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Database: UniProt
Entry: P10275
LinkDB: P10275
Original site: P10275 
ID   ANDR_HUMAN              Reviewed;         920 AA.
AC   P10275; A0A0B4J1T2; A2RUN2; B1AKD7; C0JKD3; C0JKD4; E7EVX6; Q9UD95;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   16-MAR-2016, sequence version 3.
DT   11-DEC-2019, entry version 278.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   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 cloning,
RT   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 human
RT   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-867.
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 human
RT   androgen receptor gene and identification of a point mutation in a family
RT   with complete androgen insensitivity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:9534-9538(1989).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 binding
RT   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] (ISOFORM
RP   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), TISSUE
RP   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 [MRNA] (ISOFORMS 3 AND 4), VARIANT GLN-57, FUNCTION
RP   (ISOFORMS 3 AND 4), AND SUBCELLULAR LOCATION (ISOFORM 3).
RX   PubMed=19244107; DOI=10.1158/0008-5472.can-08-3795;
RA   Guo Z., Yang X., Sun F., Jiang R., Linn D.E., Chen H., Chen H., Kong X.,
RA   Melamed J., Tepper C.G., Kung H.J., Brodie A.M., Edwards J., Qiu Y.;
RT   "A novel androgen receptor splice variant is up-regulated during prostate
RT   cancer progression and promotes androgen depletion-resistant growth.";
RL   Cancer Res. 69:2305-2313(2009).
RN   [9]
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., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., 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., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., 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., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., 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., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., 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., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-539.
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., van der Korput J.A.G.M.,
RA   Brinkmann A.O., Trapman J.;
RT   "The N-terminal domain of the human androgen receptor is encoded by one,
RT   large exon.";
RL   Mol. Cell. Endocrinol. 61:257-262(1989).
RN   [13]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 191-920 (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 androgen
RT   receptors.";
RL   Science 240:324-326(1988).
RN   [14]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 448-476.
RC   TISSUE=Blood;
RA   Lu J., Danielsen M.;
RL   Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
RN   [15]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 470-920 (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 androgen
RT   receptor.";
RL   Biochem. Biophys. Res. Commun. 153:241-248(1988).
RN   [16]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 537-541; 587-591; 626-630; 722-726;
RP   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   [17]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 558-625 (ISOFORMS 1/2), AND VARIANT AIS
RP   HIS-616.
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 of
RT   the androgen receptor gene causes complete androgen insensitivity in two
RT   siblings with receptor-positive androgen resistance.";
RL   Mol. Endocrinol. 7:861-869(1993).
RN   [18]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 560-625 (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 to
RT   the X chromosome.";
RL   Science 240:327-330(1988).
RN   [19]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 630-724, AND VARIANTS AIS ASN-696 AND
RP   HIS-696.
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 human
RT   androgen receptor leads to a functionally inactive protein with altered
RT   hormone-binding characteristics.";
RL   Mol. Endocrinol. 5:1562-1569(1991).
RN   [20]
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 (AR).";
RL   Nucleic Acids Res. 20:1427-1427(1992).
RN   [21]
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., Brufsky A.,
RA   Talcott J., Hennekens C.H., Kantoff P.W.;
RT   "The CAG repeat within the androgen receptor gene and its relationship to
RT   prostate cancer.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:3320-3323(1997).
RN   [22]
RP   ERRATUM.
RA   Giovannucci E., Stampfer M.J., Krithivas K., Brown M., Dahl D., Brufsky A.,
RA   Talcott J., Hennekens C.H., Kantoff P.W.;
RL   Proc. Natl. Acad. Sci. U.S.A. 94:8272-8272(1997).
RN   [23]
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   [24]
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, in
RT   human prostate.";
RL   J. Biol. Chem. 274:8316-8321(1999).
RN   [25]
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-dependent
RT   transcription.";
RL   J. Biol. Chem. 274:19441-19446(1999).
RN   [26]
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 identified
RT   androgen receptor polyglutamine region-associated coactivator.";
RL   J. Biol. Chem. 274:20229-20234(1999).
RN   [27]
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   [28]
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   [29]
RP   SUMOYLATION AT LYS-388 AND LYS-521.
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-like
RT   modifier 1 (SUMO-1).";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14145-14150(2000).
RN   [30]
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., 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   [31]
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., Takayanagi R.,
RA   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   [32]
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   [33]
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., Lim B.,
RA   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   [34]
RP   INTERACTION WITH RACK1, 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   [35]
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   [36]
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 antagonizes
RT   this inhibition by abrogation of this complex.";
RL   Mol. Cancer Res. 1:247-261(2003).
RN   [37]
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., 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   [38]
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 activity of
RT   nuclear hormone receptors.";
RL   J. Cell Biol. 170:191-200(2005).
RN   [39]
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., Sun Z.;
RT   "hZimp7, a novel PIAS-like protein, enhances androgen receptor-mediated
RT   transcription and interacts with SWI/SNF-like BAF complexes.";
RL   Mol. Endocrinol. 19:2915-2929(2005).
RN   [40]
RP   PHOSPHORYLATION AT TYR-225; TYR-269; TYR-309; TYR-348; TYR-359; TYR-364;
RP   TYR-365; TYR-395; TYR-535; TYR-552 AND TYR-916, MUTAGENESIS OF TYR-225;
RP   TYR-269; TYR-309; TYR-348; TYR-359; TYR-364; TYR-365; TYR-395; TYR-535;
RP   TYR-552 AND TYR-916, AND IDENTIFICATION BY MASS 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., Kong X.,
RA   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 phosphorylation.";
RL   Cancer Cell 10:309-319(2006).
RN   [41]
RP   ERRATUM.
RA   Guo Z., Dai B., Jiang T., Xu K., Xie Y., Kim O., Nesheiwat I., Kong X.,
RA   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   [42]
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., Shi X.B.,
RA   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 cells.";
RL   Cancer Res. 66:8439-8447(2006).
RN   [43]
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 a
RT   coactivator of the androgen receptor.";
RL   J. Steroid Biochem. Mol. Biol. 107:1-14(2007).
RN   [44]
RP   INTERACTION WITH RREB1.
RX   PubMed=17550981; DOI=10.1210/me.2006-0503;
RA   Mukhopadhyay N.K., Cinar B., Mukhopadhyay L., Lutchman M., Ferdinand A.S.,
RA   Kim J., Chung L.W.K., Adam R.M., Ray S.K., Leiter A.B., Richie J.P.,
RA   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 Ras
RT   pathway in enhancing androgenic signaling in prostate cancer.";
RL   Mol. Endocrinol. 21:2056-2070(2007).
RN   [45]
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   [46]
RP   INTERACTION WITH TNK2, PHOSPHORYLATION AT TYR-269 AND TYR-365 BY TNK2, AND
RP   MUTAGENESIS OF TYR-269 AND TYR-365.
RX   PubMed=17494760; DOI=10.1073/pnas.0700420104;
RA   Mahajan N.P., Liu Y., Majumder S., Warren M.R., Parker C.E., Mohler J.L.,
RA   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   [47]
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., Shinohara N.,
RA   Nonomura K., Hatakeyama S.;
RT   "TRIM68 regulates ligand-dependent transcription of androgen receptor in
RT   prostate cancer cells.";
RL   Cancer Res. 68:3486-3494(2008).
RN   [48]
RP   INTERACTION WITH LPXN.
RX   PubMed=18451096; DOI=10.1210/me.2006-0546;
RA   Kaulfuss S., Grzmil M., Hemmerlein B., Thelen P., Schweyer S., Neesen J.,
RA   Bubendorf L., Glass A.G., Jarry H., Auber B., Burfeind P.;
RT   "Leupaxin, a novel coactivator of the androgen receptor, is expressed in
RT   prostate cancer and plays a role in adhesion and invasion of prostate
RT   carcinoma cells.";
RL   Mol. Endocrinol. 22:1606-1621(2008).
RN   [49]
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   [50]
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., Tanaka J.,
RA   Imamura M., Hatakeyama S.;
RT   "TRIM24 mediates ligand-dependent activation of androgen receptor and is
RT   repressed by a bromodomain-containing protein, BRD7, in prostate cancer
RT   cells.";
RL   Biochim. Biophys. Acta 1793:1828-1836(2009).
RN   [51]
RP   FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, POLYUBIQUITINATION AT
RP   LYS-846 AND LYS-848 BY RNF6, MUTAGENESIS OF LYS-846 AND LYS-848,
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., Chen H.,
RA   Li W., Chen H., Kong X., Melamed J., Fang S., Xiao Z., Veenstra T.D.,
RA   Qiu Y.;
RT   "Regulation of androgen receptor transcriptional activity and specificity
RT   by RNF6-induced ubiquitination.";
RL   Cancer Cell 15:270-282(2009).
RN   [52]
RP   FUNCTION IN AR KINASE, PHOSPHORYLATION AT SER-83 BY CDK9, MUTAGENESIS OF
RP   SER-83, 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., Mollah S.A.,
RA   Shabanowitz J., Hunt D.F., Xenarios I., Hahn W.C., Conaway M., Carey M.F.,
RA   Gioeli D.;
RT   "CDK9 regulates AR promoter selectivity and cell growth through serine 81
RT   phosphorylation.";
RL   Mol. Endocrinol. 24:2267-2280(2010).
RN   [53]
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   [54]
RP   PHOSPHORYLATION AT TYR-269, AND ACTIVITY 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 androgen
RT   receptor activity.";
RL   Prostate 70:1274-1285(2010).
RN   [55]
RP   PHOSPHORYLATION AT SER-651, 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   [56]
RP   FUNCTION, AND INTERACTION WITH NCOR1; NCOR2 AND ZBTB7A.
RX   PubMed=20812024; DOI=10.1007/s00018-010-0511-7;
RA   Cui J., Yang Y., Zhang C., Hu P., Kan W., Bai X., Liu X., Song H.;
RT   "FBI-1 functions as a novel AR co-repressor in prostate cancer cells.";
RL   Cell. Mol. Life Sci. 68:1091-1103(2011).
RN   [57]
RP   INTERACTION WITH CRY1.
RX   PubMed=22170608; DOI=10.1038/nature10700;
RA   Lamia K.A., Papp S.J., Yu R.T., Barish G.D., Uhlenhaut N.H., Jonker J.W.,
RA   Downes M., Evans R.M.;
RT   "Cryptochromes mediate rhythmic repression of the glucocorticoid
RT   receptor.";
RL   Nature 480:552-556(2011).
RN   [58]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [59]
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 receptors.";
RL   Mol. Biol. Cell 23:188-199(2012).
RN   [60]
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., Kwon G.Y.,
RA   Lee H.M., Kim J.H.;
RT   "CCAR1 promotes chromatin loading of androgen receptor (AR) transcription
RT   complex by stabilizing the association between AR and GATA2.";
RL   Nucleic Acids Res. 41:8526-8536(2013).
RN   [61]
RP   INTERACTION WITH ARID4A.
RX   PubMed=23487765; DOI=10.1073/pnas.1218318110;
RA   Wu R.C., Jiang M., Beaudet A.L., Wu M.Y.;
RT   "ARID4A and ARID4B regulate male fertility, a functional link to the AR and
RT   RB pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:4616-4621(2013).
RN   [62]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND SER-258, 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., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [63]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 658-920.
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., Egner U.,
RA   Carrondo M.A.;
RT   "Structural evidence for ligand specificity in the binding domain of the
RT   human androgen receptor. Implications for pathogenic gene mutations.";
RL   J. Biol. Chem. 275:26164-26171(2000).
RN   [64]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 671-918.
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 prostate
RT   cancer.";
RL   J. Med. Chem. 45:1439-1446(2002).
RN   [65]
RP   X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 672-920 IN COMPLEXES WITH
RP   N-TERMINAL MODULATING DOMAIN AND NCOA2, INTERACTION WITH NCOA1, AND
RP   CHARACTERIZATION OF VARIANT PROSTATE CANCER MET-731.
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 function
RT   dominance.";
RL   Mol. Cell 16:425-438(2004).
RN   [66]
RP   X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 670-920 IN COMPLEXES WITH
RP   DIHYDROTESTOSTERONE AND NCOA1; NCOA2; NCOA3 AND NCOA4, FUNCTION,
RP   INTERACTION WITH NCOA1; NCOA2; NCOA3 AND NCOA4, AND MUTAGENESIS OF LYS-721
RP   AND GLU-898.
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., Guy R.K.;
RT   "The molecular mechanisms of coactivator utilization in ligand-dependent
RT   transactivation by the androgen receptor.";
RL   J. Biol. Chem. 280:8060-8068(2005).
RN   [67]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 665-920 IN COMPLEXES WITH
RP   NONSTEROIDAL LIGANDS, MUTAGENESIS OF TRP-742, CHARACTERIZATION OF VARIANT
RP   PROSTATE CANCER ALA-878, AND CHARACTERIZATION OF VARIANT AIS THR-896.
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 androgen
RT   receptor.";
RL   J. Biol. Chem. 280:37747-37754(2005).
RN   [68]
RP   X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 655-920 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., Labrie F.,
RA   Breton R.;
RT   "Comparison of crystal structures of human androgen receptor ligand-binding
RT   domain complexed with various agonists reveals molecular determinants
RT   responsible for binding affinity.";
RL   Protein Sci. 15:987-999(2006).
RN   [69]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 672-919 IN COMPLEX WITH 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 corepressor
RT   SHP.";
RL   Acta Crystallogr. D 63:1198-1200(2007).
RN   [70]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 671-919 OF MUTANT ALA-878 IN
RP   COMPLEX WITH THE ANTIANDROGEN CYPROTERONE ACETATE, CHARACTERIZATION OF
RP   VARIANT PROSTATE CANCER ALA-878, AND MUTAGENESIS OF LEU-702.
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-induced
RT   conformational changes and structure-based drug design.";
RL   J. Biol. Chem. 282:13648-13655(2007).
RN   [71]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 663-919 OF WILD-TYPE AND MUTANT
RP   TYR-875 IN COMPLEX WITH TESTOSTERONE AND NCOA2, ACTIVATION BY THE
RP   N-TERMINAL MODULATING DOMAIN, INTERACTION WITH NCOA2 AND MAGEA11, FUNCTION,
RP   MUTAGENESIS OF LYS-721 AND GLU-898, AND CHARACTERIZATION OF VARIANT
RP   PROSTATE CANCER TYR-875.
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 and
RT   dihydrotestosterone.";
RL   J. Biol. Chem. 282:25801-25816(2007).
RN   [72]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 655-920 IN COMPLEX WITH 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., Breton R.;
RT   "Structural characterization of the human androgen receptor ligand-binding
RT   domain complexed with EM5744, a rationally designed steroidal ligand
RT   bearing a bulky chain directed toward helix 12.";
RL   J. Biol. Chem. 282:30910-30919(2007).
RN   [73]
RP   X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 670-920 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   [74] {ECO:0000244|PDB:4OEA, ECO:0000244|PDB:4OED, ECO:0000244|PDB:4OEY, ECO:0000244|PDB:4OEZ, ECO:0000244|PDB:4OFR, ECO:0000244|PDB:4OFU, ECO:0000244|PDB:4OGH, ECO:0000244|PDB:4OH5, ECO:0000244|PDB:4OHA, ECO:0000244|PDB:4OIL}
RP   X-RAY CRYSTALLOGRAPHY (1.42 ANGSTROMS) OF 671-920 OF WILD-TYPE AND VARIANT
RP   PROSTATE CANCER ALA-878 IN COMPLEX WITH DIHYDROTESTOSTERONE AND BUD31
RP   PEPTIDES, INTERACTION WITH BUD31, FUNCTION, SUBCELLULAR LOCATION, AND
RP   DOMAIN.
RX   PubMed=25091737; DOI=10.1016/j.molonc.2014.06.009;
RA   Hsu C.L., Liu J.S., Wu P.L., Guan H.H., Chen Y.L., Lin A.C., Ting H.J.,
RA   Pang S.T., Yeh S.D., Ma W.L., Chen C.J., Wu W.G., Chang C.;
RT   "Identification of a new androgen receptor (AR) co-regulator BUD31 and
RT   related peptides to suppress wild-type and mutated AR-mediated prostate
RT   cancer growth via peptide screening and X-ray structure analysis.";
RL   Mol. Oncol. 8:1575-1587(2014).
RN   [75]
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., Vasiliou M.,
RA   Gottlieb B.;
RT   "Androgen resistance due to mutation of the androgen receptor.";
RL   Clin. Invest. Med. 15:456-472(1992).
RN   [76]
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., Murono K.,
RA   Zhou Z.;
RT   "Molecular genetics of human androgen insensitivity.";
RL   Eur. J. Pediatr. 152 Suppl. 2:S62-S69(1993).
RN   [77]
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., Lobaccaro J.-M.;
RT   "Mutations of androgen receptor gene in androgen insensitivity syndromes.";
RL   J. Steroid Biochem. Mol. Biol. 46:519-530(1993).
RN   [78]
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   [79]
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   [80]
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   [81]
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   [82]
RP   VARIANT LNCAP ALA-878.
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., Brinkmann A.O.,
RA   Mulder E.;
RT   "A mutation in the ligand binding domain of the androgen receptor of human
RT   LNCaP cells affects steroid binding characteristics and response to anti-
RT   androgens.";
RL   Biochem. Biophys. Res. Commun. 173:534-540(1990).
RN   [83]
RP   VARIANTS AIS CYS-775; GLN-832 AND MET-867.
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   [84]
RP   VARIANT CYS-775.
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 receptor at
RT   amino acid 772 (Arg-->Cys) results from a combination of decreased
RT   messenger ribonucleic acid levels and impairment of receptor function.";
RL   J. Clin. Endocrinol. Metab. 73:318-325(1991).
RN   [85]
RP   VARIANT AIS PRO-618.
RX   PubMed=1999491; DOI=10.1172/jci115076;
RA   Marcelli M., Zoppi S., Grino P.B., Griffin J.E., Wilson J.D., McPhaul M.J.;
RT   "A mutation in the DNA-binding domain of the androgen receptor gene causes
RT   complete testicular feminization in a patient with receptor-positive
RT   androgen resistance.";
RL   J. Clin. Invest. 87:1123-1126(1991).
RN   [86]
RP   VARIANT PAIS CYS-764.
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 androgen
RT   therapy.";
RL   J. Clin. Invest. 87:1413-1421(1991).
RN   [87]
RP   POLY-GLN REGION EXPANSION, AND INVOLVEMENT IN SPINAL AND BULBAR MUSCULAR
RP   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 muscular
RT   atrophy.";
RL   Nature 352:77-79(1991).
RN   [88]
RP   VARIANTS AIS CYS-775 AND HIS-775.
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 androgen
RT   receptor causes complete androgen insensitivity with different receptor
RT   phenotypes.";
RL   Am. J. Hum. Genet. 51:143-155(1992).
RN   [89]
RP   VARIANTS PAIS LYS-609 AND LEU-867.
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 with
RT   partial androgen insensitivity syndrome.";
RL   Clin. Endocrinol. (Oxf.) 37:214-220(1992).
RN   [90]
RP   VARIANT AIS THR-766.
RX   PubMed=1426313; DOI=10.1016/s0015-0282(16)55315-1;
RA   Sweet C.R., Behzadian M.A., McDonough P.G.;
RT   "A unique point mutation in the androgen receptor gene in a family with
RT   complete androgen insensitivity syndrome.";
RL   Fertil. Steril. 58:703-707(1992).
RN   [91]
RP   VARIANT AIS VAL-750.
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 gene
RT   in a family with complete androgen insensitivity syndrome (CAIS).";
RL   Hum. Genet. 90:311-312(1992).
RN   [92]
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 subjects
RT   with androgen insensitivity syndrome.";
RL   Hum. Mol. Genet. 1:497-503(1992).
RN   [93]
RP   VARIANT AIS VAL-788.
RX   PubMed=1569163; DOI=10.1210/jcem.74.5.1569163;
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-binding
RT   domain of human androgen receptor leads to complete androgen insensitivity
RT   syndrome.";
RL   J. Clin. Endocrinol. Metab. 74:1152-1157(1992).
RN   [94]
RP   VARIANTS AIS ARG-742 AND CYS-835.
RX   PubMed=1464650; DOI=10.1210/jcem.75.6.1464650;
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   [95]
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   [96]
RP   VARIANT PROSTATE CANCER ALA-878.
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 ligand
RT   binding domain which affects steroid binding characteristics and response
RT   to antiandrogens.";
RL   J. Steroid Biochem. Mol. Biol. 41:665-669(1992).
RN   [97]
RP   VARIANTS AIS TYR-560 AND ARG-577, AND VARIANTS PAIS GLY-598 AND PRO-618.
RX   PubMed=1316540; DOI=10.1210/mend.6.3.1316540;
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 androgen
RT   receptor are a frequent cause of receptor-binding positive androgen
RT   resistance.";
RL   Mol. Endocrinol. 6:409-415(1992).
RN   [98]
RP   VARIANTS AIS SER-706; VAL-750; PHE-760; HIS-775; CYS-856 AND GLY-865.
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 complete
RT   androgen insensitivity: rapid detection by a modified denaturing gradient
RT   gel electrophoresis technique.";
RL   Mol. Endocrinol. 6:1909-1920(1992).
RN   [99]
RP   VARIANT PAIS/BREAST CANCER GLN-608.
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 with
RT   breast cancer and Reifenstein syndrome.";
RL   Nat. Genet. 2:132-134(1992).
RN   [100]
RP   VARIANT MET-731.
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   [101]
RP   VARIANTS ARG-207 AND ASP-794.
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   [102]
RP   VARIANT AIS PHE-582.
RX   PubMed=8224266; DOI=10.1016/s0015-0282(16)56281-5;
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 insensitivity
RT   syndrome.";
RL   Fertil. Steril. 60:814-819(1993).
RN   [103]
RP   VARIANT AIS VAL-755.
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 receptor
RT   gene of a family with complete androgen insensitivity syndrome.";
RL   Hum. Mol. Genet. 2:1041-1043(1993).
RN   [104]
RP   VARIANT PAIS/BREAST CANCER LYS-609.
RX   PubMed=8281139; DOI=10.1093/hmg/2.11.1799;
RA   Lobaccaro J.-M., Lumbroso S., Belon C., Galtier-Dereure F., Bringer J.,
RA   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   [105]
RP   VARIANT AIS ARG-808.
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 causing
RT   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   [106]
RP   VARIANT PAIS VAL-744.
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-binding
RT   domain of the human androgen receptor leads to Reifenstein syndrome.";
RL   J. Clin. Endocrinol. Metab. 77:103-107(1993).
RN   [107]
RP   VARIANTS AIS LYS-682 AND THR-843, AND VARIANTS PAIS HIS-841 AND LEU-867.
RX   PubMed=8325950; DOI=10.1210/jcem.77.1.8325950;
RA   Hiort O., Huang Q., Sinnecker G.H., Sadeghi-Nejad A., Kruse K., Wolfe H.J.,
RA   Yandell D.W.;
RT   "Single strand conformation polymorphism analysis of androgen receptor gene
RT   mutations in patients with androgen insensitivity syndromes: application
RT   for diagnosis, genetic counseling, and therapy.";
RL   J. Clin. Endocrinol. Metab. 77:262-266(1993).
RN   [108]
RP   INVOLVEMENT IN PAIS, INVOLVEMENT IN HYSP1, AND VARIANTS PAIS HIS-856 AND
RP   MET-870.
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   [109]
RP   VARIANT AIS VAL-744.
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   [110]
RP   VARIANTS PROSTATE CANCER HIS-702 AND ALA-878.
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   [111]
RP   VARIANT AIS MET-867, AND VARIANT PAIS LEU-867.
RX   PubMed=8446106; DOI=10.1210/mend.7.1.8446106;
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 androgen
RT   receptor causes complete or partial androgen insensitivity, respectively
RT   with distinct androgen receptor phenotypes.";
RL   Mol. Endocrinol. 7:37-46(1993).
RN   [112]
RP   VARIANT PROSTATE CANCER MET-716.
RX   PubMed=8145761; DOI=10.1210/mend.7.12.8145761;
RA   Culig Z., Hobisch A., Cronauer M.V., Cato A.C.B., Hittmair A., Radmayr C.,
RA   Eberle J., Bartsch G., Klocker H.;
RT   "Mutant androgen receptor detected in an advanced-stage prostatic carcinoma
RT   is activated by adrenal androgens and progesterone.";
RL   Mol. Endocrinol. 7:1541-1550(1993).
RN   [113]
RP   VARIANTS AIS PHE-582; VAL-744; VAL-755; GLU-768 AND CYS-856.
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   [114]
RP   VARIANTS PROSTATE CANCER LEU-342 AND GLU-799.
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   [115]
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   [116]
RP   VARIANT PROSTATE CANCER ALA-878.
RX   PubMed=8187068;
RA   Gaddipati J.P., McLeod D.G., Heidenberg H.B., Sesterhenn I.A., Finger M.J.,
RA   Moul J.W., Srivastava S.;
RT   "Frequent detection of codon 877 mutation in the androgen receptor gene in
RT   advanced prostate cancers.";
RL   Cancer Res. 54:2861-2864(1994).
RN   [117]
RP   VARIANT PAIS TRP-569.
RX   PubMed=7910529;
RA   Lobaccaro J.-M., Belon C., Lumbroso S., Olewniczack G., Carre-Pigeon F.,
RA   Job J.C., Chaussain J.L., Toublanc J.E., Sultan C.;
RT   "Molecular prenatal diagnosis of partial androgen insensitivity syndrome
RT   based on the Hind III polymorphism of the androgen receptor gene.";
RL   Clin. Endocrinol. (Oxf.) 40:297-302(1994).
RN   [118]
RP   VARIANT PAIS HIS-841.
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 insensitivity
RT   (Reifenstein syndrome).";
RL   Eur. J. Endocrinol. 130:327-332(1994).
RN   [119]
RP   VARIANT PAIS HIS-841.
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 insensitivity
RT   syndrome associated with a thermolabile androgen receptor.";
RL   Eur. J. Endocrinol. 130:569-574(1994).
RN   [120]
RP   VARIANT PAIS VAL-871.
RX   PubMed=8033918; DOI=10.1007/bf01956409;
RA   Hiort O., Klauber G., Cendron M., Sinnecker G.H., Keim L., Schwinger E.,
RA   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   [121]
RP   VARIANT PAIS ASP-691 DEL.
RA   Schwartz M., Skovby F., Mueller J., Nielsen O., Skakkebaek N.E.;
RT   "Partial androgen insensitivity (PAIS) in a large eskimo kindred caused by
RT   a delD690 mutation in the androgen receptor (AR) gene (Abstract #244).";
RL   Horm. Res. 41:117-117(1994).
RN   [122]
RP   VARIANTS AIS PHE-583 DEL; ARG-616 DEL AND HIS-616.
RX   PubMed=8162033; DOI=10.1093/hmg/3.1.21;
RA   Beitel L.K., Prior L., Vasiliou D.M., Gottlieb B., Kaufman M., Lumbroso R.,
RA   Alvarado C., McGillivray B., Trifiro M.A., Pinsky L.;
RT   "Complete androgen insensitivity due to mutations in the probable alpha-
RT   helical segments of the DNA-binding domain in the human androgen
RT   receptor.";
RL   Hum. Mol. Genet. 3:21-27(1994).
RN   [123]
RP   VARIANTS PAIS SER-583; TYR-605; ALA-709; LEU-755 AND HIS-772, AND VARIANT
RP   AIS TRP-780.
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   [124]
RP   VARIANT AIS PHE-602.
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 in
RT   the steroid binding domain and a Cys-->Phe substitution in the second zinc
RT   finger of the androgen receptor.";
RL   Hum. Mol. Genet. 3:1169-1170(1994).
RN   [125]
RP   VARIANTS PAIS ARG-617; HIS-841 AND MET-890.
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 androgen
RT   insensitivity syndrome.";
RL   J. Clin. Endocrinol. Metab. 78:513-522(1994).
RN   [126]
RP   VARIANT AIS PHE-791.
RX   PubMed=7962294; DOI=10.1210/jcem.79.4.7962294;
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   [127]
RP   VARIANTS AIS CYS-841 AND HIS-841.
RX   PubMed=8040309; DOI=10.1172/jci117368;
RA   Beitel L.K., Kazemi-Esfarjani P., Kaufman M., Lumbroso R., DiGeorge A.M.,
RA   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   [128]
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 complex.";
RL   J. Clin. Invest. 94:1642-1650(1994).
RN   [129]
RP   VARIANT AIS LYS-728.
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 due to
RT   mutation in androgen receptor gene.";
RL   Lancet 344:826-827(1994).
RN   [130]
RP   VARIANTS AIS HIS-616 AND LEU-765, AND VARIANTS PAIS VAL-743 AND THR-746.
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 mutations
RT   and pedigree analysis in families with X-linked androgen insensitivity.";
RL   Pediatr. Res. 36:227-234(1994).
RN   [131]
RP   VARIANT AIS HIS-841.
RX   PubMed=8830623; DOI=10.1177/000456329503200508;
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 with
RT   receptor-negative complete testicular feminization: comparison with a
RT   single base substitution in a receptor-reduced incomplete form.";
RL   Ann. Clin. Biochem. 32:482-486(1995).
RN   [132]
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   [133]
RP   VARIANT AIS VAL-882.
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 polymorphism
RT   and direct detection of two novel mutations in the androgen receptor
RT   gene.";
RL   Clin. Endocrinol. (Oxf.) 43:69-77(1995).
RN   [134]
RP   VARIANTS AIS SER-706 AND HIS-764, AND VARIANTS PAIS LEU-726; THR-738;
RP   HIS-775 AND GLU-799.
RX   PubMed=7671849; DOI=10.1210/edrv-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   [135]
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   [136]
RP   VARIANTS AIS LEU-832 AND GLN-832.
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 830
RT   of the androgen receptor that cause complete androgen insensitivity in
RT   three families.";
RL   Hum. Mol. Genet. 4:515-521(1995).
RN   [137]
RP   VARIANT AIS PRO-678.
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 androgen
RT   insensitivity syndrome in a large Hutterite kindred.";
RL   Hum. Mutat. 5:28-33(1995).
RN   [138]
RP   VARIANT PAIS CYS-764, AND VARIANTS AIS TRP-780; VAL-808 AND CYS-856.
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 acid
RT   substitutions in the androgen receptor steroid-binding domain.";
RL   Hum. Mutat. 6:152-162(1995).
RN   [139]
RP   VARIANT PROSTATE CANCER MET-731.
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 amino-
RT   acid-sequence requirements for transactivation and ligand binding.";
RL   Int. J. Cancer 63:544-550(1995).
RN   [140]
RP   VARIANT VAL-569.
RX   PubMed=7673412; DOI=10.1210/jcem.80.9.7673412;
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   [141]
RP   VARIANT PROSTATE CANCER LEU-727.
RX   PubMed=8530589; DOI=10.1210/jcem.80.12.8530589;
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   [142]
RP   VARIANT PAIS THR-597.
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   [143]
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-independent
RT   prostate cancer.";
RL   N. Engl. J. Med. 332:1393-1398(1995).
RN   [144]
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 syndromes.";
RL   Am. J. Med. Genet. 63:218-222(1996).
RN   [145]
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 progression of
RT   human prostate cancer to androgen independence.";
RL   Clin. Cancer Res. 2:277-285(1996).
RN   [146]
RP   VARIANTS PAIS GLN-608; THR-611; LEU-755; HIS-841; THR-843 AND HIS-856, AND
RP   VARIANT AIS MET-867.
RX   PubMed=9039340; DOI=10.1046/j.1365-2265.1996.8600869.x;
RA   Weidemann W., Linck B., Haupt H., Mentrup B., Romalo G., Stockklauser K.,
RA   Brinkmann A.O., Schweikert H.-U., Spindler K.D.;
RT   "Clinical and biochemical investigations and molecular analysis of subjects
RT   with mutations in the androgen receptor gene.";
RL   Clin. Endocrinol. (Oxf.) 45:733-739(1996).
RN   [147]
RP   VARIANT AIS CYS-856.
RX   PubMed=9001799;
RA   Malmgren H., Gustavsson J., Tuvemo T., Dahl N.;
RT   "Rapid detection of a mutation hot-spot in the human androgen receptor.";
RL   Clin. Genet. 50:202-205(1996).
RN   [148]
RP   VARIANTS PAIS ILE-743; ILE-781; GLU-799; CYS-841; HIS-856 AND MET-870.
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   [149]
RP   VARIANT PAIS ARG-910.
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 mutation at
RT   amino acid 907 (Gly-->Arg) that results in decreased ligand binding
RT   affinity and reduced androgen receptor messenger ribonucleic acid levels.";
RL   J. Clin. Endocrinol. Metab. 81:236-243(1996).
RN   [150]
RP   VARIANT AIS ARG-708.
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 gene
RT   causes complete androgen resistance.";
RL   J. Clin. Endocrinol. Metab. 81:1984-1988(1996).
RN   [151]
RP   VARIANT AIS ILE-781.
RX   PubMed=8768864; DOI=10.1210/jcem.81.8.8768864;
RA   Rodien P., Mebarki F., Mowszowicz I., Chaussain J.L., Young J., Morel Y.,
RA   Schaison G.;
RT   "Different phenotypes in a family with androgen insensitivity caused by the
RT   same M780I point mutation in the androgen receptor gene.";
RL   J. Clin. Endocrinol. Metab. 81:2994-2998(1996).
RN   [152]
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   [153]
RP   VARIANT AIS ASP-574.
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   [154]
RP   VARIANT AIS SER-549.
RX   PubMed=8683794; DOI=10.1097/00005392-199608001-00077;
RA   Sutherland R.W., Wiener J.S., Hicks J.P., Marcelli M., Gonzales E.T. Jr.,
RA   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   [155]
RP   VARIANT AIS PRO-617.
RX   PubMed=8647313; DOI=10.1016/0303-7207(95)03709-8;
RA   Lobaccaro J.-M., Poujol N., Chiche L., Lumbroso S., Brown T.R., Sultan C.;
RT   "Molecular modeling and in vitro investigations of the human androgen
RT   receptor DNA-binding domain: application for the study of two mutations.";
RL   Mol. Cell. Endocrinol. 116:137-147(1996).
RN   [156]
RP   VARIANT AIS PHE-580, AND VARIANT PAIS TYR-583.
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-binding
RT   domain of the androgen receptor.";
RL   Mol. Cell. Endocrinol. 120:15-24(1996).
RN   [157]
RP   VARIANT PROSTATE CANCER GLU-799.
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   [158]
RP   VARIANT PROSTATE CANCER ALA-878.
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   [159]
RP   VARIANT AIS HIS-856.
RX   PubMed=9106550;
RA   Boehmer A.L.M., Brinkmann A.O., Niermeijer M.F., Bakker L., Halley D.J.J.,
RA   Drop S.L.S.;
RT   "Germ-line and somatic mosaicism in the androgen insensitivity syndrome:
RT   implications for genetic counseling.";
RL   Am. J. Hum. Genet. 60:1003-1006(1997).
RN   [160]
RP   VARIANT PROSTATE CANCER ALA-684.
RX   PubMed=9000575;
RA   Koivisto P., Kononen J., Palmberg C., Tammela T., Hyytinen E., Isola J.,
RA   Trapman J., Cleutjens K., Noordzij A., Visakorpi T., Kallioniemi O.-P.;
RT   "Androgen receptor gene amplification: a possible molecular mechanism for
RT   androgen deprivation therapy failure in prostate cancer.";
RL   Cancer Res. 57:314-319(1997).
RN   [161]
RP   VARIANTS PAIS LYS-609 AND GLY-773.
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., Edwards C.R.,
RA   Hargreaves T.B., Wu F.C.;
RT   "Correlation of clinical, endocrine and molecular abnormalities with in
RT   vivo responses to high-dose testosterone in patients with partial androgen
RT   insensitivity syndrome.";
RL   Clin. Endocrinol. (Oxf.) 46:497-506(1997).
RN   [162]
RP   VARIANT AIS MET-890.
RX   PubMed=9160185;
RA   Essawi M., Gad Y.Z., el-Rouby O., Temtamy S.A., Sabour Y.A., el-Awady M.K.;
RT   "Molecular analysis of androgen resistance syndromes in Egyptian
RT   patients.";
RL   Dis. Markers 13:99-105(1997).
RN   [163]
RP   VARIANT AIS TRP-780.
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 sensitivity
RT   in patients with mutations of the androgen receptor gene.";
RL   Eur. J. Pediatr. 156:7-14(1997).
RN   [164]
RP   VARIANTS AIS VAL-750; CYS-775; ILE-781 AND SER-795.
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 androgen
RT   insensitivity.";
RL   Hum. Mutat. 9:57-61(1997).
RN   [165]
RP   VARIANTS PROSTATE CANCER IN POLY-GLN REGION; HIS-702 AND ARG-911.
RX   PubMed=9438000; DOI=10.1093/jjco/27.6.389;
RA   Watanabe M., Ushijima T., Shiraishi T., Yatani R., Shimazaki J., Kotake T.,
RA   Sugimura T., Nagao M.;
RT   "Genetic alterations of androgen receptor gene in Japanese human prostate
RT   cancer.";
RL   Jpn. J. Clin. Oncol. 27:389-393(1997).
RN   [166]
RP   VARIANT PROSTATE CANCER GLN-630.
RX   PubMed=9184448; DOI=10.5980/jpnjurol1989.88.550;
RA   Wang C., Uchida T.;
RT   "Androgen receptor gene mutations in prostate cancer.";
RL   Nihon Hinyokika Gakkai Zasshi 88:550-556(1997).
RN   [167]
RP   VARIANTS AIS ARG-196 AND CYS-856.
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   [168]
RP   VARIANTS PAIS ALA-709 AND GLY-871.
RX   PubMed=9329414; DOI=10.1016/s0022-3476(97)80063-7;
RA   Albers N., Ulrichs C., Gluer S., Hiort O., Sinnecker G.H., Mildenberger H.,
RA   Brodehl J.;
RT   "Etiologic classification of severe hypospadias: implications for prognosis
RT   and management.";
RL   J. Pediatr. 131:386-392(1997).
RN   [169]
RP   VARIANTS AIS ASN-733 AND THR-766.
RX   PubMed=9252933;
RA   Ko T.M., Yang Y.S., Wu M.Y., Kao C.H., Hsu P.M., Chuang S.M., Lee T.Y.;
RT   "Complete androgen insensitivity syndrome. Molecular characterization in
RT   two Chinese women.";
RL   J. Reprod. Med. 42:424-428(1997).
RN   [170]
RP   VARIANTS AIS ASP-751; PHE-763; THR-766; ASN-865 AND PHE-908.
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   [171]
RP   VARIANT PAIS GLY-704, AND VARIANT AIS LEU-917.
RX   PubMed=9302173; DOI=10.1016/s0022-5347(01)64279-4;
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 in 2
RT   patients with androgen insensitivity syndrome.";
RL   J. Urol. 158:1553-1556(1997).
RN   [172]
RP   VARIANTS AIS CYS-572; GLN-753 AND CYS-775.
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   [173]
RP   VARIANTS AIS HIS-616 AND GLN-753.
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   [174]
RP   VARIANT ARG-216, AND CHARACTERIZATION OF VARIANT ARG-216.
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   [175]
RP   VARIANTS AIS PRO-257 AND ALA-821.
RX   PubMed=9610419; DOI=10.3109/09513599809024954;
RA   Tanaka H., Komori S., Sakata K., Shima H., Koyama K.;
RT   "One additional mutation at exon A amplifies thermolability of androgen
RT   receptor in a case with complete androgen insensitivity syndrome.";
RL   Gynecol. Endocrinol. 12:75-82(1998).
RN   [176]
RP   VARIANTS AIS THR-766; TYR-785 AND THR-896, AND VARIANT PAIS GLY-841.
RX   PubMed=9856504; DOI=10.1007/s004390050864;
RA   Lundberg Giwercman Y., Nikoshkov A., Lindsten K., Bystroem B., Pousette A.,
RA   Chibalin A.V., Arvidsson S., Tiulpakov A., Semitcheva T.V., Peterkova V.,
RA   Hagenfeldt K., Ritzen E.M., Wedell A.;
RT   "Functional characterisation of mutations in the ligand-binding domain of
RT   the androgen receptor gene in patients with androgen insensitivity
RT   syndrome.";
RL   Hum. Genet. 103:529-531(1998).
RN   [177]
RP   VARIANT AIS VAL-696.
RX   PubMed=9554754;
RA   Doerk T., Schnieders F., Jakubiczka S., Wieacker P., Schroeder-Kurth T.,
RA   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   [178]
RP   VARIANT ASP-646.
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   [179]
RP   VARIANT AIS LEU-893.
RA   Knoke I., Jakubiczka S., Rohrer T., Hanimann B., Werder E.A., Wieacker P.;
RT   "Single amino acid substitution in the hormone-binding domain of the
RT   androgen receptor in a family with complete androgen insensitivity syndrome
RT   (CAIS).";
RL   Hum. Mutat. 12:220-220(1998).
RN   [180]
RP   VARIANT PAIS GLN-608.
RX   PubMed=9543136; DOI=10.1210/jcem.83.4.4704;
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 domain of
RT   the androgen receptor.";
RL   J. Clin. Endocrinol. Metab. 83:1173-1176(1998).
RN   [181]
RP   VARIANTS PAIS VAL-744 AND CYS-841.
RX   PubMed=9768671; DOI=10.1210/jcem.83.10.5201;
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 syndrome.";
RL   J. Clin. Endocrinol. Metab. 83:3597-3603(1998).
RN   [182]
RP   VARIANT AIS GLU-799.
RX   PubMed=9851768; DOI=10.1210/jcem.83.12.5358;
RA   Wang Q., Ghadessy F.J., Trounson A., de Kretser D., McLachlan R., Ng S.C.,
RA   Yong E.L.;
RT   "Azoospermia associated with a mutation in the ligand-binding domain of an
RT   androgen receptor displaying normal ligand binding, but defective trans-
RT   activation.";
RL   J. Clin. Endocrinol. Metab. 83:4303-4309(1998).
RN   [183]
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 of
RT   single-case families.";
RL   J. Pediatr. 132:939-943(1998).
RN   [184]
RP   VARIANT PAIS THR-759.
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 three
RT   dimensional structure of the androgen receptor ligand-binding domain.";
RL   Mol. Cell. Endocrinol. 137:41-50(1998).
RN   [185]
RP   VARIANT PAIS LEU-912.
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   [186]
RP   VARIANTS PROSTATE CANCER ALA-878 AND ASN-891.
RX   PubMed=10363963;
RA   Taplin M.-E., Bubley G.J., Ko Y.J., Small E.J., Upton M., Rajeshkumar B.,
RA   Balk S.P.;
RT   "Selection for androgen receptor mutations in prostate cancers treated with
RT   androgen antagonist.";
RL   Cancer Res. 59:2511-2515(1999).
RN   [187]
RP   VARIANT PAIS SER-841.
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 Brazilian
RT   family with partial androgen insensitivity syndrome.";
RL   Hum. Mutat. 14:353-353(1999).
RN   [188]
RP   VARIANTS AIS ARG-392 AND ARG-445.
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   [189]
RP   VARIANT PAIS GLN-608, AND VARIANT AIS LYS-682.
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   [190]
RP   VARIANT AIS LEU-893.
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 and
RT   analysis of androgen receptor gene mutation.";
RL   Int. J. Urol. 6:327-330(1999).
RN   [191]
RP   VARIANT PAIS ALA-773, AND VARIANT AIS GLY-872.
RX   PubMed=10022458; DOI=10.1210/jcem.84.2.5453;
RA   Shkolny D.L., Beitel L.K., Ginsberg J., Pekeles G., Arbour L., Pinsky L.,
RA   Trifiro M.A.;
RT   "Discordant measures of androgen-binding kinetics in two mutant androgen
RT   receptors causing mild or partial androgen insensitivity, respectively.";
RL   J. Clin. Endocrinol. Metab. 84:805-810(1999).
RN   [192]
RP   VARIANTS PROSTATE CANCER IN POLY-GLN REGION AND ALA-684.
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 cancer.";
RL   J. Pathol. 189:559-563(1999).
RN   [193]
RP   VARIANTS PROSTATE CANCER HIS-702 AND ALA-878.
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., 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   [194]
RP   VARIANT PAIS THR-808.
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 androgen
RT   receptor gene mutation.";
RL   Lancet 354:1444-1445(1999).
RN   [195]
RP   VARIANT AIS LEU-893.
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 C-
RT   terminal alpha-helix of the ligand binding domain containing the AF-2
RT   transcriptional activating function core is associated with complete
RT   androgen insensitivity.";
RL   Mol. Cell. Endocrinol. 148:47-53(1999).
RN   [196]
RP   VARIANT PROSTATE CANCER TYR-620.
RX   PubMed=10598582; DOI=10.1210/mend.13.12.0382;
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., Weigel N.L.;
RT   "A C619Y mutation in the human androgen receptor causes inactivation and
RT   mislocalization of the receptor with concomitant sequestration of SRC-1.";
RL   Mol. Endocrinol. 13:2065-2075(1999).
RN   [197]
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., Weigel N.L.;
RL   Mol. Endocrinol. 14:544-544(2000).
RN   [198]
RP   VARIANT AIS THR-597.
RX   PubMed=10590024; DOI=10.1203/00006450-199912000-00008;
RA   Holterhus P.M., Wiebel J., Sinnecker G.H., Bruggenwirth H.T., Sippell W.G.,
RA   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   [199]
RP   VARIANTS AIS PHE-813 AND GLN-832.
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 receptor
RT   gene of five Japanese patients with androgen insensitivity syndrome.";
RL   Tohoku J. Exp. Med. 187:263-272(1999).
RN   [200]
RP   VARIANTS THR-598 AND LEU-726.
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   [201]
RP   VARIANTS PROSTATE CANCER ALA-576; ARG-581; VAL-587; TYR-620; ALA-758 AND
RP   GLY-847.
RX   PubMed=10706109;
RA   Marcelli M., Ittmann M., Mariani S., Sutherland R.W., Nigam R., Murthy L.,
RA   Zhao Y., DiConcini D., Puxeddu E., Esen A., Eastham J., Weigel N.L.,
RA   Lamb D.J.;
RT   "Androgen receptor mutations in prostate cancer.";
RL   Cancer Res. 60:944-949(2000).
RN   [202]
RP   VARIANTS AIS AND PAIS.
RX   PubMed=10690872; DOI=10.1210/jcem.85.2.6337;
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 analysis in
RT   278 clinical cases reported as androgen insensitivity syndrome.";
RL   J. Clin. Endocrinol. Metab. 85:658-665(2000).
RN   [203]
RP   VARIANTS PAIS THR-683 AND GLU-712, AND VARIANTS AIS GLU-744; VAL-828;
RP   ARG-875 AND TYR-880.
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   [204]
RP   INVOLVEMENT IN ANDROGENETIC ALOPECIA, AND POLYMORPHISM OF POLY-GLY REGION.
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 pattern
RT   baldness.";
RL   J. Invest. Dermatol. 116:452-455(2001).
RN   [205]
RP   VARIANT AIS TYR-706.
RX   PubMed=11744994;
RA   Sills E.S., Sholes T.E., Perloe M., Kaplan C.R., Davis J.G., Tucker M.J.;
RT   "Characterization of a novel receptor mutation A->T at exon 4 in complete
RT   androgen insensitivity syndrome and a carrier sibling via bidirectional
RT   polymorphism sequence analysis.";
RL   Int. J. Mol. Med. 9:45-48(2002).
RN   [206]
RP   INVOLVEMENT IN ANDROGENETIC ALOPECIA, AND POLYMORPHISM OF POLY-GLY REGION.
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., Metzen C.,
RA   Heyn U., Schweiger N., Betz R.C., Blaumeiser B., Hampe J., Schreiber S.,
RA   Schulze T.G., Hennies H.C., Schumacher J., Propping P., Ruzicka T.,
RA   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   [207]
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   [208]
RP   VARIANT AIS PHE-577.
RX   PubMed=14756668; DOI=10.1111/j.0009-9163.2004.00197.x;
RA   Hooper H.T., Figueiredo B.C., Pavan-Senn C.C., De Lacerda L., Sandrini R.,
RA   Mengarelli J.K., Japp K., Karaviti L.P.;
RT   "Concordance of phenotypic expression and gender identity in a large
RT   kindred with a mutation in the androgen receptor.";
RL   Clin. Genet. 65:183-190(2004).
RN   [209]
RP   CHARACTERIZATION OF VARIANTS AIS ASN-696; CYS-764; HIS-775; GLU-799;
RP   HIS-856 AND PHE-908.
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 to
RT   disrupted interaction between the N- and C-terminal domains.";
RL   J. Mol. Endocrinol. 36:361-368(2006).
RN   [210]
RP   VARIANT ARG-216.
RX   PubMed=27535533; DOI=10.1038/nature19057;
RG   Exome Aggregation Consortium;
RA   Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E., Fennell T.,
RA   O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B., Tukiainen T.,
RA   Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K., Zhao F., Zou J.,
RA   Pierce-Hoffman E., Berghout J., Cooper D.N., Deflaux N., DePristo M.,
RA   Do R., Flannick J., Fromer M., Gauthier L., Goldstein J., Gupta N.,
RA   Howrigan D., Kiezun A., Kurki M.I., Moonshine A.L., Natarajan P.,
RA   Orozco L., Peloso G.M., Poplin R., Rivas M.A., Ruano-Rubio V., Rose S.A.,
RA   Ruderfer D.M., Shakir K., Stenson P.D., Stevens C., Thomas B.P., Tiao G.,
RA   Tusie-Luna M.T., Weisburd B., Won H.H., Yu D., Altshuler D.M.,
RA   Ardissino D., Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
RA   Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S., Laakso M.,
RA   McCarroll S., McCarthy M.I., McGovern D., McPherson R., Neale B.M.,
RA   Palotie A., Purcell S.M., Saleheen D., Scharf J.M., Sklar P.,
RA   Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C., Wilson J.G.,
RA   Daly M.J., MacArthur D.G.;
RT   "Analysis of protein-coding genetic variation in 60,706 humans.";
RL   Nature 536:285-291(2016).
CC   -!- FUNCTION: Steroid hormone receptors are ligand-activated transcription
CC       factors that regulate eukaryotic gene expression and affect cellular
CC       proliferation and differentiation in target tissues. Transcription
CC       factor activity is modulated by bound coactivator and corepressor
CC       proteins like ZBTB7A that recruits NCOR1 and NCOR2 to the androgen
CC       response elements/ARE on target genes, negatively regulating androgen
CC       receptor signaling and androgen-induced cell proliferation
CC       (PubMed:20812024). Transcription activation is also down-regulated by
CC       NR0B2. Activated, but not phosphorylated, by HIPK3 and ZIPK/DAPK3.
CC       {ECO:0000269|PubMed:14664718, ECO:0000269|PubMed:15563469,
CC       ECO:0000269|PubMed:17591767, ECO:0000269|PubMed:17911242,
CC       ECO:0000269|PubMed:18084323, ECO:0000269|PubMed:19345326,
CC       ECO:0000269|PubMed:20812024, ECO:0000269|PubMed:20980437,
CC       ECO:0000269|PubMed:25091737}.
CC   -!- FUNCTION: Isoform 3 and isoform 4 lack the C-terminal ligand-binding
CC       domain and may therefore constitutively activate the transcription of a
CC       specific set of genes independently of steroid hormones.
CC       {ECO:0000269|PubMed:19244107}.
CC   -!- ACTIVITY REGULATION: AIM-100 (4-amino-5,6-biaryl-furo[2,3-d]pyrimidine)
CC       suppresses TNK2-mediated phosphorylation at Tyr-269. Inhibits the
CC       binding of the Tyr-269 phosphorylated form to androgen-responsive
CC       enhancers (AREs) and its transcriptional activity.
CC       {ECO:0000269|PubMed:20623637}.
CC   -!- SUBUNIT: Binds DNA as a homodimer. Part of a ternary complex containing
CC       AR, EFCAB6/DJBP and PARK7. Interacts with HIPK3 and NR0B2 in the
CC       presence of androgen. The ligand binding domain interacts with
CC       KAT7/HBO1 in the presence of dihydrotestosterone. Interacts with
CC       EFCAB6/DJBP, PELP1, PQBP1, RANBP9, RBAK, SPDEF, SRA1, TGFB1I1 and
CC       RREB1. Interacts with ZMIZ1/ZIMP10 and ZMIZ2/ZMIP7 which both enhance
CC       its transactivation activity. Interacts with SLC30A9 and RAD54L2/ARIP4.
CC       Interacts via the ligand-binding domain with LXXLL and FXXLF motifs
CC       from NCOA1, NCOA2, NCOA3, NCOA4 and MAGEA11. The AR N-terminal poly-Gln
CC       region binds Ran resulting in enhancement of AR-mediated
CC       transactivation. Ran-binding decreases as the poly-Gln length
CC       increases. Interacts with HIP1 (via coiled coil domain). Interacts (via
CC       ligand-binding domain) with TRIM68. Interacts with TNK2. Interacts with
CC       USP26. Interacts with RNF6. Interacts (regulated by RNF6 probably
CC       through polyubiquitination) with RNF14; regulates AR transcriptional
CC       activity. Interacts with PRMT2 and TRIM24. Interacts with RACK1.
CC       Interacts with RANBP10; this interaction enhances dihydrotestosterone-
CC       induced AR transcriptional activity. Interacts with PRPF6 in a hormone-
CC       independent way; this interaction enhances dihydrotestosterone-induced
CC       AR transcriptional activity. Interacts with STK4/MST1. Interacts with
CC       ZIPK/DAPK3. Interacts with LPXN. Interacts with MAK. Part of a complex
CC       containing AR, MAK and NCOA3. Interacts with CRY1. Interacts with CCAR1
CC       and GATA2. Interacts with ZNF318 (By similarity). Interacts with BUD31
CC       (PubMed:25091737). Interacts with ARID4A (PubMed:23487765). Interacts
CC       with ARID4B (By similarity). Interacts (via NR LBD domain) with ZBTB7A;
CC       the interaction is direct and androgen-dependent (PubMed:20812024).
CC       Interacts with NCOR1 (PubMed:20812024). Interacts with NCOR2
CC       (PubMed:20812024). Interacts with CRY2 in a ligand-dependent manner (By
CC       similarity). {ECO:0000250|UniProtKB:P15207,
CC       ECO:0000250|UniProtKB:P19091, ECO:0000269|PubMed:10075738,
CC       ECO:0000269|PubMed:10332029, ECO:0000269|PubMed:10383460,
CC       ECO:0000269|PubMed:10400640, ECO:0000269|PubMed:10625666,
CC       ECO:0000269|PubMed:10930412, ECO:0000269|PubMed:12039962,
CC       ECO:0000269|PubMed:12361945, ECO:0000269|PubMed:12415108,
CC       ECO:0000269|PubMed:12612053, ECO:0000269|PubMed:12958311,
CC       ECO:0000269|PubMed:14609956, ECO:0000269|PubMed:14664718,
CC       ECO:0000269|PubMed:15525515, ECO:0000269|PubMed:15563469,
CC       ECO:0000269|PubMed:16027218, ECO:0000269|PubMed:16051670,
CC       ECO:0000269|PubMed:16951154, ECO:0000269|PubMed:17311914,
CC       ECO:0000269|PubMed:17494760, ECO:0000269|PubMed:17550981,
CC       ECO:0000269|PubMed:17587566, ECO:0000269|PubMed:17591767,
CC       ECO:0000269|PubMed:17711855, ECO:0000269|PubMed:17911242,
CC       ECO:0000269|PubMed:18007036, ECO:0000269|PubMed:18084323,
CC       ECO:0000269|PubMed:18222118, ECO:0000269|PubMed:18451096,
CC       ECO:0000269|PubMed:18451177, ECO:0000269|PubMed:19345326,
CC       ECO:0000269|PubMed:19909775, ECO:0000269|PubMed:20501646,
CC       ECO:0000269|PubMed:20812024, ECO:0000269|PubMed:20980437,
CC       ECO:0000269|PubMed:21512132, ECO:0000269|PubMed:22170608,
CC       ECO:0000269|PubMed:23487765, ECO:0000269|PubMed:23887938,
CC       ECO:0000269|PubMed:25091737}.
CC   -!- INTERACTION:
CC       P00519:ABL1; NbExp=2; IntAct=EBI-608057, EBI-375543;
CC       Q9UBL3:ASH2L; NbExp=2; IntAct=EBI-608057, EBI-540797;
CC       P51451:BLK; NbExp=3; IntAct=EBI-608057, EBI-2105445;
CC       Q8WV28:BLNK; NbExp=2; IntAct=EBI-608057, EBI-2623522;
CC       O60885-1:BRD4; NbExp=6; IntAct=EBI-608057, EBI-9345088;
CC       P78543:BTG2; NbExp=4; IntAct=EBI-608057, EBI-1047576;
CC       Q14790:CASP8; NbExp=3; IntAct=EBI-608057, EBI-78060;
CC       P24385:CCND1; NbExp=4; IntAct=EBI-608057, EBI-375001;
CC       Q92793:CREBBP; NbExp=2; IntAct=EBI-608057, EBI-81215;
CC       O14595:CTDSP2; NbExp=3; IntAct=EBI-608057, EBI-2802973;
CC       P35222:CTNNB1; NbExp=11; 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=4; 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       Q02790:FKBP4; NbExp=2; IntAct=EBI-608057, EBI-1047444;
CC       P55317:FOXA1; NbExp=3; IntAct=EBI-608057, EBI-3918034;
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       P06396:GSN; NbExp=2; IntAct=EBI-608057, EBI-351506;
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       Q9BY66:KDM5D; NbExp=2; IntAct=EBI-608057, EBI-1246860;
CC       Q9BY66-3:KDM5D; NbExp=2; IntAct=EBI-608057, EBI-12559887;
CC       P07288:KLK3; NbExp=3; IntAct=EBI-608057, EBI-1220791;
CC       Q03164:KMT2A; NbExp=2; IntAct=EBI-608057, EBI-591370;
CC       O14686:KMT2D; NbExp=2; IntAct=EBI-608057, EBI-996065;
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       O96028:NSD2; NbExp=5; IntAct=EBI-608057, EBI-2693298;
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       P78527:PRKDC; NbExp=3; IntAct=EBI-608057, EBI-352053;
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       P07947:YES1; NbExp=5; IntAct=EBI-608057, EBI-515331;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12958311,
CC       ECO:0000269|PubMed:15634333, ECO:0000269|PubMed:17587566,
CC       ECO:0000269|PubMed:19244107, ECO:0000269|PubMed:19345326,
CC       ECO:0000269|PubMed:25091737}. Cytoplasm {ECO:0000269|PubMed:12958311,
CC       ECO:0000269|PubMed:17587566, ECO:0000269|PubMed:19244107}.
CC       Note=Detected at the promoter of target genes (PubMed:25091737).
CC       Predominantly cytoplasmic in unligated form but translocates to the
CC       nucleus upon ligand-binding. Can also translocate to the nucleus in
CC       unligated form in the presence of RACK1. {ECO:0000269|PubMed:12958311,
CC       ECO:0000269|PubMed:17587566, ECO:0000269|PubMed:25091737}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
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       Name=3; Synonyms=AR3;
CC         IsoId=P10275-3; Sequence=VSP_058166, VSP_058168;
CC       Name=4; Synonyms=AR4;
CC         IsoId=P10275-4; Sequence=VSP_058167, VSP_058169;
CC   -!- TISSUE SPECIFICITY: Isoform 2 is mainly expressed in heart and skeletal
CC       muscle (PubMed:15634333). Isoform 3 is expressed by basal and stromal
CC       cells of prostate (at protein level) (PubMed:19244107).
CC       {ECO:0000269|PubMed:15634333, ECO:0000269|PubMed:19244107}.
CC   -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC       DNA-binding domain and a C-terminal ligand-binding domain. In the
CC       presence of bound steroid the ligand-binding domain interacts with the
CC       N-terminal modulating domain, and thereby activates AR transcription
CC       factor activity. Agonist binding is required for dimerization and
CC       binding to target DNA. The transcription factor activity of the complex
CC       formed by ligand-activated AR and DNA is modulated by interactions with
CC       coactivator and corepressor proteins (PubMed:25091737). Interaction
CC       with RANBP9 is mediated by both the N-terminal domain and the DNA-
CC       binding domain. Interaction with EFCAB6/DJBP is mediated by the DNA-
CC       binding domain. {ECO:0000269|PubMed:25091737}.
CC   -!- PTM: Sumoylated on Lys-388 (major) and Lys-521. Ubiquitinated.
CC       Deubiquitinated by USP26. 'Lys-6' and 'Lys-27'-linked
CC       polyubiquitination by RNF6 modulates AR transcriptional activity and
CC       specificity. {ECO:0000269|PubMed:11121022, ECO:0000269|PubMed:19345326,
CC       ECO:0000269|PubMed:20501646}.
CC   -!- PTM: Phosphorylated in prostate cancer cells in response to several
CC       growth factors including EGF. Phosphorylation is induced by c-Src
CC       kinase (CSK). Tyr-535 is one of the major phosphorylation sites and an
CC       increase in phosphorylation and Src kinase activity is associated with
CC       prostate cancer progression. Phosphorylation by TNK2 enhances the DNA-
CC       binding and transcriptional activity and may be responsible for
CC       androgen-independent progression of prostate cancer. Phosphorylation at
CC       Ser-83 by CDK9 regulates AR promoter selectivity and cell growth.
CC       Phosphorylation by PAK6 leads to AR-mediated transcription inhibition.
CC       {ECO:0000269|PubMed:14573606, ECO:0000269|PubMed:17045208,
CC       ECO:0000269|PubMed:17494760, ECO:0000269|PubMed:20623637,
CC       ECO:0000269|PubMed:20980437, ECO:0000269|PubMed:21512132}.
CC   -!- PTM: Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is required
CC       for plasma membrane targeting and for rapid intracellular signaling via
CC       ERK and AKT kinases and cAMP generation. {ECO:0000269|PubMed:22031296}.
CC   -!- POLYMORPHISM: The poly-Gln region of AR is highly polymorphic and the
CC       number of Gln varies in the population (from 17 to 26). A smaller size
CC       of the poly-Gln region may be associated with the development of
CC       prostate cancer. {ECO:0000269|PubMed:1561105,
CC       ECO:0000269|PubMed:2062380, ECO:0000269|PubMed:8292051,
CC       ECO:0000269|PubMed:9096391}.
CC   -!- POLYMORPHISM: The poly-Gly region of AR is polymorphic and ranges from
CC       24 to 31 Gly. A poly-Gly region shorter or equal to 23 may be
CC       associated with the development of androgenetic alopecia.
CC       {ECO:0000269|PubMed:11231320, ECO:0000269|PubMed:15902657}.
CC   -!- DISEASE: Androgen insensitivity syndrome (AIS) [MIM:300068]: An X-
CC       linked recessive form of pseudohermaphroditism due end-organ resistance
CC       to androgen. Affected males have female external genitalia, female
CC       breast development, blind vagina, absent uterus and female adnexa, and
CC       abdominal or inguinal testes, despite a normal 46,XY karyotype.
CC       {ECO:0000269|PubMed:10022458, ECO:0000269|PubMed:10221692,
CC       ECO:0000269|PubMed:10221770, ECO:0000269|PubMed:10404311,
CC       ECO:0000269|PubMed:10458483, ECO:0000269|PubMed:10571951,
CC       ECO:0000269|PubMed:10590024, ECO:0000269|PubMed:10690872,
CC       ECO:0000269|PubMed:11587068, ECO:0000269|PubMed:11744994,
CC       ECO:0000269|PubMed:1307250, ECO:0000269|PubMed:1316540,
CC       ECO:0000269|PubMed:1426313, ECO:0000269|PubMed:1430233,
CC       ECO:0000269|PubMed:1464650, ECO:0000269|PubMed:14756668,
CC       ECO:0000269|PubMed:1480178, ECO:0000269|PubMed:1487249,
CC       ECO:0000269|PubMed:1569163, ECO:0000269|PubMed:1609793,
CC       ECO:0000269|PubMed:16129672, ECO:0000269|PubMed:16595706,
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:8339746, ECO:0000269|PubMed:8413310,
CC       ECO:0000269|PubMed:8446106, ECO:0000269|PubMed:8626869,
CC       ECO:0000269|PubMed:8647313, ECO:0000269|PubMed:8683794,
CC       ECO:0000269|PubMed:8723113, ECO:0000269|PubMed:8768864,
CC       ECO:0000269|PubMed:8809734, ECO:0000269|PubMed:8830623,
CC       ECO:0000269|PubMed:8918984, ECO:0000269|PubMed:8990010,
CC       ECO:0000269|PubMed:9001799, ECO:0000269|PubMed:9007482,
CC       ECO:0000269|PubMed:9039340, ECO:0000269|PubMed:9106550,
CC       ECO:0000269|PubMed:9160185, ECO:0000269|PubMed:9252933,
CC       ECO:0000269|PubMed:9255042, ECO:0000269|PubMed:9302173,
CC       ECO:0000269|PubMed:9328206, ECO:0000269|PubMed:9544375,
CC       ECO:0000269|PubMed:9554754, ECO:0000269|PubMed:9610419,
CC       ECO:0000269|PubMed:9627582, ECO:0000269|PubMed:9698822,
CC       ECO:0000269|PubMed:9851768, ECO:0000269|PubMed:9856504,
CC       ECO:0000269|Ref.113, ECO:0000269|Ref.179}. Note=The disease is caused
CC       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 atrophy.
CC       Spinal muscular atrophy refers to a group of neuromuscular disorders
CC       characterized by degeneration of the anterior horn cells of the spinal
CC       cord, leading to symmetrical muscle weakness and atrophy. SMAX1 occurs
CC       only in men. Age at onset is usually in the third to fifth decade of
CC       life, but earlier involvement has been reported. It is characterized by
CC       slowly progressive limb and bulbar muscle weakness with fasciculations,
CC       muscle atrophy, and gynecomastia. The disorder is clinically similar to
CC       classic forms of autosomal spinal muscular atrophy.
CC       {ECO:0000269|PubMed:15851746}. Note=The disease is caused by mutations
CC       affecting the gene represented in this entry. Caused by trinucleotide
CC       CAG repeat expansion. In SMAX1 patients the number of Gln ranges from
CC       38 to 62. Longer expansions result in earlier onset and more severe
CC       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 metastases
CC       development despite of androgen ablation. This treatment can reduce
CC       primary and metastatic lesions probably by inducing apoptosis of tumor
CC       cells when they express the wild-type receptor.
CC       {ECO:0000269|PubMed:10363963, ECO:0000269|PubMed:10569618,
CC       ECO:0000269|PubMed:1562539, ECO:0000269|PubMed:16129672,
CC       ECO:0000269|PubMed:17311914, ECO:0000269|PubMed:2260966,
CC       ECO:0000269|PubMed:25091737, ECO:0000269|PubMed:8187068,
CC       ECO:0000269|PubMed:8274409, ECO:0000269|PubMed:8827083}.
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 pedigree
CC       pattern consistent with X-linked recessive inheritance. Some patients
CC       present azoospermia or severe oligospermia without other clinical
CC       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:14756668, ECO:0000269|PubMed:2010552,
CC       ECO:0000269|PubMed:7581399, ECO:0000269|PubMed:7649358,
CC       ECO:0000269|PubMed:7671849, ECO:0000269|PubMed:7909256,
CC       ECO:0000269|PubMed:7910529, ECO:0000269|PubMed:7929841,
CC       ECO:0000269|PubMed:7970939, ECO:0000269|PubMed:7981687,
CC       ECO:0000269|PubMed:8033918, ECO:0000269|PubMed:8097257,
CC       ECO:0000269|PubMed:8126121, ECO:0000269|PubMed:8205256,
CC       ECO:0000269|PubMed:8281139, ECO:0000269|PubMed:8325932,
CC       ECO:0000269|PubMed:8325950, ECO:0000269|PubMed:8446106,
CC       ECO:0000269|PubMed:8550758, ECO:0000269|PubMed:8809734,
CC       ECO:0000269|PubMed:8823308, ECO:0000269|PubMed:8824883,
CC       ECO:0000269|PubMed:9039340, ECO:0000269|PubMed:9196614,
CC       ECO:0000269|PubMed:9302173, ECO:0000269|PubMed:9329414,
CC       ECO:0000269|PubMed:9543136, ECO:0000269|PubMed:9607727,
CC       ECO:0000269|PubMed:9768671, ECO:0000269|PubMed:9856504,
CC       ECO:0000269|Ref.121}. Note=The disease is caused by mutations affecting
CC       the gene represented in this entry.
CC   -!- DISEASE: Hypospadias 1, X-linked (HYSP1) [MIM:300633]: A common
CC       malformation in which the urethra opens on the ventral side of the
CC       penis, due to developmental arrest of urethral fusion. The opening can
CC       be located glandular, penile, or even more posterior in the scrotum or
CC       perineum. Hypospadias is a feature of several syndromic disorders,
CC       including the androgen insensitivity syndrome and Opitz syndrome.
CC       {ECO:0000269|PubMed:8097257}. Note=The disease is caused by mutations
CC       affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: In the absence of ligand, steroid hormone receptors are
CC       thought to be weakly associated with nuclear components; hormone
CC       binding greatly increases receptor affinity. The hormone-receptor
CC       complex appears to recognize discrete DNA sequences upstream of
CC       transcriptional start sites.
CC   -!- MISCELLANEOUS: Transcriptional activity is enhanced by binding to
CC       RANBP9.
CC   -!- MISCELLANEOUS: The level of tyrosine phosphorylation may serve as a
CC       diagnostic tool to predict patient outcome in response to hormone-
CC       ablation therapy. Inhibition of tyrosine phosphorylation may be an
CC       effective intervention target for hormone-refractory prostate cancer.
CC   -!- MISCELLANEOUS: [Isoform 3]: Minor isoform up-regulated in prostate
CC       cancer cells. {ECO:0000269|PubMed:19244107}.
CC   -!- MISCELLANEOUS: [Isoform 4]: Minor isoform identified in prostate cancer
CC       cells. {ECO:0000269|PubMed:19244107}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC       subfamily. {ECO:0000305}.
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 and
CC       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 (AR);
CC       Note=Leiden Open Variation Database (LOVD);
CC       URL="http://www.lovd.nl/AR";
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; FJ235916; ACN39559.1; -; mRNA.
DR   EMBL; FJ235917; ACN39560.1; -; mRNA.
DR   EMBL; AL049564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL158016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL356358; -; NOT_ANNOTATED_CDS; 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; S79368; AAB21257.2; -; Genomic_DNA.
DR   CCDS; CCDS14387.1; -. [P10275-1]
DR   CCDS; CCDS43965.1; -. [P10275-2]
DR   CCDS; CCDS87754.1; -. [P10275-3]
DR   PIR; A39248; A39248.
DR   RefSeq; NP_000035.2; NM_000044.4. [P10275-1]
DR   RefSeq; NP_001011645.1; NM_001011645.3. [P10275-2]
DR   RefSeq; NP_001334990.1; NM_001348061.1. [P10275-3]
DR   RefSeq; NP_001334992.1; NM_001348063.1. [P10275-4]
DR   RefSeq; NP_001334993.1; NM_001348064.1.
DR   PDB; 1E3G; X-ray; 2.40 A; A=658-920.
DR   PDB; 1GS4; X-ray; 1.95 A; A=671-918.
DR   PDB; 1T5Z; X-ray; 2.30 A; A=670-920.
DR   PDB; 1T63; X-ray; 2.07 A; A=670-919.
DR   PDB; 1T65; X-ray; 1.66 A; A=670-920.
DR   PDB; 1XJ7; X-ray; 2.70 A; A=664-920.
DR   PDB; 1XOW; X-ray; 1.80 A; A=672-920, B=20-30.
DR   PDB; 1XQ3; X-ray; 2.25 A; A=672-920.
DR   PDB; 1Z95; X-ray; 1.80 A; A=673-918.
DR   PDB; 2AM9; X-ray; 1.64 A; A=655-920.
DR   PDB; 2AMA; X-ray; 1.90 A; A=655-920.
DR   PDB; 2AMB; X-ray; 1.75 A; A=655-920.
DR   PDB; 2AO6; X-ray; 1.89 A; A=672-920.
DR   PDB; 2AX6; X-ray; 1.50 A; A=665-920.
DR   PDB; 2AX7; X-ray; 1.90 A; A=665-920.
DR   PDB; 2AX8; X-ray; 1.70 A; A=665-920.
DR   PDB; 2AX9; X-ray; 1.65 A; A=665-920.
DR   PDB; 2AXA; X-ray; 1.80 A; A=665-920.
DR   PDB; 2HVC; X-ray; 2.10 A; A=670-919.
DR   PDB; 2OZ7; X-ray; 1.80 A; A=672-920.
DR   PDB; 2PIO; X-ray; 2.03 A; A=670-920.
DR   PDB; 2PIP; X-ray; 1.80 A; L=670-920.
DR   PDB; 2PIQ; X-ray; 2.40 A; A=670-920.
DR   PDB; 2PIR; X-ray; 2.10 A; A=670-920.
DR   PDB; 2PIT; X-ray; 1.76 A; A=670-920.
DR   PDB; 2PIU; X-ray; 2.12 A; A=670-920.
DR   PDB; 2PIV; X-ray; 1.95 A; A=670-920.
DR   PDB; 2PIW; X-ray; 2.58 A; A=670-920.
DR   PDB; 2PIX; X-ray; 2.40 A; A=670-920.
DR   PDB; 2PKL; X-ray; 2.49 A; A=670-920.
DR   PDB; 2PNU; X-ray; 1.65 A; A=655-920.
DR   PDB; 2Q7I; X-ray; 1.87 A; A=664-920, B=20-30.
DR   PDB; 2Q7J; X-ray; 1.90 A; A=664-920.
DR   PDB; 2Q7K; X-ray; 1.80 A; A=664-920, B=20-30.
DR   PDB; 2Q7L; X-ray; 1.92 A; A=664-920.
DR   PDB; 2YHD; X-ray; 2.20 A; A=672-920.
DR   PDB; 2YLO; X-ray; 2.50 A; A=665-920.
DR   PDB; 2YLP; X-ray; 2.30 A; A=665-920.
DR   PDB; 2YLQ; X-ray; 2.40 A; A=665-920.
DR   PDB; 2Z4J; X-ray; 2.60 A; A=672-919.
DR   PDB; 3B5R; X-ray; 1.80 A; A=672-920.
DR   PDB; 3B65; X-ray; 1.80 A; A=672-920.
DR   PDB; 3B66; X-ray; 1.65 A; A=672-920.
DR   PDB; 3B67; X-ray; 1.90 A; A=672-920.
DR   PDB; 3B68; X-ray; 1.90 A; A=672-920.
DR   PDB; 3BTR; X-ray; 2.60 A; B=622-636.
DR   PDB; 3L3X; X-ray; 1.55 A; A=671-919.
DR   PDB; 3L3Z; X-ray; 2.00 A; A=671-919.
DR   PDB; 3RLJ; X-ray; 1.90 A; A=672-918.
DR   PDB; 3RLL; X-ray; 1.70 A; A=672-918.
DR   PDB; 3V49; X-ray; 1.70 A; A=655-920, B=21-31.
DR   PDB; 3V4A; X-ray; 1.95 A; A=672-920, B=21-31.
DR   PDB; 3ZQT; X-ray; 2.29 A; A=665-920.
DR   PDB; 4HLW; X-ray; 2.50 A; A=665-920.
DR   PDB; 4K7A; X-ray; 2.44 A; A=671-919.
DR   PDB; 4OEA; X-ray; 2.12 A; A=671-920.
DR   PDB; 4OED; X-ray; 2.79 A; A=671-920.
DR   PDB; 4OEY; X-ray; 1.83 A; A=671-920.
DR   PDB; 4OEZ; X-ray; 1.80 A; A=671-920.
DR   PDB; 4OFR; X-ray; 2.26 A; A=671-920.
DR   PDB; 4OFU; X-ray; 2.12 A; A=671-920.
DR   PDB; 4OGH; X-ray; 2.98 A; A=671-920.
DR   PDB; 4OH5; X-ray; 2.00 A; A=671-920.
DR   PDB; 4OH6; X-ray; 3.56 A; A=671-920.
DR   PDB; 4OHA; X-ray; 1.42 A; A=671-920.
DR   PDB; 4OIL; X-ray; 2.51 A; A=671-920.
DR   PDB; 4OIU; X-ray; 3.01 A; A=671-920.
DR   PDB; 4OJ9; X-ray; 3.31 A; A=671-920.
DR   PDB; 4OJB; X-ray; 2.00 A; A=671-920.
DR   PDB; 4OK1; X-ray; 2.09 A; A=671-920.
DR   PDB; 4OKB; X-ray; 2.95 A; A=671-920.
DR   PDB; 4OKT; X-ray; 2.50 A; A=671-920.
DR   PDB; 4OKW; X-ray; 2.00 A; A=671-920.
DR   PDB; 4OKX; X-ray; 2.10 A; A=671-920.
DR   PDB; 4OLM; X-ray; 2.80 A; A=671-920.
DR   PDB; 4QL8; X-ray; 2.10 A; A=663-920.
DR   PDB; 5CJ6; X-ray; 2.07 A; A=642-920, B=21-30.
DR   PDB; 5JJM; X-ray; 2.15 A; A/B/C/D=669-920.
DR   PDB; 5T8E; X-ray; 2.71 A; A=672-920.
DR   PDB; 5T8J; X-ray; 2.70 A; A=672-920.
DR   PDB; 5V8Q; X-ray; 1.44 A; A=672-920.
DR   PDB; 5VO4; X-ray; 2.35 A; A=671-920.
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; 5CJ6; -.
DR   PDBsum; 5JJM; -.
DR   PDBsum; 5T8E; -.
DR   PDBsum; 5T8J; -.
DR   PDBsum; 5V8Q; -.
DR   PDBsum; 5VO4; -.
DR   SMR; P10275; -.
DR   BioGrid; 106862; 291.
DR   CORUM; P10275; -.
DR   DIP; DIP-125N; -.
DR   ELM; P10275; -.
DR   IntAct; P10275; 135.
DR   MINT; P10275; -.
DR   STRING; 9606.ENSP00000363822; -.
DR   BindingDB; P10275; -.
DR   ChEMBL; CHEMBL1871; -.
DR   DrugBank; DB07422; (2S)-2-hydroxy-2-methyl-N-[4-nitro-3-(trifluoromethyl)phenyl]-3-(pentafluorophenoxy)propanamide.
DR   DrugBank; DB07423; (2S)-3-[4-(acetylamino)phenoxy]-2-hydroxy-2-methyl-N-[4-nitro-3-(trifluoromethyl)phenyl]propanamide.
DR   DrugBank; DB07039; (2S)-N-(4-cyano-3-iodophenyl)-3-(4-cyanophenoxy)-2-hydroxy-2-methylpropanamide.
DR   DrugBank; DB04709; (3AALPHA,4ALPHA,7ALPHA,7AALPHA)- 3A,4,7,7A-TETRAHYDRO-2-(4-NITRO-1-NAPHTHALENYL)-4,7-ETHANO-1H-ISOINDOLE-1,3(2H)-DIONE.
DR   DrugBank; DB07717; (5S,8R,9S,10S,13R,14S,17S)-13-{2-[(3,5-DIFLUOROBENZYL)OXY]ETHYL}-17-HYDROXY-10-METHYLHEXADECAHYDRO-3H-CYCLOPENTA[A]PHENANTHREN-3-ONE.
DR   DrugBank; DB07454; (R)-3-BROMO-2-HYDROXY-2-METHYL-N-[4-NITRO-3-(TRIFLUOROMETHYL)PHENYL]PROPANAMIDE.
DR   DrugBank; DB02932; (R)-Bicalutamide.
DR   DrugBank; DB08035; 1-TERT-BUTYL-3-(2,5-DIMETHYLBENZYL)-1H-PYRAZOLO[3,4-D]PYRIMIDIN-4-AMINE.
DR   DrugBank; DB01481; 1-Testosterone.
DR   DrugBank; DB06870; 17-HYDROXY-18A-HOMO-19-NOR-17ALPHA-PREGNA-4,9,11-TRIEN-3-ONE.
DR   DrugBank; DB08088; 2-chloro-4-{[(1R,3Z,7S,7aS)-7-hydroxy-1-(trifluoromethyl)tetrahydro-1H-pyrrolo[1,2-c][1,3]oxazol-3-ylidene]amino}-3-methylbenzonitrile.
DR   DrugBank; DB08461; 3-[(4-AMINO-1-TERT-BUTYL-1H-PYRAZOLO[3,4-D]PYRIMIDIN-3-YL)METHYL]PHENOL.
DR   DrugBank; DB08087; 4-[(7R,7AS)-7-HYDROXY-1,3-DIOXOTETRAHYDRO-1H-PYRROLO[1,2-C]IMIDAZOL-2(3H)-YL]-1-NAPHTHONITRILE.
DR   DrugBank; DB07421; 4-{[(1R,2S)-1,2-dihydroxy-2-methyl-3-(4-nitrophenoxy)propyl]amino}-2-(trifluoromethyl)benzonitrile.
DR   DrugBank; DB01063; Acetophenazine.
DR   DrugBank; DB11901; Apalutamide.
DR   DrugBank; DB01128; Bicalutamide.
DR   DrugBank; DB07286; BMS-564929.
DR   DrugBank; DB01541; Boldenone.
DR   DrugBank; DB14639; Boldenone undecylenate.
DR   DrugBank; DB01564; Calusterone.
DR   DrugBank; DB04839; Cyproterone acetate.
DR   DrugBank; DB01406; Danazol.
DR   DrugBank; DB09123; Dienogest.
DR   DrugBank; DB00255; Diethylstilbestrol.
DR   DrugBank; DB06133; Dimethylcurcumin.
DR   DrugBank; DB01395; Drospirenone.
DR   DrugBank; DB00858; Drostanolone.
DR   DrugBank; DB11219; Enzacamene.
DR   DrugBank; DB08899; Enzalutamide.
DR   DrugBank; DB13155; Esculin.
DR   DrugBank; DB00655; Estrone.
DR   DrugBank; DB09086; Eugenol.
DR   DrugBank; DB00687; Fludrocortisone.
DR   DrugBank; DB02266; Flufenamic Acid.
DR   DrugBank; DB01185; Fluoxymesterone.
DR   DrugBank; DB00623; Fluphenazine.
DR   DrugBank; DB00499; Flutamide.
DR   DrugBank; DB11619; Gestrinone.
DR   DrugBank; DB11064; Homosalate.
DR   DrugBank; DB01026; Ketoconazole.
DR   DrugBank; DB00367; Levonorgestrel.
DR   DrugBank; DB08089; LGD-2226.
DR   DrugBank; DB05234; LGD2941.
DR   DrugBank; DB13934; Ligandrol.
DR   DrugBank; DB06710; Methyltestosterone.
DR   DrugBank; DB02998; Metribolone.
DR   DrugBank; DB11429; Mibolerone.
DR   DrugBank; DB00648; Mitotane.
DR   DrugBank; DB08804; Nandrolone decanoate.
DR   DrugBank; DB00984; Nandrolone phenpropionate.
DR   DrugBank; DB00665; Nilutamide.
DR   DrugBank; DB06713; Norelgestromin.
DR   DrugBank; DB09371; Norethynodrel.
DR   DrugBank; DB00957; Norgestimate.
DR   DrugBank; DB09389; Norgestrel.
DR   DrugBank; DB00621; Oxandrolone.
DR   DrugBank; DB01428; Oxybenzone.
DR   DrugBank; DB06412; Oxymetholone.
DR   DrugBank; DB01608; Periciazine.
DR   DrugBank; DB11447; Phenothiazine.
DR   DrugBank; DB01708; Prasterone.
DR   DrugBank; DB00396; Progesterone.
DR   DrugBank; DB07419; S-23.
DR   DrugBank; DB07769; S-3-(4-FLUOROPHENOXY)-2-HYDROXY-2-METHYL-N-[4-NITRO-3-(TRIFLUOROMETHYL)PHENYL]PROPANAMIDE.
DR   DrugBank; DB14583; Segesterone acetate.
DR   DrugBank; DB00421; Spironolactone.
DR   DrugBank; DB02901; Stanolone.
DR   DrugBank; DB13951; Stanolone acetate.
DR   DrugBank; DB00675; Tamoxifen.
DR   DrugBank; DB00624; Testosterone.
DR   DrugBank; DB13943; Testosterone cypionate.
DR   DrugBank; DB13944; Testosterone enanthate.
DR   DrugBank; DB01420; Testosterone propionate.
DR   DrugBank; DB13946; Testosterone undecanoate.
DR   DrugBank; DB08604; Triclosan.
DR   DrugBank; DB08867; Ulipristal.
DR   DrugCentral; P10275; -.
DR   GuidetoPHARMACOLOGY; 628; -.
DR   SwissLipids; SLP:000001553; -.
DR   MoonDB; P10275; Predicted.
DR   iPTMnet; P10275; -.
DR   PhosphoSitePlus; P10275; -.
DR   SwissPalm; P10275; -.
DR   BioMuta; AR; -.
DR   DMDM; 113830; -.
DR   jPOST; P10275; -.
DR   MassIVE; P10275; -.
DR   MaxQB; P10275; -.
DR   PaxDb; P10275; -.
DR   PeptideAtlas; P10275; -.
DR   PRIDE; P10275; -.
DR   ProteomicsDB; 18721; -.
DR   ProteomicsDB; 52590; -. [P10275-1]
DR   ProteomicsDB; 52591; -. [P10275-2]
DR   TopDownProteomics; P10275-1; -. [P10275-1]
DR   Ensembl; ENST00000374690; ENSP00000363822; ENSG00000169083. [P10275-1]
DR   Ensembl; ENST00000396043; ENSP00000379358; ENSG00000169083. [P10275-2]
DR   Ensembl; ENST00000504326; ENSP00000421155; ENSG00000169083. [P10275-3]
DR   GeneID; 367; -.
DR   KEGG; hsa:367; -.
DR   UCSC; uc004dwv.3; human. [P10275-1]
DR   UCSC; uc011mpf.2; human.
DR   CTD; 367; -.
DR   DisGeNET; 367; -.
DR   EuPathDB; HostDB:ENSG00000169083.15; -.
DR   GeneCards; AR; -.
DR   GeneReviews; AR; -.
DR   HGNC; HGNC:644; AR.
DR   HPA; CAB000001; -.
DR   HPA; CAB065764; -.
DR   HPA; HPA065701; -.
DR   MalaCards; AR; -.
DR   MIM; 300068; phenotype.
DR   MIM; 300633; phenotype.
DR   MIM; 312300; phenotype.
DR   MIM; 313200; phenotype.
DR   MIM; 313700; gene.
DR   neXtProt; NX_P10275; -.
DR   OpenTargets; ENSG00000169083; -.
DR   Orphanet; 99429; Complete androgen insensitivity syndrome.
DR   Orphanet; 481; Kennedy disease.
DR   Orphanet; 90797; Partial androgen insensitivity syndrome.
DR   Orphanet; 95706; Posterior hypospadias.
DR   PharmGKB; PA57; -.
DR   eggNOG; KOG3575; Eukaryota.
DR   eggNOG; ENOG410XRZC; LUCA.
DR   GeneTree; ENSGT00940000155516; -.
DR   InParanoid; P10275; -.
DR   KO; K08557; -.
DR   OMA; GPWMENY; -.
DR   OrthoDB; 998086at2759; -.
DR   PhylomeDB; P10275; -.
DR   TreeFam; TF350286; -.
DR   Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
DR   Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
DR   Reactome; R-HSA-4090294; SUMOylation of intracellular receptors.
DR   Reactome; R-HSA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR   Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR   Reactome; R-HSA-8940973; RUNX2 regulates osteoblast differentiation.
DR   SignaLink; P10275; -.
DR   SIGNOR; P10275; -.
DR   ChiTaRS; AR; human.
DR   EvolutionaryTrace; P10275; -.
DR   GeneWiki; Androgen_receptor; -.
DR   GenomeRNAi; 367; -.
DR   Pharos; P10275; Tclin.
DR   PRO; PR:P10275; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; P10275; protein.
DR   Bgee; ENSG00000169083; Expressed in 199 organ(s), highest expression level in uterine cervix.
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:0016607; C:nuclear speck; IDA:CAFA.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR   GO; GO:0005497; F:androgen binding; 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:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0004879; F:nuclear receptor activity; IDA:UniProtKB.
DR   GO; GO:0070974; F:POU domain binding; IEA:Ensembl.
DR   GO; GO:0046983; F:protein dimerization activity; NAS:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0001091; F:RNA polymerase II general transcription initiation factor binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0001085; F:RNA polymerase II transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR   GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR   GO; GO:0003707; F:steroid hormone receptor activity; IDA:BHF-UCL.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0060520; P:activation of prostate induction by androgen receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0030521; P:androgen receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0048645; P:animal organ formation; IEA:Ensembl.
DR   GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR   GO; GO:0071383; P:cellular response to steroid hormone stimulus; IMP:CAFA.
DR   GO; GO:0071394; P:cellular response to testosterone stimulus; IEA:Ensembl.
DR   GO; GO:0060742; P:epithelial cell differentiation involved in prostate gland development; IEA:Ensembl.
DR   GO; GO:0003382; P:epithelial cell morphogenesis; IEA:Ensembl.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0030522; P:intracellular receptor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0060599; P:lateral sprouting involved in mammary gland duct morphogenesis; IEA:Ensembl.
DR   GO; GO:0033327; P:Leydig cell differentiation; IEA:Ensembl.
DR   GO; GO:0048808; P:male genitalia morphogenesis; IEA:Ensembl.
DR   GO; GO:0019102; P:male somatic sex determination; IEA:Ensembl.
DR   GO; GO:0060749; P:mammary gland alveolus development; IEA:Ensembl.
DR   GO; GO:0060571; P:morphogenesis of an epithelial fold; IEA:Ensembl.
DR   GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR   GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
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:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:CAFA.
DR   GO; GO:0045597; P:positive regulation of cell differentiation; IMP:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL.
DR   GO; GO:0060769; P:positive regulation of epithelial cell proliferation involved in prostate gland development; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR   GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0045726; P:positive regulation of integrin biosynthetic process; IDA:BHF-UCL.
DR   GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
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 by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IDA:BHF-UCL.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0060740; P:prostate gland epithelium morphogenesis; IEA:Ensembl.
DR   GO; GO:0060736; P:prostate gland growth; IEA:Ensembl.
DR   GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
DR   GO; GO:0048638; P:regulation of developmental growth; IEA:Ensembl.
DR   GO; GO:1903076; P:regulation of protein localization to plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0003073; P:regulation of systemic arterial blood pressure; IEA:Ensembl.
DR   GO; GO:0072520; P:seminiferous tubule development; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   GO; GO:0007338; P:single fertilization; IEA:Ensembl.
DR   GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR   GO; GO:0060748; P:tertiary branching involved in mammary gland duct morphogenesis; IEA:Ensembl.
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   DisProt; DP00492; -.
DR   Gene3D; 1.10.565.10; -; 1.
DR   Gene3D; 3.30.50.10; -; 1.
DR   InterPro; IPR001103; Andrgn_rcpt.
DR   InterPro; IPR035500; NHR-like_dom_sf.
DR   InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR   InterPro; IPR001628; Znf_hrmn_rcpt.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   Pfam; PF02166; Androgen_recep; 1.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   Pfam; PF00105; zf-C4; 1.
DR   PRINTS; PR00521; ANDROGENR.
DR   PRINTS; PR00047; STROIDFINGER.
DR   SMART; SM00430; HOLI; 1.
DR   SMART; SM00399; ZnF_C4; 1.
DR   SUPFAM; SSF48508; SSF48508; 1.
DR   PROSITE; PS51843; NR_LBD; 1.
DR   PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative splicing; Cytoplasm; Disease mutation;
KW   DNA-binding; Isopeptide bond; Lipid-binding; Lipoprotein; Metal-binding;
KW   Neurodegeneration; Nucleus; Palmitate; Phosphoprotein; Polymorphism;
KW   Pseudohermaphroditism; Receptor; Reference proteome; Steroid-binding;
KW   Transcription; Transcription regulation; Triplet repeat expansion;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..920
FT                   /note="Androgen receptor"
FT                   /id="PRO_0000053704"
FT   DOMAIN          669..900
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        560..632
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         560..580
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         596..620
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          1..587
FT                   /note="Interaction with ZNF318"
FT                   /evidence="ECO:0000250|UniProtKB:P19091"
FT   REGION          1..559
FT                   /note="Modulating"
FT   REGION          552..919
FT                   /note="Interaction with LPXN"
FT                   /evidence="ECO:0000269|PubMed:18451096"
FT   REGION          572..662
FT                   /note="Interaction with HIPK3"
FT                   /evidence="ECO:0000250|UniProtKB:P15207"
FT   REGION          592..919
FT                   /note="Interaction with CCAR1"
FT                   /evidence="ECO:0000269|PubMed:23887938"
FT   REGION          625..919
FT                   /note="Interaction with KAT7"
FT                   /evidence="ECO:0000269|PubMed:10930412"
FT   COMPBIAS        58..120
FT                   /note="Gln-rich"
FT   COMPBIAS        58..80
FT                   /note="Poly-Gln"
FT   COMPBIAS        86..91
FT                   /note="Poly-Gln"
FT   COMPBIAS        195..199
FT                   /note="Poly-Gln"
FT   COMPBIAS        374..383
FT                   /note="Poly-Pro"
FT   COMPBIAS        398..404
FT                   /note="Poly-Ala"
FT   COMPBIAS        451..473
FT                   /note="Poly-Gly"
FT   BINDING         706
FT                   /note="Androgen"
FT                   /evidence="ECO:0000244|PDB:1T5Z, ECO:0000244|PDB:1T63,
FT                   ECO:0000244|PDB:1T65, ECO:0000244|PDB:1XJ7,
FT                   ECO:0000244|PDB:2AM9, ECO:0000244|PDB:2AMA,
FT                   ECO:0000244|PDB:2AMB, ECO:0000244|PDB:2PIO,
FT                   ECO:0000244|PDB:2PIP, ECO:0000244|PDB:2PIR,
FT                   ECO:0000244|PDB:2PIT, ECO:0000244|PDB:2PIU,
FT                   ECO:0000244|PDB:2PIV, ECO:0000244|PDB:2PIW,
FT                   ECO:0000244|PDB:2PIX, ECO:0000244|PDB:2PKL,
FT                   ECO:0000244|PDB:2PNU, ECO:0000244|PDB:2Q7I,
FT                   ECO:0000244|PDB:2Q7J, ECO:0000244|PDB:2Q7K,
FT                   ECO:0000244|PDB:2Q7L, ECO:0000244|PDB:2YHD,
FT                   ECO:0000244|PDB:2YLO, ECO:0000244|PDB:2YLP,
FT                   ECO:0000244|PDB:2YLQ, ECO:0000244|PDB:3L3X,
FT                   ECO:0000244|PDB:3L3Z, ECO:0000244|PDB:3ZQT,
FT                   ECO:0000244|PDB:4HLW, ECO:0000244|PDB:4K7A,
FT                   ECO:0000244|PDB:4OEA, ECO:0000244|PDB:4OED,
FT                   ECO:0000244|PDB:4OEY, ECO:0000244|PDB:4OEZ,
FT                   ECO:0000244|PDB:4OFR, ECO:0000244|PDB:4OFU,
FT                   ECO:0000244|PDB:5JJM, ECO:0000269|PubMed:15563469,
FT                   ECO:0000269|PubMed:16641486, ECO:0000269|PubMed:17591767,
FT                   ECO:0000269|PubMed:25091737"
FT   BINDING         753
FT                   /note="Androgen"
FT                   /evidence="ECO:0000244|PDB:1T5Z, ECO:0000244|PDB:1T63,
FT                   ECO:0000244|PDB:1T65, ECO:0000244|PDB:1XJ7,
FT                   ECO:0000244|PDB:2AM9, ECO:0000244|PDB:2AMA,
FT                   ECO:0000244|PDB:2PIO, ECO:0000244|PDB:2PIP,
FT                   ECO:0000244|PDB:2PIQ, ECO:0000244|PDB:2PIR,
FT                   ECO:0000244|PDB:2PIT, ECO:0000244|PDB:2PIU,
FT                   ECO:0000244|PDB:2PIV, ECO:0000244|PDB:2PIW,
FT                   ECO:0000244|PDB:2PIX, ECO:0000244|PDB:2PKL,
FT                   ECO:0000244|PDB:2Q7I, ECO:0000244|PDB:2Q7J,
FT                   ECO:0000244|PDB:2Q7K, ECO:0000244|PDB:2Q7L,
FT                   ECO:0000244|PDB:2YHD, ECO:0000244|PDB:2YLO,
FT                   ECO:0000244|PDB:2YLP, ECO:0000244|PDB:2YLQ,
FT                   ECO:0000244|PDB:2Z4J, ECO:0000244|PDB:3L3X,
FT                   ECO:0000244|PDB:3L3Z, ECO:0000244|PDB:3ZQT,
FT                   ECO:0000244|PDB:4HLW, ECO:0000244|PDB:4K7A,
FT                   ECO:0000244|PDB:4OEA, ECO:0000244|PDB:4OED,
FT                   ECO:0000244|PDB:4OEY, ECO:0000244|PDB:4OEZ,
FT                   ECO:0000244|PDB:4OFR, ECO:0000244|PDB:4OFU,
FT                   ECO:0000244|PDB:5JJM, ECO:0000269|PubMed:15563469,
FT                   ECO:0000269|PubMed:16641486, ECO:0000269|PubMed:17591767,
FT                   ECO:0000269|PubMed:25091737"
FT   BINDING         878
FT                   /note="Androgen"
FT                   /evidence="ECO:0000244|PDB:1T5Z, ECO:0000244|PDB:1T63,
FT                   ECO:0000244|PDB:1T65, ECO:0000244|PDB:1XJ7,
FT                   ECO:0000244|PDB:2AM9, ECO:0000244|PDB:2AMA,
FT                   ECO:0000244|PDB:2PIO, ECO:0000244|PDB:2PIP,
FT                   ECO:0000244|PDB:2PIQ, ECO:0000244|PDB:2PIR,
FT                   ECO:0000244|PDB:2PIT, ECO:0000244|PDB:2PIU,
FT                   ECO:0000244|PDB:2PIV, ECO:0000244|PDB:2PIW,
FT                   ECO:0000244|PDB:2PIX, ECO:0000244|PDB:2PKL,
FT                   ECO:0000244|PDB:2Q7I, ECO:0000244|PDB:2Q7J,
FT                   ECO:0000244|PDB:2Q7K, ECO:0000244|PDB:2Q7L,
FT                   ECO:0000244|PDB:2YHD, ECO:0000244|PDB:2YLO,
FT                   ECO:0000244|PDB:2YLP, ECO:0000244|PDB:2YLQ,
FT                   ECO:0000244|PDB:2Z4J, ECO:0000244|PDB:3L3X,
FT                   ECO:0000244|PDB:3L3Z, ECO:0000244|PDB:3ZQT,
FT                   ECO:0000244|PDB:4HLW, ECO:0000244|PDB:4K7A,
FT                   ECO:0000244|PDB:4OEA, ECO:0000244|PDB:4OED,
FT                   ECO:0000244|PDB:4OEY, ECO:0000244|PDB:4OEZ,
FT                   ECO:0000244|PDB:4OFR, ECO:0000244|PDB:4OFU,
FT                   ECO:0000244|PDB:5JJM, ECO:0000269|PubMed:15563469,
FT                   ECO:0000269|PubMed:16641486, ECO:0000269|PubMed:17591767,
FT                   ECO:0000269|PubMed:25091737"
FT   SITE            721
FT                   /note="Interaction with coactivator LXXL and FXXFY motifs"
FT                   /evidence="ECO:0000269|PubMed:25091737"
FT   SITE            898
FT                   /note="Interaction with coactivator FXXLF and FXXFY motifs"
FT                   /evidence="ECO:0000269|PubMed:25091737"
FT   MOD_RES         83
FT                   /note="Phosphoserine; by CDK9"
FT                   /evidence="ECO:0000269|PubMed:20980437"
FT   MOD_RES         96
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21406692,
FT                   ECO:0000244|PubMed:24275569"
FT   MOD_RES         225
FT                   /note="Phosphotyrosine; by CSK"
FT                   /evidence="ECO:0000269|PubMed:17045208"
FT   MOD_RES         258
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   MOD_RES         269
FT                   /note="Phosphotyrosine; by CSK and TNK2"
FT                   /evidence="ECO:0000269|PubMed:17045208,
FT                   ECO:0000269|PubMed:17494760, ECO:0000269|PubMed:20623637"
FT   MOD_RES         309
FT                   /note="Phosphotyrosine; by CSK"
FT                   /evidence="ECO:0000269|PubMed:17045208"
FT   MOD_RES         348
FT                   /note="Phosphotyrosine; by CSK"
FT                   /evidence="ECO:0000269|PubMed:17045208"
FT   MOD_RES         359
FT                   /note="Phosphotyrosine; by CSK"
FT                   /evidence="ECO:0000269|PubMed:17045208"
FT   MOD_RES         364
FT                   /note="Phosphotyrosine; by CSK"
FT                   /evidence="ECO:0000269|PubMed:17045208"
FT   MOD_RES         365
FT                   /note="Phosphotyrosine; by CSK and TNK2"
FT                   /evidence="ECO:0000269|PubMed:17045208,
FT                   ECO:0000269|PubMed:17494760"
FT   MOD_RES         395
FT                   /note="Phosphotyrosine; by CSK"
FT                   /evidence="ECO:0000269|PubMed:17045208"
FT   MOD_RES         535
FT                   /note="Phosphotyrosine; by CSK"
FT                   /evidence="ECO:0000269|PubMed:17045208"
FT   MOD_RES         552
FT                   /note="Phosphotyrosine; by CSK"
FT                   /evidence="ECO:0000269|PubMed:17045208"
FT   MOD_RES         651
FT                   /note="Phosphoserine; by STK4/MST1"
FT                   /evidence="ECO:0000269|PubMed:21512132"
FT   MOD_RES         916
FT                   /note="Phosphotyrosine; by CSK"
FT                   /evidence="ECO:0000269|PubMed:17045208"
FT   CROSSLNK        388
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000269|PubMed:11121022"
FT   CROSSLNK        521
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000269|PubMed:11121022"
FT   CROSSLNK        846
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:19345326"
FT   CROSSLNK        848
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:19345326"
FT   VAR_SEQ         1..532
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_036889"
FT   VAR_SEQ         533..539
FT                   /note="GPYGDMR -> MILWLHS (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_036890"
FT   VAR_SEQ         629..644
FT                   /note="ARKLKKLGNLKLQEEG -> EKFRVGNCKHLKMTRP (in isoform 3)"
FT                   /id="VSP_058166"
FT   VAR_SEQ         630..648
FT                   /note="RKLKKLGNLKLQEEGEASS -> AVVVSERILRVFGVSEWLP (in
FT                   isoform 4)"
FT                   /id="VSP_058167"
FT   VAR_SEQ         645..920
FT                   /note="Missing (in isoform 3)"
FT                   /id="VSP_058168"
FT   VAR_SEQ         649..920
FT                   /note="Missing (in isoform 4)"
FT                   /id="VSP_058169"
FT   VARIANT         2
FT                   /note="E -> K (in PAIS; dbSNP:rs104894742)"
FT                   /evidence="ECO:0000269|PubMed:8823308"
FT                   /id="VAR_004679"
FT   VARIANT         54
FT                   /note="L -> S (in prostate cancer)"
FT                   /id="VAR_004680"
FT   VARIANT         57
FT                   /note="L -> Q (in prostate cancer; dbSNP:rs78686797)"
FT                   /evidence="ECO:0000269|PubMed:19244107"
FT                   /id="VAR_004681"
FT   VARIANT         64
FT                   /note="Q -> R (in prostate cancer)"
FT                   /id="VAR_009711"
FT   VARIANT         114
FT                   /note="Q -> H (in prostate cancer)"
FT                   /id="VAR_009712"
FT   VARIANT         182
FT                   /note="K -> R (in prostate cancer)"
FT                   /id="VAR_009713"
FT   VARIANT         196
FT                   /note="Q -> R (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:9255042"
FT                   /id="VAR_009224"
FT   VARIANT         207
FT                   /note="S -> R (in dbSNP:rs374549047)"
FT                   /evidence="ECO:0000269|PubMed:8213813"
FT                   /id="VAR_009714"
FT   VARIANT         216
FT                   /note="G -> R (functional polymorphism; 20% lower
FT                   transactivation capacity; dbSNP:rs199554641)"
FT                   /evidence="ECO:0000269|PubMed:27535533,
FT                   ECO:0000269|PubMed:9788719"
FT                   /id="VAR_009715"
FT   VARIANT         257
FT                   /note="L -> P (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:9610419"
FT                   /id="VAR_009225"
FT   VARIANT         268
FT                   /note="M -> T (in prostate cancer)"
FT                   /id="VAR_009716"
FT   VARIANT         271
FT                   /note="P -> S (in prostate cancer)"
FT                   /id="VAR_009717"
FT   VARIANT         342
FT                   /note="P -> L (in prostate cancer; dbSNP:rs138454018)"
FT                   /evidence="ECO:0000269|PubMed:7511268"
FT                   /id="VAR_009718"
FT   VARIANT         392
FT                   /note="P -> R (in AIS; dbSNP:rs773996740)"
FT                   /evidence="ECO:0000269|PubMed:10571951"
FT                   /id="VAR_009226"
FT   VARIANT         392
FT                   /note="P -> S (in AIS; dbSNP:rs201934623)"
FT                   /id="VAR_009227"
FT   VARIANT         445
FT                   /note="Q -> R (in AIS; unknown pathological significance;
FT                   dbSNP:rs1355285524)"
FT                   /evidence="ECO:0000269|PubMed:10571951"
FT                   /id="VAR_009228"
FT   VARIANT         492
FT                   /note="G -> S (in AIS)"
FT                   /id="VAR_009719"
FT   VARIANT         529
FT                   /note="D -> G (in prostate cancer)"
FT                   /id="VAR_009720"
FT   VARIANT         548
FT                   /note="L -> F (in PAIS; dbSNP:rs139524801)"
FT                   /id="VAR_009721"
FT   VARIANT         549
FT                   /note="P -> S (in AIS; dbSNP:rs137852588)"
FT                   /evidence="ECO:0000269|PubMed:8683794"
FT                   /id="VAR_009722"
FT   VARIANT         560
FT                   /note="C -> Y (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:1316540"
FT                   /id="VAR_009723"
FT   VARIANT         569
FT                   /note="G -> V (in a patient with isolated hypospadias)"
FT                   /evidence="ECO:0000269|PubMed:7673412"
FT                   /id="VAR_009725"
FT   VARIANT         569
FT                   /note="G -> W (in PAIS; dbSNP:rs1555982864)"
FT                   /evidence="ECO:0000269|PubMed:7910529"
FT                   /id="VAR_009726"
FT   VARIANT         572
FT                   /note="Y -> C (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:9544375"
FT                   /id="VAR_009727"
FT   VARIANT         574
FT                   /note="A -> D (in AIS)"
FT                   /id="VAR_009728"
FT   VARIANT         575
FT                   /note="L -> P (in prostate cancer)"
FT                   /id="VAR_009729"
FT   VARIANT         576
FT                   /note="T -> A (in prostate cancer)"
FT                   /evidence="ECO:0000269|PubMed:10706109"
FT                   /id="VAR_009730"
FT   VARIANT         577
FT                   /note="C -> F (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:14756668"
FT                   /id="VAR_009731"
FT   VARIANT         577
FT                   /note="C -> R (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:1316540"
FT                   /id="VAR_009732"
FT   VARIANT         580
FT                   /note="C -> F (in AIS; reduced transcription and DNA
FT                   binding; dbSNP:rs137852586)"
FT                   /evidence="ECO:0000269|PubMed:8809734"
FT                   /id="VAR_009733"
FT   VARIANT         580
FT                   /note="C -> Y (in AIS)"
FT                   /id="VAR_009734"
FT   VARIANT         581
FT                   /note="K -> R (in prostate cancer)"
FT                   /evidence="ECO:0000269|PubMed:10706109"
FT                   /id="VAR_009735"
FT   VARIANT         582
FT                   /note="V -> F (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:8224266, ECO:0000269|Ref.113"
FT                   /id="VAR_009736"
FT   VARIANT         583
FT                   /note="F -> S (in PAIS)"
FT                   /evidence="ECO:0000269|PubMed:7981687"
FT                   /id="VAR_009737"
FT   VARIANT         583
FT                   /note="F -> Y (in PAIS; dbSNP:rs137852587)"
FT                   /evidence="ECO:0000269|PubMed:8809734"
FT                   /id="VAR_009738"
FT   VARIANT         583
FT                   /note="Missing (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:8162033"
FT                   /id="VAR_009739"
FT   VARIANT         586
FT                   /note="R -> K (in AIS)"
FT                   /id="VAR_009740"
FT   VARIANT         587
FT                   /note="A -> V (in prostate cancer; somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:10706109"
FT                   /id="VAR_009741"
FT   VARIANT         588
FT                   /note="A -> S (in prostate cancer; somatic mutation)"
FT                   /id="VAR_009742"
FT   VARIANT         597
FT                   /note="A -> T (in AIS; abolishes dimerization;
FT                   dbSNP:rs137852569)"
FT                   /evidence="ECO:0000269|PubMed:10590024,
FT                   ECO:0000269|PubMed:7649358"
FT                   /id="VAR_009743"
FT   VARIANT         598
FT                   /note="S -> G (in PAIS; associated with P-618 in a PAIS
FT                   patient; normal androgen binding; does not activate
FT                   transcription; impairs DNA binding; dbSNP:rs142280455)"
FT                   /evidence="ECO:0000269|PubMed:1316540"
FT                   /id="VAR_009744"
FT   VARIANT         598
FT                   /note="S -> T (in a patient with severe hypospadias)"
FT                   /evidence="ECO:0000269|PubMed:10092153"
FT                   /id="VAR_009745"
FT   VARIANT         602
FT                   /note="C -> F (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:7981689"
FT                   /id="VAR_009746"
FT   VARIANT         605
FT                   /note="D -> Y (in PAIS)"
FT                   /evidence="ECO:0000269|PubMed:7981687"
FT                   /id="VAR_009747"
FT   VARIANT         608
FT                   /note="R -> Q (in PAIS and breast cancer;
FT                   dbSNP:rs137852573)"
FT                   /evidence="ECO:0000269|PubMed:10221692,
FT                   ECO:0000269|PubMed:1303262, ECO:0000269|PubMed:9039340,
FT                   ECO:0000269|PubMed:9543136"
FT                   /id="VAR_004684"
FT   VARIANT         609
FT                   /note="R -> K (in PAIS and breast cancer; defective nuclear
FT                   localization; dbSNP:rs137852576)"
FT                   /evidence="ECO:0000269|PubMed:1424203,
FT                   ECO:0000269|PubMed:8281139, ECO:0000269|PubMed:9196614"
FT                   /id="VAR_004685"
FT   VARIANT         611
FT                   /note="N -> T (in PAIS)"
FT                   /evidence="ECO:0000269|PubMed:9039340"
FT                   /id="VAR_009748"
FT   VARIANT         612
FT                   /note="C -> Y (in AIS)"
FT                   /id="VAR_009749"
FT   VARIANT         616
FT                   /note="R -> H (in AIS and PAIS; dbSNP:rs754201976)"
FT                   /evidence="ECO:0000269|PubMed:7970939,
FT                   ECO:0000269|PubMed:8162033, ECO:0000269|PubMed:8413310,
FT                   ECO:0000269|PubMed:9698822"
FT                   /id="VAR_009751"
FT   VARIANT         616
FT                   /note="R -> P (in AIS)"
FT                   /id="VAR_009752"
FT   VARIANT         616
FT                   /note="Missing (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:8162033"
FT                   /id="VAR_009750"
FT   VARIANT         617
FT                   /note="L -> P (in AIS; dbSNP:rs1555990488)"
FT                   /evidence="ECO:0000269|PubMed:8647313"
FT                   /id="VAR_009753"
FT   VARIANT         617
FT                   /note="L -> R (in PAIS)"
FT                   /evidence="ECO:0000269|PubMed:8126121"
FT                   /id="VAR_009754"
FT   VARIANT         618
FT                   /note="R -> P (in AIS and PAIS; associated with G-598 in a
FT                   PAIS patient; loss of DNA-binding activity)"
FT                   /evidence="ECO:0000269|PubMed:1316540,
FT                   ECO:0000269|PubMed:1999491"
FT                   /id="VAR_009755"
FT   VARIANT         620
FT                   /note="C -> Y (in prostate cancer; loss of DNA binding;
FT                   somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:10598582,
FT                   ECO:0000269|PubMed:10706109"
FT                   /id="VAR_009756"
FT   VARIANT         630
FT                   /note="R -> Q (in prostate cancer; dbSNP:rs868669253)"
FT                   /evidence="ECO:0000269|PubMed:9184448"
FT                   /id="VAR_009757"
FT   VARIANT         631
FT                   /note="K -> T (in prostate cancer)"
FT                   /id="VAR_009758"
FT   VARIANT         646
FT                   /note="A -> D (in dbSNP:rs1800053)"
FT                   /evidence="ECO:0000269|PubMed:9554755"
FT                   /id="VAR_004686"
FT   VARIANT         648
FT                   /note="S -> N (in prostate cancer; dbSNP:rs137852584)"
FT                   /id="VAR_009760"
FT   VARIANT         665
FT                   /note="I -> N (in AIS and PAIS)"
FT                   /id="VAR_004687"
FT   VARIANT         671
FT                   /note="Q -> R (in prostate cancer)"
FT                   /id="VAR_009761"
FT   VARIANT         672
FT                   /note="P -> H (in PAIS)"
FT                   /id="VAR_009762"
FT   VARIANT         673
FT                   /note="I -> T (in prostate cancer)"
FT                   /id="VAR_009763"
FT   VARIANT         678
FT                   /note="L -> P (in AIS; dbSNP:rs137852579)"
FT                   /evidence="ECO:0000269|PubMed:7537149"
FT                   /id="VAR_004688"
FT   VARIANT         682
FT                   /note="E -> K (in AIS; dbSNP:rs1555995816)"
FT                   /evidence="ECO:0000269|PubMed:10221692,
FT                   ECO:0000269|PubMed:8325950"
FT                   /id="VAR_009764"
FT   VARIANT         683
FT                   /note="P -> T (in PAIS)"
FT                   /evidence="ECO:0000269|PubMed:11587068"
FT                   /id="VAR_013474"
FT   VARIANT         684
FT                   /note="G -> A (in prostate cancer)"
FT                   /evidence="ECO:0000269|PubMed:10629558,
FT                   ECO:0000269|PubMed:9000575"
FT                   /id="VAR_009765"
FT   VARIANT         685
FT                   /note="V -> I (in AIS; dbSNP:rs1555995822)"
FT                   /id="VAR_009766"
FT   VARIANT         687
FT                   /note="C -> R (in PAIS)"
FT                   /id="VAR_009767"
FT   VARIANT         688
FT                   /note="A -> V (in PAIS)"
FT                   /id="VAR_009768"
FT   VARIANT         689
FT                   /note="G -> E (in AIS)"
FT                   /id="VAR_009769"
FT   VARIANT         691
FT                   /note="Missing (in PAIS)"
FT                   /evidence="ECO:0000269|Ref.121"
FT                   /id="VAR_009770"
FT   VARIANT         693
FT                   /note="Missing (in AIS)"
FT                   /id="VAR_004689"
FT   VARIANT         696
FT                   /note="D -> H (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:1775137"
FT                   /id="VAR_004690"
FT   VARIANT         696
FT                   /note="D -> N (in AIS; almost complete loss of androgen
FT                   binding and transcription activation; dbSNP:rs1555995840)"
FT                   /evidence="ECO:0000269|PubMed:16595706,
FT                   ECO:0000269|PubMed:1775137"
FT                   /id="VAR_004691"
FT   VARIANT         696
FT                   /note="D -> V (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:9554754"
FT                   /id="VAR_004692"
FT   VARIANT         701
FT                   /note="L -> M (in AIS)"
FT                   /id="VAR_009771"
FT   VARIANT         702
FT                   /note="L -> F (in AIS; dbSNP:rs1555995851)"
FT                   /id="VAR_009772"
FT   VARIANT         702
FT                   /note="L -> H (in AIS and prostate cancer;
FT                   dbSNP:rs864622007)"
FT                   /evidence="ECO:0000269|PubMed:10569618,
FT                   ECO:0000269|PubMed:8274409, ECO:0000269|PubMed:9438000"
FT                   /id="VAR_009773"
FT   VARIANT         703
FT                   /note="S -> A (in AIS)"
FT                   /id="VAR_009774"
FT   VARIANT         704
FT                   /note="S -> C (in AIS)"
FT                   /id="VAR_009775"
FT   VARIANT         704
FT                   /note="S -> G (in PAIS and AIS)"
FT                   /evidence="ECO:0000269|PubMed:9302173"
FT                   /id="VAR_004693"
FT   VARIANT         706
FT                   /note="N -> S (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:1480178,
FT                   ECO:0000269|PubMed:7671849"
FT                   /id="VAR_009776"
FT   VARIANT         706
FT                   /note="N -> Y (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:11744994"
FT                   /id="VAR_013475"
FT   VARIANT         708
FT                   /note="L -> R (in AIS; dbSNP:rs137852585)"
FT                   /evidence="ECO:0000269|PubMed:8626869"
FT                   /id="VAR_004694"
FT   VARIANT         709
FT                   /note="G -> A (in PAIS)"
FT                   /evidence="ECO:0000269|PubMed:7981687,
FT                   ECO:0000269|PubMed:9329414"
FT                   /id="VAR_009777"
FT   VARIANT         709
FT                   /note="G -> V (in AIS)"
FT                   /id="VAR_009778"
FT   VARIANT         711
FT                   /note="R -> T (in AIS)"
FT                   /id="VAR_009779"
FT   VARIANT         712
FT                   /note="Q -> E (in PAIS)"
FT                   /evidence="ECO:0000269|PubMed:11587068"
FT                   /id="VAR_013476"
FT   VARIANT         713
FT                   /note="L -> F (in PAIS; dbSNP:rs137852595)"
FT                   /id="VAR_009780"
FT   VARIANT         716
FT                   /note="V -> M (in prostate cancer; gain in function;
FT                   dbSNP:rs1340026226)"
FT                   /evidence="ECO:0000269|PubMed:8145761"
FT                   /id="VAR_009781"
FT   VARIANT         718
FT                   /note="K -> E (in prostate cancer)"
FT                   /id="VAR_009782"
FT   VARIANT         721
FT                   /note="K -> E (in prostate cancer; found in bone
FT                   metastases)"
FT                   /id="VAR_009783"
FT   VARIANT         722
FT                   /note="A -> T (in prostate cancer; somatic mutation;
FT                   dbSNP:rs137852583)"
FT                   /id="VAR_009784"
FT   VARIANT         723
FT                   /note="L -> F (in AIS)"
FT                   /id="VAR_009785"
FT   VARIANT         724
FT                   /note="P -> S (in AIS)"
FT                   /id="VAR_009786"
FT   VARIANT         725
FT                   /note="G -> D (in AIS and prostate cancer)"
FT                   /id="VAR_009787"
FT   VARIANT         726
FT                   /note="F -> L (in a patient with severe hypospadias;
FT                   dbSNP:rs1555996810)"
FT                   /evidence="ECO:0000269|PubMed:10092153,
FT                   ECO:0000269|PubMed:7671849"
FT                   /id="VAR_009788"
FT   VARIANT         727
FT                   /note="R -> L (in prostate cancer; dbSNP:rs137852593)"
FT                   /evidence="ECO:0000269|PubMed:8530589"
FT                   /id="VAR_009789"
FT   VARIANT         728
FT                   /note="N -> K (in AIS; dbSNP:rs768869912)"
FT                   /evidence="ECO:0000269|PubMed:7993455"
FT                   /id="VAR_009790"
FT   VARIANT         729
FT                   /note="L -> S (in PAIS)"
FT                   /id="VAR_009791"
FT   VARIANT         731
FT                   /note="V -> M (in prostate cancer; increases transcription
FT                   activation; dbSNP:rs137852571)"
FT                   /evidence="ECO:0000269|PubMed:15525515,
FT                   ECO:0000269|PubMed:1631125, ECO:0000269|PubMed:7591265"
FT                   /id="VAR_004695"
FT   VARIANT         733
FT                   /note="D -> N (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:9252933"
FT                   /id="VAR_004696"
FT   VARIANT         733
FT                   /note="D -> Y (in AIS)"
FT                   /id="VAR_004697"
FT   VARIANT         734
FT                   /note="Q -> H (in PAIS)"
FT                   /id="VAR_009792"
FT   VARIANT         738
FT                   /note="I -> T (in PAIS)"
FT                   /evidence="ECO:0000269|PubMed:7671849"
FT                   /id="VAR_009793"
FT   VARIANT         742
FT                   /note="W -> R (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:1464650"
FT                   /id="VAR_009794"
FT   VARIANT         743
FT                   /note="M -> I (in PAIS)"
FT                   /evidence="ECO:0000269|PubMed:8824883"
FT                   /id="VAR_004698"
FT   VARIANT         743
FT                   /note="M -> V (in PAIS)"
FT                   /evidence="ECO:0000269|PubMed:7970939"
FT                   /id="VAR_009795"
FT   VARIANT         744
FT                   /note="G -> E (in AIS; dbSNP:rs137852600)"
FT                   /evidence="ECO:0000269|PubMed:11587068"
FT                   /id="VAR_013477"
FT   VARIANT         744
FT                   /note="G -> V (in PAIS and AIS; dbSNP:rs137852600)"
FT                   /evidence="ECO:0000269|PubMed:8096390,
FT                   ECO:0000269|PubMed:8325932, ECO:0000269|PubMed:9768671,
FT                   ECO:0000269|Ref.113"
FT                   /id="VAR_004699"
FT   VARIANT         745
FT                   /note="L -> F (in AIS and prostate cancer)"
FT                   /id="VAR_009796"
FT   VARIANT         746
FT                   /note="M -> T (in PAIS)"
FT                   /evidence="ECO:0000269|PubMed:7970939"
FT                   /id="VAR_009797"
FT   VARIANT         747
FT                   /note="V -> M (in PAIS)"
FT                   /id="VAR_009798"
FT   VARIANT         749
FT                   /note="A -> D (in PAIS)"
FT                   /id="VAR_009799"
FT   VARIANT         749
FT                   /note="A -> T (in prostate cancer)"
FT                   /id="VAR_009800"
FT   VARIANT         749
FT                   /note="A -> V (in prostate cancer)"
FT                   /id="VAR_009801"
FT   VARIANT         750
FT                   /note="M -> I (in prostate cancer)"
FT                   /id="VAR_009802"
FT   VARIANT         750
FT                   /note="M -> V (in PAIS and AIS; dbSNP:rs1085307685)"
FT                   /evidence="ECO:0000269|PubMed:1480178,
FT                   ECO:0000269|PubMed:1487249, ECO:0000269|PubMed:8990010"
FT                   /id="VAR_004700"
FT   VARIANT         751
FT                   /note="G -> D (in AIS; loss of androgen binding)"
FT                   /evidence="ECO:0000269|PubMed:9328206"
FT                   /id="VAR_004701"
FT   VARIANT         751
FT                   /note="G -> S (in prostate cancer)"
FT                   /id="VAR_009803"
FT   VARIANT         752
FT                   /note="W -> R (in AIS)"
FT                   /id="VAR_009804"
FT   VARIANT         753
FT                   /note="R -> Q (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:9544375,
FT                   ECO:0000269|PubMed:9698822"
FT                   /id="VAR_004702"
FT   VARIANT         755
FT                   /note="F -> L (in PAIS and prostate cancer)"
FT                   /evidence="ECO:0000269|PubMed:7981687,
FT                   ECO:0000269|PubMed:9039340"
FT                   /id="VAR_009805"
FT   VARIANT         755
FT                   /note="F -> V (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:8103398, ECO:0000269|Ref.113"
FT                   /id="VAR_004703"
FT   VARIANT         756
FT                   /note="T -> A (in prostate cancer)"
FT                   /id="VAR_009806"
FT   VARIANT         757
FT                   /note="N -> S (in PAIS; dbSNP:rs141425171)"
FT                   /id="VAR_009807"
FT   VARIANT         758
FT                   /note="V -> A (in prostate cancer)"
FT                   /evidence="ECO:0000269|PubMed:10706109"
FT                   /id="VAR_009808"
FT   VARIANT         759
FT                   /note="N -> T (in PAIS; 50% reduction in transactivation)"
FT                   /evidence="ECO:0000269|PubMed:9607727"
FT                   /id="VAR_009809"
FT   VARIANT         760
FT                   /note="S -> F (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:1480178"
FT                   /id="VAR_009810"
FT   VARIANT         760
FT                   /note="S -> P (in prostate cancer)"
FT                   /id="VAR_009811"
FT   VARIANT         763
FT                   /note="L -> F (in AIS; loss of androgen binding)"
FT                   /evidence="ECO:0000269|PubMed:9328206"
FT                   /id="VAR_004704"
FT   VARIANT         764
FT                   /note="Y -> C (in PAIS and prostate cancer; partial loss of
FT                   androgen binding; dbSNP:rs137852567)"
FT                   /evidence="ECO:0000269|PubMed:16595706,
FT                   ECO:0000269|PubMed:2010552, ECO:0000269|PubMed:7581399"
FT                   /id="VAR_004705"
FT   VARIANT         764
FT                   /note="Y -> H (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:7671849"
FT                   /id="VAR_009812"
FT   VARIANT         765
FT                   /note="F -> L (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:7970939"
FT                   /id="VAR_009813"
FT   VARIANT         766
FT                   /note="A -> T (in AIS; loss of androgen binding;
FT                   dbSNP:rs1555996863)"
FT                   /evidence="ECO:0000269|PubMed:1426313,
FT                   ECO:0000269|PubMed:9252933, ECO:0000269|PubMed:9328206,
FT                   ECO:0000269|PubMed:9856504"
FT                   /id="VAR_004707"
FT   VARIANT         766
FT                   /note="A -> V (in AIS)"
FT                   /id="VAR_009814"
FT   VARIANT         767
FT                   /note="P -> S (in AIS)"
FT                   /id="VAR_009815"
FT   VARIANT         768
FT                   /note="D -> E (in AIS)"
FT                   /evidence="ECO:0000269|Ref.113"
FT                   /id="VAR_009816"
FT   VARIANT         769
FT                   /note="L -> P (in AIS)"
FT                   /id="VAR_009817"
FT   VARIANT         772
FT                   /note="N -> H (in PAIS; dbSNP:rs886041352)"
FT                   /evidence="ECO:0000269|PubMed:7981687"
FT                   /id="VAR_009818"
FT   VARIANT         773
FT                   /note="E -> A (in PAIS)"
FT                   /evidence="ECO:0000269|PubMed:10022458"
FT                   /id="VAR_009819"
FT   VARIANT         773
FT                   /note="E -> G (in PAIS)"
FT                   /evidence="ECO:0000269|PubMed:9196614"
FT                   /id="VAR_009820"
FT   VARIANT         775
FT                   /note="R -> C (in AIS; frequent mutation; loss of androgen
FT                   binding; dbSNP:rs137852562)"
FT                   /evidence="ECO:0000269|PubMed:1609793,
FT                   ECO:0000269|PubMed:1856263, ECO:0000269|PubMed:2082179,
FT                   ECO:0000269|PubMed:8990010, ECO:0000269|PubMed:9544375"
FT                   /id="VAR_004709"
FT   VARIANT         775
FT                   /note="R -> H (in AIS and PAIS; almost complete loss of
FT                   androgen binding; dbSNP:rs137852572)"
FT                   /evidence="ECO:0000269|PubMed:1480178,
FT                   ECO:0000269|PubMed:1609793, ECO:0000269|PubMed:16595706,
FT                   ECO:0000269|PubMed:7671849"
FT                   /id="VAR_004708"
FT   VARIANT         780
FT                   /note="R -> W (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:7581399,
FT                   ECO:0000269|PubMed:7981687, ECO:0000269|PubMed:9007482"
FT                   /id="VAR_004710"
FT   VARIANT         781
FT                   /note="M -> I (in PAIS and AIS; dbSNP:rs137852589)"
FT                   /evidence="ECO:0000269|PubMed:8768864,
FT                   ECO:0000269|PubMed:8824883, ECO:0000269|PubMed:8990010"
FT                   /id="VAR_004711"
FT   VARIANT         783
FT                   /note="S -> N (in prostate cancer; somatic mutation)"
FT                   /id="VAR_009821"
FT   VARIANT         785
FT                   /note="C -> Y (in AIS; loss of androgen binding and of
FT                   transactivation)"
FT                   /evidence="ECO:0000269|PubMed:9856504"
FT                   /id="VAR_004712"
FT   VARIANT         788
FT                   /note="M -> V (in AIS; dbSNP:rs137852570)"
FT                   /evidence="ECO:0000269|PubMed:1569163"
FT                   /id="VAR_004713"
FT   VARIANT         789
FT                   /note="R -> S (in AIS; dbSNP:rs1254203917)"
FT                   /id="VAR_009822"
FT   VARIANT         791
FT                   /note="L -> F (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:7962294"
FT                   /id="VAR_009823"
FT   VARIANT         792
FT                   /note="S -> P (in prostate cancer)"
FT                   /id="VAR_009824"
FT   VARIANT         794
FT                   /note="E -> D (in dbSNP:rs1414341563)"
FT                   /evidence="ECO:0000269|PubMed:8213813"
FT                   /id="VAR_009825"
FT   VARIANT         795
FT                   /note="F -> S (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:8990010"
FT                   /id="VAR_004714"
FT   VARIANT         799
FT                   /note="Q -> E (in PAIS, AIS and prostate cancer; reduced
FT                   transcription activation; dbSNP:rs137852591)"
FT                   /evidence="ECO:0000269|PubMed:16595706,
FT                   ECO:0000269|PubMed:7511268, ECO:0000269|PubMed:7671849,
FT                   ECO:0000269|PubMed:8628719, ECO:0000269|PubMed:8824883,
FT                   ECO:0000269|PubMed:9851768"
FT                   /id="VAR_004715"
FT   VARIANT         807
FT                   /note="C -> Y (in PAIS; dbSNP:rs1064793480)"
FT                   /id="VAR_009826"
FT   VARIANT         808
FT                   /note="M -> R (in AIS; loss of transactivation)"
FT                   /evidence="ECO:0000269|PubMed:8281140"
FT                   /id="VAR_004716"
FT   VARIANT         808
FT                   /note="M -> T (in PAIS; dbSNP:rs137852592)"
FT                   /evidence="ECO:0000269|PubMed:10543676"
FT                   /id="VAR_009827"
FT   VARIANT         808
FT                   /note="M -> V (in AIS; 25% androgen binding)"
FT                   /evidence="ECO:0000269|PubMed:7581399"
FT                   /id="VAR_004717"
FT   VARIANT         813
FT                   /note="L -> F (in AIS; dbSNP:rs1555997625)"
FT                   /evidence="ECO:0000269|PubMed:10458483"
FT                   /id="VAR_009828"
FT   VARIANT         815
FT                   /note="S -> N (in AIS and PAIS)"
FT                   /id="VAR_004718"
FT   VARIANT         821
FT                   /note="G -> A (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:9610419"
FT                   /id="VAR_009829"
FT   VARIANT         822
FT                   /note="L -> V (in PAIS)"
FT                   /id="VAR_009830"
FT   VARIANT         828
FT                   /note="F -> V (in PAIS)"
FT                   /evidence="ECO:0000269|PubMed:11587068"
FT                   /id="VAR_013478"
FT   VARIANT         831
FT                   /note="L -> P (in prostate cancer)"
FT                   /id="VAR_009831"
FT   VARIANT         832
FT                   /note="R -> L (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:7633398"
FT                   /id="VAR_004719"
FT   VARIANT         832
FT                   /note="R -> Q (in AIS; loss of androgen binding;
FT                   dbSNP:rs1386577803)"
FT                   /evidence="ECO:0000269|PubMed:10458483,
FT                   ECO:0000269|PubMed:2082179, ECO:0000269|PubMed:7633398"
FT                   /id="VAR_004720"
FT   VARIANT         835
FT                   /note="Y -> C (in AIS; loss of androgen binding;
FT                   dbSNP:rs1057521122)"
FT                   /evidence="ECO:0000269|PubMed:1464650"
FT                   /id="VAR_009832"
FT   VARIANT         841
FT                   /note="R -> C (in AIS; dbSNP:rs137852577)"
FT                   /evidence="ECO:0000269|PubMed:8040309,
FT                   ECO:0000269|PubMed:8824883, ECO:0000269|PubMed:9768671"
FT                   /id="VAR_004721"
FT   VARIANT         841
FT                   /note="R -> G (in PAIS)"
FT                   /evidence="ECO:0000269|PubMed:9856504"
FT                   /id="VAR_004722"
FT   VARIANT         841
FT                   /note="R -> H (in AIS; dbSNP:rs9332969)"
FT                   /evidence="ECO:0000269|PubMed:7909256,
FT                   ECO:0000269|PubMed:8040309, ECO:0000269|PubMed:8126121,
FT                   ECO:0000269|PubMed:8205256, ECO:0000269|PubMed:8325950,
FT                   ECO:0000269|PubMed:8830623, ECO:0000269|PubMed:9039340"
FT                   /id="VAR_004723"
FT   VARIANT         841
FT                   /note="R -> S (in PAIS)"
FT                   /evidence="ECO:0000269|PubMed:10502786"
FT                   /id="VAR_009229"
FT   VARIANT         842
FT                   /note="I -> S (in PAIS)"
FT                   /id="VAR_009833"
FT   VARIANT         843
FT                   /note="I -> T (in AIS; dbSNP:rs9332970)"
FT                   /evidence="ECO:0000269|PubMed:8325950,
FT                   ECO:0000269|PubMed:9039340"
FT                   /id="VAR_004724"
FT   VARIANT         847
FT                   /note="R -> G (in prostate cancer)"
FT                   /evidence="ECO:0000269|PubMed:10706109"
FT                   /id="VAR_009834"
FT   VARIANT         855
FT                   /note="R -> K (in PAIS)"
FT                   /id="VAR_009835"
FT   VARIANT         856
FT                   /note="R -> C (in AIS; dbSNP:rs886041132)"
FT                   /evidence="ECO:0000269|PubMed:1480178,
FT                   ECO:0000269|PubMed:7581399, ECO:0000269|PubMed:9001799,
FT                   ECO:0000269|PubMed:9255042, ECO:0000269|Ref.113"
FT                   /id="VAR_004725"
FT   VARIANT         856
FT                   /note="R -> H (in AIS; strongly reduced transcription
FT                   activation; dbSNP:rs9332971)"
FT                   /evidence="ECO:0000269|PubMed:16595706,
FT                   ECO:0000269|PubMed:8097257, ECO:0000269|PubMed:8824883,
FT                   ECO:0000269|PubMed:9039340, ECO:0000269|PubMed:9106550"
FT                   /id="VAR_004726"
FT   VARIANT         857
FT                   /note="F -> L (in AIS; dbSNP:rs137852598)"
FT                   /id="VAR_009836"
FT   VARIANT         864
FT                   /note="L -> R (in AIS)"
FT                   /id="VAR_009837"
FT   VARIANT         865
FT                   /note="D -> G (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:1480178"
FT                   /id="VAR_009838"
FT   VARIANT         865
FT                   /note="D -> N (in AIS; loss of androgen binding;
FT                   dbSNP:rs1555997810)"
FT                   /evidence="ECO:0000269|PubMed:9328206"
FT                   /id="VAR_004727"
FT   VARIANT         866
FT                   /note="S -> P (in AIS; dbSNP:rs137852597)"
FT                   /id="VAR_009839"
FT   VARIANT         867
FT                   /note="V -> E (in AIS)"
FT                   /id="VAR_004728"
FT   VARIANT         867
FT                   /note="V -> L (in PAIS; dbSNP:rs137852564)"
FT                   /evidence="ECO:0000269|PubMed:1424203,
FT                   ECO:0000269|PubMed:8325950, ECO:0000269|PubMed:8446106"
FT                   /id="VAR_004729"
FT   VARIANT         867
FT                   /note="V -> M (in AIS and prostate cancer;
FT                   dbSNP:rs137852564)"
FT                   /evidence="ECO:0000269|PubMed:2082179,
FT                   ECO:0000269|PubMed:2594783, ECO:0000269|PubMed:8446106,
FT                   ECO:0000269|PubMed:9039340"
FT                   /id="VAR_004730"
FT   VARIANT         870
FT                   /note="I -> M (in PAIS; dbSNP:rs137852574)"
FT                   /evidence="ECO:0000269|PubMed:8097257,
FT                   ECO:0000269|PubMed:8824883"
FT                   /id="VAR_004731"
FT   VARIANT         871
FT                   /note="A -> G (in PAIS)"
FT                   /evidence="ECO:0000269|PubMed:9329414"
FT                   /id="VAR_009840"
FT   VARIANT         871
FT                   /note="A -> V (in PAIS; dbSNP:rs143040492)"
FT                   /evidence="ECO:0000269|PubMed:8033918"
FT                   /id="VAR_009841"
FT   VARIANT         872
FT                   /note="R -> G (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:10022458"
FT                   /id="VAR_009842"
FT   VARIANT         875
FT                   /note="H -> R (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:11587068"
FT                   /id="VAR_013479"
FT   VARIANT         875
FT                   /note="H -> Y (in prostate cancer; increases affinity for
FT                   testosterone and androgen sensitivity; increased
FT                   transcription activation; dbSNP:rs137852581)"
FT                   /evidence="ECO:0000269|PubMed:17591767"
FT                   /id="VAR_009843"
FT   VARIANT         878
FT                   /note="T -> A (in prostate cancer; found in bone
FT                   metastases; alters receptor specificity so that
FT                   transcription is activated by antiandrogens such as
FT                   cyproterone acetate; dbSNP:rs137852578)"
FT                   /evidence="ECO:0000269|PubMed:10363963,
FT                   ECO:0000269|PubMed:10569618, ECO:0000269|PubMed:1562539,
FT                   ECO:0000269|PubMed:16129672, ECO:0000269|PubMed:17311914,
FT                   ECO:0000269|PubMed:2260966, ECO:0000269|PubMed:25091737,
FT                   ECO:0000269|PubMed:8187068, ECO:0000269|PubMed:8274409,
FT                   ECO:0000269|PubMed:8827083"
FT                   /id="VAR_004732"
FT   VARIANT         878
FT                   /note="T -> S (in prostate cancer; dbSNP:rs137852580)"
FT                   /id="VAR_009844"
FT   VARIANT         880
FT                   /note="D -> Y (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:11587068"
FT                   /id="VAR_013480"
FT   VARIANT         881
FT                   /note="L -> Q (in prostate cancer)"
FT                   /id="VAR_009845"
FT   VARIANT         882
FT                   /note="L -> V (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:7641413"
FT                   /id="VAR_009846"
FT   VARIANT         887
FT                   /note="M -> V (in AIS; dbSNP:rs755226547)"
FT                   /id="VAR_009847"
FT   VARIANT         890
FT                   /note="V -> M (in AIS and PAIS; dbSNP:rs886041133)"
FT                   /evidence="ECO:0000269|PubMed:8126121,
FT                   ECO:0000269|PubMed:9160185"
FT                   /id="VAR_009848"
FT   VARIANT         891
FT                   /note="D -> N (in prostate cancer)"
FT                   /evidence="ECO:0000269|PubMed:10363963"
FT                   /id="VAR_009849"
FT   VARIANT         892
FT                   /note="F -> L (in prostate cancer)"
FT                   /id="VAR_009850"
FT   VARIANT         893
FT                   /note="P -> L (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:10221770,
FT                   ECO:0000269|PubMed:10404311, ECO:0000269|Ref.179"
FT                   /id="VAR_004733"
FT   VARIANT         896
FT                   /note="M -> T (in AIS; low androgen binding and
FT                   transactivation)"
FT                   /evidence="ECO:0000269|PubMed:16129672,
FT                   ECO:0000269|PubMed:9856504"
FT                   /id="VAR_004734"
FT   VARIANT         897
FT                   /note="A -> T (in prostate cancer)"
FT                   /id="VAR_009851"
FT   VARIANT         899
FT                   /note="I -> T (in AIS; dbSNP:rs1555998105)"
FT                   /id="VAR_009852"
FT   VARIANT         903
FT                   /note="Q -> R (in prostate cancer; dbSNP:rs137852582)"
FT                   /id="VAR_009853"
FT   VARIANT         904
FT                   /note="V -> M (in PAIS)"
FT                   /id="VAR_009854"
FT   VARIANT         905
FT                   /note="P -> H (in AIS)"
FT                   /id="VAR_009855"
FT   VARIANT         905
FT                   /note="P -> S (in AIS)"
FT                   /id="VAR_009856"
FT   VARIANT         908
FT                   /note="L -> F (in AIS; almost complete loss of
FT                   transcription activation)"
FT                   /evidence="ECO:0000269|PubMed:16595706,
FT                   ECO:0000269|PubMed:9328206"
FT                   /id="VAR_004735"
FT   VARIANT         910
FT                   /note="G -> E (in prostate cancer)"
FT                   /id="VAR_009857"
FT   VARIANT         910
FT                   /note="G -> R (in PAIS)"
FT                   /evidence="ECO:0000269|PubMed:8550758"
FT                   /id="VAR_009858"
FT   VARIANT         911
FT                   /note="K -> R (in prostate cancer)"
FT                   /evidence="ECO:0000269|PubMed:9438000"
FT                   /id="VAR_009859"
FT   VARIANT         912
FT                   /note="V -> L (in PAIS)"
FT                   /evidence="ECO:0000269|PubMed:10470409"
FT                   /id="VAR_009860"
FT   VARIANT         914
FT                   /note="P -> S (in PAIS)"
FT                   /id="VAR_004736"
FT   VARIANT         917
FT                   /note="F -> L (in AIS)"
FT                   /evidence="ECO:0000269|PubMed:9302173"
FT                   /id="VAR_009861"
FT   VARIANT         918
FT                   /note="H -> R (in AIS)"
FT                   /id="VAR_009862"
FT   VARIANT         920
FT                   /note="Q -> R (in prostate cancer)"
FT                   /id="VAR_009863"
FT   MUTAGEN         83
FT                   /note="S->A: Reduced cell growth."
FT                   /evidence="ECO:0000269|PubMed:20980437"
FT   MUTAGEN         225
FT                   /note="Y->F: Decrease of CSK-induced phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:17045208"
FT   MUTAGEN         269
FT                   /note="Y->F: Decrease of CSK-induced phosphorylation and
FT                   phosphorylation by TNK2. Complete loss of TNK2-dependent
FT                   phosphorylation; when associated with F-365."
FT                   /evidence="ECO:0000269|PubMed:17045208,
FT                   ECO:0000269|PubMed:17494760"
FT   MUTAGEN         309
FT                   /note="Y->F: Decrease of CSK-induced phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:17045208"
FT   MUTAGEN         348
FT                   /note="Y->F: Decrease of CSK-induced phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:17045208"
FT   MUTAGEN         359
FT                   /note="Y->F: Decrease of CSK-induced phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:17045208"
FT   MUTAGEN         364
FT                   /note="Y->F: Decrease of CSK-induced phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:17045208"
FT   MUTAGEN         365
FT                   /note="Y->F: Decrease of CSK-induced phosphorylation and
FT                   phosphorylation by TNK2. Complete loss of TNK2-dependent
FT                   phosphorylation; when associated with F-269."
FT                   /evidence="ECO:0000269|PubMed:17045208,
FT                   ECO:0000269|PubMed:17494760"
FT   MUTAGEN         395
FT                   /note="Y->F: Decrease of CSK-induced phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:17045208"
FT   MUTAGEN         535
FT                   /note="Y->F: Greatest decrease of CSK-induced
FT                   phosphorylation and inhibition of transcriptional activity
FT                   induced by EGF."
FT                   /evidence="ECO:0000269|PubMed:17045208"
FT   MUTAGEN         552
FT                   /note="Y->F: Decrease in CSK-induced phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:17045208"
FT   MUTAGEN         702
FT                   /note="L->A: Alters receptor specificity, so that
FT                   transcription is activated by the antiandrogen cyproterone
FT                   acetate."
FT                   /evidence="ECO:0000269|PubMed:17311914"
FT   MUTAGEN         721
FT                   /note="K->A: Loss of transcription activation in the
FT                   presence of androgen and of interaction with NCOA2."
FT                   /evidence="ECO:0000269|PubMed:15563469,
FT                   ECO:0000269|PubMed:17591767"
FT   MUTAGEN         742
FT                   /note="W->L: Strongly decreased transcription activation in
FT                   the presence of androgen."
FT                   /evidence="ECO:0000269|PubMed:16129672"
FT   MUTAGEN         846
FT                   /note="K->R: Prevents ubiquitination by RNF6. Prevents AR
FT                   transcriptional activation by RNF14 in absence of hormone."
FT                   /evidence="ECO:0000269|PubMed:19345326"
FT   MUTAGEN         848
FT                   /note="K->R: Partially prevents ubiquitination by RNF6."
FT                   /evidence="ECO:0000269|PubMed:19345326"
FT   MUTAGEN         898
FT                   /note="E->A,Q: Reduced transcription activation in the
FT                   presence of androgen."
FT                   /evidence="ECO:0000269|PubMed:15563469,
FT                   ECO:0000269|PubMed:17591767"
FT   MUTAGEN         898
FT                   /note="E->K,R: Loss of transcription activation in the
FT                   presence of androgen."
FT                   /evidence="ECO:0000269|PubMed:15563469,
FT                   ECO:0000269|PubMed:17591767"
FT   MUTAGEN         916
FT                   /note="Y->F: Decrease in CSK-induced phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:17045208"
FT   CONFLICT        168
FT                   /note="G -> A (in Ref. 5; AAA51780)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        214
FT                   /note="A -> R (in Ref. 3 and 6; AAA51771/AAA51772)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        476
FT                   /note="G -> E (in Ref. 2; AAA51775 and 13; AAA51770)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        566
FT                   /note="E -> K (in Ref. 15; AAA51774)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        635
FT                   /note="L -> P (in Ref. 19; AAB21256/AAB21257)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        676
FT                   /note="N -> I (in Ref. 19; AAB21256/AAB21257)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        811
FT                   /note="L -> M (in Ref. 5; AAA51780)"
FT                   /evidence="ECO:0000305"
FT   HELIX           22..29
FT                   /evidence="ECO:0000244|PDB:3V49"
FT   STRAND          667..669
FT                   /evidence="ECO:0000244|PDB:1XJ7"
FT   HELIX           673..681
FT                   /evidence="ECO:0000244|PDB:4OHA"
FT   STRAND          692..694
FT                   /evidence="ECO:0000244|PDB:5VO4"
FT   HELIX           698..721
FT                   /evidence="ECO:0000244|PDB:4OHA"
FT   HELIX           726..728
FT                   /evidence="ECO:0000244|PDB:4OHA"
FT   HELIX           731..758
FT                   /evidence="ECO:0000244|PDB:4OHA"
FT   STRAND          761..766
FT                   /evidence="ECO:0000244|PDB:4OHA"
FT   STRAND          769..771
FT                   /evidence="ECO:0000244|PDB:4OHA"
FT   HELIX           773..778
FT                   /evidence="ECO:0000244|PDB:4OHA"
FT   HELIX           782..797
FT                   /evidence="ECO:0000244|PDB:4OHA"
FT   HELIX           802..812
FT                   /evidence="ECO:0000244|PDB:4OHA"
FT   STRAND          815..818
FT                   /evidence="ECO:0000244|PDB:4OHA"
FT   HELIX           825..843
FT                   /evidence="ECO:0000244|PDB:4OHA"
FT   TURN            844..846
FT                   /evidence="ECO:0000244|PDB:2PKL"
FT   TURN            850..852
FT                   /evidence="ECO:0000244|PDB:2PIV"
FT   HELIX           853..883
FT                   /evidence="ECO:0000244|PDB:4OHA"
FT   HELIX           885..888
FT                   /evidence="ECO:0000244|PDB:4OHA"
FT   HELIX           894..902
FT                   /evidence="ECO:0000244|PDB:4OHA"
FT   HELIX           904..908
FT                   /evidence="ECO:0000244|PDB:4OHA"
FT   STRAND          911..914
FT                   /evidence="ECO:0000244|PDB:4OHA"
SQ   SEQUENCE   920 AA;  99188 MW;  A73432C55D39AE06 CRC64;
     MEVQLGLGRV YPRPPSKTYR GAFQNLFQSV REVIQNPGPR HPEAASAAPP GASLLLLQQQ
     QQQQQQQQQQ QQQQQQQQQQ ETSPRQQQQQ QGEDGSPQAH RRGPTGYLVL DEEQQPSQPQ
     SALECHPERG CVPEPGAAVA ASKGLPQQLP APPDEDDSAA PSTLSLLGPT FPGLSSCSAD
     LKDILSEAST MQLLQQQQQE AVSEGSSSGR AREASGAPTS SKDNYLGGTS TISDNAKELC
     KAVSVSMGLG VEALEHLSPG EQLRGDCMYA PLLGVPPAVR PTPCAPLAEC KGSLLDDSAG
     KSTEDTAEYS PFKGGYTKGL EGESLGCSGS AAAGSSGTLE LPSTLSLYKS GALDEAAAYQ
     SRDYYNFPLA LAGPPPPPPP PHPHARIKLE NPLDYGSAWA AAAAQCRYGD LASLHGAGAA
     GPGSGSPSAA ASSSWHTLFT AEEGQLYGPC GGGGGGGGGG GGGGGGGGGG GGGEAGAVAP
     YGYTRPPQGL AGQESDFTAP DVWYPGGMVS RVPYPSPTCV KSEMGPWMDS YSGPYGDMRL
     ETARDHVLPI DYYFPPQKTC LICGDEASGC HYGALTCGSC KVFFKRAAEG KQKYLCASRN
     DCTIDKFRRK NCPSCRLRKC YEAGMTLGAR KLKKLGNLKL QEEGEASSTT SPTEETTQKL
     TVSHIEGYEC QPIFLNVLEA IEPGVVCAGH DNNQPDSFAA LLSSLNELGE RQLVHVVKWA
     KALPGFRNLH VDDQMAVIQY SWMGLMVFAM GWRSFTNVNS RMLYFAPDLV FNEYRMHKSR
     MYSQCVRMRH LSQEFGWLQI TPQEFLCMKA LLLFSIIPVD GLKNQKFFDE LRMNYIKELD
     RIIACKRKNP TSCSRRFYQL TKLLDSVQPI ARELHQFTFD LLIKSHMVSV DFPEMMAEII
     SVQVPKILSG KVKPIYFHTQ
//
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