EBI-346930;
CC       Q92569:PIK3R3; NbExp=37; IntAct=EBI-608057, EBI-79893;
CC       P19174:PLCG1; NbExp=22; IntAct=EBI-608057, EBI-79387;
CC       P16885:PLCG2; NbExp=6; IntAct=EBI-608057, EBI-617403;
CC       Q06830:PRDX1; NbExp=3; IntAct=EBI-608057, EBI-353193;
CC       Q06124:PTPN11; NbExp=12; IntAct=EBI-608057, EBI-297779;
CC       P20936:RASA1; NbExp=16; IntAct=EBI-608057, EBI-1026476;
CC       Q9UBS8:RNF14; NbExp=2; IntAct=EBI-608057, EBI-2130308;
CC       Q9Y252:RNF6; NbExp=10; IntAct=EBI-608057, EBI-2341483;
CC       O14796:SH2D1B; NbExp=3; IntAct=EBI-608057, EBI-3923013;
CC       Q9NP31:SH2D2A; NbExp=6; IntAct=EBI-608057, EBI-490630;
CC       P29353:SHC1; NbExp=14; IntAct=EBI-608057, EBI-78835;
CC       Q6S5L8:SHC4; NbExp=3; IntAct=EBI-608057, EBI-9453524;
CC       Q5VZ18:SHE; NbExp=3; IntAct=EBI-608057, EBI-3956977;
CC       Q06986:Siah2 (xeno); NbExp=6; IntAct=EBI-608057, EBI-957413;
CC       Q15797:SMAD1; NbExp=6; IntAct=EBI-608057, EBI-1567153;
CC       O14544:SOCS6; NbExp=4; IntAct=EBI-608057, EBI-3929549;
CC       P12931:SRC; NbExp=7; IntAct=EBI-608057, EBI-621482;
CC       Q9ULZ2:STAP1; NbExp=2; IntAct=EBI-608057, EBI-6083058;
CC       P63165:SUMO1; NbExp=7; IntAct=EBI-608057, EBI-80140;
CC       Q9HBL0:TNS1; NbExp=3; IntAct=EBI-608057, EBI-3389814;
CC       O96028:WHSC1; NbExp=5; IntAct=EBI-608057, EBI-2693298;
CC       P07947:YES1; NbExp=5; IntAct=EBI-608057, EBI-515331;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly
CC       cytoplasmic in unligated form but translocates to the nucleus upon
CC       ligand-binding. Can also translocate to the nucleus in unligated
CC       form in the presence of GNB2L1.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=AR-B;
CC         IsoId=P10275-1; Sequence=Displayed;
CC       Name=2; Synonyms=AR-A, Variant AR45;
CC         IsoId=P10275-2; Sequence=VSP_036889, VSP_036890;
CC   -!- TISSUE SPECIFICITY: Isoform 2 is mainly expressed in heart and
CC       skeletal muscle. {ECO:0000269|PubMed:15634333}.
CC   -!- DOMAIN: Composed of three domains: a modulating N-terminal domain,
CC       a DNA-binding domain and a C-terminal ligand-binding domain. In
CC       the presence of bound steroid the ligand-binding domain interacts
CC       with the N-terminal modulating domain, and thereby activates AR
CC       transcription factor activity. Agonist binding is required for
CC       dimerization and binding to target DNA. The transcription factor
CC       activity of the complex formed by ligand-activated AR and DNA is
CC       modulated by interactions with coactivator and corepressor
CC       proteins. Interaction with RANBP9 is mediated by both the N-
CC       terminal domain and the DNA-binding domain. Interaction with
CC       EFCAB6/DJBP is mediated by the DNA-binding domain.
CC   -!- PTM: Sumoylated on Lys-386 (major) and Lys-520. Ubiquitinated.
CC       Deubiquitinated by USP26. 'Lys-6' and 'Lys-27'-linked
CC       polyubiquitination by RNF6 modulates AR transcriptional activity
CC       and specificity. {ECO:0000269|PubMed:11121022,
CC       ECO:0000269|PubMed:19345326, ECO:0000269|PubMed:20501646}.
CC   -!- PTM: Phosphorylated in prostate cancer cells in response to
CC       several growth factors including EGF. Phosphorylation is induced
CC       by c-Src kinase (CSK). Tyr-534 is one of the major phosphorylation
CC       sites and an increase in phosphorylation and Src kinase activity
CC       is associated with prostate cancer progression. Phosphorylation by
CC       TNK2 enhances the DNA-binding and transcriptional activity and may
CC       be responsible for androgen-independent progression of prostate
CC       cancer. Phosphorylation at Ser-81 by CDK9 regulates AR promoter
CC       selectivity and cell growth. Phosphorylation by PAK6 leads to AR-
CC       mediated transcription inhibition. {ECO:0000269|PubMed:14573606,
CC       ECO:0000269|PubMed:17045208, ECO:0000269|PubMed:17494760,
CC       ECO:0000269|PubMed:20623637, ECO:0000269|PubMed:20980437,
CC       ECO:0000269|PubMed:21512132}.
CC   -!- PTM: Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is
CC       required for plasma membrane targeting and for rapid intracellular
CC       signaling via ERK and AKT kinases and cAMP generation.
CC       {ECO:0000269|PubMed:22031296}.
CC   -!- POLYMORPHISM: The poly-Gln region of AR is highly polymorphic and
CC       the number of Gln varies in the population (from 17 to 26). A
CC       smaller size of the poly-Gln region may be associated with the
CC       development of prostate cancer.
CC   -!- POLYMORPHISM: The poly-Gly region of AR is polymorphic and ranges
CC       from 24 to 31 Gly. A poly-Gly region shorter or equal to 23 may be
CC       associated with the development of androgenetic alopecia.
CC   -!- DISEASE: Androgen insensitivity syndrome (AIS) [MIM:300068]: An X-
CC       linked recessive form of pseudohermaphroditism due end-organ
CC       resistance to androgen. Affected males have female external
CC       genitalia, female breast development, blind vagina, absent uterus
CC       and female adnexa, and abdominal or inguinal testes, despite a
CC       normal 46,XY karyotype. {ECO:0000269|PubMed:10022458,
CC       ECO:0000269|PubMed:10221692, ECO:0000269|PubMed:10221770,
CC       ECO:0000269|PubMed:10404311, ECO:0000269|PubMed:10458483,
CC       ECO:0000269|PubMed:10571951, ECO:0000269|PubMed:10590024,
CC       ECO:0000269|PubMed:10690872, ECO:0000269|PubMed:11587068,
CC       ECO:0000269|PubMed:11744994, ECO:0000269|PubMed:1307250,
CC       ECO:0000269|PubMed:1316540, ECO:0000269|PubMed:1426313,
CC       ECO:0000269|PubMed:1430233, ECO:0000269|PubMed:1464650,
CC       ECO:0000269|PubMed:1480178, ECO:0000269|PubMed:1487249,
CC       ECO:0000269|PubMed:1569163, ECO:0000269|PubMed:1609793,
CC       ECO:0000269|PubMed:1775137, ECO:0000269|PubMed:1999491,
CC       ECO:0000269|PubMed:2082179, ECO:0000269|PubMed:2594783,
CC       ECO:0000269|PubMed:7537149, ECO:0000269|PubMed:7581399,
CC       ECO:0000269|PubMed:7633398, ECO:0000269|PubMed:7641413,
CC       ECO:0000269|PubMed:7671849, ECO:0000269|PubMed:7929841,
CC       ECO:0000269|PubMed:7962294, ECO:0000269|PubMed:7970939,
CC       ECO:0000269|PubMed:7981687, ECO:0000269|PubMed:7981689,
CC       ECO:0000269|PubMed:7993455, ECO:0000269|PubMed:8040309,
CC       ECO:0000269|PubMed:8096390, ECO:0000269|PubMed:8103398,
CC       ECO:0000269|PubMed:8162033, ECO:0000269|PubMed:8224266,
CC       ECO:0000269|PubMed:8281140, ECO:0000269|PubMed:8325950,
CC       ECO:0000269|PubMed:8413310, ECO:0000269|PubMed:8446106,
CC       ECO:0000269|PubMed:8626869, ECO:0000269|PubMed:8647313,
CC       ECO:0000269|PubMed:8683794, ECO:0000269|PubMed:8723113,
CC       ECO:0000269|PubMed:8768864, ECO:0000269|PubMed:8809734,
CC       ECO:0000269|PubMed:8830623, ECO:0000269|PubMed:8918984,
CC       ECO:0000269|PubMed:8990010, ECO:0000269|PubMed:9001799,
CC       ECO:0000269|PubMed:9007482, ECO:0000269|PubMed:9039340,
CC       ECO:0000269|PubMed:9106550, ECO:0000269|PubMed:9160185,
CC       ECO:0000269|PubMed:9252933, ECO:0000269|PubMed:9255042,
CC       ECO:0000269|PubMed:9302173, ECO:0000269|PubMed:9328206,
CC       ECO:0000269|PubMed:9544375, ECO:0000269|PubMed:9554754,
CC       ECO:0000269|PubMed:9610419, ECO:0000269|PubMed:9627582,
CC       ECO:0000269|PubMed:9698822, ECO:0000269|PubMed:9788719,
CC       ECO:0000269|PubMed:9851768, ECO:0000269|PubMed:9856504,
CC       ECO:0000269|Ref.109, ECO:0000269|Ref.175}. Note=The disease is
CC       caused by mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Spinal and bulbar muscular atrophy X-linked 1 (SMAX1)
CC       [MIM:313200]: An X-linked recessive form of spinal muscular
CC       atrophy. Spinal muscular atrophy refers to a group of
CC       neuromuscular disorders characterized by degeneration of the
CC       anterior horn cells of the spinal cord, leading to symmetrical
CC       muscle weakness and atrophy. SMAX1 occurs only in men. Age at
CC       onset is usually in the third to fifth decade of life, but earlier
CC       involvement has been reported. It is characterized by slowly
CC       progressive limb and bulbar muscle weakness with fasciculations,
CC       muscle atrophy, and gynecomastia. The disorder is clinically
CC       similar to classic forms of autosomal spinal muscular atrophy.
CC       {ECO:0000269|PubMed:15851746}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry. Caused by
CC       trinucleotide CAG repeat expansion. In SMAX1 patients the number
CC       of Gln ranges from 38 to 62. Longer expansions result in earlier
CC       onset and more severe clinical manifestations of the disease.
CC   -!- DISEASE: Note=Defects in AR may play a role in metastatic prostate
CC       cancer. The mutated receptor stimulates prostate growth and
CC       metastases development despite of androgen ablation. This
CC       treatment can reduce primary and metastatic lesions probably by
CC       inducing apoptosis of tumor cells when they express the wild-type
CC       receptor.
CC   -!- DISEASE: Androgen insensitivity, partial (PAIS) [MIM:312300]: A
CC       disorder that is characterized by hypospadias, hypogonadism,
CC       gynecomastia, genital ambiguity, normal XY karyotype, and a
CC       pedigree pattern consistent with X-linked recessive inheritance.
CC       Some patients present azoospermia or severe oligospermia without
CC       other clinical manifestations. {ECO:0000269|PubMed:10022458,
CC       ECO:0000269|PubMed:10221692, ECO:0000269|PubMed:10470409,
CC       ECO:0000269|PubMed:10502786, ECO:0000269|PubMed:10543676,
CC       ECO:0000269|PubMed:11587068, ECO:0000269|PubMed:1303262,
CC       ECO:0000269|PubMed:1307250, ECO:0000269|PubMed:1316540,
CC       ECO:0000269|PubMed:1424203, ECO:0000269|PubMed:1430233,
CC       ECO:0000269|PubMed:2010552, ECO:0000269|PubMed:7581399,
CC       ECO:0000269|PubMed:7649358, ECO:0000269|PubMed:7671849,
CC       ECO:0000269|PubMed:7909256, ECO:0000269|PubMed:7910529,
CC       ECO:0000269|PubMed:7929841, ECO:0000269|PubMed:7970939,
CC       ECO:0000269|PubMed:7981687, ECO:0000269|PubMed:8033918,
CC       ECO:0000269|PubMed:8097257, ECO:0000269|PubMed:8126121,
CC       ECO:0000269|PubMed:8205256, ECO:0000269|PubMed:8281139,
CC       ECO:0000269|PubMed:8325932, ECO:0000269|PubMed:8325950,
CC       ECO:0000269|PubMed:8446106, ECO:0000269|PubMed:8550758,
CC       ECO:0000269|PubMed:8809734, ECO:0000269|PubMed:8823308,
CC       ECO:0000269|PubMed:8824883, ECO:0000269|PubMed:9039340,
CC       ECO:0000269|PubMed:9196614, ECO:0000269|PubMed:9302173,
CC       ECO:0000269|PubMed:9329414, ECO:0000269|PubMed:9543136,
CC       ECO:0000269|PubMed:9607727, ECO:0000269|PubMed:9768671,
CC       ECO:0000269|PubMed:9856504, ECO:0000269|Ref.117}. Note=The disease
CC       is caused by mutations affecting the gene represented in this
CC       entry.
CC   -!- MISCELLANEOUS: In the absence of ligand, steroid hormone receptors
CC       are thought to be weakly associated with nuclear components;
CC       hormone binding greatly increases receptor affinity. The hormone-
CC       receptor complex appears to recognize discrete DNA sequences
CC       upstream of transcriptional start sites.
CC   -!- MISCELLANEOUS: Transcriptional activity is enhanced by binding to
CC       RANBP9.
CC   -!- MISCELLANEOUS: The level of tyrosine phosphorylation may serve as
CC       a diagnostic tool to predict patient outcome in response to
CC       hormone-ablation therapy. Inhibition of tyrosine phosphorylation
CC       may be an effective intervention target for hormone-refractory
CC       prostate cancer.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC       subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 nuclear receptor DNA-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC   -!- WEB RESOURCE: Name=Androgen receptor gene mutations database;
CC       URL="http://androgendb.mcgill.ca";
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/ARID685chXq12.html";
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Androgen receptor entry;
CC       URL="https://en.wikipedia.org/wiki/Androgen_receptor";
CC   -!- WEB RESOURCE: Name=X-chromosome gene database, androgen receptor
CC       (AR); Note=Leiden Open Variation Database (LOVD);
CC       URL="http://www.lovd.nl/AR";
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DR   EMBL; M20132; AAA51729.1; -; mRNA.
DR   EMBL; M23263; AAA51775.1; -; mRNA.
DR   EMBL; M27430; AAA51886.1; -; Genomic_DNA.
DR   EMBL; M27423; AAA51886.1; JOINED; Genomic_DNA.
DR   EMBL; M27424; AAA51886.1; JOINED; Genomic_DNA.
DR   EMBL; M27425; AAA51886.1; JOINED; Genomic_DNA.
DR   EMBL; M27426; AAA51886.1; JOINED; Genomic_DNA.
DR   EMBL; M27427; AAA51886.1; JOINED; Genomic_DNA.
DR   EMBL; M27428; AAA51886.1; JOINED; Genomic_DNA.
DR   EMBL; M27429; AAA51886.1; JOINED; Genomic_DNA.
DR   EMBL; M34233; AAA51780.1; -; mRNA.
DR   EMBL; M21748; AAA51771.1; -; mRNA.
DR   EMBL; M35851; AAA51772.1; -; Genomic_DNA.
DR   EMBL; M35844; AAA51772.1; JOINED; Genomic_DNA.
DR   EMBL; M35845; AAA51772.1; JOINED; Genomic_DNA.
DR   EMBL; M35846; AAA51772.1; JOINED; Genomic_DNA.
DR   EMBL; M35847; AAA51772.1; JOINED; Genomic_DNA.
DR   EMBL; M35848; AAA51772.1; JOINED; Genomic_DNA.
DR   EMBL; M35849; AAA51772.1; JOINED; Genomic_DNA.
DR   EMBL; M35850; AAA51772.1; JOINED; Genomic_DNA.
DR   EMBL; AX453758; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR   EMBL; AL049564; CAI43080.1; -; Genomic_DNA.
DR   EMBL; AL158016; CAI43080.1; JOINED; Genomic_DNA.
DR   EMBL; AL356358; CAI43080.1; JOINED; Genomic_DNA.
DR   EMBL; AL158016; CAI40853.1; -; Genomic_DNA.
DR   EMBL; AL049564; CAI40853.1; JOINED; Genomic_DNA.
DR   EMBL; AL356358; CAI40853.1; JOINED; Genomic_DNA.
DR   EMBL; AL356358; CAI40496.1; -; Genomic_DNA.
DR   EMBL; AL049564; CAI40496.1; JOINED; Genomic_DNA.
DR   EMBL; AL158016; CAI40496.1; JOINED; Genomic_DNA.
DR   EMBL; CH471132; EAX05380.1; -; Genomic_DNA.
DR   EMBL; BC132975; AAI32976.1; -; mRNA.
DR   EMBL; L29496; AAA51770.1; -; mRNA.
DR   EMBL; U16371; AAB60346.1; -; Genomic_DNA.
DR   EMBL; M20260; AAA51774.1; -; mRNA.
DR   EMBL; S79366; AAB21256.2; -; Genomic_DNA.
DR   EMBL; S79366; AAB21257.2; -; Genomic_DNA.
DR   CCDS; CCDS43965.1; -. [P10275-2]
DR   PIR; A39248; A39248.
DR   RefSeq; NP_000035.2; NM_000044.3.
DR   RefSeq; NP_001011645.1; NM_001011645.2. [P10275-2]
DR   UniGene; Hs.76704; -.
DR   PDB; 1E3G; X-ray; 2.40 A; A=657-919.
DR   PDB; 1GS4; X-ray; 1.95 A; A=670-917.
DR   PDB; 1T5Z; X-ray; 2.30 A; A=669-919.
DR   PDB; 1T63; X-ray; 2.07 A; A=669-918.
DR   PDB; 1T65; X-ray; 1.66 A; A=669-919.
DR   PDB; 1XJ7; X-ray; 2.70 A; A=663-919.
DR   PDB; 1XOW; X-ray; 1.80 A; A=671-919, B=20-30.
DR   PDB; 1XQ3; X-ray; 2.25 A; A=671-919.
DR   PDB; 1Z95; X-ray; 1.80 A; A=672-917.
DR   PDB; 2AM9; X-ray; 1.64 A; A=654-919.
DR   PDB; 2AMA; X-ray; 1.90 A; A=654-919.
DR   PDB; 2AMB; X-ray; 1.75 A; A=654-919.
DR   PDB; 2AO6; X-ray; 1.89 A; A=671-919.
DR   PDB; 2AX6; X-ray; 1.50 A; A=664-919.
DR   PDB; 2AX7; X-ray; 1.90 A; A=664-919.
DR   PDB; 2AX8; X-ray; 1.70 A; A=664-919.
DR   PDB; 2AX9; X-ray; 1.65 A; A=664-919.
DR   PDB; 2AXA; X-ray; 1.80 A; A=664-919.
DR   PDB; 2HVC; X-ray; 2.10 A; A=669-918.
DR   PDB; 2OZ7; X-ray; 1.80 A; A=671-919.
DR   PDB; 2PIO; X-ray; 2.03 A; A=669-919.
DR   PDB; 2PIP; X-ray; 1.80 A; L=669-919.
DR   PDB; 2PIQ; X-ray; 2.40 A; A=669-919.
DR   PDB; 2PIR; X-ray; 2.10 A; A=669-919.
DR   PDB; 2PIT; X-ray; 1.76 A; A=669-919.
DR   PDB; 2PIU; X-ray; 2.12 A; A=669-919.
DR   PDB; 2PIV; X-ray; 1.95 A; A=669-919.
DR   PDB; 2PIW; X-ray; 2.58 A; A=669-919.
DR   PDB; 2PIX; X-ray; 2.40 A; A=669-919.
DR   PDB; 2PKL; X-ray; 2.49 A; A=669-919.
DR   PDB; 2PNU; X-ray; 1.65 A; A=654-919.
DR   PDB; 2Q7I; X-ray; 1.87 A; A=663-919, B=20-30.
DR   PDB; 2Q7J; X-ray; 1.90 A; A=663-919.
DR   PDB; 2Q7K; X-ray; 1.80 A; A=663-919, B=20-30.
DR   PDB; 2Q7L; X-ray; 1.92 A; A=663-919.
DR   PDB; 2YHD; X-ray; 2.20 A; A=671-919.
DR   PDB; 2YLO; X-ray; 2.50 A; A=664-919.
DR   PDB; 2YLP; X-ray; 2.30 A; A=664-919.
DR   PDB; 2YLQ; X-ray; 2.40 A; A=664-919.
DR   PDB; 2Z4J; X-ray; 2.60 A; A=671-918.
DR   PDB; 3B5R; X-ray; 1.80 A; A=671-919.
DR   PDB; 3B65; X-ray; 1.80 A; A=671-919.
DR   PDB; 3B66; X-ray; 1.65 A; A=671-919.
DR   PDB; 3B67; X-ray; 1.90 A; A=671-919.
DR   PDB; 3B68; X-ray; 1.90 A; A=671-919.
DR   PDB; 3BTR; X-ray; 2.60 A; B=621-635.
DR   PDB; 3L3X; X-ray; 1.55 A; A=670-918.
DR   PDB; 3L3Z; X-ray; 2.00 A; A=670-918.
DR   PDB; 3RLJ; X-ray; 1.90 A; A=671-917.
DR   PDB; 3RLL; X-ray; 1.70 A; A=671-917.
DR   PDB; 3V49; X-ray; 1.70 A; A=654-919, B=21-31.
DR   PDB; 3V4A; X-ray; 1.95 A; A=671-919, B=21-31.
DR   PDB; 3ZQT; X-ray; 2.29 A; A=664-919.
DR   PDB; 4HLW; X-ray; 2.50 A; A=664-919.
DR   PDB; 4K7A; X-ray; 2.44 A; A=670-918.
DR   PDB; 4OEA; X-ray; 2.12 A; A=670-919.
DR   PDB; 4OED; X-ray; 2.79 A; A=670-919.
DR   PDB; 4OEY; X-ray; 1.83 A; A=670-919.
DR   PDB; 4OEZ; X-ray; 1.80 A; A=670-919.
DR   PDB; 4OFR; X-ray; 2.26 A; A=670-919.
DR   PDB; 4OFU; X-ray; 2.12 A; A=670-919.
DR   PDB; 4OGH; X-ray; 2.98 A; A=670-919.
DR   PDB; 4OH5; X-ray; 2.00 A; A=670-919.
DR   PDB; 4OH6; X-ray; 3.56 A; A=670-919.
DR   PDB; 4OHA; X-ray; 1.42 A; A=670-919.
DR   PDB; 4OIL; X-ray; 2.51 A; A=670-919.
DR   PDB; 4OIU; X-ray; 3.01 A; A=670-919.
DR   PDB; 4OJ9; X-ray; 3.31 A; A=670-919.
DR   PDB; 4OJB; X-ray; 2.00 A; A=670-919.
DR   PDB; 4OK1; X-ray; 2.09 A; A=670-919.
DR   PDB; 4OKB; X-ray; 2.95 A; A=670-919.
DR   PDB; 4OKT; X-ray; 2.50 A; A=670-919.
DR   PDB; 4OKW; X-ray; 2.00 A; A=670-919.
DR   PDB; 4OKX; X-ray; 2.10 A; A=670-919.
DR   PDB; 4OLM; X-ray; 2.80 A; A=670-919.
DR   PDB; 4QL8; X-ray; 2.10 A; A=662-919.
DR   PDB; 4U4K; X-ray; 1.20 A; A=664-919.
DR   PDBsum; 1E3G; -.
DR   PDBsum; 1GS4; -.
DR   PDBsum; 1T5Z; -.
DR   PDBsum; 1T63; -.
DR   PDBsum; 1T65; -.
DR   PDBsum; 1XJ7; -.
DR   PDBsum; 1XOW; -.
DR   PDBsum; 1XQ3; -.
DR   PDBsum; 1Z95; -.
DR   PDBsum; 2AM9; -.
DR   PDBsum; 2AMA; -.
DR   PDBsum; 2AMB; -.
DR   PDBsum; 2AO6; -.
DR   PDBsum; 2AX6; -.
DR   PDBsum; 2AX7; -.
DR   PDBsum; 2AX8; -.
DR   PDBsum; 2AX9; -.
DR   PDBsum; 2AXA; -.
DR   PDBsum; 2HVC; -.
DR   PDBsum; 2OZ7; -.
DR   PDBsum; 2PIO; -.
DR   PDBsum; 2PIP; -.
DR   PDBsum; 2PIQ; -.
DR   PDBsum; 2PIR; -.
DR   PDBsum; 2PIT; -.
DR   PDBsum; 2PIU; -.
DR   PDBsum; 2PIV; -.
DR   PDBsum; 2PIW; -.
DR   PDBsum; 2PIX; -.
DR   PDBsum; 2PKL; -.
DR   PDBsum; 2PNU; -.
DR   PDBsum; 2Q7I; -.
DR   PDBsum; 2Q7J; -.
DR   PDBsum; 2Q7K; -.
DR   PDBsum; 2Q7L; -.
DR   PDBsum; 2YHD; -.
DR   PDBsum; 2YLO; -.
DR   PDBsum; 2YLP; -.
DR   PDBsum; 2YLQ; -.
DR   PDBsum; 2Z4J; -.
DR   PDBsum; 3B5R; -.
DR   PDBsum; 3B65; -.
DR   PDBsum; 3B66; -.
DR   PDBsum; 3B67; -.
DR   PDBsum; 3B68; -.
DR   PDBsum; 3BTR; -.
DR   PDBsum; 3L3X; -.
DR   PDBsum; 3L3Z; -.
DR   PDBsum; 3RLJ; -.
DR   PDBsum; 3RLL; -.
DR   PDBsum; 3V49; -.
DR   PDBsum; 3V4A; -.
DR   PDBsum; 3ZQT; -.
DR   PDBsum; 4HLW; -.
DR   PDBsum; 4K7A; -.
DR   PDBsum; 4OEA; -.
DR   PDBsum; 4OED; -.
DR   PDBsum; 4OEY; -.
DR   PDBsum; 4OEZ; -.
DR   PDBsum; 4OFR; -.
DR   PDBsum; 4OFU; -.
DR   PDBsum; 4OGH; -.
DR   PDBsum; 4OH5; -.
DR   PDBsum; 4OH6; -.
DR   PDBsum; 4OHA; -.
DR   PDBsum; 4OIL; -.
DR   PDBsum; 4OIU; -.
DR   PDBsum; 4OJ9; -.
DR   PDBsum; 4OJB; -.
DR   PDBsum; 4OK1; -.
DR   PDBsum; 4OKB; -.
DR   PDBsum; 4OKT; -.
DR   PDBsum; 4OKW; -.
DR   PDBsum; 4OKX; -.
DR   PDBsum; 4OLM; -.
DR   PDBsum; 4QL8; -.
DR   PDBsum; 4U4K; -.
DR   DisProt; DP00492; -.
DR   ProteinModelPortal; P10275; -.
DR   SMR; P10275; 555-918.
DR   BioGrid; 106862; 225.
DR   DIP; DIP-125N; -.
DR   IntAct; P10275; 107.
DR   MINT; MINT-94801; -.
DR   STRING; 9606.ENSP00000363822; -.
DR   BindingDB; P10275; -.
DR   ChEMBL; CHEMBL1871; -.
DR   DrugBank; DB01128; Bicalutamide.
DR   DrugBank; DB04839; Cyproterone acetate.
DR   DrugBank; DB01406; Danazol.
DR   DrugBank; DB01395; Drospirenone.
DR   DrugBank; DB00858; Drostanolone.
DR   DrugBank; DB08899; Enzalutamide.
DR   DrugBank; DB00687; Fludrocortisone.
DR   DrugBank; DB01185; Fluoxymesterone.
DR   DrugBank; DB00499; Flutamide.
DR   DrugBank; DB01026; Ketoconazole.
DR   DrugBank; DB00367; Levonorgestrel.
DR   DrugBank; DB06710; Methyltestosterone.
DR   DrugBank; DB08804; Nandrolone decanoate.
DR   DrugBank; DB00984; Nandrolone phenpropionate.
DR   DrugBank; DB00665; Nilutamide.
DR   DrugBank; DB00621; Oxandrolone.
DR   DrugBank; DB00421; Spironolactone.
DR   DrugBank; DB00624; Testosterone.
DR   DrugBank; DB01420; Testosterone Propionate.
DR   GuidetoPHARMACOLOGY; 628; -.
DR   PhosphoSite; P10275; -.
DR   BioMuta; AR; -.
DR   DMDM; 113830; -.
DR   MaxQB; P10275; -.
DR   PaxDb; P10275; -.
DR   PRIDE; P10275; -.
DR   Ensembl; ENST00000396043; ENSP00000379358; ENSG00000169083. [P10275-2]
DR   GeneID; 367; -.
DR   KEGG; hsa:367; -.
DR   CTD; 367; -.
DR   GeneCards; AR; -.
DR   GeneReviews; AR; -.
DR   H-InvDB; HIX0056152; -.
DR   HGNC; HGNC:644; AR.
DR   HPA; CAB000001; -.
DR   MIM; 300068; phenotype.
DR   MIM; 312300; phenotype.
DR   MIM; 313200; phenotype.
DR   MIM; 313700; gene.
DR   neXtProt; NX_P10275; -.
DR   Orphanet; 99429; Complete androgen insensitivity syndrome.
DR   Orphanet; 440; Familial hypospadias.
DR   Orphanet; 481; Kennedy disease.
DR   Orphanet; 90797; Partial androgen insensitivity syndrome.
DR   PharmGKB; PA57; -.
DR   eggNOG; KOG3575; Eukaryota.
DR   eggNOG; ENOG410XRZC; LUCA.
DR   GeneTree; ENSGT00760000118887; -.
DR   HOVERGEN; HBG007583; -.
DR   InParanoid; P10275; -.
DR   KO; K08557; -.
DR   OrthoDB; EOG7J17Z7; -.
DR   PhylomeDB; P10275; -.
DR   TreeFam; TF350286; -.
DR   Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
DR   Reactome; R-HSA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR   SignaLink; P10275; -.
DR   ChiTaRS; AR; human.
DR   EvolutionaryTrace; P10275; -.
DR   GeneWiki; Androgen_receptor; -.
DR   GenomeRNAi; 367; -.
DR   NextBio; 1531; -.
DR   PMAP-CutDB; B1AKD7; -.
DR   PRO; PR:P10275; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   Bgee; P10275; -.
DR   CleanEx; HS_AR; -.
DR   ExpressionAtlas; P10275; baseline and differential.
DR   Genevisible; P10275; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0043234; C:protein complex; IDA:MGI.
DR   GO; GO:0005497; F:androgen binding; NAS:UniProtKB.
DR   GO; GO:0004882; F:androgen receptor activity; IDA:UniProtKB.
DR   GO; GO:0051117; F:ATPase binding; IDA:MGI.
DR   GO; GO:0008013; F:beta-catenin binding; IDA:BHF-UCL.
DR   GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0046983; F:protein dimerization activity; NAS:UniProtKB.
DR   GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0004879; F:RNA polymerase II transcription factor activity, ligand-activated sequence-specific DNA binding; IDA:BHF-UCL.
DR   GO; GO:0001085; F:RNA polymerase II transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0008134; F:transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
DR   GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030521; P:androgen receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0016049; P:cell growth; NAS:UniProtKB.
DR   GO; GO:0008283; P:cell proliferation; NAS:UniProtKB.
DR   GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR   GO; GO:0010467; P:gene expression; TAS:Reactome.
DR   GO; GO:0030522; P:intracellular receptor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
DR   GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0045720; P:negative regulation of integrin biosynthetic process; IDA:BHF-UCL.
DR   GO; GO:0045597; P:positive regulation of cell differentiation; IMP:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IDA:BHF-UCL.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0045726; P:positive regulation of integrin biosynthetic process; IDA:BHF-UCL.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:BHF-UCL.
DR   GO; GO:0042327; P:positive regulation of phosphorylation; IMP:BHF-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR   GO; GO:0045945; P:positive regulation of transcription from RNA polymerase III promoter; IDA:BHF-UCL.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0030850; P:prostate gland development; NAS:UniProtKB.
DR   GO; GO:0051259; P:protein oligomerization; IDA:MGI.
DR   GO; GO:0090003; P:regulation of establishment of protein localization to plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0007548; P:sex differentiation; NAS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
DR   GO; GO:0006351; P:transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0006810; P:transport; TAS:ProtInc.
DR   Gene3D; 1.10.565.10; -; 2.
DR   Gene3D; 3.30.50.10; -; 1.
DR   InterPro; IPR001103; Andrgn_rcpt.
DR   InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR   InterPro; IPR001628; Znf_hrmn_rcpt.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   Pfam; PF02166; Androgen_recep; 1.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   Pfam; PF00105; zf-C4; 1.
DR   PRINTS; PR00521; ANDROGENR.
DR   PRINTS; PR00047; STROIDFINGER.
DR   SMART; SM00430; HOLI; 1.
DR   SMART; SM00399; ZnF_C4; 1.
DR   SUPFAM; SSF48508; SSF48508; 1.
DR   PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative splicing; Complete proteome;
KW   Cytoplasm; Disease mutation; DNA-binding; Isopeptide bond;
KW   Lipid-binding; Lipoprotein; Metal-binding; Neurodegeneration; Nucleus;
KW   Palmitate; Phosphoprotein; Polymorphism; Pseudohermaphroditism;
KW   Receptor; Reference proteome; Steroid-binding; Transcription;
KW   Transcription regulation; Triplet repeat expansion; Ubl conjugation;
KW   Zinc; Zinc-finger.
FT   CHAIN         1    919       Androgen receptor.
FT                                /FTId=PRO_0000053704.
FT   DNA_BIND    559    631       Nuclear receptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00407}.
FT   ZN_FING     559    579       NR C4-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00407}.
FT   ZN_FING     595    619       NR C4-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00407}.
FT   REGION        1    558       Modulating.
FT   REGION      551    919       Interaction with LPXN.
FT   REGION      571    661       Interaction with HIPK3. {ECO:0000250}.
FT   REGION      591    919       Interaction with CCAR1.
FT                                {ECO:0000269|PubMed:23887938}.
FT   REGION      624    919       Interaction with KAT7.
FT   REGION      690    919       Ligand-binding.
FT   COMPBIAS     54     57       Poly-Leu.
FT   COMPBIAS     58     89       Gln-rich.
FT   COMPBIAS     58     78       Poly-Gln.
FT   COMPBIAS     84     89       Poly-Gln.
FT   COMPBIAS    193    197       Poly-Gln.
FT   COMPBIAS    372    381       Poly-Pro.
FT   COMPBIAS    396    402       Poly-Ala.
FT   COMPBIAS    449    472       Poly-Gly.
FT   BINDING     705    705       Androgen.
FT   BINDING     752    752       Androgen.
FT   BINDING     877    877       Androgen.
FT   SITE        720    720       Interaction with coactivator LXXL motif.
FT   SITE        897    897       Interaction with coactivator FXXLF motif.
FT   MOD_RES      81     81       Phosphoserine; by CDK9.
FT                                {ECO:0000269|PubMed:20980437}.
FT   MOD_RES      94     94       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES     223    223       Phosphotyrosine; by CSK.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MOD_RES     256    256       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     267    267       Phosphotyrosine; by CSK and TNK2.
FT                                {ECO:0000269|PubMed:17045208,
FT                                ECO:0000269|PubMed:17494760,
FT                                ECO:0000269|PubMed:20623637}.
FT   MOD_RES     307    307       Phosphotyrosine; by CSK.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MOD_RES     346    346       Phosphotyrosine; by CSK.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MOD_RES     357    357       Phosphotyrosine; by CSK.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MOD_RES     362    362       Phosphotyrosine; by CSK.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MOD_RES     363    363       Phosphotyrosine; by CSK and TNK2.
FT                                {ECO:0000269|PubMed:17045208,
FT                                ECO:0000269|PubMed:17494760}.
FT   MOD_RES     393    393       Phosphotyrosine; by CSK.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MOD_RES     534    534       Phosphotyrosine; by CSK.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MOD_RES     551    551       Phosphotyrosine; by CSK.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MOD_RES     650    650       Phosphoserine; by STK4/MST1.
FT                                {ECO:0000269|PubMed:21512132}.
FT   MOD_RES     915    915       Phosphotyrosine; by CSK.
FT                                {ECO:0000269|PubMed:17045208}.
FT   CROSSLNK    386    386       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT   CROSSLNK    520    520       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT   CROSSLNK    845    845       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000269|PubMed:19345326}.
FT   CROSSLNK    847    847       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000269|PubMed:19345326}.
FT   VAR_SEQ       1    531       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_036889.
FT   VAR_SEQ     532    538       GPYGDMR -> MILWLHS (in isoform 2).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_036890.
FT   VARIANT       2      2       E -> K (in PAIS).
FT                                {ECO:0000269|PubMed:8823308}.
FT                                /FTId=VAR_004679.
FT   VARIANT      54     54       L -> S (in prostate cancer).
FT                                /FTId=VAR_004680.
FT   VARIANT      57     57       L -> Q (in prostate cancer).
FT                                /FTId=VAR_004681.
FT   VARIANT      64     64       Q -> R (in prostate cancer).
FT                                /FTId=VAR_009711.
FT   VARIANT      74     78       Missing.
FT                                /FTId=VAR_004682.
FT   VARIANT     112    112       Q -> H (in prostate cancer).
FT                                /FTId=VAR_009712.
FT   VARIANT     180    180       K -> R (in prostate cancer).
FT                                /FTId=VAR_009713.
FT   VARIANT     194    194       Q -> R (in AIS).
FT                                {ECO:0000269|PubMed:9255042}.
FT                                /FTId=VAR_009224.
FT   VARIANT     205    205       S -> R. {ECO:0000269|PubMed:8213813}.
FT                                /FTId=VAR_009714.
FT   VARIANT     214    214       G -> R (in AIS; 20% lower transactivation
FT                                capacity). {ECO:0000269|PubMed:9788719}.
FT                                /FTId=VAR_009715.
FT   VARIANT     255    255       L -> P (in AIS).
FT                                {ECO:0000269|PubMed:9610419}.
FT                                /FTId=VAR_009225.
FT   VARIANT     266    266       M -> T (in prostate cancer).
FT                                /FTId=VAR_009716.
FT   VARIANT     269    269       P -> S (in prostate cancer).
FT                                /FTId=VAR_009717.
FT   VARIANT     340    340       P -> L (in prostate cancer).
FT                                {ECO:0000269|PubMed:7511268}.
FT                                /FTId=VAR_009718.
FT   VARIANT     390    390       P -> R (in AIS).
FT                                {ECO:0000269|PubMed:10571951}.
FT                                /FTId=VAR_009226.
FT   VARIANT     390    390       P -> S (in AIS).
FT                                /FTId=VAR_009227.
FT   VARIANT     443    443       Q -> R (in AIS; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:10571951}.
FT                                /FTId=VAR_009228.
FT   VARIANT     465    472       Missing.
FT                                /FTId=VAR_004683.
FT   VARIANT     491    491       G -> S (in AIS).
FT                                /FTId=VAR_009719.
FT   VARIANT     528    528       D -> G (in prostate cancer).
FT                                /FTId=VAR_009720.
FT   VARIANT     547    547       L -> F (in PAIS).
FT                                /FTId=VAR_009721.
FT   VARIANT     548    548       P -> S (in AIS).
FT                                {ECO:0000269|PubMed:8683794}.
FT                                /FTId=VAR_009722.
FT   VARIANT     559    559       C -> Y (in AIS).
FT                                {ECO:0000269|PubMed:1316540}.
FT                                /FTId=VAR_009723.
FT   VARIANT     568    568       G -> V (in a patient with isolated
FT                                hypospadias).
FT                                {ECO:0000269|PubMed:7673412}.
FT                                /FTId=VAR_009725.
FT   VARIANT     568    568       G -> W (in PAIS).
FT                                {ECO:0000269|PubMed:7910529}.
FT                                /FTId=VAR_009726.
FT   VARIANT     571    571       Y -> C (in AIS).
FT                                {ECO:0000269|PubMed:9544375}.
FT                                /FTId=VAR_009727.
FT   VARIANT     573    573       A -> D (in AIS; defective DNA binding and
FT                                transactivation).
FT                                {ECO:0000269|PubMed:8918984}.
FT                                /FTId=VAR_009728.
FT   VARIANT     574    574       L -> P (in prostate cancer).
FT                                /FTId=VAR_009729.
FT   VARIANT     575    575       T -> A (in prostate cancer).
FT                                {ECO:0000269|PubMed:10706109}.
FT                                /FTId=VAR_009730.
FT   VARIANT     576    576       C -> F (in AIS; lack of DNA binding).
FT                                /FTId=VAR_009731.
FT   VARIANT     576    576       C -> R (in AIS).
FT                                {ECO:0000269|PubMed:1316540}.
FT                                /FTId=VAR_009732.
FT   VARIANT     579    579       C -> F (in AIS; reduced transcription and
FT                                DNA binding).
FT                                {ECO:0000269|PubMed:8809734}.
FT                                /FTId=VAR_009733.
FT   VARIANT     579    579       C -> Y (in AIS).
FT                                /FTId=VAR_009734.
FT   VARIANT     580    580       K -> R (in prostate cancer).
FT                                {ECO:0000269|PubMed:10706109}.
FT                                /FTId=VAR_009735.
FT   VARIANT     581    581       V -> F (in AIS).
FT                                {ECO:0000269|PubMed:8224266,
FT                                ECO:0000269|Ref.109}.
FT                                /FTId=VAR_009736.
FT   VARIANT     582    582       F -> S (in PAIS).
FT                                {ECO:0000269|PubMed:7981687}.
FT                                /FTId=VAR_009737.
FT   VARIANT     582    582       F -> Y (in PAIS).
FT                                {ECO:0000269|PubMed:8809734}.
FT                                /FTId=VAR_009738.
FT   VARIANT     582    582       Missing (in AIS).
FT                                {ECO:0000269|PubMed:8162033}.
FT                                /FTId=VAR_009739.
FT   VARIANT     585    585       R -> K (in AIS).
FT                                /FTId=VAR_009740.
FT   VARIANT     586    586       A -> V (in prostate cancer; somatic
FT                                mutation). {ECO:0000269|PubMed:10706109}.
FT                                /FTId=VAR_009741.
FT   VARIANT     587    587       A -> S (in prostate cancer; somatic
FT                                mutation).
FT                                /FTId=VAR_009742.
FT   VARIANT     596    596       A -> T (in AIS; abolishes dimerization).
FT                                {ECO:0000269|PubMed:10590024,
FT                                ECO:0000269|PubMed:7649358}.
FT                                /FTId=VAR_009743.
FT   VARIANT     597    597       S -> G (in PAIS; associated with P-617 in
FT                                a PAIS patient; high dissociation rate;
FT                                partially restores DNA-binding activity
FT                                of P-617 mutant receptors).
FT                                {ECO:0000269|PubMed:1316540}.
FT                                /FTId=VAR_009744.
FT   VARIANT     597    597       S -> T (in a patient with severe
FT                                hypospadias).
FT                                {ECO:0000269|PubMed:10092153}.
FT                                /FTId=VAR_009745.
FT   VARIANT     601    601       C -> F (in AIS).
FT                                {ECO:0000269|PubMed:7981689}.
FT                                /FTId=VAR_009746.
FT   VARIANT     604    604       D -> Y (in PAIS).
FT                                {ECO:0000269|PubMed:7981687}.
FT                                /FTId=VAR_009747.
FT   VARIANT     607    607       R -> Q (in PAIS and breast cancer).
FT                                {ECO:0000269|PubMed:10221692,
FT                                ECO:0000269|PubMed:1303262,
FT                                ECO:0000269|PubMed:9039340,
FT                                ECO:0000269|PubMed:9543136}.
FT                                /FTId=VAR_004684.
FT   VARIANT     608    608       R -> K (in PAIS and breast cancer;
FT                                defective nuclear localization).
FT                                {ECO:0000269|PubMed:1424203,
FT                                ECO:0000269|PubMed:8281139,
FT                                ECO:0000269|PubMed:9196614}.
FT                                /FTId=VAR_004685.
FT   VARIANT     610    610       N -> T (in PAIS).
FT                                {ECO:0000269|PubMed:9039340}.
FT                                /FTId=VAR_009748.
FT   VARIANT     611    611       C -> Y (in AIS).
FT                                /FTId=VAR_009749.
FT   VARIANT     615    615       R -> H (in AIS and PAIS).
FT                                {ECO:0000269|PubMed:7970939,
FT                                ECO:0000269|PubMed:8162033,
FT                                ECO:0000269|PubMed:8413310,
FT                                ECO:0000269|PubMed:9698822}.
FT                                /FTId=VAR_009751.
FT   VARIANT     615    615       R -> P (in AIS).
FT                                /FTId=VAR_009752.
FT   VARIANT     615    615       Missing (in AIS).
FT                                {ECO:0000269|PubMed:8162033}.
FT                                /FTId=VAR_009750.
FT   VARIANT     616    616       L -> P (in AIS).
FT                                {ECO:0000269|PubMed:8647313}.
FT                                /FTId=VAR_009753.
FT   VARIANT     616    616       L -> R (in PAIS).
FT                                {ECO:0000269|PubMed:8126121}.
FT                                /FTId=VAR_009754.
FT   VARIANT     617    617       R -> P (in AIS and PAIS; associated with
FT                                G-597 in a PAIS patient; loss of DNA-
FT                                binding activity).
FT                                {ECO:0000269|PubMed:1316540,
FT                                ECO:0000269|PubMed:1999491}.
FT                                /FTId=VAR_009755.
FT   VARIANT     619    619       C -> Y (in prostate cancer; loss of DNA
FT                                binding; somatic mutation).
FT                                {ECO:0000269|PubMed:10598582,
FT                                ECO:0000269|PubMed:10706109}.
FT                                /FTId=VAR_009756.
FT   VARIANT     629    629       R -> Q (in prostate cancer).
FT                                {ECO:0000269|PubMed:9184448}.
FT                                /FTId=VAR_009757.
FT   VARIANT     630    630       K -> T (in prostate cancer).
FT                                /FTId=VAR_009758.
FT   VARIANT     645    645       A -> D (in dbSNP:rs1800053).
FT                                {ECO:0000269|PubMed:9554755}.
FT                                /FTId=VAR_004686.
FT   VARIANT     647    647       S -> N (in prostate cancer).
FT                                /FTId=VAR_009760.
FT   VARIANT     664    664       I -> N (in AIS and PAIS).
FT                                /FTId=VAR_004687.
FT   VARIANT     670    670       Q -> R (in prostate cancer).
FT                                /FTId=VAR_009761.
FT   VARIANT     671    671       P -> H (in PAIS).
FT                                /FTId=VAR_009762.
FT   VARIANT     672    672       I -> T (in prostate cancer).
FT                                /FTId=VAR_009763.
FT   VARIANT     677    677       L -> P (in AIS).
FT                                {ECO:0000269|PubMed:7537149}.
FT                                /FTId=VAR_004688.
FT   VARIANT     681    681       E -> K (in AIS).
FT                                {ECO:0000269|PubMed:10221692,
FT                                ECO:0000269|PubMed:8325950}.
FT                                /FTId=VAR_009764.
FT   VARIANT     682    682       P -> T (in PAIS).
FT                                {ECO:0000269|PubMed:11587068}.
FT                                /FTId=VAR_013474.
FT   VARIANT     683    683       G -> A (in prostate cancer).
FT                                {ECO:0000269|PubMed:10629558,
FT                                ECO:0000269|PubMed:9000575}.
FT                                /FTId=VAR_009765.
FT   VARIANT     684    684       V -> I (in AIS).
FT                                /FTId=VAR_009766.
FT   VARIANT     686    686       C -> R (in PAIS).
FT                                /FTId=VAR_009767.
FT   VARIANT     687    687       A -> V (in PAIS).
FT                                /FTId=VAR_009768.
FT   VARIANT     688    688       G -> E (in AIS).
FT                                /FTId=VAR_009769.
FT   VARIANT     690    690       Missing (in PAIS). {ECO:0000269|Ref.117}.
FT                                /FTId=VAR_009770.
FT   VARIANT     692    692       Missing (in AIS).
FT                                /FTId=VAR_004689.
FT   VARIANT     695    695       D -> H (in AIS).
FT                                {ECO:0000269|PubMed:1775137}.
FT                                /FTId=VAR_004690.
FT   VARIANT     695    695       D -> N (in AIS; almost complete loss of
FT                                androgen binding and transcription
FT                                activation).
FT                                {ECO:0000269|PubMed:16595706,
FT                                ECO:0000269|PubMed:1775137}.
FT                                /FTId=VAR_004691.
FT   VARIANT     695    695       D -> V (in AIS).
FT                                {ECO:0000269|PubMed:9554754}.
FT                                /FTId=VAR_004692.
FT   VARIANT     700    700       L -> M (in AIS).
FT                                /FTId=VAR_009771.
FT   VARIANT     701    701       L -> F (in AIS).
FT                                /FTId=VAR_009772.
FT   VARIANT     701    701       L -> H (in AIS and prostate cancer).
FT                                {ECO:0000269|PubMed:10569618,
FT                                ECO:0000269|PubMed:8274409,
FT                                ECO:0000269|PubMed:9438000}.
FT                                /FTId=VAR_009773.
FT   VARIANT     702    702       S -> A (in AIS).
FT                                /FTId=VAR_009774.
FT   VARIANT     703    703       S -> C (in AIS).
FT                                /FTId=VAR_009775.
FT   VARIANT     703    703       S -> G (in PAIS and AIS).
FT                                {ECO:0000269|PubMed:9302173}.
FT                                /FTId=VAR_004693.
FT   VARIANT     705    705       N -> S (in AIS).
FT                                {ECO:0000269|PubMed:1480178,
FT                                ECO:0000269|PubMed:7671849}.
FT                                /FTId=VAR_009776.
FT   VARIANT     705    705       N -> Y (in AIS).
FT                                {ECO:0000269|PubMed:11744994}.
FT                                /FTId=VAR_013475.
FT   VARIANT     707    707       L -> R (in AIS).
FT                                {ECO:0000269|PubMed:8626869}.
FT                                /FTId=VAR_004694.
FT   VARIANT     708    708       G -> A (in PAIS).
FT                                {ECO:0000269|PubMed:7981687,
FT                                ECO:0000269|PubMed:9329414}.
FT                                /FTId=VAR_009777.
FT   VARIANT     708    708       G -> V (in AIS).
FT                                /FTId=VAR_009778.
FT   VARIANT     710    710       R -> T (in AIS).
FT                                /FTId=VAR_009779.
FT   VARIANT     711    711       Q -> E (in PAIS).
FT                                {ECO:0000269|PubMed:11587068}.
FT                                /FTId=VAR_013476.
FT   VARIANT     712    712       L -> F (in PAIS).
FT                                /FTId=VAR_009780.
FT   VARIANT     715    715       V -> M (in prostate cancer; gain in
FT                                function). {ECO:0000269|PubMed:8145761}.
FT                                /FTId=VAR_009781.
FT   VARIANT     717    717       K -> E (in prostate cancer).
FT                                /FTId=VAR_009782.
FT   VARIANT     720    720       K -> E (in prostate cancer; found in bone
FT                                metastases).
FT                                /FTId=VAR_009783.
FT   VARIANT     721    721       A -> T (in prostate cancer; somatic
FT                                mutation).
FT                                /FTId=VAR_009784.
FT   VARIANT     722    722       L -> F (in AIS).
FT                                /FTId=VAR_009785.
FT   VARIANT     723    723       P -> S (in AIS).
FT                                /FTId=VAR_009786.
FT   VARIANT     724    724       G -> D (in AIS and prostate cancer).
FT                                /FTId=VAR_009787.
FT   VARIANT     725    725       F -> L (in a patient with severe
FT                                hypospadias).
FT                                {ECO:0000269|PubMed:10092153,
FT                                ECO:0000269|PubMed:7671849}.
FT                                /FTId=VAR_009788.
FT   VARIANT     726    726       R -> L (in prostate cancer).
FT                                {ECO:0000269|PubMed:8530589}.
FT                                /FTId=VAR_009789.
FT   VARIANT     727    727       N -> K (in AIS).
FT                                {ECO:0000269|PubMed:7993455}.
FT                                /FTId=VAR_009790.
FT   VARIANT     728    728       L -> S (in PAIS).
FT                                /FTId=VAR_009791.
FT   VARIANT     730    730       V -> M (in prostate cancer; increases
FT                                transcription activation).
FT                                {ECO:0000269|PubMed:1631125,
FT                                ECO:0000269|PubMed:7591265}.
FT                                /FTId=VAR_004695.
FT   VARIANT     732    732       D -> N (in AIS).
FT                                {ECO:0000269|PubMed:9252933}.
FT                                /FTId=VAR_004696.
FT   VARIANT     732    732       D -> Y (in AIS).
FT                                /FTId=VAR_004697.
FT   VARIANT     733    733       Q -> H (in PAIS).
FT                                /FTId=VAR_009792.
FT   VARIANT     737    737       I -> T (in PAIS).
FT                                {ECO:0000269|PubMed:7671849}.
FT                                /FTId=VAR_009793.
FT   VARIANT     741    741       W -> R (in AIS).
FT                                {ECO:0000269|PubMed:1464650}.
FT                                /FTId=VAR_009794.
FT   VARIANT     742    742       M -> I (in PAIS).
FT                                {ECO:0000269|PubMed:8824883}.
FT                                /FTId=VAR_004698.
FT   VARIANT     742    742       M -> V (in PAIS).
FT                                {ECO:0000269|PubMed:7970939}.
FT                                /FTId=VAR_009795.
FT   VARIANT     743    743       G -> E (in AIS).
FT                                {ECO:0000269|PubMed:11587068}.
FT                                /FTId=VAR_013477.
FT   VARIANT     743    743       G -> V (in PAIS and AIS).
FT                                {ECO:0000269|PubMed:8096390,
FT                                ECO:0000269|PubMed:8325932,
FT                                ECO:0000269|PubMed:9768671,
FT                                ECO:0000269|Ref.109}.
FT                                /FTId=VAR_004699.
FT   VARIANT     744    744       L -> F (in AIS and prostate cancer).
FT                                /FTId=VAR_009796.
FT   VARIANT     745    745       M -> T (in PAIS).
FT                                {ECO:0000269|PubMed:7970939}.
FT                                /FTId=VAR_009797.
FT   VARIANT     746    746       V -> M (in PAIS).
FT                                /FTId=VAR_009798.
FT   VARIANT     748    748       A -> D (in PAIS).
FT                                /FTId=VAR_009799.
FT   VARIANT     748    748       A -> T (in prostate cancer).
FT                                /FTId=VAR_009800.
FT   VARIANT     748    748       A -> V (in prostate cancer).
FT                                /FTId=VAR_009801.
FT   VARIANT     749    749       M -> I (in prostate cancer).
FT                                /FTId=VAR_009802.
FT   VARIANT     749    749       M -> V (in PAIS and AIS).
FT                                {ECO:0000269|PubMed:1480178,
FT                                ECO:0000269|PubMed:1487249,
FT                                ECO:0000269|PubMed:8990010}.
FT                                /FTId=VAR_004700.
FT   VARIANT     750    750       G -> D (in AIS; loss of androgen
FT                                binding). {ECO:0000269|PubMed:9328206}.
FT                                /FTId=VAR_004701.
FT   VARIANT     750    750       G -> S (in prostate cancer).
FT                                /FTId=VAR_009803.
FT   VARIANT     751    751       W -> R (in AIS).
FT                                /FTId=VAR_009804.
FT   VARIANT     752    752       R -> Q (in AIS).
FT                                {ECO:0000269|PubMed:9544375,
FT                                ECO:0000269|PubMed:9698822}.
FT                                /FTId=VAR_004702.
FT   VARIANT     754    754       F -> L (in PAIS and prostate cancer).
FT                                {ECO:0000269|PubMed:7981687,
FT                                ECO:0000269|PubMed:9039340}.
FT                                /FTId=VAR_009805.
FT   VARIANT     754    754       F -> V (in AIS).
FT                                {ECO:0000269|PubMed:8103398,
FT                                ECO:0000269|Ref.109}.
FT                                /FTId=VAR_004703.
FT   VARIANT     755    755       T -> A (in prostate cancer).
FT                                /FTId=VAR_009806.
FT   VARIANT     756    756       N -> S (in PAIS).
FT                                /FTId=VAR_009807.
FT   VARIANT     757    757       V -> A (in prostate cancer).
FT                                {ECO:0000269|PubMed:10706109}.
FT                                /FTId=VAR_009808.
FT   VARIANT     758    758       N -> T (in PAIS; 50% reduction in
FT                                transactivation).
FT                                {ECO:0000269|PubMed:9607727}.
FT                                /FTId=VAR_009809.
FT   VARIANT     759    759       S -> F (in AIS).
FT                                {ECO:0000269|PubMed:1480178}.
FT                                /FTId=VAR_009810.
FT   VARIANT     759    759       S -> P (in prostate cancer).
FT                                /FTId=VAR_009811.
FT   VARIANT     762    762       L -> F (in AIS; loss of androgen
FT                                binding). {ECO:0000269|PubMed:9328206}.
FT                                /FTId=VAR_004704.
FT   VARIANT     763    763       Y -> C (in PAIS and prostate cancer;
FT                                partial loss of androgen binding).
FT                                {ECO:0000269|PubMed:16595706,
FT                                ECO:0000269|PubMed:2010552,
FT                                ECO:0000269|PubMed:7581399}.
FT                                /FTId=VAR_004705.
FT   VARIANT     763    763       Y -> H (in AIS).
FT                                {ECO:0000269|PubMed:7671849}.
FT                                /FTId=VAR_009812.
FT   VARIANT     764    764       F -> L (in AIS).
FT                                {ECO:0000269|PubMed:7970939}.
FT                                /FTId=VAR_009813.
FT   VARIANT     765    765       A -> T (in AIS; loss of androgen
FT                                binding). {ECO:0000269|PubMed:1426313,
FT                                ECO:0000269|PubMed:9252933,
FT                                ECO:0000269|PubMed:9328206,
FT                                ECO:0000269|PubMed:9856504}.
FT                                /FTId=VAR_004707.
FT   VARIANT     765    765       A -> V (in AIS).
FT                                /FTId=VAR_009814.
FT   VARIANT     766    766       P -> S (in AIS).
FT                                /FTId=VAR_009815.
FT   VARIANT     767    767       D -> E (in AIS). {ECO:0000269|Ref.109}.
FT                                /FTId=VAR_009816.
FT   VARIANT     768    768       L -> P (in AIS).
FT                                /FTId=VAR_009817.
FT   VARIANT     771    771       N -> H (in PAIS).
FT                                {ECO:0000269|PubMed:7981687}.
FT                                /FTId=VAR_009818.
FT   VARIANT     772    772       E -> A (in PAIS).
FT                                {ECO:0000269|PubMed:10022458}.
FT                                /FTId=VAR_009819.
FT   VARIANT     772    772       E -> G (in PAIS).
FT                                {ECO:0000269|PubMed:9196614}.
FT                                /FTId=VAR_009820.
FT   VARIANT     774    774       R -> C (in AIS; frequent mutation; loss
FT                                of androgen binding).
FT                                {ECO:0000269|PubMed:1609793,
FT                                ECO:0000269|PubMed:1856263,
FT                                ECO:0000269|PubMed:2082179,
FT                                ECO:0000269|PubMed:8990010,
FT                                ECO:0000269|PubMed:9544375}.
FT                                /FTId=VAR_004709.
FT   VARIANT     774    774       R -> H (in AIS and PAIS; almost complete
FT                                loss of androgen binding).
FT                                {ECO:0000269|PubMed:1480178,
FT                                ECO:0000269|PubMed:1609793,
FT                                ECO:0000269|PubMed:16595706,
FT                                ECO:0000269|PubMed:7671849}.
FT                                /FTId=VAR_004708.
FT   VARIANT     779    779       R -> W (in AIS).
FT                                {ECO:0000269|PubMed:7581399,
FT                                ECO:0000269|PubMed:7981687,
FT                                ECO:0000269|PubMed:9007482}.
FT                                /FTId=VAR_004710.
FT   VARIANT     780    780       M -> I (in PAIS and AIS).
FT                                {ECO:0000269|PubMed:8768864,
FT                                ECO:0000269|PubMed:8824883,
FT                                ECO:0000269|PubMed:8990010}.
FT                                /FTId=VAR_004711.
FT   VARIANT     782    782       S -> N (in prostate cancer; somatic
FT                                mutation).
FT                                /FTId=VAR_009821.
FT   VARIANT     784    784       C -> Y (in AIS; loss of androgen binding
FT                                and of transactivation).
FT                                {ECO:0000269|PubMed:9856504}.
FT                                /FTId=VAR_004712.
FT   VARIANT     787    787       M -> V (in AIS).
FT                                {ECO:0000269|PubMed:1569163}.
FT                                /FTId=VAR_004713.
FT   VARIANT     788    788       R -> S (in AIS).
FT                                /FTId=VAR_009822.
FT   VARIANT     790    790       L -> F (in AIS).
FT                                {ECO:0000269|PubMed:7962294}.
FT                                /FTId=VAR_009823.
FT   VARIANT     791    791       S -> P (in prostate cancer).
FT                                /FTId=VAR_009824.
FT   VARIANT     793    793       E -> D. {ECO:0000269|PubMed:8213813}.
FT                                /FTId=VAR_009825.
FT   VARIANT     794    794       F -> S (in AIS).
FT                                {ECO:0000269|PubMed:8990010}.
FT                                /FTId=VAR_004714.
FT   VARIANT     798    798       Q -> E (in PAIS, AIS and prostate cancer;
FT                                reduced transcription activation).
FT                                {ECO:0000269|PubMed:16595706,
FT                                ECO:0000269|PubMed:7511268,
FT                                ECO:0000269|PubMed:7671849,
FT                                ECO:0000269|PubMed:8628719,
FT                                ECO:0000269|PubMed:8824883,
FT                                ECO:0000269|PubMed:9851768}.
FT                                /FTId=VAR_004715.
FT   VARIANT     806    806       C -> Y (in PAIS).
FT                                /FTId=VAR_009826.
FT   VARIANT     807    807       M -> R (in AIS; loss of transactivation).
FT                                {ECO:0000269|PubMed:8281140}.
FT                                /FTId=VAR_004716.
FT   VARIANT     807    807       M -> T (in PAIS).
FT                                {ECO:0000269|PubMed:10543676}.
FT                                /FTId=VAR_009827.
FT   VARIANT     807    807       M -> V (in AIS; 25% androgen binding).
FT                                {ECO:0000269|PubMed:7581399}.
FT                                /FTId=VAR_004717.
FT   VARIANT     812    812       L -> F (in AIS).
FT                                {ECO:0000269|PubMed:10458483}.
FT                                /FTId=VAR_009828.
FT   VARIANT     814    814       S -> N (in AIS and PAIS).
FT                                /FTId=VAR_004718.
FT   VARIANT     820    820       G -> A (in AIS).
FT                                {ECO:0000269|PubMed:9610419}.
FT                                /FTId=VAR_009829.
FT   VARIANT     821    821       L -> V (in PAIS).
FT                                /FTId=VAR_009830.
FT   VARIANT     827    827       F -> V (in PAIS).
FT                                {ECO:0000269|PubMed:11587068}.
FT                                /FTId=VAR_013478.
FT   VARIANT     830    830       L -> P (in prostate cancer).
FT                                /FTId=VAR_009831.
FT   VARIANT     831    831       R -> L (in AIS).
FT                                {ECO:0000269|PubMed:7633398}.
FT                                /FTId=VAR_004719.
FT   VARIANT     831    831       R -> Q (in AIS; loss of androgen
FT                                binding). {ECO:0000269|PubMed:10458483,
FT                                ECO:0000269|PubMed:2082179,
FT                                ECO:0000269|PubMed:7633398}.
FT                                /FTId=VAR_004720.
FT   VARIANT     834    834       Y -> C (in AIS; loss of androgen
FT                                binding). {ECO:0000269|PubMed:1464650}.
FT                                /FTId=VAR_009832.
FT   VARIANT     840    840       R -> C (in AIS).
FT                                {ECO:0000269|PubMed:8040309,
FT                                ECO:0000269|PubMed:8824883,
FT                                ECO:0000269|PubMed:9768671}.
FT                                /FTId=VAR_004721.
FT   VARIANT     840    840       R -> G (in PAIS).
FT                                {ECO:0000269|PubMed:9856504}.
FT                                /FTId=VAR_004722.
FT   VARIANT     840    840       R -> H (in AIS).
FT                                {ECO:0000269|PubMed:7909256,
FT                                ECO:0000269|PubMed:8040309,
FT                                ECO:0000269|PubMed:8126121,
FT                                ECO:0000269|PubMed:8205256,
FT                                ECO:0000269|PubMed:8325950,
FT                                ECO:0000269|PubMed:8830623,
FT                                ECO:0000269|PubMed:9039340}.
FT                                /FTId=VAR_004723.
FT   VARIANT     840    840       R -> S (in PAIS).
FT                                {ECO:0000269|PubMed:10502786}.
FT                                /FTId=VAR_009229.
FT   VARIANT     841    841       I -> S (in PAIS).
FT                                /FTId=VAR_009833.
FT   VARIANT     842    842       I -> T (in AIS).
FT                                {ECO:0000269|PubMed:8325950,
FT                                ECO:0000269|PubMed:9039340}.
FT                                /FTId=VAR_004724.
FT   VARIANT     846    846       R -> G (in prostate cancer).
FT                                {ECO:0000269|PubMed:10706109}.
FT                                /FTId=VAR_009834.
FT   VARIANT     854    854       R -> K (in PAIS).
FT                                /FTId=VAR_009835.
FT   VARIANT     855    855       R -> C (in AIS).
FT                                {ECO:0000269|PubMed:1480178,
FT                                ECO:0000269|PubMed:7581399,
FT                                ECO:0000269|PubMed:9001799,
FT                                ECO:0000269|PubMed:9255042,
FT                                ECO:0000269|Ref.109}.
FT                                /FTId=VAR_004725.
FT   VARIANT     855    855       R -> H (in AIS; strongly reduced
FT                                transcription activation).
FT                                {ECO:0000269|PubMed:16595706,
FT                                ECO:0000269|PubMed:8097257,
FT                                ECO:0000269|PubMed:8824883,
FT                                ECO:0000269|PubMed:9039340,
FT                                ECO:0000269|PubMed:9106550}.
FT                                /FTId=VAR_004726.
FT   VARIANT     856    856       F -> L (in AIS).
FT                                /FTId=VAR_009836.
FT   VARIANT     863    863       L -> R (in AIS).
FT                                /FTId=VAR_009837.
FT   VARIANT     864    864       D -> G (in AIS).
FT                                {ECO:0000269|PubMed:1480178}.
FT                                /FTId=VAR_009838.
FT   VARIANT     864    864       D -> N (in AIS; loss of androgen
FT                                binding). {ECO:0000269|PubMed:9328206}.
FT                                /FTId=VAR_004727.
FT   VARIANT     865    865       S -> P (in AIS).
FT                                /FTId=VAR_009839.
FT   VARIANT     866    866       V -> E (in AIS).
FT                                /FTId=VAR_004728.
FT   VARIANT     866    866       V -> L (in PAIS).
FT                                {ECO:0000269|PubMed:1424203,
FT                                ECO:0000269|PubMed:8325950,
FT                                ECO:0000269|PubMed:8446106}.
FT                                /FTId=VAR_004729.
FT   VARIANT     866    866       V -> M (in AIS and prostate cancer).
FT                                {ECO:0000269|PubMed:2082179,
FT                                ECO:0000269|PubMed:2594783,
FT                                ECO:0000269|PubMed:8446106,
FT                                ECO:0000269|PubMed:9039340}.
FT                                /FTId=VAR_004730.
FT   VARIANT     869    869       I -> M (in PAIS).
FT                                {ECO:0000269|PubMed:8097257,
FT                                ECO:0000269|PubMed:8824883}.
FT                                /FTId=VAR_004731.
FT   VARIANT     870    870       A -> G (in PAIS).
FT                                {ECO:0000269|PubMed:9329414}.
FT                                /FTId=VAR_009840.
FT   VARIANT     870    870       A -> V (in PAIS).
FT                                {ECO:0000269|PubMed:8033918}.
FT                                /FTId=VAR_009841.
FT   VARIANT     871    871       R -> G (in AIS).
FT                                {ECO:0000269|PubMed:10022458}.
FT                                /FTId=VAR_009842.
FT   VARIANT     874    874       H -> R (in AIS).
FT                                {ECO:0000269|PubMed:11587068}.
FT                                /FTId=VAR_013479.
FT   VARIANT     874    874       H -> Y (in prostate cancer; increases
FT                                affinity for testosterone and androgen
FT                                sensitivity; increased transcription
FT                                activation).
FT                                {ECO:0000269|PubMed:17591767}.
FT                                /FTId=VAR_009843.
FT   VARIANT     877    877       T -> A (in prostate cancer; found in bone
FT                                metastases; alters receptor specificity
FT                                so that transcription is activated by
FT                                antiandrogens such as cyproterone
FT                                acetate). {ECO:0000269|PubMed:10363963,
FT                                ECO:0000269|PubMed:10569618,
FT                                ECO:0000269|PubMed:1562539,
FT                                ECO:0000269|PubMed:16129672,
FT                                ECO:0000269|PubMed:17311914,
FT                                ECO:0000269|PubMed:2260966,
FT                                ECO:0000269|PubMed:8187068,
FT                                ECO:0000269|PubMed:8274409,
FT                                ECO:0000269|PubMed:8827083}.
FT                                /FTId=VAR_004732.
FT   VARIANT     877    877       T -> S (in prostate cancer).
FT                                /FTId=VAR_009844.
FT   VARIANT     879    879       D -> Y (in AIS).
FT                                {ECO:0000269|PubMed:11587068}.
FT                                /FTId=VAR_013480.
FT   VARIANT     880    880       L -> Q (in prostate cancer).
FT                                /FTId=VAR_009845.
FT   VARIANT     881    881       L -> V (in AIS).
FT                                {ECO:0000269|PubMed:7641413}.
FT                                /FTId=VAR_009846.
FT   VARIANT     886    886       M -> V (in AIS).
FT                                /FTId=VAR_009847.
FT   VARIANT     889    889       V -> M (in AIS and PAIS).
FT                                {ECO:0000269|PubMed:8126121,
FT                                ECO:0000269|PubMed:9160185}.
FT                                /FTId=VAR_009848.
FT   VARIANT     890    890       D -> N (in prostate cancer).
FT                                {ECO:0000269|PubMed:10363963}.
FT                                /FTId=VAR_009849.
FT   VARIANT     891    891       F -> L (in prostate cancer).
FT                                /FTId=VAR_009850.
FT   VARIANT     892    892       P -> L (in AIS).
FT                                {ECO:0000269|PubMed:10221770,
FT                                ECO:0000269|PubMed:10404311,
FT                                ECO:0000269|Ref.175}.
FT                                /FTId=VAR_004733.
FT   VARIANT     895    895       M -> T (in AIS; low androgen binding and
FT                                transactivation).
FT                                {ECO:0000269|PubMed:16129672,
FT                                ECO:0000269|PubMed:9856504}.
FT                                /FTId=VAR_004734.
FT   VARIANT     896    896       A -> T (in prostate cancer).
FT                                /FTId=VAR_009851.
FT   VARIANT     898    898       I -> T (in AIS).
FT                                /FTId=VAR_009852.
FT   VARIANT     902    902       Q -> R (in prostate cancer).
FT                                /FTId=VAR_009853.
FT   VARIANT     903    903       V -> M (in PAIS).
FT                                /FTId=VAR_009854.
FT   VARIANT     904    904       P -> H (in AIS).
FT                                /FTId=VAR_009855.
FT   VARIANT     904    904       P -> S (in AIS).
FT                                /FTId=VAR_009856.
FT   VARIANT     907    907       L -> F (in AIS; almost complete loss of
FT                                transcription activation).
FT                                {ECO:0000269|PubMed:16595706,
FT                                ECO:0000269|PubMed:9328206}.
FT                                /FTId=VAR_004735.
FT   VARIANT     909    909       G -> E (in prostate cancer).
FT                                /FTId=VAR_009857.
FT   VARIANT     909    909       G -> R (in PAIS).
FT                                {ECO:0000269|PubMed:8550758}.
FT                                /FTId=VAR_009858.
FT   VARIANT     910    910       K -> R (in prostate cancer).
FT                                {ECO:0000269|PubMed:9438000}.
FT                                /FTId=VAR_009859.
FT   VARIANT     911    911       V -> L (in PAIS).
FT                                {ECO:0000269|PubMed:10470409}.
FT                                /FTId=VAR_009860.
FT   VARIANT     913    913       P -> S (in PAIS).
FT                                /FTId=VAR_004736.
FT   VARIANT     916    916       F -> L (in AIS).
FT                                {ECO:0000269|PubMed:9302173}.
FT                                /FTId=VAR_009861.
FT   VARIANT     917    917       H -> R (in AIS).
FT                                /FTId=VAR_009862.
FT   VARIANT     919    919       Q -> R (in prostate cancer).
FT                                /FTId=VAR_009863.
FT   MUTAGEN      81     81       S->A: Reduced cell growth.
FT                                {ECO:0000269|PubMed:20980437}.
FT   MUTAGEN     223    223       Y->F: Decrease of CSK-induced
FT                                phosphorylation.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MUTAGEN     267    267       Y->F: Decrease of CSK-induced
FT                                phosphorylation and phosphorylation by
FT                                TNK2. Complete loss of TNK2-dependent
FT                                phosphorylation; when associated with F-
FT                                363. {ECO:0000269|PubMed:17045208,
FT                                ECO:0000269|PubMed:17494760}.
FT   MUTAGEN     307    307       Y->F: Decrease of CSK-induced
FT                                phosphorylation.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MUTAGEN     346    346       Y->F: Decrease of CSK-induced
FT                                phosphorylation.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MUTAGEN     357    357       Y->F: Decrease of CSK-induced
FT                                phosphorylation.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MUTAGEN     362    362       Y->F: Decrease of CSK-induced
FT                                phosphorylation.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MUTAGEN     363    363       Y->F: Decrease of CSK-induced
FT                                phosphorylation and phosphorylation by
FT                                TNK2. Complete loss of TNK2-dependent
FT                                phosphorylation; when associated with F-
FT                                267. {ECO:0000269|PubMed:17045208,
FT                                ECO:0000269|PubMed:17494760}.
FT   MUTAGEN     393    393       Y->F: Decrease of CSK-induced
FT                                phosphorylation.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MUTAGEN     534    534       Y->F: Greatest decrease of CSK-induced
FT                                phosphorylation and inhibition of
FT                                transcriptional activity induced by EGF.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MUTAGEN     551    551       Y->F: Decrease in CSK-induced
FT                                phosphorylation.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MUTAGEN     701    701       L->A: Alters receptor specificity, so
FT                                that transcription is activated by the
FT                                antiandrogen cyproterone acetate.
FT                                {ECO:0000269|PubMed:17311914}.
FT   MUTAGEN     720    720       K->A: Loss of transcription activation in
FT                                the presence of androgen and of
FT                                interaction with NCOA2.
FT                                {ECO:0000269|PubMed:15563469,
FT                                ECO:0000269|PubMed:17591767}.
FT   MUTAGEN     741    741       W->L: Strongly decreased transcription
FT                                activation in the presence of androgen.
FT                                {ECO:0000269|PubMed:16129672}.
FT   MUTAGEN     845    845       K->R: Prevents ubiquitination by RNF6.
FT                                Prevents AR transcriptional activation by
FT                                RNF14 in absence of hormone.
FT                                {ECO:0000269|PubMed:19345326}.
FT   MUTAGEN     847    847       K->R: Partially prevents ubiquitination
FT                                by RNF6. {ECO:0000269|PubMed:19345326}.
FT   MUTAGEN     897    897       E->A,Q: Reduced transcription activation
FT                                in the presence of androgen.
FT                                {ECO:0000269|PubMed:15563469,
FT                                ECO:0000269|PubMed:17591767}.
FT   MUTAGEN     897    897       E->K,R: Loss of transcription activation
FT                                in the presence of androgen.
FT                                {ECO:0000269|PubMed:15563469,
FT                                ECO:0000269|PubMed:17591767}.
FT   MUTAGEN     915    915       Y->F: Decrease in CSK-induced
FT                                phosphorylation.
FT                                {ECO:0000269|PubMed:17045208}.
FT   CONFLICT    166    166       G -> A (in Ref. 5; AAA51780).
FT                                {ECO:0000305}.
FT   CONFLICT    212    212       A -> R (in Ref. 3 and 6; AAA51771/
FT                                AAA51772). {ECO:0000305}.
FT   CONFLICT    475    475       G -> E (in Ref. 2; AAA51775 and 12;
FT                                AAA51770). {ECO:0000305}.
FT   CONFLICT    565    565       E -> K (in Ref. 14; AAA51774).
FT                                {ECO:0000305}.
FT   CONFLICT    634    634       L -> P (in Ref. 18; AAB21256/AAB21257).
FT                                {ECO:0000305}.
FT   CONFLICT    675    675       N -> I (in Ref. 18; AAB21256/AAB21257).
FT                                {ECO:0000305}.
FT   CONFLICT    810    810       L -> M (in Ref. 5; AAA51780).
FT                                {ECO:0000305}.
FT   HELIX        22     29       {ECO:0000244|PDB:3V49}.
FT   STRAND      666    668       {ECO:0000244|PDB:1XJ7}.
FT   HELIX       672    680       {ECO:0000244|PDB:4U4K}.
FT   STRAND      691    693       {ECO:0000244|PDB:1XJ7}.
FT   HELIX       697    720       {ECO:0000244|PDB:4U4K}.
FT   HELIX       725    727       {ECO:0000244|PDB:4U4K}.
FT   HELIX       730    757       {ECO:0000244|PDB:4U4K}.
FT   STRAND      760    765       {ECO:0000244|PDB:4U4K}.
FT   STRAND      768    770       {ECO:0000244|PDB:4U4K}.
FT   HELIX       772    777       {ECO:0000244|PDB:4U4K}.
FT   HELIX       781    796       {ECO:0000244|PDB:4U4K}.
FT   HELIX       801    812       {ECO:0000244|PDB:4U4K}.
FT   STRAND      814    817       {ECO:0000244|PDB:4U4K}.
FT   HELIX       824    843       {ECO:0000244|PDB:4U4K}.
FT   HELIX       849    882       {ECO:0000244|PDB:4U4K}.
FT   HELIX       884    887       {ECO:0000244|PDB:4U4K}.
FT   HELIX       893    901       {ECO:0000244|PDB:4U4K}.
FT   HELIX       903    907       {ECO:0000244|PDB:4U4K}.
FT   STRAND      910    913       {ECO:0000244|PDB:4U4K}.
SQ   SEQUENCE   919 AA;  98989 MW;  93B096927740B6FF CRC64;
     MEVQLGLGRV YPRPPSKTYR GAFQNLFQSV REVIQNPGPR HPEAASAAPP GASLLLLQQQ
     QQQQQQQQQQ QQQQQQQQET SPRQQQQQQG EDGSPQAHRR GPTGYLVLDE EQQPSQPQSA
     LECHPERGCV PEPGAAVAAS KGLPQQLPAP PDEDDSAAPS TLSLLGPTFP GLSSCSADLK
     DILSEASTMQ LLQQQQQEAV SEGSSSGRAR EASGAPTSSK DNYLGGTSTI SDNAKELCKA
     VSVSMGLGVE ALEHLSPGEQ LRGDCMYAPL LGVPPAVRPT PCAPLAECKG SLLDDSAGKS
     TEDTAEYSPF KGGYTKGLEG ESLGCSGSAA AGSSGTLELP STLSLYKSGA LDEAAAYQSR
     DYYNFPLALA GPPPPPPPPH PHARIKLENP LDYGSAWAAA AAQCRYGDLA SLHGAGAAGP
     GSGSPSAAAS SSWHTLFTAE EGQLYGPCGG GGGGGGGGGG GGGGGGGGGG GGEAGAVAPY
     GYTRPPQGLA GQESDFTAPD VWYPGGMVSR VPYPSPTCVK SEMGPWMDSY SGPYGDMRLE
     TARDHVLPID YYFPPQKTCL ICGDEASGCH YGALTCGSCK VFFKRAAEGK QKYLCASRND
     CTIDKFRRKN CPSCRLRKCY EAGMTLGARK LKKLGNLKLQ EEGEASSTTS PTEETTQKLT
     VSHIEGYECQ PIFLNVLEAI EPGVVCAGHD NNQPDSFAAL LSSLNELGER QLVHVVKWAK
     ALPGFRNLHV DDQMAVIQYS WMGLMVFAMG WRSFTNVNSR MLYFAPDLVF NEYRMHKSRM
     YSQCVRMRHL SQEFGWLQIT PQEFLCMKAL LLFSIIPVDG LKNQKFFDEL RMNYIKELDR
     IIACKRKNPT SCSRRFYQLT KLLDSVQPIA RELHQFTFDL LIKSHMVSVD FPEMMAEIIS
     VQVPKILSGK VKPIYFHTQ
//