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   28-FEB-2018, entry version 259.
DE   RecName: Full=Androgen receptor;
DE   AltName: Full=Dihydrotestosterone receptor;
DE   AltName: Full=Nuclear receptor subfamily 3 group C member 4;
GN   Name=AR; Synonyms=DHTR, NR3C4;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=3216866; DOI=10.1210/mend-2-12-1265;
RA   Lubahn D.B., Joseph D.R., Sar M., Tan J., Higgs H.N., Larson R.E.,
RA   French F.S., Wilson E.M.;
RT   "The human androgen receptor: complementary deoxyribonucleic acid
RT   cloning, sequence analysis and gene expression in prostate.";
RL   Mol. Endocrinol. 2:1265-1275(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Prostate;
RX   PubMed=3174628; DOI=10.1073/pnas.85.19.7211;
RA   Chang C., Kokontis J., Liao S.;
RT   "Structural analysis of complementary DNA and amino acid sequences of
RT   human and rat androgen receptors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:7211-7215(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Prostate;
RX   PubMed=2911578; DOI=10.1073/pnas.86.1.327;
RA   Tilley W.D., Marcelli M., Wilson J.D., McPhaul M.J.;
RT   "Characterization and expression of a cDNA encoding the human androgen
RT   receptor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:327-331(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT AIS MET-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
RT   human androgen receptor gene and identification of a point mutation in
RT   a family with complete androgen insensitivity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:9534-9538(1989).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=2342476; DOI=10.1210/mend-4-3-417;
RA   Govindan M.V.;
RT   "Specific region in hormone binding domain is essential for hormone
RT   binding and trans-activation by human androgen receptor.";
RL   Mol. Endocrinol. 4:417-427(1990).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND NUCLEOTIDE SEQUENCE [MRNA]
RP   (ISOFORM 1).
RC   TISSUE=Prostate;
RX   PubMed=2293020; DOI=10.1210/mend-4-8-1105;
RA   Marcelli M., Tilley W.D., Wilson C.M., Griffin J.E., Wilson J.D.,
RA   McPhaul M.J.;
RT   "Definition of the human androgen receptor gene structure permits the
RT   identification of mutations that cause androgen resistance: premature
RT   termination of the receptor protein at amino acid residue 588 causes
RT   complete androgen resistance.";
RL   Mol. Endocrinol. 4:1105-1116(1990).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2),
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=15634333; DOI=10.1111/j.1432-1033.2004.04395.x;
RA   Ahrens-Fath I., Politz O., Geserick C., Haendler B.;
RT   "Androgen receptor function is modulated by the tissue-specific AR45
RT   variant.";
RL   FEBS J. 272:74-84(2005).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), VARIANT GLN-57,
RP   FUNCTION (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.,
RA   Kong X., Melamed J., Tepper C.G., Kung H.J., Brodie A.M., Edwards J.,
RA   Qiu Y.;
RT   "A novel androgen receptor splice variant is up-regulated during
RT   prostate cancer progression and promotes androgen depletion-resistant
RT   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.,
RA   Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA   Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA   Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA   Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA   Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA   Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA   Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA   Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA   Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA   Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA   Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA   Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA   Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA   Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA   Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA   Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA   Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA   Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA   Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA   Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA   Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA   Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA   Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA   de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA   Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA   Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA   Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA   Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA   Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA   Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA   Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA   Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA   Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA   Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA   Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA   Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA   Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA   Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA   Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA   Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA   Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA   Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA   Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [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
RT   project: 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.,
RA   van der Korput J.A.G.M., Brinkmann A.O., Trapman J.;
RT   "The N-terminal domain of the human androgen receptor is encoded by
RT   one, large exon.";
RL   Mol. Cell. Endocrinol. 61:257-262(1989).
RN   [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
RT   androgen 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
RT   androgen receptor.";
RL   Biochem. Biophys. Res. Commun. 153:241-248(1988).
RN   [16]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 537-541; 587-591; 626-630;
RP   722-726; 770-774; 814-817 AND 866-870.
RX   PubMed=2546571; DOI=10.1677/jme.0.002R001;
RA   Kuiper G.G., Faber P.W., van Rooij H.C., van der Korput J.A.,
RA   Ris-Stalpers C., Klaassen P., Trapman J., Brinkmann A.O.;
RT   "Structural organization of the human androgen receptor gene.";
RL   J. Mol. Endocrinol. 2:R1-R4(1989).
RN   [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
RT   of the androgen receptor gene causes complete androgen insensitivity
RT   in two siblings with receptor-positive androgen resistance.";
RL   Mol. Endocrinol. 7:861-869(1993).
RN   [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
RT   to the X chromosome.";
RL   Science 240:327-330(1988).
RN   [19]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 630-724, AND VARIANTS AIS ASN-696
RP   AND 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
RT   human androgen receptor leads to a functionally inactive protein with
RT   altered 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
RT   (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.,
RA   Brufsky A., Talcott J., Hennekens C.H., Kantoff P.W.;
RT   "The CAG repeat within the androgen receptor gene and its relationship
RT   to prostate cancer.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:3320-3323(1997).
RN   [22]
RP   ERRATUM.
RA   Giovannucci E., Stampfer M.J., Krithivas K., Brown M., Dahl D.,
RA   Brufsky A., Talcott J., Hennekens C.H., Kantoff P.W.;
RL   Proc. Natl. Acad. Sci. U.S.A. 94:8272-8272(1997).
RN   [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,
RT   in 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-
RT   dependent 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
RT   identified androgen receptor polyglutamine region-associated
RT   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-
RT   like 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.,
RA   Rennie P.S.;
RT   "RanBPM, a nuclear protein that interacts with and regulates
RT   transcriptional activity of androgen receptor and glucocorticoid
RT   receptor.";
RL   J. Biol. Chem. 277:48020-48027(2002).
RN   [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.,
RA   Takayanagi R., Nawata H.;
RT   "Activation function-1 domain of androgen receptor contributes to the
RT   interaction between subnuclear splicing factor compartment and nuclear
RT   receptor compartment. Identification of the p102 U5 small nuclear
RT   ribonucleoprotein particle-binding protein as a coactivator for the
RT   receptor.";
RL   J. Biol. Chem. 277:30031-30039(2002).
RN   [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.,
RA   Lim B., Sun Z.;
RT   "hZimp10 is an androgen receptor co-activator and forms a complex with
RT   SUMO-1 at replication foci.";
RL   EMBO J. 22:6101-6114(2003).
RN   [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
RT   antagonizes 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.,
RA   Bokoch G.M.;
RT   "Mechanism of p21-activated kinase 6-mediated inhibition of androgen
RT   receptor signaling.";
RL   J. Biol. Chem. 279:1922-1931(2004).
RN   [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
RT   activity of 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.,
RA   Sun Z.;
RT   "hZimp7, a novel PIAS-like protein, enhances androgen receptor-
RT   mediated transcription and interacts with SWI/SNF-like BAF
RT   complexes.";
RL   Mol. Endocrinol. 19:2915-2929(2005).
RN   [40]
RP   PHOSPHORYLATION AT TYR-225; TYR-269; TYR-309; TYR-348; TYR-359;
RP   TYR-364; TYR-365; TYR-395; TYR-535; TYR-552 AND TYR-916, MUTAGENESIS
RP   OF TYR-225; TYR-269; TYR-309; TYR-348; TYR-359; TYR-364; TYR-365;
RP   TYR-395; TYR-535; TYR-552 AND TYR-916, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=17045208; DOI=10.1016/j.ccr.2006.08.021;
RA   Guo Z., Dai B., Jiang T., Xu K., Xie Y., Kim O., Nesheiwat I.,
RA   Kong X., Melamed J., Handratta V.D., Njar V.C., Brodie A.M., Yu L.-R.,
RA   Veenstra T.D., Chen H., Qiu Y.;
RT   "Regulation of androgen receptor activity by tyrosine
RT   phosphorylation.";
RL   Cancer Cell 10:309-319(2006).
RN   [41]
RP   ERRATUM.
RA   Guo Z., Dai B., Jiang T., Xu K., Xie Y., Kim O., Nesheiwat I.,
RA   Kong X., Melamed J., Handratta V.D., Njar V.C., Brodie A.M., Yu L.-R.,
RA   Veenstra T.D., Chen H., Qiu Y.;
RL   Cancer Cell 11:97-97(2007).
RN   [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.,
RA   Shi X.B., deVere White R.W., Chen H.W., Tepper C.G., Kung H.J.;
RT   "Male germ cell-associated kinase, a male-specific kinase regulated by
RT   androgen, is a coactivator of androgen receptor in prostate cancer
RT   cells.";
RL   Cancer Res. 66:8439-8447(2006).
RN   [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
RT   a 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.,
RA   Ferdinand A.S., Kim J., Chung L.W.K., Adam R.M., Ray S.K.,
RA   Leiter A.B., Richie J.P., Liu B.C.-S., Freeman M.R.;
RT   "The zinc finger protein Ras-responsive element binding protein-1 is a
RT   coregulator of the androgen receptor: implications for the role of the
RT   Ras pathway in enhancing androgenic signaling in prostate cancer.";
RL   Mol. Endocrinol. 21:2056-2070(2007).
RN   [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,
RP   AND 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.,
RA   Mohler J.L., Earp H.S., Whang Y.E.;
RT   "Activated Cdc42-associated kinase Ack1 promotes prostate cancer
RT   progression via androgen receptor tyrosine phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8438-8443(2007).
RN   [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.,
RA   Shinohara N., Nonomura K., Hatakeyama S.;
RT   "TRIM68 regulates ligand-dependent transcription of androgen receptor
RT   in prostate cancer cells.";
RL   Cancer Res. 68:3486-3494(2008).
RN   [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.,
RA   Neesen J., Bubendorf L., Glass A.G., Jarry H., Auber B., Burfeind P.;
RT   "Leupaxin, a novel coactivator of the androgen receptor, is expressed
RT   in prostate cancer and plays a role in adhesion and invasion of
RT   prostate carcinoma cells.";
RL   Mol. Endocrinol. 22:1606-1621(2008).
RN   [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.,
RA   Tanaka J., Imamura M., Hatakeyama S.;
RT   "TRIM24 mediates ligand-dependent activation of androgen receptor and
RT   is repressed by a bromodomain-containing protein, BRD7, in prostate
RT   cancer cells.";
RL   Biochim. Biophys. Acta 1793:1828-1836(2009).
RN   [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.,
RA   Chen H., Li W., Chen H., Kong X., Melamed J., Fang S., Xiao Z.,
RA   Veenstra T.D., Qiu Y.;
RT   "Regulation of androgen receptor transcriptional activity and
RT   specificity by RNF6-induced ubiquitination.";
RL   Cancer Cell 15:270-282(2009).
RN   [52]
RP   FUNCTION IN AR KINASE, PHOSPHORYLATION AT SER-83 BY CDK9, MUTAGENESIS
RP   OF 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.,
RA   Mollah S.A., Shabanowitz J., Hunt D.F., Xenarios I., Hahn W.C.,
RA   Conaway M., Carey M.F., Gioeli D.;
RT   "CDK9 regulates AR promoter selectivity and cell growth through serine
RT   81 phosphorylation.";
RL   Mol. Endocrinol. 24:2267-2280(2010).
RN   [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 ENZYME REGULATION.
RX   PubMed=20623637; DOI=10.1002/pros.21163;
RA   Mahajan K., Challa S., Coppola D., Lawrence H., Luo Y., Gevariya H.,
RA   Zhu W., Chen Y.A., Lawrence N.J., Mahajan N.P.;
RT   "Effect of Ack1 tyrosine kinase inhibitor on ligand-independent
RT   androgen receptor activity.";
RL   Prostate 70:1274-1285(2010).
RN   [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   INTERACTION WITH CRY1.
RX   PubMed=22170608; DOI=10.1038/nature10700;
RA   Lamia K.A., Papp S.J., Yu R.T., Barish G.D., Uhlenhaut N.H.,
RA   Jonker J.W., Downes M., Evans R.M.;
RT   "Cryptochromes mediate rhythmic repression of the glucocorticoid
RT   receptor.";
RL   Nature 480:552-556(2011).
RN   [57]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [58]
RP   PALMITOYLATION.
RX   PubMed=22031296; DOI=10.1091/mbc.E11-07-0638;
RA   Pedram A., Razandi M., Deschenes R.J., Levin E.R.;
RT   "DHHC-7 and -21 are palmitoylacyltransferases for sex steroid
RT   receptors.";
RL   Mol. Biol. Cell 23:188-199(2012).
RN   [59]
RP   INTERACTION WITH CCAR1 AND GATA2.
RX   PubMed=23887938; DOI=10.1093/nar/gkt644;
RA   Seo W.Y., Jeong B.C., Yu E.J., Kim H.J., Kim S.H., Lim J.E.,
RA   Kwon G.Y., Lee H.M., Kim J.H.;
RT   "CCAR1 promotes chromatin loading of androgen receptor (AR)
RT   transcription complex by stabilizing the association between AR and
RT   GATA2.";
RL   Nucleic Acids Res. 41:8526-8536(2013).
RN   [60]
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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [61]
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.,
RA   Egner U., Carrondo M.A.;
RT   "Structural evidence for ligand specificity in the binding domain of
RT   the human androgen receptor. Implications for pathogenic gene
RT   mutations.";
RL   J. Biol. Chem. 275:26164-26171(2000).
RN   [62]
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
RT   prostate cancer.";
RL   J. Med. Chem. 45:1439-1446(2002).
RN   [63]
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
RT   function dominance.";
RL   Mol. Cell 16:425-438(2004).
RN   [64]
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
RP   LYS-721 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.,
RA   Guy R.K.;
RT   "The molecular mechanisms of coactivator utilization in ligand-
RT   dependent transactivation by the androgen receptor.";
RL   J. Biol. Chem. 280:8060-8068(2005).
RN   [65]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 665-920 IN COMPLEXES WITH
RP   NONSTEROIDAL LIGANDS, MUTAGENESIS OF TRP-742, CHARACTERIZATION OF
RP   VARIANT PROSTATE CANCER ALA-878, AND CHARACTERIZATION OF VARIANT AIS
RP   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
RT   androgen receptor.";
RL   J. Biol. Chem. 280:37747-37754(2005).
RN   [66]
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.,
RA   Labrie F., Breton R.;
RT   "Comparison of crystal structures of human androgen receptor ligand-
RT   binding domain complexed with various agonists reveals molecular
RT   determinants responsible for binding affinity.";
RL   Protein Sci. 15:987-999(2006).
RN   [67]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 672-919 IN COMPLEX WITH
RP   NR0B2.
RX   PubMed=18007036; DOI=10.1107/S0907444907045702;
RA   Jouravel N., Sablin E., Arnold L.A., Guy R.K., Fletterick R.J.;
RT   "Interaction between the androgen receptor and a segment of its
RT   corepressor SHP.";
RL   Acta Crystallogr. D 63:1198-1200(2007).
RN   [68]
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-
RT   induced conformational changes and structure-based drug design.";
RL   J. Biol. Chem. 282:13648-13655(2007).
RN   [69]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 663-919 OF WILD-TYPE AND
RP   MUTANT TYR-875 IN COMPLEX WITH TESTOSTERONE AND NCOA2, ACTIVATION BY
RP   THE N-TERMINAL MODULATING DOMAIN, INTERACTION WITH NCOA2 AND MAGEA11,
RP   FUNCTION, MUTAGENESIS OF LYS-721 AND GLU-898, AND CHARACTERIZATION OF
RP   VARIANT 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
RT   and dihydrotestosterone.";
RL   J. Biol. Chem. 282:25801-25816(2007).
RN   [70]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 655-920 IN COMPLEX WITH
RP   EM5744.
RX   PubMed=17711855; DOI=10.1074/jbc.M705524200;
RA   Cantin L., Faucher F., Couture J.-F., de Jesus-Tran K.P., Legrand P.,
RA   Ciobanu L.C., Frechette Y., Labrecque R., Singh S.M., Labrie F.,
RA   Breton R.;
RT   "Structural characterization of the human androgen receptor ligand-
RT   binding domain complexed with EM5744, a rationally designed steroidal
RT   ligand bearing a bulky chain directed toward helix 12.";
RL   J. Biol. Chem. 282:30910-30919(2007).
RN   [71]
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   [72]
RP   REVIEW ON VARIANTS.
RX   PubMed=1458719;
RA   Pinsky L., Trifiro M.A., Kaufman M., Beitel L.K., Mhatre A.,
RA   Kazemi-Esfarjani P., Sabbaghian N., Lumbroso R., Alvarado C.,
RA   Vasiliou M., Gottlieb B.;
RT   "Androgen resistance due to mutation of the androgen receptor.";
RL   Clin. Invest. Med. 15:456-472(1992).
RN   [73]
RP   REVIEW ON VARIANTS AIS.
RX   PubMed=8339746; DOI=10.1007/BF02125442;
RA   Brown T.R., Scherer P.A., Chang Y.-T., Migeon C.J., Ghirri P.,
RA   Murono K., Zhou Z.;
RT   "Molecular genetics of human androgen insensitivity.";
RL   Eur. J. Pediatr. 152 Suppl. 2:S62-S69(1993).
RN   [74]
RP   REVIEW ON VARIANTS.
RX   PubMed=8240973; DOI=10.1016/0960-0760(93)90178-Y;
RA   Sultan C., Lumbroso S., Poujol N., Belon C., Boudon C.,
RA   Lobaccaro J.-M.;
RT   "Mutations of androgen receptor gene in androgen insensitivity
RT   syndromes.";
RL   J. Steroid Biochem. Mol. Biol. 46:519-530(1993).
RN   [75]
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   [76]
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   [77]
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   [78]
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   [79]
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.,
RA   Brinkmann A.O., Mulder E.;
RT   "A mutation in the ligand binding domain of the androgen receptor of
RT   human LNCaP cells affects steroid binding characteristics and response
RT   to anti-androgens.";
RL   Biochem. Biophys. Res. Commun. 173:534-540(1990).
RN   [80]
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   [81]
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
RT   receptor at amino acid 772 (Arg-->Cys) results from a combination of
RT   decreased messenger ribonucleic acid levels and impairment of receptor
RT   function.";
RL   J. Clin. Endocrinol. Metab. 73:318-325(1991).
RN   [82]
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.,
RA   McPhaul M.J.;
RT   "A mutation in the DNA-binding domain of the androgen receptor gene
RT   causes complete testicular feminization in a patient with receptor-
RT   positive androgen resistance.";
RL   J. Clin. Invest. 87:1123-1126(1991).
RN   [83]
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
RT   androgen therapy.";
RL   J. Clin. Invest. 87:1413-1421(1991).
RN   [84]
RP   POLY-GLN REGION EXPANSION, AND INVOLVEMENT IN SPINAL AND BULBAR
RP   MUSCULAR ATROPHY.
RX   PubMed=2062380; DOI=10.1038/352077a0;
RA   la Spada A.R., Wilson E.M., Lubahn D.B., Harding A.E., Fischbeck K.H.;
RT   "Androgen receptor gene mutations in X-linked spinal and bulbar
RT   muscular atrophy.";
RL   Nature 352:77-79(1991).
RN   [85]
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
RT   androgen receptor causes complete androgen insensitivity with
RT   different receptor phenotypes.";
RL   Am. J. Hum. Genet. 51:143-155(1992).
RN   [86]
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
RT   with partial androgen insensitivity syndrome.";
RL   Clin. Endocrinol. (Oxf.) 37:214-220(1992).
RN   [87]
RP   VARIANT AIS THR-766.
RX   PubMed=1426313;
RA   Sweet C.R., Behzadian M.A., McDonough P.G.;
RT   "A unique point mutation in the androgen receptor gene in a family
RT   with complete androgen insensitivity syndrome.";
RL   Fertil. Steril. 58:703-707(1992).
RN   [88]
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
RT   gene in a family with complete androgen insensitivity syndrome
RT   (CAIS).";
RL   Hum. Genet. 90:311-312(1992).
RN   [89]
RP   VARIANTS AIS, AND VARIANTS PAIS.
RX   PubMed=1307250; DOI=10.1093/hmg/1.7.497;
RA   Batch J.A., Williams D.M., Davies H.R., Brown B.D., Evans B.A.J.,
RA   Hughes I.A., Patterson M.N.;
RT   "Androgen receptor gene mutations identified by SSCP in fourteen
RT   subjects with androgen insensitivity syndrome.";
RL   Hum. Mol. Genet. 1:497-503(1992).
RN   [90]
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-
RT   binding domain of human androgen receptor leads to complete androgen
RT   insensitivity syndrome.";
RL   J. Clin. Endocrinol. Metab. 74:1152-1157(1992).
RN   [91]
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   [92]
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   [93]
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
RT   ligand binding domain which affects steroid binding characteristics
RT   and response to antiandrogens.";
RL   J. Steroid Biochem. Mol. Biol. 41:665-669(1992).
RN   [94]
RP   VARIANTS AIS TYR-560 AND ARG-577, AND VARIANTS PAIS GLY-598 AND
RP   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
RT   androgen receptor are a frequent cause of receptor-binding positive
RT   androgen resistance.";
RL   Mol. Endocrinol. 6:409-415(1992).
RN   [95]
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
RT   complete androgen insensitivity: rapid detection by a modified
RT   denaturing gradient gel electrophoresis technique.";
RL   Mol. Endocrinol. 6:1909-1920(1992).
RN   [96]
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
RT   with breast cancer and Reifenstein syndrome.";
RL   Nat. Genet. 2:132-134(1992).
RN   [97]
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   [98]
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   [99]
RP   VARIANT AIS PHE-582.
RX   PubMed=8224266;
RA   Lumbroso S., Lobaccaro J.-M., Belon C., Martin D., Chaussain J.-L.,
RA   Sultan C.;
RT   "A new mutation within the deoxyribonucleic acid-binding domain of the
RT   androgen receptor gene in a family with complete androgen
RT   insensitivity syndrome.";
RL   Fertil. Steril. 60:814-819(1993).
RN   [100]
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
RT   receptor gene of a family with complete androgen insensitivity
RT   syndrome.";
RL   Hum. Mol. Genet. 2:1041-1043(1993).
RN   [101]
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.,
RA   Bringer J., Lesimple T., Namer M., Cutuli B.F., Pujol H., Sultan C.;
RT   "Androgen receptor gene mutation in male breast cancer.";
RL   Hum. Mol. Genet. 2:1799-1802(1993).
RN   [102]
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
RT   causing complete androgen insensitivity: the mutated receptor fails to
RT   transactivate but binds to DNA in vitro.";
RL   Hum. Mol. Genet. 2:1809-1812(1993).
RN   [103]
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-
RT   binding domain of the human androgen receptor leads to Reifenstein
RT   syndrome.";
RL   J. Clin. Endocrinol. Metab. 77:103-107(1993).
RN   [104]
RP   VARIANTS AIS LYS-682 AND THR-843, AND VARIANTS PAIS HIS-841 AND
RP   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.,
RA   Wolfe H.J., Yandell D.W.;
RT   "Single strand conformation polymorphism analysis of androgen receptor
RT   gene mutations in patients with androgen insensitivity syndromes:
RT   application for diagnosis, genetic counseling, and therapy.";
RL   J. Clin. Endocrinol. Metab. 77:262-266(1993).
RN   [105]
RP   VARIANTS PAIS HIS-856 AND 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   [106]
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   [107]
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   [108]
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
RT   androgen receptor causes complete or partial androgen insensitivity,
RT   respectively with distinct androgen receptor phenotypes.";
RL   Mol. Endocrinol. 7:37-46(1993).
RN   [109]
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.,
RA   Radmayr C., Eberle J., Bartsch G., Klocker H.;
RT   "Mutant androgen receptor detected in an advanced-stage prostatic
RT   carcinoma is activated by adrenal androgens and progesterone.";
RL   Mol. Endocrinol. 7:1541-1550(1993).
RN   [110]
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   [111]
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   [112]
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   [113]
RP   VARIANT PROSTATE CANCER ALA-878.
RX   PubMed=8187068;
RA   Gaddipati J.P., McLeod D.G., Heidenberg H.B., Sesterhenn I.A.,
RA   Finger M.J., Moul J.W., Srivastava S.;
RT   "Frequent detection of codon 877 mutation in the androgen receptor
RT   gene in advanced prostate cancers.";
RL   Cancer Res. 54:2861-2864(1994).
RN   [114]
RP   VARIANT PAIS TRP-569.
RX   PubMed=7910529;
RA   Lobaccaro J.-M., Belon C., Lumbroso S., Olewniczack G.,
RA   Carre-Pigeon F., Job J.C., Chaussain J.L., Toublanc J.E., Sultan C.;
RT   "Molecular prenatal diagnosis of partial androgen insensitivity
RT   syndrome based on the Hind III polymorphism of the androgen receptor
RT   gene.";
RL   Clin. Endocrinol. (Oxf.) 40:297-302(1994).
RN   [115]
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
RT   insensitivity (Reifenstein syndrome).";
RL   Eur. J. Endocrinol. 130:327-332(1994).
RN   [116]
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
RT   insensitivity syndrome associated with a thermolabile androgen
RT   receptor.";
RL   Eur. J. Endocrinol. 130:569-574(1994).
RN   [117]
RP   VARIANT PAIS VAL-871.
RX   PubMed=8033918; DOI=10.1007/BF01956409;
RA   Hiort O., Klauber G., Cendron M., Sinnecker G.H., Keim L.,
RA   Schwinger E., Wolfe H.J., Yandell D.W.;
RT   "Molecular characterization of the androgen receptor gene in boys with
RT   hypospadias.";
RL   Eur. J. Pediatr. 153:317-321(1994).
RN   [118]
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
RT   caused by a delD690 mutation in the androgen receptor (AR) gene
RT   (Abstract #244).";
RL   Horm. Res. 41:117-117(1994).
RN   [119]
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.,
RA   Lumbroso R., Alvarado C., McGillivray B., Trifiro M.A., Pinsky L.;
RT   "Complete androgen insensitivity due to mutations in the probable
RT   alpha-helical segments of the DNA-binding domain in the human androgen
RT   receptor.";
RL   Hum. Mol. Genet. 3:21-27(1994).
RN   [120]
RP   VARIANTS PAIS SER-583; TYR-605; ALA-709; LEU-755 AND HIS-772, AND
RP   VARIANT 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   [121]
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
RT   in the steroid binding domain and a Cys-->Phe substitution in the
RT   second zinc finger of the androgen receptor.";
RL   Hum. Mol. Genet. 3:1169-1170(1994).
RN   [122]
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
RT   androgen insensitivity syndrome.";
RL   J. Clin. Endocrinol. Metab. 78:513-522(1994).
RN   [123]
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   [124]
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.,
RA   DiGeorge A.M., Killinger D.W., Trifiro M.A., Pinsky L.;
RT   "Substitution of arginine-839 by cysteine or histidine in the androgen
RT   receptor causes different receptor phenotypes in cultured cells and
RT   coordinate degrees of clinical androgen resistance.";
RL   J. Clin. Invest. 94:546-554(1994).
RN   [125]
RP   VARIANTS AIS, AND VARIANTS PAIS.
RX   PubMed=7929841; DOI=10.1172/JCI117507;
RA   Marcelli M., Zoppi S., Wilson C.M., Griffin J.E., McPhaul M.J.;
RT   "Amino acid substitutions in the hormone-binding domain of the human
RT   androgen receptor alter the stability of the hormone receptor
RT   complex.";
RL   J. Clin. Invest. 94:1642-1650(1994).
RN   [126]
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
RT   due to mutation in androgen receptor gene.";
RL   Lancet 344:826-827(1994).
RN   [127]
RP   VARIANTS AIS HIS-616 AND LEU-765, AND VARIANTS PAIS VAL-743 AND
RP   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
RT   mutations and pedigree analysis in families with X-linked androgen
RT   insensitivity.";
RL   Pediatr. Res. 36:227-234(1994).
RN   [128]
RP   VARIANT AIS HIS-841.
RX   PubMed=8830623;
RA   Imai A., Ohno T., Iida K., Ohsuye K., Okano Y., Tamaya T.;
RT   "A frame-shift mutation of the androgen receptor gene in a patient
RT   with receptor-negative complete testicular feminization: comparison
RT   with a single base substitution in a receptor-reduced incomplete
RT   form.";
RL   Ann. Clin. Biochem. 32:482-486(1995).
RN   [129]
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   [130]
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
RT   polymorphism and direct detection of two novel mutations in the
RT   androgen receptor gene.";
RL   Clin. Endocrinol. (Oxf.) 43:69-77(1995).
RN   [131]
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   [132]
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   [133]
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
RT   830 of the androgen receptor that cause complete androgen
RT   insensitivity in three families.";
RL   Hum. Mol. Genet. 4:515-521(1995).
RN   [134]
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
RT   androgen insensitivity syndrome in a large Hutterite kindred.";
RL   Hum. Mutat. 5:28-33(1995).
RN   [135]
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
RT   acid substitutions in the androgen receptor steroid-binding domain.";
RL   Hum. Mutat. 6:152-162(1995).
RN   [136]
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
RT   amino-acid-sequence requirements for transactivation and ligand
RT   binding.";
RL   Int. J. Cancer 63:544-550(1995).
RN   [137]
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   [138]
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   [139]
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   [140]
RP   VARIANTS PROSTATE CANCER.
RX   PubMed=7723794; DOI=10.1056/NEJM199505253322101;
RA   Taplin M.-E., Bubley G.J., Shuster T.D., Frantz M.E., Spooner A.E.,
RA   Ogata G.K., Keer H.N., Balk S.P.;
RT   "Mutation of the androgen-receptor gene in metastatic androgen-
RT   independent prostate cancer.";
RL   N. Engl. J. Med. 332:1393-1398(1995).
RN   [141]
RP   VARIANTS AIS AND PAIS.
RX   PubMed=8723113;
RX   DOI=10.1002/(SICI)1096-8628(19960503)63:1<218::AID-AJMG38>3.0.CO;2-P;
RA   Hiort O., Sinnecker G.H., Holterhus P.M., Nitsche E.M., Kruse K.;
RT   "The clinical and molecular spectrum of androgen insensitivity
RT   syndromes.";
RL   Am. J. Med. Genet. 63:218-222(1996).
RN   [142]
RP   VARIANTS PROSTATE CANCER.
RX   PubMed=9816170;
RA   Tilley W.D., Buchanan G., Hickey T.E., Bentel J.M.;
RT   "Mutations in the androgen receptor gene are associated with
RT   progression of human prostate cancer to androgen independence.";
RL   Clin. Cancer Res. 2:277-285(1996).
RN   [143]
RP   VARIANTS PAIS GLN-608; THR-611; LEU-755; HIS-841; THR-843 AND HIS-856,
RP   AND 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.,
RA   Stockklauser K., Brinkmann A.O., Schweikert H.-U., Spindler K.D.;
RT   "Clinical and biochemical investigations and molecular analysis of
RT   subjects with mutations in the androgen receptor gene.";
RL   Clin. Endocrinol. (Oxf.) 45:733-739(1996).
RN   [144]
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
RT   receptor.";
RL   Clin. Genet. 50:202-205(1996).
RN   [145]
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   [146]
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
RT   mutation at amino acid 907 (Gly-->Arg) that results in decreased
RT   ligand binding affinity and reduced androgen receptor messenger
RT   ribonucleic acid levels.";
RL   J. Clin. Endocrinol. Metab. 81:236-243(1996).
RN   [147]
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
RT   gene causes complete androgen resistance.";
RL   J. Clin. Endocrinol. Metab. 81:1984-1988(1996).
RN   [148]
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.,
RA   Morel Y., Schaison G.;
RT   "Different phenotypes in a family with androgen insensitivity caused
RT   by the same M780I point mutation in the androgen receptor gene.";
RL   J. Clin. Endocrinol. Metab. 81:2994-2998(1996).
RN   [149]
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   [150]
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   [151]
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.,
RA   Gonzales E.T. Jr., Roth D.R., Lamb D.J.;
RT   "Androgen receptor gene mutations are rarely associated with isolated
RT   penile hypospadias.";
RL   J. Urol. 156:828-831(1996).
RN   [152]
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.,
RA   Sultan C.;
RT   "Molecular modeling and in vitro investigations of the human androgen
RT   receptor DNA-binding domain: application for the study of two
RT   mutations.";
RL   Mol. Cell. Endocrinol. 116:137-147(1996).
RN   [153]
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-
RT   binding domain of the androgen receptor.";
RL   Mol. Cell. Endocrinol. 120:15-24(1996).
RN   [154]
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   [155]
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   [156]
RP   VARIANT AIS HIS-856.
RX   PubMed=9106550;
RA   Boehmer A.L.M., Brinkmann A.O., Niermeijer M.F., Bakker L.,
RA   Halley D.J.J., Drop S.L.S.;
RT   "Germ-line and somatic mosaicism in the androgen insensitivity
RT   syndrome: implications for genetic counseling.";
RL   Am. J. Hum. Genet. 60:1003-1006(1997).
RN   [157]
RP   VARIANT PROSTATE CANCER ALA-684.
RX   PubMed=9000575;
RA   Koivisto P., Kononen J., Palmberg C., Tammela T., Hyytinen E.,
RA   Isola J., Trapman J., Cleutjens K., Noordzij A., Visakorpi T.,
RA   Kallioniemi O.-P.;
RT   "Androgen receptor gene amplification: a possible molecular mechanism
RT   for androgen deprivation therapy failure in prostate cancer.";
RL   Cancer Res. 57:314-319(1997).
RN   [158]
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.,
RA   Edwards C.R., Hargreaves T.B., Wu F.C.;
RT   "Correlation of clinical, endocrine and molecular abnormalities with
RT   in vivo responses to high-dose testosterone in patients with partial
RT   androgen insensitivity syndrome.";
RL   Clin. Endocrinol. (Oxf.) 46:497-506(1997).
RN   [159]
RP   VARIANT AIS MET-890.
RX   PubMed=9160185;
RA   Essawi M., Gad Y.Z., el-Rouby O., Temtamy S.A., Sabour Y.A.,
RA   el-Awady M.K.;
RT   "Molecular analysis of androgen resistance syndromes in Egyptian
RT   patients.";
RL   Dis. Markers 13:99-105(1997).
RN   [160]
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
RT   sensitivity in patients with mutations of the androgen receptor
RT   gene.";
RL   Eur. J. Pediatr. 156:7-14(1997).
RN   [161]
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
RT   androgen insensitivity.";
RL   Hum. Mutat. 9:57-61(1997).
RN   [162]
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.,
RA   Kotake T., Sugimura T., Nagao M.;
RT   "Genetic alterations of androgen receptor gene in Japanese human
RT   prostate cancer.";
RL   Jpn. J. Clin. Oncol. 27:389-393(1997).
RN   [163]
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   [164]
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   [165]
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.,
RA   Mildenberger H., Brodehl J.;
RT   "Etiologic classification of severe hypospadias: implications for
RT   prognosis and management.";
RL   J. Pediatr. 131:386-392(1997).
RN   [166]
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.,
RA   Lee T.Y.;
RT   "Complete androgen insensitivity syndrome. Molecular characterization
RT   in two Chinese women.";
RL   J. Reprod. Med. 42:424-428(1997).
RN   [167]
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   [168]
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
RT   in 2 patients with androgen insensitivity syndrome.";
RL   J. Urol. 158:1553-1556(1997).
RN   [169]
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   [170]
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   [171]
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   [172]
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
RT   androgen receptor in a case with complete androgen insensitivity
RT   syndrome.";
RL   Gynecol. Endocrinol. 12:75-82(1998).
RN   [173]
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.,
RA   Pousette A., Chibalin A.V., Arvidsson S., Tiulpakov A.,
RA   Semitcheva T.V., Peterkova V., Hagenfeldt K., Ritzen E.M., Wedell A.;
RT   "Functional characterisation of mutations in the ligand-binding domain
RT   of the androgen receptor gene in patients with androgen insensitivity
RT   syndrome.";
RL   Hum. Genet. 103:529-531(1998).
RN   [174]
RP   VARIANT AIS VAL-696.
RX   PubMed=9554754;
RA   Doerk T., Schnieders F., Jakubiczka S., Wieacker P.,
RA   Schroeder-Kurth T., Schmidtke J.;
RT   "A new missense substitution at a mutational hot spot of the androgen
RT   receptor in siblings with complete androgen insensitivity syndrome.";
RL   Hum. Mutat. 11:337-339(1998).
RN   [175]
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   [176]
RP   VARIANT AIS LEU-893.
RA   Knoke I., Jakubiczka S., Rohrer T., Hanimann B., Werder E.A.,
RA   Wieacker P.;
RT   "Single amino acid substitution in the hormone-binding domain of the
RT   androgen receptor in a family with complete androgen insensitivity
RT   syndrome (CAIS).";
RL   Hum. Mutat. 12:220-220(1998).
RN   [177]
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
RT   domain of the androgen receptor.";
RL   J. Clin. Endocrinol. Metab. 83:1173-1176(1998).
RN   [178]
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
RT   syndrome.";
RL   J. Clin. Endocrinol. Metab. 83:3597-3603(1998).
RN   [179]
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.,
RA   Ng S.C., Yong E.L.;
RT   "Azoospermia associated with a mutation in the ligand-binding domain
RT   of an androgen receptor displaying normal ligand binding, but
RT   defective trans-activation.";
RL   J. Clin. Endocrinol. Metab. 83:4303-4309(1998).
RN   [180]
RP   VARIANTS AIS.
RX   PubMed=9627582; DOI=10.1016/S0022-3476(98)70387-7;
RA   Hiort O., Sinnecker G.H., Holterhus P.M., Nitsche E.M., Kruse K.;
RT   "Inherited and de novo androgen receptor gene mutations: investigation
RT   of single-case families.";
RL   J. Pediatr. 132:939-943(1998).
RN   [181]
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
RT   three dimensional structure of the androgen receptor ligand-binding
RT   domain.";
RL   Mol. Cell. Endocrinol. 137:41-50(1998).
RN   [182]
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   [183]
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.,
RA   Rajeshkumar B., Balk S.P.;
RT   "Selection for androgen receptor mutations in prostate cancers treated
RT   with androgen antagonist.";
RL   Cancer Res. 59:2511-2515(1999).
RN   [184]
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
RT   Brazilian family with partial androgen insensitivity syndrome.";
RL   Hum. Mutat. 14:353-353(1999).
RN   [185]
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   [186]
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   [187]
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
RT   and analysis of androgen receptor gene mutation.";
RL   Int. J. Urol. 6:327-330(1999).
RN   [188]
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.,
RA   Pinsky L., Trifiro M.A.;
RT   "Discordant measures of androgen-binding kinetics in two mutant
RT   androgen receptors causing mild or partial androgen insensitivity,
RT   respectively.";
RL   J. Clin. Endocrinol. Metab. 84:805-810(1999).
RN   [189]
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
RT   cancer.";
RL   J. Pathol. 189:559-563(1999).
RN   [190]
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.,
RA   Feldman D.;
RT   "Two mutations identified in the androgen receptor of the new human
RT   prostate cancer cell line MDA PCa 2a.";
RL   J. Urol. 162:2192-2199(1999).
RN   [191]
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
RT   androgen receptor gene mutation.";
RL   Lancet 354:1444-1445(1999).
RN   [192]
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
RT   C-terminal alpha-helix of the ligand binding domain containing the AF-
RT   2 transcriptional activating function core is associated with complete
RT   androgen insensitivity.";
RL   Mol. Cell. Endocrinol. 148:47-53(1999).
RN   [193]
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.,
RA   Weigel N.L.;
RT   "A C619Y mutation in the human androgen receptor causes inactivation
RT   and mislocalization of the receptor with concomitant sequestration of
RT   SRC-1.";
RL   Mol. Endocrinol. 13:2065-2075(1999).
RN   [194]
RP   ERRATUM.
RA   Nazareth L.V., Stenoien D.L., Bingman W.E. III, James A.J., Wu C.,
RA   Zhang Y., Edwards D.P., Mancini M., Marcelli M., Lamb D.J.,
RA   Weigel N.L.;
RL   Mol. Endocrinol. 14:544-544(2000).
RN   [195]
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.,
RA   Sippell W.G., Brinkmann A.O., Kruse K., Hiort O.;
RT   "Clinical and molecular spectrum of somatic mosaicism in androgen
RT   insensitivity syndrome.";
RL   Pediatr. Res. 46:684-690(1999).
RN   [196]
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
RT   receptor gene of five Japanese patients with androgen insensitivity
RT   syndrome.";
RL   Tohoku J. Exp. Med. 187:263-272(1999).
RN   [197]
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   [198]
RP   VARIANTS PROSTATE CANCER ALA-576; ARG-581; VAL-587; TYR-620; ALA-758
RP   AND GLY-847.
RX   PubMed=10706109;
RA   Marcelli M., Ittmann M., Mariani S., Sutherland R.W., Nigam R.,
RA   Murthy L., Zhao Y., DiConcini D., Puxeddu E., Esen A., Eastham J.,
RA   Weigel N.L., Lamb D.J.;
RT   "Androgen receptor mutations in prostate cancer.";
RL   Cancer Res. 60:944-949(2000).
RN   [199]
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
RT   analysis in 278 clinical cases reported as androgen insensitivity
RT   syndrome.";
RL   J. Clin. Endocrinol. Metab. 85:658-665(2000).
RN   [200]
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   [201]
RP   INVOLVEMENT IN ANDROGENETIC ALOPECIA, AND POLYMORPHISM OF POLY-GLY
RP   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
RT   pattern baldness.";
RL   J. Invest. Dermatol. 116:452-455(2001).
RN   [202]
RP   VARIANT AIS TYR-706.
RX   PubMed=11744994;
RA   Sills E.S., Sholes T.E., Perloe M., Kaplan C.R., Davis J.G.,
RA   Tucker M.J.;
RT   "Characterization of a novel receptor mutation A->T at exon 4 in
RT   complete androgen insensitivity syndrome and a carrier sibling via
RT   bidirectional polymorphism sequence analysis.";
RL   Int. J. Mol. Med. 9:45-48(2002).
RN   [203]
RP   INVOLVEMENT IN ANDROGENETIC ALOPECIA, AND POLYMORPHISM OF POLY-GLY
RP   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.,
RA   Metzen C., Heyn U., Schweiger N., Betz R.C., Blaumeiser B., Hampe J.,
RA   Schreiber S., Schulze T.G., Hennies H.C., Schumacher J., Propping P.,
RA   Ruzicka T., Cichon S., Wienker T.F., Kruse R., Noethen M.M.;
RT   "Genetic variation in the human androgen receptor gene is the major
RT   determinant of common early-onset androgenetic alopecia.";
RL   Am. J. Hum. Genet. 77:140-148(2005).
RN   [204]
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   [205]
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.,
RA   Sandrini R., 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   [206]
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
RT   to disrupted interaction between the N- and C-terminal domains.";
RL   J. Mol. Endocrinol. 36:361-368(2006).
RN   [207]
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.,
RA   Fennell T., O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B.,
RA   Tukiainen T., Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K.,
RA   Zhao F., Zou J., Pierce-Hoffman E., Berghout J., Cooper D.N.,
RA   Deflaux N., DePristo M., Do R., Flannick J., Fromer M., Gauthier L.,
RA   Goldstein J., Gupta N., Howrigan D., Kiezun A., Kurki M.I.,
RA   Moonshine A.L., Natarajan P., Orozco L., Peloso G.M., Poplin R.,
RA   Rivas M.A., Ruano-Rubio V., Rose S.A., Ruderfer D.M., Shakir K.,
RA   Stenson P.D., Stevens C., Thomas B.P., Tiao G., Tusie-Luna M.T.,
RA   Weisburd B., Won H.H., Yu D., Altshuler D.M., Ardissino D.,
RA   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.,
RA   Laakso M., McCarroll S., McCarthy M.I., McGovern D., McPherson R.,
RA   Neale B.M., Palotie A., Purcell S.M., Saleheen D., Scharf J.M.,
RA   Sklar P., Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C.,
RA   Wilson J.G., 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
CC       transcription factors that regulate eukaryotic gene expression and
CC       affect cellular proliferation and differentiation in target
CC       tissues. Transcription factor activity is modulated by bound
CC       coactivator and corepressor proteins. Transcription activation is
CC       down-regulated by NR0B2. Activated, but not phosphorylated, by
CC       HIPK3 and ZIPK/DAPK3. {ECO:0000269|PubMed:14664718,
CC       ECO:0000269|PubMed:15563469, ECO:0000269|PubMed:17591767,
CC       ECO:0000269|PubMed:17911242, ECO:0000269|PubMed:18084323,
CC       ECO:0000269|PubMed:19345326, ECO:0000269|PubMed:20980437}.
CC   -!- FUNCTION: Isoform 3 and isoform 4 lack the C-terminal ligand-
CC       binding domain and may therefore constitutively activate the
CC       transcription of a specific set of genes independently of steroid
CC       hormones. {ECO:0000269|PubMed:19244107}.
CC   -!- ENZYME REGULATION: AIM-100 (4-amino-5,6-biaryl-furo[2,3-
CC       d]pyrimidine) suppresses TNK2-mediated phosphorylation at Tyr-269.
CC       Inhibits the binding of the Tyr-269 phosphorylated form to
CC       androgen-responsive enhancers (AREs) and its transcriptional
CC       activity. {ECO:0000269|PubMed:20623637}.
CC   -!- SUBUNIT: Binds DNA as a homodimer. Part of a ternary complex
CC       containing AR, EFCAB6/DJBP and PARK7. Interacts with HIPK3 and
CC       NR0B2 in the presence of androgen. The ligand binding domain
CC       interacts with KAT7/HBO1 in the presence of dihydrotestosterone.
CC       Interacts with EFCAB6/DJBP, PELP1, PQBP1, RANBP9, RBAK, SPDEF,
CC       SRA1, TGFB1I1 and RREB1. Interacts with ZMIZ1/ZIMP10 and
CC       ZMIZ2/ZMIP7 which both enhance its transactivation activity.
CC       Interacts with SLC30A9 and RAD54L2/ARIP4. Interacts via the
CC       ligand-binding domain with LXXLL and FXXLF motifs from NCOA1,
CC       NCOA2, NCOA3, NCOA4 and MAGEA11. The AR N-terminal poly-Gln region
CC       binds Ran resulting in enhancement of AR-mediated transactivation.
CC       Ran-binding decreases as the poly-Gln length increases. Interacts
CC       with HIP1 (via coiled coil domain). Interacts (via ligand-binding
CC       domain) with TRIM68. Interacts with TNK2. Interacts with USP26.
CC       Interacts with RNF6. Interacts (regulated by RNF6 probably through
CC       polyubiquitination) with RNF14; regulates AR transcriptional
CC       activity. Interacts with PRMT2 and TRIM24. Interacts with RACK1.
CC       Interacts with RANBP10; this interaction enhances
CC       dihydrotestosterone-induced AR transcriptional activity. Interacts
CC       with PRPF6 in a hormone-independent way; this interaction enhances
CC       dihydrotestosterone-induced AR transcriptional activity. Interacts
CC       with STK4/MST1. Interacts with ZIPK/DAPK3. Interacts with LPXN.
CC       Interacts with MAK. Part of a complex containing AR, MAK and
CC       NCOA3. Interacts with CRY1. Interacts with CCAR1 and GATA2.
CC       Interacts with ZNF318 (By similarity).
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:20980437, ECO:0000269|PubMed:21512132,
CC       ECO:0000269|PubMed:22170608, ECO:0000269|PubMed:23887938}.
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       Cytoplasm {ECO:0000269|PubMed:12958311,
CC       ECO:0000269|PubMed:17587566, ECO:0000269|PubMed:19244107}.
CC       Note=Predominantly cytoplasmic in unligated form but translocates
CC       to the nucleus upon ligand-binding. Can also translocate to the
CC       nucleus in unligated form in the presence of RACK1.
CC       {ECO:0000269|PubMed:12958311, ECO:0000269|PubMed:17587566}.
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         Note=Minor isoform up-regulated in prostate cancer cells.
CC         {ECO:0000269|PubMed:19244107};
CC       Name=4; Synonyms=AR4;
CC         IsoId=P10275-4; Sequence=VSP_058167, VSP_058169;
CC         Note=Minor isoform identified in prostate cancer cells.
CC         {ECO:0000269|PubMed:19244107};
CC   -!- TISSUE SPECIFICITY: Isoform 2 is mainly expressed in heart and
CC       skeletal muscle (PubMed:15634333). Isoform 3 is expressed by basal
CC       and stromal cells of prostate (at protein level)
CC       (PubMed:19244107). {ECO:0000269|PubMed:15634333,
CC       ECO:0000269|PubMed:19244107}.
CC   -!- DOMAIN: Composed of three domains: a modulating N-terminal domain,
CC       a DNA-binding domain and a C-terminal ligand-binding domain. In
CC       the presence of bound steroid the ligand-binding domain interacts
CC       with the N-terminal modulating domain, and thereby activates AR
CC       transcription factor activity. Agonist binding is required for
CC       dimerization and binding to target DNA. The transcription factor
CC       activity of the complex formed by ligand-activated AR and DNA is
CC       modulated by interactions with coactivator and corepressor
CC       proteins. Interaction with RANBP9 is mediated by both the N-
CC       terminal domain and the DNA-binding domain. Interaction with
CC       EFCAB6/DJBP is mediated by the DNA-binding domain.
CC   -!- PTM: Sumoylated on Lys-388 (major) and Lys-521. Ubiquitinated.
CC       Deubiquitinated by USP26. 'Lys-6' and 'Lys-27'-linked
CC       polyubiquitination by RNF6 modulates AR transcriptional activity
CC       and specificity. {ECO:0000269|PubMed:11121022,
CC       ECO:0000269|PubMed:19345326, ECO:0000269|PubMed:20501646}.
CC   -!- PTM: Phosphorylated in prostate cancer cells in response to
CC       several growth factors including EGF. Phosphorylation is induced
CC       by c-Src kinase (CSK). Tyr-535 is one of the major phosphorylation
CC       sites and an increase in phosphorylation and Src kinase activity
CC       is associated with prostate cancer progression. Phosphorylation by
CC       TNK2 enhances the DNA-binding and transcriptional activity and may
CC       be responsible for androgen-independent progression of prostate
CC       cancer. Phosphorylation at Ser-83 by CDK9 regulates AR promoter
CC       selectivity and cell growth. Phosphorylation by PAK6 leads to AR-
CC       mediated transcription inhibition. {ECO:0000269|PubMed:14573606,
CC       ECO:0000269|PubMed:17045208, ECO:0000269|PubMed:17494760,
CC       ECO:0000269|PubMed:20623637, ECO:0000269|PubMed:20980437,
CC       ECO:0000269|PubMed:21512132}.
CC   -!- PTM: Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is
CC       required for plasma membrane targeting and for rapid intracellular
CC       signaling via ERK and AKT kinases and cAMP generation.
CC       {ECO:0000269|PubMed:22031296}.
CC   -!- POLYMORPHISM: The poly-Gln region of AR is highly polymorphic and
CC       the number of Gln varies in the population (from 17 to 26). A
CC       smaller size of the poly-Gln region may be associated with the
CC       development of prostate cancer. {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
CC       from 24 to 31 Gly. A poly-Gly region shorter or equal to 23 may be
CC       associated with the development of androgenetic alopecia.
CC       {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
CC       resistance to androgen. Affected males have female external
CC       genitalia, female breast development, blind vagina, absent uterus
CC       and female adnexa, and abdominal or inguinal testes, despite a
CC       normal 46,XY karyotype. {ECO:0000269|PubMed:10022458,
CC       ECO:0000269|PubMed:10221692, ECO:0000269|PubMed:10221770,
CC       ECO:0000269|PubMed:10404311, ECO:0000269|PubMed:10458483,
CC       ECO:0000269|PubMed:10571951, ECO:0000269|PubMed:10590024,
CC       ECO:0000269|PubMed:10690872, ECO:0000269|PubMed:11587068,
CC       ECO:0000269|PubMed:11744994, ECO:0000269|PubMed:1307250,
CC       ECO:0000269|PubMed:1316540, ECO:0000269|PubMed:1426313,
CC       ECO:0000269|PubMed:1430233, ECO:0000269|PubMed:1464650,
CC       ECO:0000269|PubMed:14756668, ECO:0000269|PubMed:1480178,
CC       ECO:0000269|PubMed:1487249, ECO:0000269|PubMed:1569163,
CC       ECO:0000269|PubMed:1609793, ECO:0000269|PubMed:16129672,
CC       ECO:0000269|PubMed:16595706, ECO:0000269|PubMed:1775137,
CC       ECO:0000269|PubMed:1999491, ECO:0000269|PubMed:2082179,
CC       ECO:0000269|PubMed:2594783, ECO:0000269|PubMed:7537149,
CC       ECO:0000269|PubMed:7581399, ECO:0000269|PubMed:7633398,
CC       ECO:0000269|PubMed:7641413, ECO:0000269|PubMed:7671849,
CC       ECO:0000269|PubMed:7929841, ECO:0000269|PubMed:7962294,
CC       ECO:0000269|PubMed:7970939, ECO:0000269|PubMed:7981687,
CC       ECO:0000269|PubMed:7981689, ECO:0000269|PubMed:7993455,
CC       ECO:0000269|PubMed:8040309, ECO:0000269|PubMed:8096390,
CC       ECO:0000269|PubMed:8103398, ECO:0000269|PubMed:8162033,
CC       ECO:0000269|PubMed:8224266, ECO:0000269|PubMed:8281140,
CC       ECO:0000269|PubMed:8325950, ECO:0000269|PubMed:8339746,
CC       ECO:0000269|PubMed:8413310, ECO:0000269|PubMed:8446106,
CC       ECO:0000269|PubMed:8626869, ECO:0000269|PubMed:8647313,
CC       ECO:0000269|PubMed:8683794, ECO:0000269|PubMed:8723113,
CC       ECO:0000269|PubMed:8768864, ECO:0000269|PubMed:8809734,
CC       ECO:0000269|PubMed:8830623, ECO:0000269|PubMed:8918984,
CC       ECO:0000269|PubMed:8990010, ECO:0000269|PubMed:9001799,
CC       ECO:0000269|PubMed:9007482, ECO:0000269|PubMed:9039340,
CC       ECO:0000269|PubMed:9106550, ECO:0000269|PubMed:9160185,
CC       ECO:0000269|PubMed:9252933, ECO:0000269|PubMed:9255042,
CC       ECO:0000269|PubMed:9302173, ECO:0000269|PubMed:9328206,
CC       ECO:0000269|PubMed:9544375, ECO:0000269|PubMed:9554754,
CC       ECO:0000269|PubMed:9610419, ECO:0000269|PubMed:9627582,
CC       ECO:0000269|PubMed:9698822, ECO:0000269|PubMed:9851768,
CC       ECO:0000269|PubMed:9856504, ECO:0000269|Ref.110,
CC       ECO:0000269|Ref.176}. Note=The disease is caused by mutations
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Spinal and bulbar muscular atrophy X-linked 1 (SMAX1)
CC       [MIM:313200]: An X-linked recessive form of spinal muscular
CC       atrophy. Spinal muscular atrophy refers to a group of
CC       neuromuscular disorders characterized by degeneration of the
CC       anterior horn cells of the spinal cord, leading to symmetrical
CC       muscle weakness and atrophy. SMAX1 occurs only in men. Age at
CC       onset is usually in the third to fifth decade of life, but earlier
CC       involvement has been reported. It is characterized by slowly
CC       progressive limb and bulbar muscle weakness with fasciculations,
CC       muscle atrophy, and gynecomastia. The disorder is clinically
CC       similar to classic forms of autosomal spinal muscular atrophy.
CC       {ECO:0000269|PubMed:15851746}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry. Caused by
CC       trinucleotide CAG repeat expansion. In SMAX1 patients the number
CC       of Gln ranges from 38 to 62. Longer expansions result in earlier
CC       onset and more severe clinical manifestations of the disease.
CC   -!- DISEASE: Note=Defects in AR may play a role in metastatic prostate
CC       cancer. The mutated receptor stimulates prostate growth and
CC       metastases development despite of androgen ablation. This
CC       treatment can reduce primary and metastatic lesions probably by
CC       inducing apoptosis of tumor cells when they express the wild-type
CC       receptor.
CC   -!- DISEASE: Androgen insensitivity, partial (PAIS) [MIM:312300]: A
CC       disorder that is characterized by hypospadias, hypogonadism,
CC       gynecomastia, genital ambiguity, normal XY karyotype, and a
CC       pedigree pattern consistent with X-linked recessive inheritance.
CC       Some patients present azoospermia or severe oligospermia without
CC       other clinical manifestations. {ECO:0000269|PubMed:10022458,
CC       ECO:0000269|PubMed:10221692, ECO:0000269|PubMed:10470409,
CC       ECO:0000269|PubMed:10502786, ECO:0000269|PubMed:10543676,
CC       ECO:0000269|PubMed:11587068, ECO:0000269|PubMed:1303262,
CC       ECO:0000269|PubMed:1307250, ECO:0000269|PubMed:1316540,
CC       ECO:0000269|PubMed:1424203, ECO:0000269|PubMed:1430233,
CC       ECO:0000269|PubMed: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.118}. 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
CC       are thought to be weakly associated with nuclear components;
CC       hormone binding greatly increases receptor affinity. The hormone-
CC       receptor complex appears to recognize discrete DNA sequences
CC       upstream of transcriptional start sites.
CC   -!- MISCELLANEOUS: Transcriptional activity is enhanced by binding to
CC       RANBP9.
CC   -!- MISCELLANEOUS: The level of tyrosine phosphorylation may serve as
CC       a diagnostic tool to predict patient outcome in response to
CC       hormone-ablation therapy. Inhibition of tyrosine phosphorylation
CC       may be an effective intervention target for hormone-refractory
CC       prostate cancer.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC       subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Androgen receptor gene mutations database;
CC       URL="http://androgendb.mcgill.ca";
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/ARID685chXq12.html";
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Androgen receptor entry;
CC       URL="https://en.wikipedia.org/wiki/Androgen_receptor";
CC   -!- WEB RESOURCE: Name=X-chromosome gene database, androgen receptor
CC       (AR); Note=Leiden Open Variation Database (LOVD);
CC       URL="http://www.lovd.nl/AR";
CC   ---------------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; CAI43080.1; -; Genomic_DNA.
DR   EMBL; AL158016; CAI43080.1; JOINED; Genomic_DNA.
DR   EMBL; AL356358; CAI43080.1; JOINED; Genomic_DNA.
DR   EMBL; AL158016; CAI40853.1; -; Genomic_DNA.
DR   EMBL; AL049564; CAI40853.1; JOINED; Genomic_DNA.
DR   EMBL; AL356358; CAI40853.1; JOINED; Genomic_DNA.
DR   EMBL; AL356358; CAI40496.1; -; Genomic_DNA.
DR   EMBL; AL049564; CAI40496.1; JOINED; Genomic_DNA.
DR   EMBL; AL158016; CAI40496.1; JOINED; Genomic_DNA.
DR   EMBL; CH471132; EAX05380.1; -; Genomic_DNA.
DR   EMBL; BC132975; AAI32976.1; -; mRNA.
DR   EMBL; L29496; AAA51770.1; -; mRNA.
DR   EMBL; U16371; AAB60346.1; -; Genomic_DNA.
DR   EMBL; M20260; AAA51774.1; -; mRNA.
DR   EMBL; S79366; AAB21256.2; -; Genomic_DNA.
DR   EMBL; S79366; AAB21257.2; -; Genomic_DNA.
DR   CCDS; CCDS14387.1; -. [P10275-1]
DR   CCDS; CCDS43965.1; -. [P10275-2]
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   UniGene; Hs.76704; -.
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   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   DisProt; DP00492; -.
DR   ProteinModelPortal; P10275; -.
DR   SMR; P10275; -.
DR   BioGrid; 106862; 265.
DR   CORUM; P10275; -.
DR   DIP; DIP-125N; -.
DR   ELM; P10275; -.
DR   IntAct; P10275; 131.
DR   MINT; P10275; -.
DR   STRING; 9606.ENSP00000363822; -.
DR   BindingDB; P10275; -.
DR   ChEMBL; CHEMBL1871; -.
DR   DrugBank; DB02932; (2r)-N-[4-Cyano-3-(Trifluoromethyl)Phenyl]-3-[(4-Fluorophenyl)Sulfonyl]-2-Hydroxy-2-Methylpropanamide.
DR   DrugBank; DB07422; (2S)-2-hydroxy-2-methyl-N-[4-nitro-3-(trifluoromethyl)phenyl]-3-(pentafluorophenoxy)propanamide.
DR   DrugBank; DB07419; (2S)-3-(4-chloro-3-fluorophenoxy)-N-[4-cyano-3-(trifluoromethyl)phenyl]-2-hydroxy-2-methylpropanamide.
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; DB07454; (R)-3-BROMO-2-HYDROXY-2-METHYL-N-[4-NITRO-3-(TRIFLUOROMETHYL)PHENYL]PROPANAMIDE.
DR   DrugBank; DB01128; Bicalutamide.
DR   DrugBank; DB01541; Boldenone.
DR   DrugBank; DB01564; Calusterone.
DR   DrugBank; DB04839; Cyproterone acetate.
DR   DrugBank; DB01406; Danazol.
DR   DrugBank; DB01481; Delta1-dihydrotestosterone.
DR   DrugBank; DB02901; Dihydrotestosterone.
DR   DrugBank; DB01395; Drospirenone.
DR   DrugBank; DB00858; Drostanolone.
DR   DrugBank; DB08899; Enzalutamide.
DR   DrugBank; DB13155; Esculin.
DR   DrugBank; DB00687; Fludrocortisone.
DR   DrugBank; DB02266; Flufenamic Acid.
DR   DrugBank; DB01185; Fluoxymesterone.
DR   DrugBank; DB00499; Flutamide.
DR   DrugBank; DB01026; Ketoconazole.
DR   DrugBank; DB00367; Levonorgestrel.
DR   DrugBank; DB05234; LGD2941.
DR   DrugBank; DB05094; MDV3100.
DR   DrugBank; DB06710; Methyltestosterone.
DR   DrugBank; DB02998; Methyltrienolone.
DR   DrugBank; DB08804; Nandrolone decanoate.
DR   DrugBank; DB00984; Nandrolone phenpropionate.
DR   DrugBank; DB00665; Nilutamide.
DR   DrugBank; DB09389; Norgestrel.
DR   DrugBank; DB00621; Oxandrolone.
DR   DrugBank; DB06412; Oxymetholone.
DR   DrugBank; DB01708; Prasterone.
DR   DrugBank; DB07769; S-3-(4-FLUOROPHENOXY)-2-HYDROXY-2-METHYL-N-[4-NITRO-3-(TRIFLUOROMETHYL)PHENYL]PROPANAMIDE.
DR   DrugBank; DB00421; Spironolactone.
DR   DrugBank; DB00624; Testosterone.
DR   DrugBank; DB01420; Testosterone Propionate.
DR   DrugBank; DB08867; Ulipristal.
DR   GuidetoPHARMACOLOGY; 628; -.
DR   SwissLipids; SLP:000001553; -.
DR   iPTMnet; P10275; -.
DR   PhosphoSitePlus; P10275; -.
DR   SwissPalm; P10275; -.
DR   BioMuta; AR; -.
DR   DMDM; 113830; -.
DR   MaxQB; P10275; -.
DR   PaxDb; P10275; -.
DR   PeptideAtlas; P10275; -.
DR   PRIDE; P10275; -.
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   H-InvDB; HIX0056152; -.
DR   HGNC; HGNC:644; AR.
DR   HPA; CAB000001; -.
DR   HPA; CAB065764; -.
DR   HPA; HPA065701; -.
DR   MalaCards; AR; -.
DR   MIM; 300068; 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; 440; Familial hypospadias.
DR   Orphanet; 481; Kennedy disease.
DR   Orphanet; 90797; Partial androgen insensitivity syndrome.
DR   PharmGKB; PA57; -.
DR   eggNOG; KOG3575; Eukaryota.
DR   eggNOG; ENOG410XRZC; LUCA.
DR   GeneTree; ENSGT00760000118887; -.
DR   HOVERGEN; HBG007583; -.
DR   InParanoid; P10275; -.
DR   KO; K08557; -.
DR   OMA; YGDMRLE; -.
DR   OrthoDB; EOG091G032J; -.
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-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   PMAP-CutDB; B1AKD7; -.
DR   PRO; PR:P10275; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   Bgee; ENSG00000169083; -.
DR   CleanEx; HS_AR; -.
DR   ExpressionAtlas; P10275; baseline and differential.
DR   Genevisible; P10275; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
DR   GO; GO: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:0043234; C:protein complex; IDA:MGI.
DR   GO; GO:0005497; F:androgen binding; IDA:UniProtKB.
DR   GO; GO:0004882; F:androgen receptor activity; IDA:UniProtKB.
DR   GO; GO:0051117; F:ATPase binding; IDA:MGI.
DR   GO; GO:0008013; F:beta-catenin binding; IDA:BHF-UCL.
DR   GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR   GO; GO:0003700; F:DNA binding transcription factor activity; IDA:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0004879; F:nuclear receptor activity; IDA:BHF-UCL.
DR   GO; GO:0070974; F:POU domain binding; IEA:Ensembl.
DR   GO; GO:0046983; F:protein dimerization activity; NAS:UniProtKB.
DR   GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0001085; F:RNA polymerase II transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR   GO; GO:0008134; F:transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
DR   GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
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:0016049; P:cell growth; NAS:UniProtKB.
DR   GO; GO:0008283; P:cell proliferation; NAS:UniProtKB.
DR   GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR   GO; GO: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 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 from RNA polymerase II promoter; IMP:CAFA.
DR   GO; GO:0045597; P:positive regulation of cell differentiation; IMP:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IDA:BHF-UCL.
DR   GO; GO: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; IMP: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 from RNA polymerase II promoter; IDA:UniProtKB.
DR   GO; GO:0045945; P:positive regulation of transcription from RNA polymerase III promoter; IDA:BHF-UCL.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0030850; P:prostate gland development; NAS:UniProtKB.
DR   GO; GO: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:0051259; P:protein oligomerization; IDA:MGI.
DR   GO; GO:0050790; P:regulation of catalytic activity; IEA:Ensembl.
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:0007548; P:sex differentiation; NAS:UniProtKB.
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   GO; GO:0006810; P:transport; TAS:ProtInc.
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; Complete proteome;
KW   Cytoplasm; Disease mutation; DNA-binding; Isopeptide bond;
KW   Lipid-binding; Lipoprotein; Metal-binding; Neurodegeneration; Nucleus;
KW   Palmitate; Phosphoprotein; Polymorphism; Pseudohermaphroditism;
KW   Receptor; Reference proteome; Steroid-binding; Transcription;
KW   Transcription regulation; Triplet repeat expansion; Ubl conjugation;
KW   Zinc; Zinc-finger.
FT   CHAIN         1    920       Androgen receptor.
FT                                /FTId=PRO_0000053704.
FT   DOMAIN      669    900       NR LBD. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01189}.
FT   DNA_BIND    560    632       Nuclear receptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00407}.
FT   ZN_FING     560    580       NR C4-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00407}.
FT   ZN_FING     596    620       NR C4-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00407}.
FT   REGION        1    587       Interaction with ZNF318.
FT                                {ECO:0000250|UniProtKB:P19091}.
FT   REGION        1    559       Modulating.
FT   REGION      552    919       Interaction with LPXN.
FT                                {ECO:0000269|PubMed:18451096}.
FT   REGION      572    662       Interaction with HIPK3. {ECO:0000250}.
FT   REGION      592    919       Interaction with CCAR1.
FT                                {ECO:0000269|PubMed:23887938}.
FT   REGION      625    919       Interaction with KAT7.
FT                                {ECO:0000269|PubMed:10930412}.
FT   COMPBIAS     58    120       Gln-rich.
FT   COMPBIAS     58     80       Poly-Gln.
FT   COMPBIAS     86     91       Poly-Gln.
FT   COMPBIAS    195    199       Poly-Gln.
FT   COMPBIAS    374    383       Poly-Pro.
FT   COMPBIAS    398    404       Poly-Ala.
FT   COMPBIAS    451    473       Poly-Gly.
FT   BINDING     706    706       Androgen.
FT   BINDING     753    753       Androgen.
FT   BINDING     878    878       Androgen.
FT   SITE        721    721       Interaction with coactivator LXXL motif.
FT   SITE        898    898       Interaction with coactivator FXXLF motif.
FT   MOD_RES      83     83       Phosphoserine; by CDK9.
FT                                {ECO:0000269|PubMed:20980437}.
FT   MOD_RES      96     96       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES     225    225       Phosphotyrosine; by CSK.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MOD_RES     258    258       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     269    269       Phosphotyrosine; by CSK and TNK2.
FT                                {ECO:0000269|PubMed:17045208,
FT                                ECO:0000269|PubMed:17494760,
FT                                ECO:0000269|PubMed:20623637}.
FT   MOD_RES     309    309       Phosphotyrosine; by CSK.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MOD_RES     348    348       Phosphotyrosine; by CSK.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MOD_RES     359    359       Phosphotyrosine; by CSK.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MOD_RES     364    364       Phosphotyrosine; by CSK.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MOD_RES     365    365       Phosphotyrosine; by CSK and TNK2.
FT                                {ECO:0000269|PubMed:17045208,
FT                                ECO:0000269|PubMed:17494760}.
FT   MOD_RES     395    395       Phosphotyrosine; by CSK.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MOD_RES     535    535       Phosphotyrosine; by CSK.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MOD_RES     552    552       Phosphotyrosine; by CSK.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MOD_RES     651    651       Phosphoserine; by STK4/MST1.
FT                                {ECO:0000269|PubMed:21512132}.
FT   MOD_RES     916    916       Phosphotyrosine; by CSK.
FT                                {ECO:0000269|PubMed:17045208}.
FT   CROSSLNK    388    388       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT                                {ECO:0000269|PubMed:11121022}.
FT   CROSSLNK    521    521       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT                                {ECO:0000269|PubMed:11121022}.
FT   CROSSLNK    846    846       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000269|PubMed:19345326}.
FT   CROSSLNK    848    848       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000269|PubMed:19345326}.
FT   VAR_SEQ       1    532       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_036889.
FT   VAR_SEQ     533    539       GPYGDMR -> MILWLHS (in isoform 2).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_036890.
FT   VAR_SEQ     629    644       ARKLKKLGNLKLQEEG -> EKFRVGNCKHLKMTRP (in
FT                                isoform 3).
FT                                /FTId=VSP_058166.
FT   VAR_SEQ     630    648       RKLKKLGNLKLQEEGEASS -> AVVVSERILRVFGVSEWL
FT                                P (in isoform 4).
FT                                /FTId=VSP_058167.
FT   VAR_SEQ     645    920       Missing (in isoform 3).
FT                                /FTId=VSP_058168.
FT   VAR_SEQ     649    920       Missing (in isoform 4).
FT                                /FTId=VSP_058169.
FT   VARIANT       2      2       E -> K (in PAIS; dbSNP:rs104894742).
FT                                {ECO:0000269|PubMed:8823308}.
FT                                /FTId=VAR_004679.
FT   VARIANT      54     54       L -> S (in prostate cancer).
FT                                /FTId=VAR_004680.
FT   VARIANT      57     57       L -> Q (in prostate cancer;
FT                                dbSNP:rs78686797).
FT                                {ECO:0000269|PubMed:19244107}.
FT                                /FTId=VAR_004681.
FT   VARIANT      64     64       Q -> R (in prostate cancer).
FT                                /FTId=VAR_009711.
FT   VARIANT     114    114       Q -> H (in prostate cancer).
FT                                /FTId=VAR_009712.
FT   VARIANT     182    182       K -> R (in prostate cancer).
FT                                /FTId=VAR_009713.
FT   VARIANT     196    196       Q -> R (in AIS).
FT                                {ECO:0000269|PubMed:9255042}.
FT                                /FTId=VAR_009224.
FT   VARIANT     207    207       S -> R (in dbSNP:rs374549047).
FT                                {ECO:0000269|PubMed:8213813}.
FT                                /FTId=VAR_009714.
FT   VARIANT     216    216       G -> R (functional polymorphism; 20%
FT                                lower transactivation capacity;
FT                                dbSNP:rs199554641).
FT                                {ECO:0000269|PubMed:27535533,
FT                                ECO:0000269|PubMed:9788719}.
FT                                /FTId=VAR_009715.
FT   VARIANT     257    257       L -> P (in AIS).
FT                                {ECO:0000269|PubMed:9610419}.
FT                                /FTId=VAR_009225.
FT   VARIANT     268    268       M -> T (in prostate cancer).
FT                                /FTId=VAR_009716.
FT   VARIANT     271    271       P -> S (in prostate cancer).
FT                                /FTId=VAR_009717.
FT   VARIANT     342    342       P -> L (in prostate cancer;
FT                                dbSNP:rs138454018).
FT                                {ECO:0000269|PubMed:7511268}.
FT                                /FTId=VAR_009718.
FT   VARIANT     392    392       P -> R (in AIS; dbSNP:rs773996740).
FT                                {ECO:0000269|PubMed:10571951}.
FT                                /FTId=VAR_009226.
FT   VARIANT     392    392       P -> S (in AIS; dbSNP:rs201934623).
FT                                /FTId=VAR_009227.
FT   VARIANT     445    445       Q -> R (in AIS; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:10571951}.
FT                                /FTId=VAR_009228.
FT   VARIANT     492    492       G -> S (in AIS).
FT                                /FTId=VAR_009719.
FT   VARIANT     529    529       D -> G (in prostate cancer).
FT                                /FTId=VAR_009720.
FT   VARIANT     548    548       L -> F (in PAIS; dbSNP:rs139524801).
FT                                /FTId=VAR_009721.
FT   VARIANT     549    549       P -> S (in AIS; dbSNP:rs137852588).
FT                                {ECO:0000269|PubMed:8683794}.
FT                                /FTId=VAR_009722.
FT   VARIANT     560    560       C -> Y (in AIS).
FT                                {ECO:0000269|PubMed:1316540}.
FT                                /FTId=VAR_009723.
FT   VARIANT     569    569       G -> V (in a patient with isolated
FT                                hypospadias).
FT                                {ECO:0000269|PubMed:7673412}.
FT                                /FTId=VAR_009725.
FT   VARIANT     569    569       G -> W (in PAIS).
FT                                {ECO:0000269|PubMed:7910529}.
FT                                /FTId=VAR_009726.
FT   VARIANT     572    572       Y -> C (in AIS).
FT                                {ECO:0000269|PubMed:9544375}.
FT                                /FTId=VAR_009727.
FT   VARIANT     574    574       A -> D (in AIS).
FT                                /FTId=VAR_009728.
FT   VARIANT     575    575       L -> P (in prostate cancer).
FT                                /FTId=VAR_009729.
FT   VARIANT     576    576       T -> A (in prostate cancer).
FT                                {ECO:0000269|PubMed:10706109}.
FT                                /FTId=VAR_009730.
FT   VARIANT     577    577       C -> F (in AIS).
FT                                {ECO:0000269|PubMed:14756668}.
FT                                /FTId=VAR_009731.
FT   VARIANT     577    577       C -> R (in AIS).
FT                                {ECO:0000269|PubMed:1316540}.
FT                                /FTId=VAR_009732.
FT   VARIANT     580    580       C -> F (in AIS; reduced transcription and
FT                                DNA binding; dbSNP:rs137852586).
FT                                {ECO:0000269|PubMed:8809734}.
FT                                /FTId=VAR_009733.
FT   VARIANT     580    580       C -> Y (in AIS).
FT                                /FTId=VAR_009734.
FT   VARIANT     581    581       K -> R (in prostate cancer).
FT                                {ECO:0000269|PubMed:10706109}.
FT                                /FTId=VAR_009735.
FT   VARIANT     582    582       V -> F (in AIS).
FT                                {ECO:0000269|PubMed:8224266,
FT                                ECO:0000269|Ref.110}.
FT                                /FTId=VAR_009736.
FT   VARIANT     583    583       F -> S (in PAIS).
FT                                {ECO:0000269|PubMed:7981687}.
FT                                /FTId=VAR_009737.
FT   VARIANT     583    583       F -> Y (in PAIS; dbSNP:rs137852587).
FT                                {ECO:0000269|PubMed:8809734}.
FT                                /FTId=VAR_009738.
FT   VARIANT     583    583       Missing (in AIS).
FT                                {ECO:0000269|PubMed:8162033}.
FT                                /FTId=VAR_009739.
FT   VARIANT     586    586       R -> K (in AIS).
FT                                /FTId=VAR_009740.
FT   VARIANT     587    587       A -> V (in prostate cancer; somatic
FT                                mutation). {ECO:0000269|PubMed:10706109}.
FT                                /FTId=VAR_009741.
FT   VARIANT     588    588       A -> S (in prostate cancer; somatic
FT                                mutation).
FT                                /FTId=VAR_009742.
FT   VARIANT     597    597       A -> T (in AIS; abolishes dimerization;
FT                                dbSNP:rs137852569).
FT                                {ECO:0000269|PubMed:10590024,
FT                                ECO:0000269|PubMed:7649358}.
FT                                /FTId=VAR_009743.
FT   VARIANT     598    598       S -> G (in PAIS; associated with P-618 in
FT                                a PAIS patient; normal androgen binding;
FT                                does not activate transcription; impairs
FT                                DNA binding; dbSNP:rs142280455).
FT                                {ECO:0000269|PubMed:1316540}.
FT                                /FTId=VAR_009744.
FT   VARIANT     598    598       S -> T (in a patient with severe
FT                                hypospadias).
FT                                {ECO:0000269|PubMed:10092153}.
FT                                /FTId=VAR_009745.
FT   VARIANT     602    602       C -> F (in AIS).
FT                                {ECO:0000269|PubMed:7981689}.
FT                                /FTId=VAR_009746.
FT   VARIANT     605    605       D -> Y (in PAIS).
FT                                {ECO:0000269|PubMed:7981687}.
FT                                /FTId=VAR_009747.
FT   VARIANT     608    608       R -> Q (in PAIS and breast cancer;
FT                                dbSNP:rs137852573).
FT                                {ECO:0000269|PubMed:10221692,
FT                                ECO:0000269|PubMed:1303262,
FT                                ECO:0000269|PubMed:9039340,
FT                                ECO:0000269|PubMed:9543136}.
FT                                /FTId=VAR_004684.
FT   VARIANT     609    609       R -> K (in PAIS and breast cancer;
FT                                defective nuclear localization;
FT                                dbSNP:rs137852576).
FT                                {ECO:0000269|PubMed:1424203,
FT                                ECO:0000269|PubMed:8281139,
FT                                ECO:0000269|PubMed:9196614}.
FT                                /FTId=VAR_004685.
FT   VARIANT     611    611       N -> T (in PAIS).
FT                                {ECO:0000269|PubMed:9039340}.
FT                                /FTId=VAR_009748.
FT   VARIANT     612    612       C -> Y (in AIS).
FT                                /FTId=VAR_009749.
FT   VARIANT     616    616       R -> H (in AIS and PAIS;
FT                                dbSNP:rs754201976).
FT                                {ECO:0000269|PubMed:7970939,
FT                                ECO:0000269|PubMed:8162033,
FT                                ECO:0000269|PubMed:8413310,
FT                                ECO:0000269|PubMed:9698822}.
FT                                /FTId=VAR_009751.
FT   VARIANT     616    616       R -> P (in AIS).
FT                                /FTId=VAR_009752.
FT   VARIANT     616    616       Missing (in AIS).
FT                                {ECO:0000269|PubMed:8162033}.
FT                                /FTId=VAR_009750.
FT   VARIANT     617    617       L -> P (in AIS).
FT                                {ECO:0000269|PubMed:8647313}.
FT                                /FTId=VAR_009753.
FT   VARIANT     617    617       L -> R (in PAIS).
FT                                {ECO:0000269|PubMed:8126121}.
FT                                /FTId=VAR_009754.
FT   VARIANT     618    618       R -> P (in AIS and PAIS; associated with
FT                                G-598 in a PAIS patient; loss of DNA-
FT                                binding activity).
FT                                {ECO:0000269|PubMed:1316540,
FT                                ECO:0000269|PubMed:1999491}.
FT                                /FTId=VAR_009755.
FT   VARIANT     620    620       C -> Y (in prostate cancer; loss of DNA
FT                                binding; somatic mutation).
FT                                {ECO:0000269|PubMed:10598582,
FT                                ECO:0000269|PubMed:10706109}.
FT                                /FTId=VAR_009756.
FT   VARIANT     630    630       R -> Q (in prostate cancer).
FT                                {ECO:0000269|PubMed:9184448}.
FT                                /FTId=VAR_009757.
FT   VARIANT     631    631       K -> T (in prostate cancer).
FT                                /FTId=VAR_009758.
FT   VARIANT     646    646       A -> D (in dbSNP:rs1800053).
FT                                {ECO:0000269|PubMed:9554755}.
FT                                /FTId=VAR_004686.
FT   VARIANT     648    648       S -> N (in prostate cancer;
FT                                dbSNP:rs137852584).
FT                                /FTId=VAR_009760.
FT   VARIANT     665    665       I -> N (in AIS and PAIS).
FT                                /FTId=VAR_004687.
FT   VARIANT     671    671       Q -> R (in prostate cancer).
FT                                /FTId=VAR_009761.
FT   VARIANT     672    672       P -> H (in PAIS).
FT                                /FTId=VAR_009762.
FT   VARIANT     673    673       I -> T (in prostate cancer).
FT                                /FTId=VAR_009763.
FT   VARIANT     678    678       L -> P (in AIS; dbSNP:rs137852579).
FT                                {ECO:0000269|PubMed:7537149}.
FT                                /FTId=VAR_004688.
FT   VARIANT     682    682       E -> K (in AIS).
FT                                {ECO:0000269|PubMed:10221692,
FT                                ECO:0000269|PubMed:8325950}.
FT                                /FTId=VAR_009764.
FT   VARIANT     683    683       P -> T (in PAIS).
FT                                {ECO:0000269|PubMed:11587068}.
FT                                /FTId=VAR_013474.
FT   VARIANT     684    684       G -> A (in prostate cancer).
FT                                {ECO:0000269|PubMed:10629558,
FT                                ECO:0000269|PubMed:9000575}.
FT                                /FTId=VAR_009765.
FT   VARIANT     685    685       V -> I (in AIS).
FT                                /FTId=VAR_009766.
FT   VARIANT     687    687       C -> R (in PAIS).
FT                                /FTId=VAR_009767.
FT   VARIANT     688    688       A -> V (in PAIS).
FT                                /FTId=VAR_009768.
FT   VARIANT     689    689       G -> E (in AIS).
FT                                /FTId=VAR_009769.
FT   VARIANT     691    691       Missing (in PAIS). {ECO:0000269|Ref.118}.
FT                                /FTId=VAR_009770.
FT   VARIANT     693    693       Missing (in AIS).
FT                                /FTId=VAR_004689.
FT   VARIANT     696    696       D -> H (in AIS).
FT                                {ECO:0000269|PubMed:1775137}.
FT                                /FTId=VAR_004690.
FT   VARIANT     696    696       D -> N (in AIS; almost complete loss of
FT                                androgen binding and transcription
FT                                activation).
FT                                {ECO:0000269|PubMed:16595706,
FT                                ECO:0000269|PubMed:1775137}.
FT                                /FTId=VAR_004691.
FT   VARIANT     696    696       D -> V (in AIS).
FT                                {ECO:0000269|PubMed:9554754}.
FT                                /FTId=VAR_004692.
FT   VARIANT     701    701       L -> M (in AIS).
FT                                /FTId=VAR_009771.
FT   VARIANT     702    702       L -> F (in AIS).
FT                                /FTId=VAR_009772.
FT   VARIANT     702    702       L -> H (in AIS and prostate cancer;
FT                                dbSNP:rs864622007).
FT                                {ECO:0000269|PubMed:10569618,
FT                                ECO:0000269|PubMed:8274409,
FT                                ECO:0000269|PubMed:9438000}.
FT                                /FTId=VAR_009773.
FT   VARIANT     703    703       S -> A (in AIS).
FT                                /FTId=VAR_009774.
FT   VARIANT     704    704       S -> C (in AIS).
FT                                /FTId=VAR_009775.
FT   VARIANT     704    704       S -> G (in PAIS and AIS).
FT                                {ECO:0000269|PubMed:9302173}.
FT                                /FTId=VAR_004693.
FT   VARIANT     706    706       N -> S (in AIS).
FT                                {ECO:0000269|PubMed:1480178,
FT                                ECO:0000269|PubMed:7671849}.
FT                                /FTId=VAR_009776.
FT   VARIANT     706    706       N -> Y (in AIS).
FT                                {ECO:0000269|PubMed:11744994}.
FT                                /FTId=VAR_013475.
FT   VARIANT     708    708       L -> R (in AIS; dbSNP:rs137852585).
FT                                {ECO:0000269|PubMed:8626869}.
FT                                /FTId=VAR_004694.
FT   VARIANT     709    709       G -> A (in PAIS).
FT                                {ECO:0000269|PubMed:7981687,
FT                                ECO:0000269|PubMed:9329414}.
FT                                /FTId=VAR_009777.
FT   VARIANT     709    709       G -> V (in AIS).
FT                                /FTId=VAR_009778.
FT   VARIANT     711    711       R -> T (in AIS).
FT                                /FTId=VAR_009779.
FT   VARIANT     712    712       Q -> E (in PAIS).
FT                                {ECO:0000269|PubMed:11587068}.
FT                                /FTId=VAR_013476.
FT   VARIANT     713    713       L -> F (in PAIS; dbSNP:rs137852595).
FT                                /FTId=VAR_009780.
FT   VARIANT     716    716       V -> M (in prostate cancer; gain in
FT                                function). {ECO:0000269|PubMed:8145761}.
FT                                /FTId=VAR_009781.
FT   VARIANT     718    718       K -> E (in prostate cancer).
FT                                /FTId=VAR_009782.
FT   VARIANT     721    721       K -> E (in prostate cancer; found in bone
FT                                metastases).
FT                                /FTId=VAR_009783.
FT   VARIANT     722    722       A -> T (in prostate cancer; somatic
FT                                mutation; dbSNP:rs137852583).
FT                                /FTId=VAR_009784.
FT   VARIANT     723    723       L -> F (in AIS).
FT                                /FTId=VAR_009785.
FT   VARIANT     724    724       P -> S (in AIS).
FT                                /FTId=VAR_009786.
FT   VARIANT     725    725       G -> D (in AIS and prostate cancer).
FT                                /FTId=VAR_009787.
FT   VARIANT     726    726       F -> L (in a patient with severe
FT                                hypospadias).
FT                                {ECO:0000269|PubMed:10092153,
FT                                ECO:0000269|PubMed:7671849}.
FT                                /FTId=VAR_009788.
FT   VARIANT     727    727       R -> L (in prostate cancer;
FT                                dbSNP:rs137852593).
FT                                {ECO:0000269|PubMed:8530589}.
FT                                /FTId=VAR_009789.
FT   VARIANT     728    728       N -> K (in AIS; dbSNP:rs768869912).
FT                                {ECO:0000269|PubMed:7993455}.
FT                                /FTId=VAR_009790.
FT   VARIANT     729    729       L -> S (in PAIS).
FT                                /FTId=VAR_009791.
FT   VARIANT     731    731       V -> M (in prostate cancer; increases
FT                                transcription activation;
FT                                dbSNP:rs137852571).
FT                                {ECO:0000269|PubMed:15525515,
FT                                ECO:0000269|PubMed:1631125,
FT                                ECO:0000269|PubMed:7591265}.
FT                                /FTId=VAR_004695.
FT   VARIANT     733    733       D -> N (in AIS).
FT                                {ECO:0000269|PubMed:9252933}.
FT                                /FTId=VAR_004696.
FT   VARIANT     733    733       D -> Y (in AIS).
FT                                /FTId=VAR_004697.
FT   VARIANT     734    734       Q -> H (in PAIS).
FT                                /FTId=VAR_009792.
FT   VARIANT     738    738       I -> T (in PAIS).
FT                                {ECO:0000269|PubMed:7671849}.
FT                                /FTId=VAR_009793.
FT   VARIANT     742    742       W -> R (in AIS).
FT                                {ECO:0000269|PubMed:1464650}.
FT                                /FTId=VAR_009794.
FT   VARIANT     743    743       M -> I (in PAIS).
FT                                {ECO:0000269|PubMed:8824883}.
FT                                /FTId=VAR_004698.
FT   VARIANT     743    743       M -> V (in PAIS).
FT                                {ECO:0000269|PubMed:7970939}.
FT                                /FTId=VAR_009795.
FT   VARIANT     744    744       G -> E (in AIS; dbSNP:rs137852600).
FT                                {ECO:0000269|PubMed:11587068}.
FT                                /FTId=VAR_013477.
FT   VARIANT     744    744       G -> V (in PAIS and AIS;
FT                                dbSNP:rs137852600).
FT                                {ECO:0000269|PubMed:8096390,
FT                                ECO:0000269|PubMed:8325932,
FT                                ECO:0000269|PubMed:9768671,
FT                                ECO:0000269|Ref.110}.
FT                                /FTId=VAR_004699.
FT   VARIANT     745    745       L -> F (in AIS and prostate cancer).
FT                                /FTId=VAR_009796.
FT   VARIANT     746    746       M -> T (in PAIS).
FT                                {ECO:0000269|PubMed:7970939}.
FT                                /FTId=VAR_009797.
FT   VARIANT     747    747       V -> M (in PAIS).
FT                                /FTId=VAR_009798.
FT   VARIANT     749    749       A -> D (in PAIS).
FT                                /FTId=VAR_009799.
FT   VARIANT     749    749       A -> T (in prostate cancer).
FT                                /FTId=VAR_009800.
FT   VARIANT     749    749       A -> V (in prostate cancer).
FT                                /FTId=VAR_009801.
FT   VARIANT     750    750       M -> I (in prostate cancer).
FT                                /FTId=VAR_009802.
FT   VARIANT     750    750       M -> V (in PAIS and AIS).
FT                                {ECO:0000269|PubMed:1480178,
FT                                ECO:0000269|PubMed:1487249,
FT                                ECO:0000269|PubMed:8990010}.
FT                                /FTId=VAR_004700.
FT   VARIANT     751    751       G -> D (in AIS; loss of androgen
FT                                binding). {ECO:0000269|PubMed:9328206}.
FT                                /FTId=VAR_004701.
FT   VARIANT     751    751       G -> S (in prostate cancer).
FT                                /FTId=VAR_009803.
FT   VARIANT     752    752       W -> R (in AIS).
FT                                /FTId=VAR_009804.
FT   VARIANT     753    753       R -> Q (in AIS).
FT                                {ECO:0000269|PubMed:9544375,
FT                                ECO:0000269|PubMed:9698822}.
FT                                /FTId=VAR_004702.
FT   VARIANT     755    755       F -> L (in PAIS and prostate cancer).
FT                                {ECO:0000269|PubMed:7981687,
FT                                ECO:0000269|PubMed:9039340}.
FT                                /FTId=VAR_009805.
FT   VARIANT     755    755       F -> V (in AIS).
FT                                {ECO:0000269|PubMed:8103398,
FT                                ECO:0000269|Ref.110}.
FT                                /FTId=VAR_004703.
FT   VARIANT     756    756       T -> A (in prostate cancer).
FT                                /FTId=VAR_009806.
FT   VARIANT     757    757       N -> S (in PAIS; dbSNP:rs141425171).
FT                                /FTId=VAR_009807.
FT   VARIANT     758    758       V -> A (in prostate cancer).
FT                                {ECO:0000269|PubMed:10706109}.
FT                                /FTId=VAR_009808.
FT   VARIANT     759    759       N -> T (in PAIS; 50% reduction in
FT                                transactivation).
FT                                {ECO:0000269|PubMed:9607727}.
FT                                /FTId=VAR_009809.
FT   VARIANT     760    760       S -> F (in AIS).
FT                                {ECO:0000269|PubMed:1480178}.
FT                                /FTId=VAR_009810.
FT   VARIANT     760    760       S -> P (in prostate cancer).
FT                                /FTId=VAR_009811.
FT   VARIANT     763    763       L -> F (in AIS; loss of androgen
FT                                binding). {ECO:0000269|PubMed:9328206}.
FT                                /FTId=VAR_004704.
FT   VARIANT     764    764       Y -> C (in PAIS and prostate cancer;
FT                                partial loss of androgen binding;
FT                                dbSNP:rs137852567).
FT                                {ECO:0000269|PubMed:16595706,
FT                                ECO:0000269|PubMed:2010552,
FT                                ECO:0000269|PubMed:7581399}.
FT                                /FTId=VAR_004705.
FT   VARIANT     764    764       Y -> H (in AIS).
FT                                {ECO:0000269|PubMed:7671849}.
FT                                /FTId=VAR_009812.
FT   VARIANT     765    765       F -> L (in AIS).
FT                                {ECO:0000269|PubMed:7970939}.
FT                                /FTId=VAR_009813.
FT   VARIANT     766    766       A -> T (in AIS; loss of androgen
FT                                binding). {ECO:0000269|PubMed:1426313,
FT                                ECO:0000269|PubMed:9252933,
FT                                ECO:0000269|PubMed:9328206,
FT                                ECO:0000269|PubMed:9856504}.
FT                                /FTId=VAR_004707.
FT   VARIANT     766    766       A -> V (in AIS).
FT                                /FTId=VAR_009814.
FT   VARIANT     767    767       P -> S (in AIS).
FT                                /FTId=VAR_009815.
FT   VARIANT     768    768       D -> E (in AIS). {ECO:0000269|Ref.110}.
FT                                /FTId=VAR_009816.
FT   VARIANT     769    769       L -> P (in AIS).
FT                                /FTId=VAR_009817.
FT   VARIANT     772    772       N -> H (in PAIS; dbSNP:rs886041352).
FT                                {ECO:0000269|PubMed:7981687}.
FT                                /FTId=VAR_009818.
FT   VARIANT     773    773       E -> A (in PAIS).
FT                                {ECO:0000269|PubMed:10022458}.
FT                                /FTId=VAR_009819.
FT   VARIANT     773    773       E -> G (in PAIS).
FT                                {ECO:0000269|PubMed:9196614}.
FT                                /FTId=VAR_009820.
FT   VARIANT     775    775       R -> C (in AIS; frequent mutation; loss
FT                                of androgen binding; dbSNP:rs137852562).
FT                                {ECO:0000269|PubMed:1609793,
FT                                ECO:0000269|PubMed:1856263,
FT                                ECO:0000269|PubMed:2082179,
FT                                ECO:0000269|PubMed:8990010,
FT                                ECO:0000269|PubMed:9544375}.
FT                                /FTId=VAR_004709.
FT   VARIANT     775    775       R -> H (in AIS and PAIS; almost complete
FT                                loss of androgen binding;
FT                                dbSNP:rs137852572).
FT                                {ECO:0000269|PubMed:1480178,
FT                                ECO:0000269|PubMed:1609793,
FT                                ECO:0000269|PubMed:16595706,
FT                                ECO:0000269|PubMed:7671849}.
FT                                /FTId=VAR_004708.
FT   VARIANT     780    780       R -> W (in AIS).
FT                                {ECO:0000269|PubMed:7581399,
FT                                ECO:0000269|PubMed:7981687,
FT                                ECO:0000269|PubMed:9007482}.
FT                                /FTId=VAR_004710.
FT   VARIANT     781    781       M -> I (in PAIS and AIS;
FT                                dbSNP:rs137852589).
FT                                {ECO:0000269|PubMed:8768864,
FT                                ECO:0000269|PubMed:8824883,
FT                                ECO:0000269|PubMed:8990010}.
FT                                /FTId=VAR_004711.
FT   VARIANT     783    783       S -> N (in prostate cancer; somatic
FT                                mutation).
FT                                /FTId=VAR_009821.
FT   VARIANT     785    785       C -> Y (in AIS; loss of androgen binding
FT                                and of transactivation).
FT                                {ECO:0000269|PubMed:9856504}.
FT                                /FTId=VAR_004712.
FT   VARIANT     788    788       M -> V (in AIS; dbSNP:rs137852570).
FT                                {ECO:0000269|PubMed:1569163}.
FT                                /FTId=VAR_004713.
FT   VARIANT     789    789       R -> S (in AIS).
FT                                /FTId=VAR_009822.
FT   VARIANT     791    791       L -> F (in AIS).
FT                                {ECO:0000269|PubMed:7962294}.
FT                                /FTId=VAR_009823.
FT   VARIANT     792    792       S -> P (in prostate cancer).
FT                                /FTId=VAR_009824.
FT   VARIANT     794    794       E -> D. {ECO:0000269|PubMed:8213813}.
FT                                /FTId=VAR_009825.
FT   VARIANT     795    795       F -> S (in AIS).
FT                                {ECO:0000269|PubMed:8990010}.
FT                                /FTId=VAR_004714.
FT   VARIANT     799    799       Q -> E (in PAIS, AIS and prostate cancer;
FT                                reduced transcription activation;
FT                                dbSNP:rs137852591).
FT                                {ECO:0000269|PubMed:16595706,
FT                                ECO:0000269|PubMed:7511268,
FT                                ECO:0000269|PubMed:7671849,
FT                                ECO:0000269|PubMed:8628719,
FT                                ECO:0000269|PubMed:8824883,
FT                                ECO:0000269|PubMed:9851768}.
FT                                /FTId=VAR_004715.
FT   VARIANT     807    807       C -> Y (in PAIS).
FT                                /FTId=VAR_009826.
FT   VARIANT     808    808       M -> R (in AIS; loss of transactivation).
FT                                {ECO:0000269|PubMed:8281140}.
FT                                /FTId=VAR_004716.
FT   VARIANT     808    808       M -> T (in PAIS; dbSNP:rs137852592).
FT                                {ECO:0000269|PubMed:10543676}.
FT                                /FTId=VAR_009827.
FT   VARIANT     808    808       M -> V (in AIS; 25% androgen binding).
FT                                {ECO:0000269|PubMed:7581399}.
FT                                /FTId=VAR_004717.
FT   VARIANT     813    813       L -> F (in AIS).
FT                                {ECO:0000269|PubMed:10458483}.
FT                                /FTId=VAR_009828.
FT   VARIANT     815    815       S -> N (in AIS and PAIS).
FT                                /FTId=VAR_004718.
FT   VARIANT     821    821       G -> A (in AIS).
FT                                {ECO:0000269|PubMed:9610419}.
FT                                /FTId=VAR_009829.
FT   VARIANT     822    822       L -> V (in PAIS).
FT                                /FTId=VAR_009830.
FT   VARIANT     828    828       F -> V (in PAIS).
FT                                {ECO:0000269|PubMed:11587068}.
FT                                /FTId=VAR_013478.
FT   VARIANT     831    831       L -> P (in prostate cancer).
FT                                /FTId=VAR_009831.
FT   VARIANT     832    832       R -> L (in AIS).
FT                                {ECO:0000269|PubMed:7633398}.
FT                                /FTId=VAR_004719.
FT   VARIANT     832    832       R -> Q (in AIS; loss of androgen
FT                                binding). {ECO:0000269|PubMed:10458483,
FT                                ECO:0000269|PubMed:2082179,
FT                                ECO:0000269|PubMed:7633398}.
FT                                /FTId=VAR_004720.
FT   VARIANT     835    835       Y -> C (in AIS; loss of androgen
FT                                binding). {ECO:0000269|PubMed:1464650}.
FT                                /FTId=VAR_009832.
FT   VARIANT     841    841       R -> C (in AIS; dbSNP:rs137852577).
FT                                {ECO:0000269|PubMed:8040309,
FT                                ECO:0000269|PubMed:8824883,
FT                                ECO:0000269|PubMed:9768671}.
FT                                /FTId=VAR_004721.
FT   VARIANT     841    841       R -> G (in PAIS).
FT                                {ECO:0000269|PubMed:9856504}.
FT                                /FTId=VAR_004722.
FT   VARIANT     841    841       R -> H (in AIS; dbSNP:rs9332969).
FT                                {ECO:0000269|PubMed:7909256,
FT                                ECO:0000269|PubMed:8040309,
FT                                ECO:0000269|PubMed:8126121,
FT                                ECO:0000269|PubMed:8205256,
FT                                ECO:0000269|PubMed:8325950,
FT                                ECO:0000269|PubMed:8830623,
FT                                ECO:0000269|PubMed:9039340}.
FT                                /FTId=VAR_004723.
FT   VARIANT     841    841       R -> S (in PAIS).
FT                                {ECO:0000269|PubMed:10502786}.
FT                                /FTId=VAR_009229.
FT   VARIANT     842    842       I -> S (in PAIS).
FT                                /FTId=VAR_009833.
FT   VARIANT     843    843       I -> T (in AIS; dbSNP:rs9332970).
FT                                {ECO:0000269|PubMed:8325950,
FT                                ECO:0000269|PubMed:9039340}.
FT                                /FTId=VAR_004724.
FT   VARIANT     847    847       R -> G (in prostate cancer).
FT                                {ECO:0000269|PubMed:10706109}.
FT                                /FTId=VAR_009834.
FT   VARIANT     855    855       R -> K (in PAIS).
FT                                /FTId=VAR_009835.
FT   VARIANT     856    856       R -> C (in AIS; dbSNP:rs886041132).
FT                                {ECO:0000269|PubMed:1480178,
FT                                ECO:0000269|PubMed:7581399,
FT                                ECO:0000269|PubMed:9001799,
FT                                ECO:0000269|PubMed:9255042,
FT                                ECO:0000269|Ref.110}.
FT                                /FTId=VAR_004725.
FT   VARIANT     856    856       R -> H (in AIS; strongly reduced
FT                                transcription activation;
FT                                dbSNP:rs9332971).
FT                                {ECO:0000269|PubMed:16595706,
FT                                ECO:0000269|PubMed:8097257,
FT                                ECO:0000269|PubMed:8824883,
FT                                ECO:0000269|PubMed:9039340,
FT                                ECO:0000269|PubMed:9106550}.
FT                                /FTId=VAR_004726.
FT   VARIANT     857    857       F -> L (in AIS; dbSNP:rs137852598).
FT                                /FTId=VAR_009836.
FT   VARIANT     864    864       L -> R (in AIS).
FT                                /FTId=VAR_009837.
FT   VARIANT     865    865       D -> G (in AIS).
FT                                {ECO:0000269|PubMed:1480178}.
FT                                /FTId=VAR_009838.
FT   VARIANT     865    865       D -> N (in AIS; loss of androgen
FT                                binding). {ECO:0000269|PubMed:9328206}.
FT                                /FTId=VAR_004727.
FT   VARIANT     866    866       S -> P (in AIS; dbSNP:rs137852597).
FT                                /FTId=VAR_009839.
FT   VARIANT     867    867       V -> E (in AIS).
FT                                /FTId=VAR_004728.
FT   VARIANT     867    867       V -> L (in PAIS; dbSNP:rs137852564).
FT                                {ECO:0000269|PubMed:1424203,
FT                                ECO:0000269|PubMed:8325950,
FT                                ECO:0000269|PubMed:8446106}.
FT                                /FTId=VAR_004729.
FT   VARIANT     867    867       V -> M (in AIS and prostate cancer;
FT                                dbSNP:rs137852564).
FT                                {ECO:0000269|PubMed:2082179,
FT                                ECO:0000269|PubMed:2594783,
FT                                ECO:0000269|PubMed:8446106,
FT                                ECO:0000269|PubMed:9039340}.
FT                                /FTId=VAR_004730.
FT   VARIANT     870    870       I -> M (in PAIS; dbSNP:rs137852574).
FT                                {ECO:0000269|PubMed:8097257,
FT                                ECO:0000269|PubMed:8824883}.
FT                                /FTId=VAR_004731.
FT   VARIANT     871    871       A -> G (in PAIS).
FT                                {ECO:0000269|PubMed:9329414}.
FT                                /FTId=VAR_009840.
FT   VARIANT     871    871       A -> V (in PAIS; dbSNP:rs143040492).
FT                                {ECO:0000269|PubMed:8033918}.
FT                                /FTId=VAR_009841.
FT   VARIANT     872    872       R -> G (in AIS).
FT                                {ECO:0000269|PubMed:10022458}.
FT                                /FTId=VAR_009842.
FT   VARIANT     875    875       H -> R (in AIS).
FT                                {ECO:0000269|PubMed:11587068}.
FT                                /FTId=VAR_013479.
FT   VARIANT     875    875       H -> Y (in prostate cancer; increases
FT                                affinity for testosterone and androgen
FT                                sensitivity; increased transcription
FT                                activation; dbSNP:rs137852581).
FT                                {ECO:0000269|PubMed:17591767}.
FT                                /FTId=VAR_009843.
FT   VARIANT     878    878       T -> A (in prostate cancer; found in bone
FT                                metastases; alters receptor specificity
FT                                so that transcription is activated by
FT                                antiandrogens such as cyproterone
FT                                acetate; dbSNP:rs137852578).
FT                                {ECO:0000269|PubMed:10363963,
FT                                ECO:0000269|PubMed:10569618,
FT                                ECO:0000269|PubMed:1562539,
FT                                ECO:0000269|PubMed:16129672,
FT                                ECO:0000269|PubMed:17311914,
FT                                ECO:0000269|PubMed:2260966,
FT                                ECO:0000269|PubMed:8187068,
FT                                ECO:0000269|PubMed:8274409,
FT                                ECO:0000269|PubMed:8827083}.
FT                                /FTId=VAR_004732.
FT   VARIANT     878    878       T -> S (in prostate cancer;
FT                                dbSNP:rs137852580).
FT                                /FTId=VAR_009844.
FT   VARIANT     880    880       D -> Y (in AIS).
FT                                {ECO:0000269|PubMed:11587068}.
FT                                /FTId=VAR_013480.
FT   VARIANT     881    881       L -> Q (in prostate cancer).
FT                                /FTId=VAR_009845.
FT   VARIANT     882    882       L -> V (in AIS).
FT                                {ECO:0000269|PubMed:7641413}.
FT                                /FTId=VAR_009846.
FT   VARIANT     887    887       M -> V (in AIS; dbSNP:rs755226547).
FT                                /FTId=VAR_009847.
FT   VARIANT     890    890       V -> M (in AIS and PAIS;
FT                                dbSNP:rs886041133).
FT                                {ECO:0000269|PubMed:8126121,
FT                                ECO:0000269|PubMed:9160185}.
FT                                /FTId=VAR_009848.
FT   VARIANT     891    891       D -> N (in prostate cancer).
FT                                {ECO:0000269|PubMed:10363963}.
FT                                /FTId=VAR_009849.
FT   VARIANT     892    892       F -> L (in prostate cancer).
FT                                /FTId=VAR_009850.
FT   VARIANT     893    893       P -> L (in AIS).
FT                                {ECO:0000269|PubMed:10221770,
FT                                ECO:0000269|PubMed:10404311,
FT                                ECO:0000269|Ref.176}.
FT                                /FTId=VAR_004733.
FT   VARIANT     896    896       M -> T (in AIS; low androgen binding and
FT                                transactivation).
FT                                {ECO:0000269|PubMed:16129672,
FT                                ECO:0000269|PubMed:9856504}.
FT                                /FTId=VAR_004734.
FT   VARIANT     897    897       A -> T (in prostate cancer).
FT                                /FTId=VAR_009851.
FT   VARIANT     899    899       I -> T (in AIS).
FT                                /FTId=VAR_009852.
FT   VARIANT     903    903       Q -> R (in prostate cancer;
FT                                dbSNP:rs137852582).
FT                                /FTId=VAR_009853.
FT   VARIANT     904    904       V -> M (in PAIS).
FT                                /FTId=VAR_009854.
FT   VARIANT     905    905       P -> H (in AIS).
FT                                /FTId=VAR_009855.
FT   VARIANT     905    905       P -> S (in AIS).
FT                                /FTId=VAR_009856.
FT   VARIANT     908    908       L -> F (in AIS; almost complete loss of
FT                                transcription activation).
FT                                {ECO:0000269|PubMed:16595706,
FT                                ECO:0000269|PubMed:9328206}.
FT                                /FTId=VAR_004735.
FT   VARIANT     910    910       G -> E (in prostate cancer).
FT                                /FTId=VAR_009857.
FT   VARIANT     910    910       G -> R (in PAIS).
FT                                {ECO:0000269|PubMed:8550758}.
FT                                /FTId=VAR_009858.
FT   VARIANT     911    911       K -> R (in prostate cancer).
FT                                {ECO:0000269|PubMed:9438000}.
FT                                /FTId=VAR_009859.
FT   VARIANT     912    912       V -> L (in PAIS).
FT                                {ECO:0000269|PubMed:10470409}.
FT                                /FTId=VAR_009860.
FT   VARIANT     914    914       P -> S (in PAIS).
FT                                /FTId=VAR_004736.
FT   VARIANT     917    917       F -> L (in AIS).
FT                                {ECO:0000269|PubMed:9302173}.
FT                                /FTId=VAR_009861.
FT   VARIANT     918    918       H -> R (in AIS).
FT                                /FTId=VAR_009862.
FT   VARIANT     920    920       Q -> R (in prostate cancer).
FT                                /FTId=VAR_009863.
FT   MUTAGEN      83     83       S->A: Reduced cell growth.
FT                                {ECO:0000269|PubMed:20980437}.
FT   MUTAGEN     225    225       Y->F: Decrease of CSK-induced
FT                                phosphorylation.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MUTAGEN     269    269       Y->F: Decrease of CSK-induced
FT                                phosphorylation and phosphorylation by
FT                                TNK2. Complete loss of TNK2-dependent
FT                                phosphorylation; when associated with F-
FT                                365. {ECO:0000269|PubMed:17045208,
FT                                ECO:0000269|PubMed:17494760}.
FT   MUTAGEN     309    309       Y->F: Decrease of CSK-induced
FT                                phosphorylation.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MUTAGEN     348    348       Y->F: Decrease of CSK-induced
FT                                phosphorylation.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MUTAGEN     359    359       Y->F: Decrease of CSK-induced
FT                                phosphorylation.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MUTAGEN     364    364       Y->F: Decrease of CSK-induced
FT                                phosphorylation.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MUTAGEN     365    365       Y->F: Decrease of CSK-induced
FT                                phosphorylation and phosphorylation by
FT                                TNK2. Complete loss of TNK2-dependent
FT                                phosphorylation; when associated with F-
FT                                269. {ECO:0000269|PubMed:17045208,
FT                                ECO:0000269|PubMed:17494760}.
FT   MUTAGEN     395    395       Y->F: Decrease of CSK-induced
FT                                phosphorylation.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MUTAGEN     535    535       Y->F: Greatest decrease of CSK-induced
FT                                phosphorylation and inhibition of
FT                                transcriptional activity induced by EGF.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MUTAGEN     552    552       Y->F: Decrease in CSK-induced
FT                                phosphorylation.
FT                                {ECO:0000269|PubMed:17045208}.
FT   MUTAGEN     702    702       L->A: Alters receptor specificity, so
FT                                that transcription is activated by the
FT                                antiandrogen cyproterone acetate.
FT                                {ECO:0000269|PubMed:17311914}.
FT   MUTAGEN     721    721       K->A: Loss of transcription activation in
FT                                the presence of androgen and of
FT                                interaction with NCOA2.
FT                                {ECO:0000269|PubMed:15563469,
FT                                ECO:0000269|PubMed:17591767}.
FT   MUTAGEN     742    742       W->L: Strongly decreased transcription
FT                                activation in the presence of androgen.
FT                                {ECO:0000269|PubMed:16129672}.
FT   MUTAGEN     846    846       K->R: Prevents ubiquitination by RNF6.
FT                                Prevents AR transcriptional activation by
FT                                RNF14 in absence of hormone.
FT                                {ECO:0000269|PubMed:19345326}.
FT   MUTAGEN     848    848       K->R: Partially prevents ubiquitination
FT                                by RNF6. {ECO:0000269|PubMed:19345326}.
FT   MUTAGEN     898    898       E->A,Q: Reduced transcription activation
FT                                in the presence of androgen.
FT                                {ECO:0000269|PubMed:15563469,
FT                                ECO:0000269|PubMed:17591767}.
FT   MUTAGEN     898    898       E->K,R: Loss of transcription activation
FT                                in the presence of androgen.
FT                                {ECO:0000269|PubMed:15563469,
FT                                ECO:0000269|PubMed:17591767}.
FT   MUTAGEN     916    916       Y->F: Decrease in CSK-induced
FT                                phosphorylation.
FT                                {ECO:0000269|PubMed:17045208}.
FT   CONFLICT    168    168       G -> A (in Ref. 5; AAA51780).
FT                                {ECO:0000305}.
FT   CONFLICT    214    214       A -> R (in Ref. 3 and 6; AAA51771/
FT                                AAA51772). {ECO:0000305}.
FT   CONFLICT    476    476       G -> E (in Ref. 2; AAA51775 and 13;
FT                                AAA51770). {ECO:0000305}.
FT   CONFLICT    566    566       E -> K (in Ref. 15; AAA51774).
FT                                {ECO:0000305}.
FT   CONFLICT    635    635       L -> P (in Ref. 19; AAB21256/AAB21257).
FT                                {ECO:0000305}.
FT   CONFLICT    676    676       N -> I (in Ref. 19; AAB21256/AAB21257).
FT                                {ECO:0000305}.
FT   CONFLICT    811    811       L -> M (in Ref. 5; AAA51780).
FT                                {ECO:0000305}.
FT   HELIX        22     29       {ECO:0000244|PDB:3V49}.
FT   STRAND      667    669       {ECO:0000244|PDB:1XJ7}.
FT   HELIX       673    681       {ECO:0000244|PDB:4OHA}.
FT   STRAND      692    694       {ECO:0000244|PDB:1XJ7}.
FT   HELIX       698    721       {ECO:0000244|PDB:4OHA}.
FT   HELIX       726    728       {ECO:0000244|PDB:4OHA}.
FT   HELIX       731    758       {ECO:0000244|PDB:4OHA}.
FT   STRAND      761    766       {ECO:0000244|PDB:4OHA}.
FT   STRAND      769    771       {ECO:0000244|PDB:4OHA}.
FT   HELIX       773    778       {ECO:0000244|PDB:4OHA}.
FT   HELIX       782    797       {ECO:0000244|PDB:4OHA}.
FT   HELIX       802    812       {ECO:0000244|PDB:4OHA}.
FT   STRAND      815    818       {ECO:0000244|PDB:4OHA}.
FT   HELIX       825    843       {ECO:0000244|PDB:4OHA}.
FT   TURN        844    846       {ECO:0000244|PDB:2PKL}.
FT   TURN        850    852       {ECO:0000244|PDB:2PIV}.
FT   HELIX       853    883       {ECO:0000244|PDB:4OHA}.
FT   HELIX       885    888       {ECO:0000244|PDB:4OHA}.
FT   HELIX       894    902       {ECO:0000244|PDB:4OHA}.
FT   HELIX       904    908       {ECO:0000244|PDB:4OHA}.
FT   STRAND      911    914       {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
//