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 24-JAN-2024, entry version 299. DE RecName: Full=Androgen receptor; DE AltName: Full=Dihydrotestosterone receptor; DE AltName: Full=Nuclear receptor subfamily 3 group C member 4; GN Name=AR; Synonyms=DHTR, NR3C4; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=3216866; DOI=10.1210/mend-2-12-1265; RA Lubahn D.B., Joseph D.R., Sar M., Tan J., Higgs H.N., Larson R.E., RA French F.S., Wilson E.M.; RT "The human androgen receptor: complementary deoxyribonucleic acid cloning, RT sequence analysis and gene expression in prostate."; RL Mol. Endocrinol. 2:1265-1275(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Prostate; RX PubMed=3174628; DOI=10.1073/pnas.85.19.7211; RA Chang C., Kokontis J., Liao S.; RT "Structural analysis of complementary DNA and amino acid sequences of human RT and rat androgen receptors."; RL Proc. Natl. Acad. Sci. U.S.A. 85:7211-7215(1988). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Prostate; RX PubMed=2911578; DOI=10.1073/pnas.86.1.327; RA Tilley W.D., Marcelli M., Wilson J.D., McPhaul M.J.; RT "Characterization and expression of a cDNA encoding the human androgen RT receptor."; RL Proc. Natl. Acad. Sci. U.S.A. 86:327-331(1989). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT AIS MET-867. RX PubMed=2594783; DOI=10.1073/pnas.86.23.9534; RA Lubahn D.B., Brown T.R., Simental J.A., Higgs H.N., Migeon C.J., RA Wilson E.M., French F.S.; RT "Sequence of the intron/exon junctions of the coding region of the human RT androgen receptor gene and identification of a point mutation in a family RT with complete androgen insensitivity."; RL Proc. Natl. Acad. Sci. U.S.A. 86:9534-9538(1989). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2342476; DOI=10.1210/mend-4-3-417; RA Govindan M.V.; RT "Specific region in hormone binding domain is essential for hormone binding RT and trans-activation by human androgen receptor."; RL Mol. Endocrinol. 4:417-427(1990). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RP 1). RC TISSUE=Prostate; RX PubMed=2293020; DOI=10.1210/mend-4-8-1105; RA Marcelli M., Tilley W.D., Wilson C.M., Griffin J.E., Wilson J.D., RA McPhaul M.J.; RT "Definition of the human androgen receptor gene structure permits the RT identification of mutations that cause androgen resistance: premature RT termination of the receptor protein at amino acid residue 588 causes RT complete androgen resistance."; RL Mol. Endocrinol. 4:1105-1116(1990). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2), TISSUE RP SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=15634333; DOI=10.1111/j.1742-4658.2004.04395.x; RA Ahrens-Fath I., Politz O., Geserick C., Haendler B.; RT "Androgen receptor function is modulated by the tissue-specific AR45 RT variant."; RL FEBS J. 272:74-84(2005). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), VARIANT GLN-57, FUNCTION RP (ISOFORMS 3 AND 4), AND SUBCELLULAR LOCATION (ISOFORM 3). RX PubMed=19244107; DOI=10.1158/0008-5472.can-08-3795; RA Guo Z., Yang X., Sun F., Jiang R., Linn D.E., Chen H., Chen H., Kong X., RA Melamed J., Tepper C.G., Kung H.J., Brodie A.M., Edwards J., Qiu Y.; RT "A novel androgen receptor splice variant is up-regulated during prostate RT cancer progression and promotes androgen depletion-resistant growth."; RL Cancer Res. 69:2305-2313(2009). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-539. RX PubMed=2917688; DOI=10.1016/0303-7207(89)90137-8; RA Faber P.W., Kuiper G.G.J.M., van Rooij H.C.J., van der Korput J.A.G.M., RA Brinkmann A.O., Trapman J.; RT "The N-terminal domain of the human androgen receptor is encoded by one, RT large exon."; RL Mol. Cell. Endocrinol. 61:257-262(1989). RN [13] RP NUCLEOTIDE SEQUENCE [MRNA] OF 191-920 (ISOFORM 1). RX PubMed=3353726; DOI=10.1126/science.3353726; RA Chang C., Kokontis J., Liao S.; RT "Molecular cloning of human and rat complementary DNA encoding androgen RT receptors."; RL Science 240:324-326(1988). RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 448-476. RC TISSUE=Blood; RA Lu J., Danielsen M.; RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases. RN [15] RP NUCLEOTIDE SEQUENCE [MRNA] OF 470-920 (ISOFORM 1). RX PubMed=3377788; DOI=10.1016/s0006-291x(88)81214-2; RA Trapman J., Klaassen P., Kuiper G.G.J.M., van der Korput J.A.G.M., RA Faber P.W., van Rooij H.C.J., Geurts van Kessel A., Voorhorst M.M., RA Mulder E., Brinkmann A.O.; RT "Cloning, structure and expression of a cDNA encoding the human androgen RT receptor."; RL Biochem. Biophys. Res. Commun. 153:241-248(1988). RN [16] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 537-541; 587-591; 626-630; 722-726; RP 770-774; 814-817 AND 866-870. RX PubMed=2546571; DOI=10.1677/jme.0.002r001; RA Kuiper G.G., Faber P.W., van Rooij H.C., van der Korput J.A., RA Ris-Stalpers C., Klaassen P., Trapman J., Brinkmann A.O.; RT "Structural organization of the human androgen receptor gene."; RL J. Mol. Endocrinol. 2:R1-R4(1989). RN [17] RP NUCLEOTIDE SEQUENCE [MRNA] OF 558-625 (ISOFORMS 1/2), AND VARIANT AIS RP HIS-616. RC TISSUE=Fibroblast; RX PubMed=8413310; DOI=10.1210/mend.7.7.8413310; RA Mowszowicz I., Lee H.-J., Chen H.-T., Mestayer C., Portois M.-C., RA Cabrol S., Mauvais-Jarvis P., Chang C.; RT "A point mutation in the second zinc finger of the DNA-binding domain of RT the androgen receptor gene causes complete androgen insensitivity in two RT siblings with receptor-positive androgen resistance."; RL Mol. Endocrinol. 7:861-869(1993). RN [18] RP NUCLEOTIDE SEQUENCE [MRNA] OF 560-625 (ISOFORMS 1/2). RX PubMed=3353727; DOI=10.1126/science.3353727; RA Lubahn D.B., Joseph D.R., Sullivan P.M., Willard H.F., French F.S., RA Wilson E.M.; RT "Cloning of human androgen receptor complementary DNA and localization to RT the X chromosome."; RL Science 240:327-330(1988). RN [19] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 630-724, AND VARIANTS AIS ASN-696 AND RP HIS-696. RX PubMed=1775137; DOI=10.1210/mend-5-10-1562; RA Ris-Stalpers C., Trifiro M.A., Kuiper G.G.J.M., Jenster G., Romalo G., RA Sai T., van Rooij H.C.J., Kaufman M., Rosenfield R.L., Liao S., RA Schweikert H.-U., Trapman J., Pinsky L., Brinkmann A.O.; RT "Substitution of aspartic acid-686 by histidine or asparagine in the human RT androgen receptor leads to a functionally inactive protein with altered RT hormone-binding characteristics."; RL Mol. Endocrinol. 5:1562-1569(1991). RN [20] RP POLYMORPHISM OF POLY-GLN REGION. RX PubMed=1561105; DOI=10.1093/nar/20.6.1427-a; RA Sleddens H.F.B.M., Oostra B.A., Brinkmann A.O., Trapman J.; RT "Trinucleotide repeat polymorphism in the androgen receptor gene (AR)."; RL Nucleic Acids Res. 20:1427-1427(1992). RN [21] RP POLYMORPHISM OF POLY-GLN REGION. RX PubMed=9096391; DOI=10.1073/pnas.94.7.3320; RA Giovannucci E., Stampfer M.J., Krithivas K., Brown M., Dahl D., Brufsky A., RA Talcott J., Hennekens C.H., Kantoff P.W.; RT "The CAG repeat within the androgen receptor gene and its relationship to RT prostate cancer."; RL Proc. Natl. Acad. Sci. U.S.A. 94:3320-3323(1997). RN [22] RP ERRATUM OF PUBMED:9096391. RA Giovannucci E., Stampfer M.J., Krithivas K., Brown M., Dahl D., Brufsky A., RA Talcott J., Hennekens C.H., Kantoff P.W.; RL Proc. Natl. Acad. Sci. U.S.A. 94:8272-8272(1997). RN [23] RP INTERACTION WITH PQBP1. RC TISSUE=Brain; RX PubMed=10332029; DOI=10.1093/hmg/8.6.977; RA Waragai M., Lammers C.-H., Takeuchi S., Imafuku I., Udagawa Y., RA Kanazawa I., Kawabata M., Mouradian M.M., Okazawa H.; RT "PQBP-1, a novel polyglutamine tract binding protein, inhibits RT transcription activation by Brn-2 and affects cell survival."; RL Hum. Mol. Genet. 8:977-987(1999). RN [24] RP INTERACTION WITH TGFB1I1. RX PubMed=10075738; DOI=10.1074/jbc.274.12.8316; RA Fujimoto N., Yeh S., Kang H.-Y., Inui S., Chang H.-C., Mizokami A., RA Chang C.; RT "Cloning and characterization of androgen receptor coactivator, ARA55, in RT human prostate."; RL J. Biol. Chem. 274:8316-8321(1999). RN [25] RP INTERACTION WITH UBE2I. RX PubMed=10383460; DOI=10.1074/jbc.274.27.19441; RA Poukka H., Aarnisalo P., Karvonen U., Palvimo J.J., Jaenne O.A.; RT "Ubc9 interacts with the androgen receptor and activates receptor-dependent RT transcription."; RL J. Biol. Chem. 274:19441-19446(1999). RN [26] RP INTERACTION WITH RAN. RX PubMed=10400640; DOI=10.1074/jbc.274.29.20229; RA Hsiao P.-W., Lin D.-L., Nakao R., Chang C.; RT "The linkage of Kennedy's neuron disease to ARA24, the first identified RT androgen receptor polyglutamine region-associated coactivator."; RL J. Biol. Chem. 274:20229-20234(1999). RN [27] RP INTERACTION WITH SPDEF. RX PubMed=10625666; DOI=10.1074/jbc.275.2.1216; RA Oettgen P., Finger E., Sun Z., Akbarali Y., Thamrongsak U., Boltax J., RA Grall F., Dube A., Weiss A., Brown L., Quinn G., Kas K., Endress G., RA Kunsch C., Libermann T.A.; RT "PDEF, a novel prostate epithelium-specific ets transcription factor, RT interacts with the androgen receptor and activates prostate-specific RT antigen gene expression."; RL J. Biol. Chem. 275:1216-1225(2000). RN [28] RP INTERACTION WITH KAT7. RX PubMed=10930412; DOI=10.1074/jbc.m004838200; RA Sharma M., Zarnegar M., Li X., Lim B., Sun Z.; RT "Androgen receptor interacts with a novel MYST protein, HBO1."; RL J. Biol. Chem. 275:35200-35208(2000). RN [29] RP SUMOYLATION AT LYS-388 AND LYS-521. RX PubMed=11121022; DOI=10.1073/pnas.97.26.14145; RA Poukka H., Karvonen U., Jaenne O.A., Palvimo J.J.; RT "Covalent modification of the androgen receptor by small ubiquitin-like RT modifier 1 (SUMO-1)."; RL Proc. Natl. Acad. Sci. U.S.A. 97:14145-14150(2000). RN [30] RP INTERACTION WITH RANBP9. RX PubMed=12361945; DOI=10.1074/jbc.m209741200; RA Rao M.A., Cheng H., Quayle A.N., Nishitani H., Nelson C.C., Rennie P.S.; RT "RanBPM, a nuclear protein that interacts with and regulates RT transcriptional activity of androgen receptor and glucocorticoid RT receptor."; RL J. Biol. Chem. 277:48020-48027(2002). RN [31] RP INTERACTION WITH PRPF6. RX PubMed=12039962; DOI=10.1074/jbc.m203811200; RA Zhao Y., Goto K., Saitoh M., Yanase T., Nomura M., Okabe T., Takayanagi R., RA Nawata H.; RT "Activation function-1 domain of androgen receptor contributes to the RT interaction between subnuclear splicing factor compartment and nuclear RT receptor compartment. Identification of the p102 U5 small nuclear RT ribonucleoprotein particle-binding protein as a coactivator for the RT receptor."; RL J. Biol. Chem. 277:30031-30039(2002). RN [32] RP RETRACTED PAPER. 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 RETRACTION NOTICE OF PUBMED:12415108. RX PubMed=19666546; DOI=10.1073/pnas.0908685106; RA Wong C.W., McNally C., Nickbarg E., Komm B.S., Cheskis B.J.; RL Proc. Natl. Acad. Sci. U.S.A. 106:14180-14180(2009). RN [34] RP INTERACTION WITH ZMIZ1. RX PubMed=14609956; DOI=10.1093/emboj/cdg585; RA Sharma M., Li X., Wang Y., Zarnegar M., Huang C.-Y., Palvimo J.J., Lim B., RA Sun Z.; RT "hZimp10 is an androgen receptor co-activator and forms a complex with RT SUMO-1 at replication foci."; RL EMBO J. 22:6101-6114(2003). RN [35] 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 [36] 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 [37] RP INTERACTION WITH EFCAB6. RX PubMed=12612053; RA Niki T., Takahashi-Niki K., Taira T., Iguchi-Ariga S.M.M., Ariga H.; RT "DJBP: a novel DJ-1-binding protein, negatively regulates the androgen RT receptor by recruiting histone deacetylase complex, and DJ-1 antagonizes RT this inhibition by abrogation of this complex."; RL Mol. Cancer Res. 1:247-261(2003). RN [38] RP PHOSPHORYLATION BY PAK6. RX PubMed=14573606; DOI=10.1074/jbc.m311145200; RA Schrantz N., da Silva Correia J., Fowler B., Ge Q., Sun Z., Bokoch G.M.; RT "Mechanism of p21-activated kinase 6-mediated inhibition of androgen RT receptor signaling."; RL J. Biol. Chem. 279:1922-1931(2004). RN [39] RP INTERACTION WITH HIP1. RX PubMed=16027218; DOI=10.1083/jcb.200503106; RA Mills I.G., Gaughan L., Robson C., Ross T., McCracken S., Kelly J., RA Neal D.E.; RT "Huntingtin interacting protein 1 modulates the transcriptional activity of RT nuclear hormone receptors."; RL J. Cell Biol. 170:191-200(2005). RN [40] RP INTERACTION WITH ZMIZ2. RX PubMed=16051670; DOI=10.1210/me.2005-0097; RA Huang C.-Y., Beliakoff J., Li X., Lee J., Li X., Sharma M., Lim B., Sun Z.; RT "hZimp7, a novel PIAS-like protein, enhances androgen receptor-mediated RT transcription and interacts with SWI/SNF-like BAF complexes."; RL Mol. Endocrinol. 19:2915-2929(2005). RN [41] RP PHOSPHORYLATION AT TYR-225; TYR-269; TYR-309; TYR-348; TYR-359; TYR-364; RP TYR-365; TYR-395; TYR-535; TYR-552 AND TYR-916, MUTAGENESIS OF TYR-225; RP TYR-269; TYR-309; TYR-348; TYR-359; TYR-364; TYR-365; TYR-395; TYR-535; RP TYR-552 AND TYR-916, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=17045208; DOI=10.1016/j.ccr.2006.08.021; RA Guo Z., Dai B., Jiang T., Xu K., Xie Y., Kim O., Nesheiwat I., Kong X., RA Melamed J., Handratta V.D., Njar V.C., Brodie A.M., Yu L.-R., RA Veenstra T.D., Chen H., Qiu Y.; RT "Regulation of androgen receptor activity by tyrosine phosphorylation."; RL Cancer Cell 10:309-319(2006). RN [42] RP ERRATUM OF PUBMED:17045208. RA Guo Z., Dai B., Jiang T., Xu K., Xie Y., Kim O., Nesheiwat I., Kong X., RA Melamed J., Handratta V.D., Njar V.C., Brodie A.M., Yu L.-R., RA Veenstra T.D., Chen H., Qiu Y.; RL Cancer Cell 11:97-97(2007). RN [43] RP INTERACTION WITH MAK, AND SUBUNIT. RX PubMed=16951154; DOI=10.1158/0008-5472.can-06-1636; RA Ma A.H., Xia L., Desai S.J., Boucher D.L., Guan Y., Shih H.M., Shi X.B., RA deVere White R.W., Chen H.W., Tepper C.G., Kung H.J.; RT "Male germ cell-associated kinase, a male-specific kinase regulated by RT androgen, is a coactivator of androgen receptor in prostate cancer cells."; RL Cancer Res. 66:8439-8447(2006). RN [44] RP INTERACTION WITH PRMT2, AND SUBCELLULAR LOCATION. RX PubMed=17587566; DOI=10.1016/j.jsbmb.2007.05.006; RA Meyer R., Wolf S.S., Obendorf M.; RT "PRMT2, a member of the protein arginine methyltransferase family, is a RT coactivator of the androgen receptor."; RL J. Steroid Biochem. Mol. Biol. 107:1-14(2007). RN [45] RP INTERACTION WITH RREB1. RX PubMed=17550981; DOI=10.1210/me.2006-0503; RA Mukhopadhyay N.K., Cinar B., Mukhopadhyay L., Lutchman M., Ferdinand A.S., RA Kim J., Chung L.W.K., Adam R.M., Ray S.K., Leiter A.B., Richie J.P., RA Liu B.C.-S., Freeman M.R.; RT "The zinc finger protein Ras-responsive element binding protein-1 is a RT coregulator of the androgen receptor: implications for the role of the Ras RT pathway in enhancing androgenic signaling in prostate cancer."; RL Mol. Endocrinol. 21:2056-2070(2007). RN [46] 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 [47] RP INTERACTION WITH TNK2, PHOSPHORYLATION AT TYR-269 AND TYR-365 BY TNK2, AND RP MUTAGENESIS OF TYR-269 AND TYR-365. RX PubMed=17494760; DOI=10.1073/pnas.0700420104; RA Mahajan N.P., Liu Y., Majumder S., Warren M.R., Parker C.E., Mohler J.L., RA Earp H.S., Whang Y.E.; RT "Activated Cdc42-associated kinase Ack1 promotes prostate cancer RT progression via androgen receptor tyrosine phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 104:8438-8443(2007). RN [48] RP INTERACTION WITH TRIM68. RX PubMed=18451177; DOI=10.1158/0008-5472.can-07-6059; RA Miyajima N., Maruyama S., Bohgaki M., Kano S., Shigemura M., Shinohara N., RA Nonomura K., Hatakeyama S.; RT "TRIM68 regulates ligand-dependent transcription of androgen receptor in RT prostate cancer cells."; RL Cancer Res. 68:3486-3494(2008). RN [49] RP INTERACTION WITH LPXN. RX PubMed=18451096; DOI=10.1210/me.2006-0546; RA Kaulfuss S., Grzmil M., Hemmerlein B., Thelen P., Schweyer S., Neesen J., RA Bubendorf L., Glass A.G., Jarry H., Auber B., Burfeind P.; RT "Leupaxin, a novel coactivator of the androgen receptor, is expressed in RT prostate cancer and plays a role in adhesion and invasion of prostate RT carcinoma cells."; RL Mol. Endocrinol. 22:1606-1621(2008). RN [50] 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 [51] RP INTERACTION WITH TRIM24. RX PubMed=19909775; DOI=10.1016/j.bbamcr.2009.11.001; RA Kikuchi M., Okumura F., Tsukiyama T., Watanabe M., Miyajima N., Tanaka J., RA Imamura M., Hatakeyama S.; RT "TRIM24 mediates ligand-dependent activation of androgen receptor and is RT repressed by a bromodomain-containing protein, BRD7, in prostate cancer RT cells."; RL Biochim. Biophys. Acta 1793:1828-1836(2009). RN [52] RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, POLYUBIQUITINATION AT RP LYS-846 AND LYS-848 BY RNF6, MUTAGENESIS OF LYS-846 AND LYS-848, RP INTERACTION WITH RNF14 AND RNF6, AND SUBCELLULAR LOCATION. RX PubMed=19345326; DOI=10.1016/j.ccr.2009.02.021; RA Xu K., Shimelis H., Linn D.E., Jiang R., Yang X., Sun F., Guo Z., Chen H., RA Li W., Chen H., Kong X., Melamed J., Fang S., Xiao Z., Veenstra T.D., RA Qiu Y.; RT "Regulation of androgen receptor transcriptional activity and specificity RT by RNF6-induced ubiquitination."; RL Cancer Cell 15:270-282(2009). RN [53] RP FUNCTION, AND INTERACTION WITH MACROD1. RX PubMed=19022849; DOI=10.1677/erc-08-0150; RA Yang J., Zhao Y.-L., Wu Z.-Q., Si Y.-L., Meng Y.G., Fu X.B., Mu Y.-M., RA Han W.-D.; RT "The single-macro domain protein LRP16 is an essential cofactor of androgen RT receptor."; RL Endocr. Relat. Cancer 16:139-153(2009). RN [54] RP FUNCTION IN AR KINASE, PHOSPHORYLATION AT SER-83 BY CDK9, MUTAGENESIS OF RP SER-83, AND INTERACTION WITH CDK9. RX PubMed=20980437; DOI=10.1210/me.2010-0238; RA Gordon V., Bhadel S., Wunderlich W., Zhang J., Ficarro S.B., Mollah S.A., RA Shabanowitz J., Hunt D.F., Xenarios I., Hahn W.C., Conaway M., Carey M.F., RA Gioeli D.; RT "CDK9 regulates AR promoter selectivity and cell growth through serine 81 RT phosphorylation."; RL Mol. Endocrinol. 24:2267-2280(2010). RN [55] 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 [56] RP PHOSPHORYLATION AT TYR-269, AND ACTIVITY REGULATION. RX PubMed=20623637; DOI=10.1002/pros.21163; RA Mahajan K., Challa S., Coppola D., Lawrence H., Luo Y., Gevariya H., RA Zhu W., Chen Y.A., Lawrence N.J., Mahajan N.P.; RT "Effect of Ack1 tyrosine kinase inhibitor on ligand-independent androgen RT receptor activity."; RL Prostate 70:1274-1285(2010). RN [57] 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 [58] RP FUNCTION, AND INTERACTION WITH NCOR1; NCOR2 AND ZBTB7A. RX PubMed=20812024; DOI=10.1007/s00018-010-0511-7; RA Cui J., Yang Y., Zhang C., Hu P., Kan W., Bai X., Liu X., Song H.; RT "FBI-1 functions as a novel AR co-repressor in prostate cancer cells."; RL Cell. Mol. Life Sci. 68:1091-1103(2011). RN [59] RP INTERACTION WITH CRY1. RX PubMed=22170608; DOI=10.1038/nature10700; RA Lamia K.A., Papp S.J., Yu R.T., Barish G.D., Uhlenhaut N.H., Jonker J.W., RA Downes M., Evans R.M.; RT "Cryptochromes mediate rhythmic repression of the glucocorticoid RT receptor."; RL Nature 480:552-556(2011). RN [60] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [61] RP PALMITOYLATION. RX PubMed=22031296; DOI=10.1091/mbc.e11-07-0638; RA Pedram A., Razandi M., Deschenes R.J., Levin E.R.; RT "DHHC-7 and -21 are palmitoylacyltransferases for sex steroid receptors."; RL Mol. Biol. Cell 23:188-199(2012). RN [62] RP INTERACTION WITH CCAR1 AND GATA2. RX PubMed=23887938; DOI=10.1093/nar/gkt644; RA Seo W.Y., Jeong B.C., Yu E.J., Kim H.J., Kim S.H., Lim J.E., Kwon G.Y., RA Lee H.M., Kim J.H.; RT "CCAR1 promotes chromatin loading of androgen receptor (AR) transcription RT complex by stabilizing the association between AR and GATA2."; RL Nucleic Acids Res. 41:8526-8536(2013). RN [63] RP INTERACTION WITH ARID4A. RX PubMed=23487765; DOI=10.1073/pnas.1218318110; RA Wu R.C., Jiang M., Beaudet A.L., Wu M.Y.; RT "ARID4A and ARID4B regulate male fertility, a functional link to the AR and RT RB pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:4616-4621(2013). RN [64] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND SER-258, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [65] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 658-920. RX PubMed=10840043; DOI=10.1074/jbc.m004571200; RA Matias P.M., Donner P., Coelho R., Thomaz M., Peixoto C., Macedo S., RA Otto N., Joschko S., Scholz P., Wegg A., Baesler S., Schaefer M., Egner U., RA Carrondo M.A.; RT "Structural evidence for ligand specificity in the binding domain of the RT human androgen receptor. Implications for pathogenic gene mutations."; RL J. Biol. Chem. 275:26164-26171(2000). RN [66] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 671-918. RX PubMed=11906285; DOI=10.1021/jm011072j; RA Matias P.M., Carrondo M.A., Coelho R., Thomaz M., Zhao X.Y., Wegg A., RA Crusius K., Egner U., Donner P.; RT "Structural basis for the glucocorticoid response in a mutant human RT androgen receptor (AR(ccr)) derived from an androgen-independent prostate RT cancer."; RL J. Med. Chem. 45:1439-1446(2002). RN [67] RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 672-920 IN COMPLEXES WITH RP N-TERMINAL MODULATING DOMAIN AND NCOA2, INTERACTION WITH NCOA1, AND RP CHARACTERIZATION OF VARIANT PROSTATE CANCER MET-731. RX PubMed=15525515; DOI=10.1016/j.molcel.2004.09.036; RA He B., Gampe R.T. Jr., Kole A.J., Hnat A.T., Stanley T.B., An G., RA Stewart E.L., Kalman R.I., Minges J.T., Wilson E.M.; RT "Structural basis for androgen receptor interdomain and coactivator RT interactions suggests a transition in nuclear receptor activation function RT dominance."; RL Mol. Cell 16:425-438(2004). RN [68] RP X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 670-920 IN COMPLEXES WITH RP DIHYDROTESTOSTERONE AND NCOA1; NCOA2; NCOA3 AND NCOA4, FUNCTION, RP INTERACTION WITH NCOA1; NCOA2; NCOA3 AND NCOA4, AND MUTAGENESIS OF LYS-721 RP AND GLU-898. RX PubMed=15563469; DOI=10.1074/jbc.m407046200; RA Estebanez-Perpina E., Moore J.M.R., Mar E., Delgado-Rodrigues E., RA Nguyen P., Baxter J.D., Buehrer B.M., Webb P., Fletterick R.J., Guy R.K.; RT "The molecular mechanisms of coactivator utilization in ligand-dependent RT transactivation by the androgen receptor."; RL J. Biol. Chem. 280:8060-8068(2005). RN [69] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 665-920 IN COMPLEXES WITH RP NONSTEROIDAL LIGANDS, MUTAGENESIS OF TRP-742, CHARACTERIZATION OF VARIANT RP PROSTATE CANCER ALA-878, AND CHARACTERIZATION OF VARIANT AIS THR-896. RX PubMed=16129672; DOI=10.1074/jbc.m507464200; RA Bohl C.E., Miller D.D., Chen J., Bell C.E., Dalton J.T.; RT "Structural basis for accommodation of nonsteroidal ligands in the androgen RT receptor."; RL J. Biol. Chem. 280:37747-37754(2005). RN [70] RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 655-920 IN COMPLEXES WITH RP TESTOSTERONE; DIHYDROTESTOSTERONE AND TETRAHYDROGESTRINONE. RX PubMed=16641486; DOI=10.1110/ps.051905906; RA Pereira de Jesus-Tran K., Cote P.-L., Cantin L., Blanchet J., Labrie F., RA Breton R.; RT "Comparison of crystal structures of human androgen receptor ligand-binding RT domain complexed with various agonists reveals molecular determinants RT responsible for binding affinity."; RL Protein Sci. 15:987-999(2006). RN [71] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 672-919 IN COMPLEX WITH NR0B2. RX PubMed=18007036; DOI=10.1107/s0907444907045702; RA Jouravel N., Sablin E., Arnold L.A., Guy R.K., Fletterick R.J.; RT "Interaction between the androgen receptor and a segment of its corepressor RT SHP."; RL Acta Crystallogr. D 63:1198-1200(2007). RN [72] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 671-919 OF MUTANT ALA-878 IN RP COMPLEX WITH THE ANTIANDROGEN CYPROTERONE ACETATE, CHARACTERIZATION OF RP VARIANT PROSTATE CANCER ALA-878, AND MUTAGENESIS OF LEU-702. RX PubMed=17311914; DOI=10.1074/jbc.m611711200; RA Bohl C.E., Wu Z., Miller D.D., Bell C.E., Dalton J.T.; RT "Crystal structure of the T877A human androgen receptor ligand-binding RT domain complexed to cyproterone acetate provides insight for ligand-induced RT conformational changes and structure-based drug design."; RL J. Biol. Chem. 282:13648-13655(2007). RN [73] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 663-919 OF WILD-TYPE AND MUTANT RP TYR-875 IN COMPLEX WITH TESTOSTERONE AND NCOA2, ACTIVATION BY THE RP N-TERMINAL MODULATING DOMAIN, INTERACTION WITH NCOA2 AND MAGEA11, FUNCTION, RP MUTAGENESIS OF LYS-721 AND GLU-898, AND CHARACTERIZATION OF VARIANT RP PROSTATE CANCER TYR-875. RX PubMed=17591767; DOI=10.1074/jbc.m703268200; RA Askew E.B., Gampe R.T. Jr., Stanley T.B., Faggart J.L., Wilson E.M.; RT "Modulation of androgen receptor activation function 2 by testosterone and RT dihydrotestosterone."; RL J. Biol. Chem. 282:25801-25816(2007). RN [74] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 655-920 IN COMPLEX WITH EM5744. RX PubMed=17711855; DOI=10.1074/jbc.m705524200; RA Cantin L., Faucher F., Couture J.-F., de Jesus-Tran K.P., Legrand P., RA Ciobanu L.C., Frechette Y., Labrecque R., Singh S.M., Labrie F., Breton R.; RT "Structural characterization of the human androgen receptor ligand-binding RT domain complexed with EM5744, a rationally designed steroidal ligand RT bearing a bulky chain directed toward helix 12."; RL J. Biol. Chem. 282:30910-30919(2007). RN [75] 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 [76] {ECO:0007744|PDB:4OEA, ECO:0007744|PDB:4OED, ECO:0007744|PDB:4OEY, ECO:0007744|PDB:4OEZ, ECO:0007744|PDB:4OFR, ECO:0007744|PDB:4OFU, ECO:0007744|PDB:4OGH, ECO:0007744|PDB:4OH5, ECO:0007744|PDB:4OHA, ECO:0007744|PDB:4OIL} RP X-RAY CRYSTALLOGRAPHY (1.42 ANGSTROMS) OF 671-920 OF VARIANT PROSTATE RP CANCER ALA-878 AND WILD-TYPE IN COMPLEX WITH DIHYDROTESTOSTERONE AND BUD31 RP PEPTIDES, INTERACTION WITH BUD31, FUNCTION, SUBCELLULAR LOCATION, AND RP DOMAIN. RX PubMed=25091737; DOI=10.1016/j.molonc.2014.06.009; RA Hsu C.L., Liu J.S., Wu P.L., Guan H.H., Chen Y.L., Lin A.C., Ting H.J., RA Pang S.T., Yeh S.D., Ma W.L., Chen C.J., Wu W.G., Chang C.; RT "Identification of a new androgen receptor (AR) co-regulator BUD31 and RT related peptides to suppress wild-type and mutated AR-mediated prostate RT cancer growth via peptide screening and X-ray structure analysis."; RL Mol. Oncol. 8:1575-1587(2014). RN [77] RP REVIEW ON VARIANTS. RX PubMed=1458719; RA Pinsky L., Trifiro M.A., Kaufman M., Beitel L.K., Mhatre A., RA Kazemi-Esfarjani P., Sabbaghian N., Lumbroso R., Alvarado C., Vasiliou M., RA Gottlieb B.; RT "Androgen resistance due to mutation of the androgen receptor."; RL Clin. Invest. Med. 15:456-472(1992). RN [78] RP REVIEW ON VARIANTS AIS. RX PubMed=8339746; DOI=10.1007/bf02125442; RA Brown T.R., Scherer P.A., Chang Y.-T., Migeon C.J., Ghirri P., Murono K., RA Zhou Z.; RT "Molecular genetics of human androgen insensitivity."; RL Eur. J. Pediatr. 152 Suppl. 2:S62-S69(1993). RN [79] RP REVIEW ON VARIANTS. RX PubMed=8240973; DOI=10.1016/0960-0760(93)90178-y; RA Sultan C., Lumbroso S., Poujol N., Belon C., Boudon C., Lobaccaro J.-M.; RT "Mutations of androgen receptor gene in androgen insensitivity syndromes."; RL J. Steroid Biochem. Mol. Biol. 46:519-530(1993). RN [80] 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 [81] 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 [82] 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 [83] 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 [84] RP VARIANT LNCAP ALA-878. RX PubMed=2260966; DOI=10.1016/s0006-291x(05)80067-1; RA Veldscholte J., Ris-Stalpers C., Kuiper G.G.J.M., Jenster G., RA Berrevoets C.A., Claassen E., van Rooij H.C.J., Trapman J., Brinkmann A.O., RA Mulder E.; RT "A mutation in the ligand binding domain of the androgen receptor of human RT LNCaP cells affects steroid binding characteristics and response to anti- RT androgens."; RL Biochem. Biophys. Res. Commun. 173:534-540(1990). RN [85] 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 [86] RP VARIANT CYS-775. RX PubMed=1856263; DOI=10.1210/jcem-73-2-318; RA Marcelli M., Tilley W.D., Zoppi S., Griffin J.E., Wilson J.D., RA McPhaul M.J.; RT "Androgen resistance associated with a mutation of the androgen receptor at RT amino acid 772 (Arg-->Cys) results from a combination of decreased RT messenger ribonucleic acid levels and impairment of receptor function."; RL J. Clin. Endocrinol. Metab. 73:318-325(1991). RN [87] RP VARIANT AIS PRO-618. RX PubMed=1999491; DOI=10.1172/jci115076; RA Marcelli M., Zoppi S., Grino P.B., Griffin J.E., Wilson J.D., McPhaul M.J.; RT "A mutation in the DNA-binding domain of the androgen receptor gene causes RT complete testicular feminization in a patient with receptor-positive RT androgen resistance."; RL J. Clin. Invest. 87:1123-1126(1991). RN [88] RP VARIANT PAIS CYS-764. RX PubMed=2010552; DOI=10.1172/jci115147; RA McPhaul M.J., Marcelli M., Tilley W.D., Griffin J.E., RA Isidro-Gutierrez R.F., Wilson J.D.; RT "Molecular basis of androgen resistance in a family with a qualitative RT abnormality of the androgen receptor and responsive to high-dose androgen RT therapy."; RL J. Clin. Invest. 87:1413-1421(1991). RN [89] RP POLY-GLN REGION EXPANSION, AND INVOLVEMENT IN SPINAL AND BULBAR MUSCULAR RP ATROPHY. RX PubMed=2062380; DOI=10.1038/352077a0; RA la Spada A.R., Wilson E.M., Lubahn D.B., Harding A.E., Fischbeck K.H.; RT "Androgen receptor gene mutations in X-linked spinal and bulbar muscular RT atrophy."; RL Nature 352:77-79(1991). RN [90] RP VARIANTS AIS CYS-775 AND HIS-775. RX PubMed=1609793; RA Prior L., Bordet S., Trifiro M.A., Mhatre A., Kaufman M., Pinsky L., RA Wrogemann K., Belsham D.D., Pereira F., Greenberg C.R., Trapman J., RA Brinkmann A.O., Chang C., Liao S.; RT "Replacement of arginine 773 by cysteine or histidine in the human androgen RT receptor causes complete androgen insensitivity with different receptor RT phenotypes."; RL Am. J. Hum. Genet. 51:143-155(1992). RN [91] RP VARIANTS PAIS LYS-609 AND LEU-867. RX PubMed=1424203; DOI=10.1111/j.1365-2265.1992.tb02313.x; RA Saunders P.T., Padayachi T., Tincello D.G., Shalet S.M., Wu F.C.; RT "Point mutations detected in the androgen receptor gene of three men with RT partial androgen insensitivity syndrome."; RL Clin. Endocrinol. (Oxf.) 37:214-220(1992). RN [92] RP VARIANT AIS THR-766. RX PubMed=1426313; DOI=10.1016/s0015-0282(16)55315-1; RA Sweet C.R., Behzadian M.A., McDonough P.G.; RT "A unique point mutation in the androgen receptor gene in a family with RT complete androgen insensitivity syndrome."; RL Fertil. Steril. 58:703-707(1992). RN [93] RP VARIANT AIS VAL-750. RX PubMed=1487249; DOI=10.1007/bf00220088; RA Jakubiczka S., Werder E.A., Wieacker P.; RT "Point mutation in the steroid-binding domain of the androgen receptor gene RT in a family with complete androgen insensitivity syndrome (CAIS)."; RL Hum. Genet. 90:311-312(1992). RN [94] RP VARIANTS AIS, AND VARIANTS PAIS. RX PubMed=1307250; DOI=10.1093/hmg/1.7.497; RA Batch J.A., Williams D.M., Davies H.R., Brown B.D., Evans B.A.J., RA Hughes I.A., Patterson M.N.; RT "Androgen receptor gene mutations identified by SSCP in fourteen subjects RT with androgen insensitivity syndrome."; RL Hum. Mol. Genet. 1:497-503(1992). RN [95] RP VARIANT AIS VAL-788. RX PubMed=1569163; DOI=10.1210/jcem.74.5.1569163; RA Nakao R., Haji M., Yanase T., Ogo A., Takayanagi R., Katsube T., RA Fukumaki Y., Nawata H.; RT "A single amino acid substitution (Met-786-->Val) in the steroid-binding RT domain of human androgen receptor leads to complete androgen insensitivity RT syndrome."; RL J. Clin. Endocrinol. Metab. 74:1152-1157(1992). RN [96] 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 [97] 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 [98] RP VARIANT PROSTATE CANCER ALA-878. RX PubMed=1562539; DOI=10.1016/0960-0760(92)90401-4; RA Veldscholte J., Berrevoets C.A., Ris-Stalpers C., Kuiper G.G.J.M., RA Jenster G., Trapman J., Brinkmann A.O., Mulder E.; RT "The androgen receptor in LNCaP cells contains a mutation in the ligand RT binding domain which affects steroid binding characteristics and response RT to antiandrogens."; RL J. Steroid Biochem. Mol. Biol. 41:665-669(1992). RN [99] RP VARIANTS AIS TYR-560 AND ARG-577, AND VARIANTS PAIS GLY-598 AND PRO-618. RX PubMed=1316540; DOI=10.1210/mend.6.3.1316540; RA Zoppi S., Marcelli M., Deslypere J.-P., Griffin J.E., Wilson J.D., RA McPhaul M.J.; RT "Amino acid substitutions in the DNA-binding domain of the human androgen RT receptor are a frequent cause of receptor-binding positive androgen RT resistance."; RL Mol. Endocrinol. 6:409-415(1992). RN [100] RP VARIANTS AIS SER-706; VAL-750; PHE-760; HIS-775; CYS-856 AND GLY-865. RX PubMed=1480178; DOI=10.1210/mend.6.11.1480178; RA De Bellis A., Quigley C.A., Cariello N.F., el-Awady M.K., Sar M., RA Lane M.V., Wilson E.M., French F.S.; RT "Single base mutations in the human androgen receptor gene causing complete RT androgen insensitivity: rapid detection by a modified denaturing gradient RT gel electrophoresis technique."; RL Mol. Endocrinol. 6:1909-1920(1992). RN [101] RP VARIANT PAIS/BREAST CANCER GLN-608. RX PubMed=1303262; DOI=10.1038/ng1092-132; RA Wooster R., Mangion J., Eeles R., Smith S., Dowsett M., Averill D., RA Barrett-Lee P., Easton D.F., Ponder B.A., Stratton M.R.; RT "A germline mutation in the androgen receptor gene in two brothers with RT breast cancer and Reifenstein syndrome."; RL Nat. Genet. 2:132-134(1992). RN [102] 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 [103] 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 [104] RP VARIANT AIS PHE-582. RX PubMed=8224266; DOI=10.1016/s0015-0282(16)56281-5; RA Lumbroso S., Lobaccaro J.-M., Belon C., Martin D., Chaussain J.-L., RA Sultan C.; RT "A new mutation within the deoxyribonucleic acid-binding domain of the RT androgen receptor gene in a family with complete androgen insensitivity RT syndrome."; RL Fertil. Steril. 60:814-819(1993). RN [105] RP VARIANT AIS VAL-755. RX PubMed=8103398; DOI=10.1093/hmg/2.7.1041; RA Lobaccaro J.-M., Lumbroso S., Ktari R., Dumas R., Sultan C.; RT "An exonic point mutation creates a MaeIII site in the androgen receptor RT gene of a family with complete androgen insensitivity syndrome."; RL Hum. Mol. Genet. 2:1041-1043(1993). RN [106] RP VARIANT PAIS/BREAST CANCER LYS-609. RX PubMed=8281139; DOI=10.1093/hmg/2.11.1799; RA Lobaccaro J.-M., Lumbroso S., Belon C., Galtier-Dereure F., Bringer J., RA Lesimple T., Namer M., Cutuli B.F., Pujol H., Sultan C.; RT "Androgen receptor gene mutation in male breast cancer."; RL Hum. Mol. Genet. 2:1799-1802(1993). RN [107] RP VARIANT AIS ARG-808. RX PubMed=8281140; DOI=10.1093/hmg/2.11.1809; RA Adeyemo O., Kallio P.J., Palvimo J.J., Kontula K., Jaenne O.A.; RT "A single-base substitution in exon 6 of the androgen receptor gene causing RT complete androgen insensitivity: the mutated receptor fails to RT transactivate but binds to DNA in vitro."; RL Hum. Mol. Genet. 2:1809-1812(1993). RN [108] RP VARIANT PAIS VAL-744. RX PubMed=8325932; DOI=10.1210/jcem.77.1.8325932; RA Nakao R., Yanase T., Sakai Y., Haji M., Nawata H.; RT "A single amino acid substitution (Gly743 --> Val) in the steroid-binding RT domain of the human androgen receptor leads to Reifenstein syndrome."; RL J. Clin. Endocrinol. Metab. 77:103-107(1993). RN [109] RP VARIANTS AIS LYS-682 AND THR-843, AND VARIANTS PAIS HIS-841 AND LEU-867. RX PubMed=8325950; DOI=10.1210/jcem.77.1.8325950; RA Hiort O., Huang Q., Sinnecker G.H., Sadeghi-Nejad A., Kruse K., Wolfe H.J., RA Yandell D.W.; RT "Single strand conformation polymorphism analysis of androgen receptor gene RT mutations in patients with androgen insensitivity syndromes: application RT for diagnosis, genetic counseling, and therapy."; RL J. Clin. Endocrinol. Metab. 77:262-266(1993). RN [110] RP INVOLVEMENT IN PAIS, INVOLVEMENT IN HYSP1, AND VARIANTS PAIS HIS-856 AND RP MET-870. RX PubMed=8097257; DOI=10.1136/jmg.30.3.198; RA Batch J.A., Evans B.A.J., Hughes I.A., Patterson M.N.; RT "Mutations of the androgen receptor gene identified in perineal RT hypospadias."; RL J. Med. Genet. 30:198-201(1993). RN [111] 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 [112] RP VARIANTS 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 [113] RP VARIANT AIS MET-867, AND VARIANT PAIS LEU-867. RX PubMed=8446106; DOI=10.1210/mend.7.1.8446106; RA Kazemi-Esfarjani P., Beitel L.K., Trifiro M.A., Kaufman M., Rennie P., RA Sheppard P., Matusik R., Pinsky L.; RT "Substitution of valine-865 by methionine or leucine in the human androgen RT receptor causes complete or partial androgen insensitivity, respectively RT with distinct androgen receptor phenotypes."; RL Mol. Endocrinol. 7:37-46(1993). RN [114] RP VARIANT PROSTATE CANCER MET-716. RX PubMed=8145761; DOI=10.1210/mend.7.12.8145761; RA Culig Z., Hobisch A., Cronauer M.V., Cato A.C.B., Hittmair A., Radmayr C., RA Eberle J., Bartsch G., Klocker H.; RT "Mutant androgen receptor detected in an advanced-stage prostatic carcinoma RT is activated by adrenal androgens and progesterone."; RL Mol. Endocrinol. 7:1541-1550(1993). RN [115] 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 [116] 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 [117] 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 [118] RP VARIANT PROSTATE CANCER ALA-878. RX PubMed=8187068; RA Gaddipati J.P., McLeod D.G., Heidenberg H.B., Sesterhenn I.A., Finger M.J., RA Moul J.W., Srivastava S.; RT "Frequent detection of codon 877 mutation in the androgen receptor gene in RT advanced prostate cancers."; RL Cancer Res. 54:2861-2864(1994). RN [119] RP VARIANT PAIS TRP-569. RX PubMed=7910529; DOI=10.1111/j.1365-2265.1994.tb03922.x; RA Lobaccaro J.-M., Belon C., Lumbroso S., Olewniczack G., Carre-Pigeon F., RA Job J.C., Chaussain J.L., Toublanc J.E., Sultan C.; RT "Molecular prenatal diagnosis of partial androgen insensitivity syndrome RT based on the Hind III polymorphism of the androgen receptor gene."; RL Clin. Endocrinol. (Oxf.) 40:297-302(1994). RN [120] RP VARIANT PAIS HIS-841. RX PubMed=7909256; DOI=10.1530/eje.0.1300327; RA Lumbroso S., Lobaccaro J.-M., Belon C., Amram S., Bachelard B., RA Garandeau P., Sultan C.; RT "Molecular prenatal exclusion of familial partial androgen insensitivity RT (Reifenstein syndrome)."; RL Eur. J. Endocrinol. 130:327-332(1994). RN [121] RP VARIANT PAIS HIS-841. RX PubMed=8205256; DOI=10.1530/eje.0.1300569; RA Imasaki K., Hasegawa T., Okabe T., Sakai Y., Haji M., Takayanagi R., RA Nawata H.; RT "Single amino acid substitution (840Arg-->His) in the hormone-binding RT domain of the androgen receptor leads to incomplete androgen insensitivity RT syndrome associated with a thermolabile androgen receptor."; RL Eur. J. Endocrinol. 130:569-574(1994). RN [122] RP VARIANT PAIS VAL-871. RX PubMed=8033918; DOI=10.1007/bf01956409; RA Hiort O., Klauber G., Cendron M., Sinnecker G.H., Keim L., Schwinger E., RA Wolfe H.J., Yandell D.W.; RT "Molecular characterization of the androgen receptor gene in boys with RT hypospadias."; RL Eur. J. Pediatr. 153:317-321(1994). RN [123] RP VARIANT PAIS ASP-691 DEL. RA Schwartz M., Skovby F., Mueller J., Nielsen O., Skakkebaek N.E.; RT "Partial androgen insensitivity (PAIS) in a large eskimo kindred caused by RT a delD690 mutation in the androgen receptor (AR) gene (Abstract #244)."; RL Horm. Res. 41:117-117(1994). RN [124] RP VARIANTS AIS PHE-583 DEL; ARG-616 DEL AND HIS-616. RX PubMed=8162033; DOI=10.1093/hmg/3.1.21; RA Beitel L.K., Prior L., Vasiliou D.M., Gottlieb B., Kaufman M., Lumbroso R., RA Alvarado C., McGillivray B., Trifiro M.A., Pinsky L.; RT "Complete androgen insensitivity due to mutations in the probable alpha- RT helical segments of the DNA-binding domain in the human androgen RT receptor."; RL Hum. Mol. Genet. 3:21-27(1994). RN [125] RP VARIANTS PAIS SER-583; TYR-605; ALA-709; LEU-755 AND HIS-772, AND VARIANT RP AIS TRP-780. RX PubMed=7981687; DOI=10.1093/hmg/3.7.1163; RA Hiort O., Wodtke A., Struve D., Zoellner A., Sinnecker G.H.; RT "Detection of point mutations in the androgen receptor gene using non- RT isotopic single strand conformation polymorphism analysis."; RL Hum. Mol. Genet. 3:1163-1166(1994). RN [126] RP VARIANT AIS PHE-602. RX PubMed=7981689; DOI=10.1093/hmg/3.7.1169; RA Baldazzi L., Baroncini C., Pirazzoli P., Balsamo A., Capelli M., RA Marchetti G., Bernardi F., Cacciari E.; RT "Two mutations causing complete androgen insensitivity: a frame-shift in RT the steroid binding domain and a Cys-->Phe substitution in the second zinc RT finger of the androgen receptor."; RL Hum. Mol. Genet. 3:1169-1170(1994). RN [127] RP VARIANTS PAIS ARG-617; HIS-841 AND MET-890. RX PubMed=8126121; DOI=10.1210/jcem.78.3.8126121; RA De Bellis A., Quigley C.A., Marschke K.B., el-Awady M.K., Lane M.V., RA Smith E.P., Sar M., Wilson E.M., French F.S.; RT "Characterization of mutant androgen receptors causing partial androgen RT insensitivity syndrome."; RL J. Clin. Endocrinol. Metab. 78:513-522(1994). RN [128] 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 [129] RP VARIANTS AIS CYS-841 AND HIS-841. RX PubMed=8040309; DOI=10.1172/jci117368; RA Beitel L.K., Kazemi-Esfarjani P., Kaufman M., Lumbroso R., DiGeorge A.M., RA Killinger D.W., Trifiro M.A., Pinsky L.; RT "Substitution of arginine-839 by cysteine or histidine in the androgen RT receptor causes different receptor phenotypes in cultured cells and RT coordinate degrees of clinical androgen resistance."; RL J. Clin. Invest. 94:546-554(1994). RN [130] RP VARIANTS AIS, AND VARIANTS PAIS. RX PubMed=7929841; DOI=10.1172/jci117507; RA Marcelli M., Zoppi S., Wilson C.M., Griffin J.E., McPhaul M.J.; RT "Amino acid substitutions in the hormone-binding domain of the human RT androgen receptor alter the stability of the hormone receptor complex."; RL J. Clin. Invest. 94:1642-1650(1994). RN [131] RP VARIANT AIS LYS-728. RX PubMed=7993455; DOI=10.1016/s0140-6736(94)92385-x; RA Yong E.L., Ng S.C., Roy A.C., Yun G., Ratnam S.S.; RT "Pregnancy after hormonal correction of severe spermatogenic defect due to RT mutation in androgen receptor gene."; RL Lancet 344:826-827(1994). RN [132] RP VARIANTS AIS HIS-616 AND LEU-765, AND VARIANTS PAIS VAL-743 AND THR-746. RX PubMed=7970939; DOI=10.1203/00006450-199408000-00015; RA Ris-Stalpers C., Hoogenboezem T., Sleddens H.F.B.M., RA Verleun-Mooijman M.C.T., Degenhart H.J., Drop S.L.S., Halley D.J.J., RA Oosterwijk J.C., Hodgins M.B., Trapman J., Brinkmann A.O.; RT "A practical approach to the detection of androgen receptor gene mutations RT and pedigree analysis in families with X-linked androgen insensitivity."; RL Pediatr. Res. 36:227-234(1994). RN [133] RP VARIANT AIS HIS-841. RX PubMed=8830623; DOI=10.1177/000456329503200508; RA Imai A., Ohno T., Iida K., Ohsuye K., Okano Y., Tamaya T.; RT "A frame-shift mutation of the androgen receptor gene in a patient with RT receptor-negative complete testicular feminization: comparison with a RT single base substitution in a receptor-reduced incomplete form."; RL Ann. Clin. Biochem. 32:482-486(1995). RN [134] 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 [135] RP VARIANT AIS VAL-882. RX PubMed=7641413; DOI=10.1111/j.1365-2265.1995.tb01895.x; RA Davies H.R., Hughes I.A., Patterson M.N.; RT "Genetic counselling in complete androgen insensitivity syndrome: RT trinucleotide repeat polymorphisms, single-strand conformation polymorphism RT and direct detection of two novel mutations in the androgen receptor RT gene."; RL Clin. Endocrinol. (Oxf.) 43:69-77(1995). RN [136] 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 [137] RP ERRATUM OF PUBMED:7671849. 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 [138] RP VARIANTS AIS LEU-832 AND GLN-832. RX PubMed=7633398; DOI=10.1093/hmg/4.4.515; RA Shkolny D.L., Brown T.R., Punnett H.H., Kaufman M., Trifiro M.A., RA Pinsky L.; RT "Characterization of alternative amino acid substitutions at arginine 830 RT of the androgen receptor that cause complete androgen insensitivity in RT three families."; RL Hum. Mol. Genet. 4:515-521(1995). RN [139] RP VARIANT AIS PRO-678. RX PubMed=7537149; DOI=10.1002/humu.1380050104; RA Belsham D.D., Pereira F., Greenberg C.R., Liao S., Wrogemann K.; RT "Leu-676-Pro mutation of the androgen receptor causes complete androgen RT insensitivity syndrome in a large Hutterite kindred."; RL Hum. Mutat. 5:28-33(1995). RN [140] RP VARIANT PAIS CYS-764, AND VARIANTS AIS TRP-780; VAL-808 AND CYS-856. RX PubMed=7581399; DOI=10.1002/humu.1380060208; RA Murono K., Mendonca B.B., Arnhold I.J.P., Rigon A.C.M.M., Migeon C.J., RA Brown T.R.; RT "Human androgen insensitivity due to point mutations encoding amino acid RT substitutions in the androgen receptor steroid-binding domain."; RL Hum. Mutat. 6:152-162(1995). RN [141] RP VARIANT PROSTATE CANCER MET-731. RX PubMed=7591265; DOI=10.1002/ijc.2910630415; RA Peterziel H., Culig Z., Stober J., Hobisch A., Radmayr C., Bartsch G., RA Klocker H., Cato A.C.B.; RT "Mutant androgen receptors in prostatic tumors distinguish between amino- RT acid-sequence requirements for transactivation and ligand binding."; RL Int. J. Cancer 63:544-550(1995). RN [142] 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 [143] 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 [144] 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 [145] RP VARIANTS PROSTATE CANCER. RX PubMed=7723794; DOI=10.1056/nejm199505253322101; RA Taplin M.-E., Bubley G.J., Shuster T.D., Frantz M.E., Spooner A.E., RA Ogata G.K., Keer H.N., Balk S.P.; RT "Mutation of the androgen-receptor gene in metastatic androgen-independent RT prostate cancer."; RL N. Engl. J. Med. 332:1393-1398(1995). RN [146] RP VARIANTS AIS AND PAIS. RX PubMed=8723113; RX DOI=10.1002/(sici)1096-8628(19960503)63:1<218::aid-ajmg38>3.0.co;2-p; RA Hiort O., Sinnecker G.H., Holterhus P.M., Nitsche E.M., Kruse K.; RT "The clinical and molecular spectrum of androgen insensitivity syndromes."; RL Am. J. Med. Genet. 63:218-222(1996). RN [147] RP VARIANTS PROSTATE CANCER. RX PubMed=9816170; RA Tilley W.D., Buchanan G., Hickey T.E., Bentel J.M.; RT "Mutations in the androgen receptor gene are associated with progression of RT human prostate cancer to androgen independence."; RL Clin. Cancer Res. 2:277-285(1996). RN [148] RP VARIANTS PAIS GLN-608; THR-611; LEU-755; HIS-841; THR-843 AND HIS-856, AND RP VARIANT AIS MET-867. RX PubMed=9039340; DOI=10.1046/j.1365-2265.1996.8600869.x; RA Weidemann W., Linck B., Haupt H., Mentrup B., Romalo G., Stockklauser K., RA Brinkmann A.O., Schweikert H.-U., Spindler K.D.; RT "Clinical and biochemical investigations and molecular analysis of subjects RT with mutations in the androgen receptor gene."; RL Clin. Endocrinol. (Oxf.) 45:733-739(1996). RN [149] RP VARIANT AIS CYS-856. RX PubMed=9001799; DOI=10.1111/j.1399-0004.1996.tb02626.x; RA Malmgren H., Gustavsson J., Tuvemo T., Dahl N.; RT "Rapid detection of a mutation hot-spot in the human androgen receptor."; RL Clin. Genet. 50:202-205(1996). RN [150] 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 [151] RP VARIANT PAIS ARG-910. RX PubMed=8550758; DOI=10.1210/jcem.81.1.8550758; RA Choong C.S., Sturm M.J., Strophair J.A., McCulloch R.K., Tilley W.D., RA Leedman P.J., Hurley D.M.; RT "Partial androgen insensitivity caused by an androgen receptor mutation at RT amino acid 907 (Gly-->Arg) that results in decreased ligand binding RT affinity and reduced androgen receptor messenger ribonucleic acid levels."; RL J. Clin. Endocrinol. Metab. 81:236-243(1996). RN [152] RP VARIANT AIS ARG-708. RX PubMed=8626869; DOI=10.1210/jcem.81.5.8626869; RA Lumbroso S., Lobaccaro J.-M., Georget V., Leger J., Poujol N., RA Terouanne B., Evain-Brion D., Czernichow P., Sultan C.; RT "A novel substitution (Leu707Arg) in exon 4 of the androgen receptor gene RT causes complete androgen resistance."; RL J. Clin. Endocrinol. Metab. 81:1984-1988(1996). RN [153] RP VARIANT AIS ILE-781. RX PubMed=8768864; DOI=10.1210/jcem.81.8.8768864; RA Rodien P., Mebarki F., Mowszowicz I., Chaussain J.L., Young J., Morel Y., RA Schaison G.; RT "Different phenotypes in a family with androgen insensitivity caused by the RT same M780I point mutation in the androgen receptor gene."; RL J. Clin. Endocrinol. Metab. 81:2994-2998(1996). RN [154] 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 [155] 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 [156] RP VARIANT AIS SER-549. RX PubMed=8683794; DOI=10.1097/00005392-199608001-00077; RA Sutherland R.W., Wiener J.S., Hicks J.P., Marcelli M., Gonzales E.T. Jr., RA Roth D.R., Lamb D.J.; RT "Androgen receptor gene mutations are rarely associated with isolated RT penile hypospadias."; RL J. Urol. 156:828-831(1996). RN [157] RP VARIANT AIS PRO-617. RX PubMed=8647313; DOI=10.1016/0303-7207(95)03709-8; RA Lobaccaro J.-M., Poujol N., Chiche L., Lumbroso S., Brown T.R., Sultan C.; RT "Molecular modeling and in vitro investigations of the human androgen RT receptor DNA-binding domain: application for the study of two mutations."; RL Mol. Cell. Endocrinol. 116:137-147(1996). RN [158] RP VARIANT AIS PHE-580, AND VARIANT PAIS TYR-583. RX PubMed=8809734; DOI=10.1016/0303-7207(96)03812-9; RA Imasaki K., Okabe T., Murakami H., Tanaka Y., Haji M., Takayanagi R., RA Nawata H.; RT "Androgen insensitivity syndrome due to new mutations in the DNA-binding RT domain of the androgen receptor."; RL Mol. Cell. Endocrinol. 120:15-24(1996). RN [159] 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 [160] 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 [161] RP VARIANT AIS HIS-856. RX PubMed=9106550; RA Boehmer A.L.M., Brinkmann A.O., Niermeijer M.F., Bakker L., Halley D.J.J., RA Drop S.L.S.; RT "Germ-line and somatic mosaicism in the androgen insensitivity syndrome: RT implications for genetic counseling."; RL Am. J. Hum. Genet. 60:1003-1006(1997). RN [162] RP VARIANT PROSTATE CANCER ALA-684. RX PubMed=9000575; RA Koivisto P., Kononen J., Palmberg C., Tammela T., Hyytinen E., Isola J., RA Trapman J., Cleutjens K., Noordzij A., Visakorpi T., Kallioniemi O.-P.; RT "Androgen receptor gene amplification: a possible molecular mechanism for RT androgen deprivation therapy failure in prostate cancer."; RL Cancer Res. 57:314-319(1997). RN [163] RP VARIANTS PAIS LYS-609 AND GLY-773. RX PubMed=9196614; DOI=10.1046/j.1365-2265.1997.1140927.x; RA Tincello D.G., Saunders P.T., Hodgins M.B., Simpson N.B., Edwards C.R., RA Hargreaves T.B., Wu F.C.; RT "Correlation of clinical, endocrine and molecular abnormalities with in RT vivo responses to high-dose testosterone in patients with partial androgen RT insensitivity syndrome."; RL Clin. Endocrinol. (Oxf.) 46:497-506(1997). RN [164] RP VARIANT AIS MET-890. RX PubMed=9160185; RA Essawi M., Gad Y.Z., el-Rouby O., Temtamy S.A., Sabour Y.A., el-Awady M.K.; RT "Molecular analysis of androgen resistance syndromes in Egyptian RT patients."; RL Dis. Markers 13:99-105(1997). RN [165] RP VARIANT AIS TRP-780. RX PubMed=9007482; DOI=10.1007/s004310050542; RA Sinnecker G.H., Hiort O., Nitsche E.M., Holterhus P.M., Kruse K.; RT "Functional assessment and clinical classification of androgen sensitivity RT in patients with mutations of the androgen receptor gene."; RL Eur. J. Pediatr. 156:7-14(1997). RN [166] 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>3.0.co;2-o; RA Jakubiczka S., Nedel S., Werder E.A., Schleiermacher E., Theile U., RA Wolff G., Wieacker P.; RT "Mutations of the androgen receptor gene in patients with complete androgen RT insensitivity."; RL Hum. Mutat. 9:57-61(1997). RN [167] RP VARIANTS HIS-702 AND ARG-911. RX PubMed=9438000; DOI=10.1093/jjco/27.6.389; RA Watanabe M., Ushijima T., Shiraishi T., Yatani R., Shimazaki J., Kotake T., RA Sugimura T., Nagao M.; RT "Genetic alterations of androgen receptor gene in Japanese human prostate RT cancer."; RL Jpn. J. Clin. Oncol. 27:389-393(1997). RN [168] 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 [169] 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 [170] RP VARIANTS PAIS ALA-709 AND GLY-871. RX PubMed=9329414; DOI=10.1016/s0022-3476(97)80063-7; RA Albers N., Ulrichs C., Gluer S., Hiort O., Sinnecker G.H., Mildenberger H., RA Brodehl J.; RT "Etiologic classification of severe hypospadias: implications for prognosis RT and management."; RL J. Pediatr. 131:386-392(1997). RN [171] RP VARIANTS AIS ASN-733 AND THR-766. RX PubMed=9252933; RA Ko T.M., Yang Y.S., Wu M.Y., Kao C.H., Hsu P.M., Chuang S.M., Lee T.Y.; RT "Complete androgen insensitivity syndrome. Molecular characterization in RT two Chinese women."; RL J. Reprod. Med. 42:424-428(1997). RN [172] 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 [173] RP VARIANT PAIS GLY-704, AND VARIANT AIS LEU-917. RX PubMed=9302173; DOI=10.1097/00005392-199710000-00075; RA Radmayr C., Culig Z., Glatzl J., Neuschmid-Kaspar F., Bartsch G., RA Klocker H.; RT "Androgen receptor point mutations as the underlying molecular defect in 2 RT patients with androgen insensitivity syndrome."; RL J. Urol. 158:1553-1556(1997). RN [174] 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 [175] 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 [176] RP VARIANT ARG-216, AND CHARACTERIZATION OF VARIANT ARG-216. RX PubMed=9788719; DOI=10.1111/j.1399-0004.1998.tb04282.x; 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 [177] RP VARIANTS AIS PRO-257 AND ALA-821. RX PubMed=9610419; DOI=10.3109/09513599809024954; RA Tanaka H., Komori S., Sakata K., Shima H., Koyama K.; RT "One additional mutation at exon A amplifies thermolability of androgen RT receptor in a case with complete androgen insensitivity syndrome."; RL Gynecol. Endocrinol. 12:75-82(1998). RN [178] RP VARIANTS AIS THR-766; TYR-785 AND THR-896, AND VARIANT PAIS GLY-841. RX PubMed=9856504; DOI=10.1007/s004390050864; RA Lundberg Giwercman Y., Nikoshkov A., Lindsten K., Bystroem B., Pousette A., RA Chibalin A.V., Arvidsson S., Tiulpakov A., Semitcheva T.V., Peterkova V., RA Hagenfeldt K., Ritzen E.M., Wedell A.; RT "Functional characterisation of mutations in the ligand-binding domain of RT the androgen receptor gene in patients with androgen insensitivity RT syndrome."; RL Hum. Genet. 103:529-531(1998). RN [179] RP VARIANT AIS VAL-696. RX PubMed=9554754; RA Doerk T., Schnieders F., Jakubiczka S., Wieacker P., Schroeder-Kurth T., RA Schmidtke J.; RT "A new missense substitution at a mutational hot spot of the androgen RT receptor in siblings with complete androgen insensitivity syndrome."; RL Hum. Mutat. 11:337-339(1998). RN [180] 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 [181] RP VARIANT AIS LEU-893. RA Knoke I., Jakubiczka S., Rohrer T., Hanimann B., Werder E.A., Wieacker P.; RT "Single amino acid substitution in the hormone-binding domain of the RT androgen receptor in a family with complete androgen insensitivity syndrome RT (CAIS)."; RL Hum. Mutat. 12:220-220(1998). RN [182] RP VARIANT PAIS GLN-608. RX PubMed=9543136; DOI=10.1210/jcem.83.4.4704; RA Weidemann W., Peters B., Romalo G., Spindler K.D., Schweikert H.-U.; RT "Response to androgen treatment in a patient with partial androgen RT insensitivity and a mutation in the deoxyribonucleic acid-binding domain of RT the androgen receptor."; RL J. Clin. Endocrinol. Metab. 83:1173-1176(1998). RN [183] RP VARIANTS PAIS VAL-744 AND CYS-841. RX PubMed=9768671; DOI=10.1210/jcem.83.10.5201; RA Georget V., Terouanne B., Lumbroso S., Nicolas J.C., Sultan C.; RT "Trafficking of androgen receptor mutants fused to green fluorescent RT protein: a new investigation of partial androgen insensitivity syndrome."; RL J. Clin. Endocrinol. Metab. 83:3597-3603(1998). RN [184] RP VARIANT AIS GLU-799. RX PubMed=9851768; DOI=10.1210/jcem.83.12.5358; RA Wang Q., Ghadessy F.J., Trounson A., de Kretser D., McLachlan R., Ng S.C., RA Yong E.L.; RT "Azoospermia associated with a mutation in the ligand-binding domain of an RT androgen receptor displaying normal ligand binding, but defective trans- RT activation."; RL J. Clin. Endocrinol. Metab. 83:4303-4309(1998). RN [185] RP VARIANTS AIS. RX PubMed=9627582; DOI=10.1016/s0022-3476(98)70387-7; RA Hiort O., Sinnecker G.H., Holterhus P.M., Nitsche E.M., Kruse K.; RT "Inherited and de novo androgen receptor gene mutations: investigation of RT single-case families."; RL J. Pediatr. 132:939-943(1998). RN [186] RP VARIANT PAIS THR-759. RX PubMed=9607727; DOI=10.1016/s0303-7207(97)00229-3; RA Yong E.L., Tut T.G., Ghadessy F.J., Prins G., Ratnam S.S.; RT "Partial androgen insensitivity and correlations with the predicted three RT dimensional structure of the androgen receptor ligand-binding domain."; RL Mol. Cell. Endocrinol. 137:41-50(1998). RN [187] 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 [188] RP VARIANTS PROSTATE CANCER ALA-878 AND ASN-891. RX PubMed=10363963; RA Taplin M.-E., Bubley G.J., Ko Y.J., Small E.J., Upton M., Rajeshkumar B., RA Balk S.P.; RT "Selection for androgen receptor mutations in prostate cancers treated with RT androgen antagonist."; RL Cancer Res. 59:2511-2515(1999). RN [189] RP VARIANT PAIS SER-841. RX PubMed=10502786; RX DOI=10.1002/(sici)1098-1004(199910)14:4<353::aid-humu16>3.0.co;2-7; RA Melo K.F.S., Latronico A.C., Costa E.M.F., Billerbeck A.E.C., RA Mendonca B.B., Arnhold I.J.P.; RT "A novel point mutation (R840S) in the androgen receptor in a Brazilian RT family with partial androgen insensitivity syndrome."; RL Hum. Mutat. 14:353-353(1999). RN [190] 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 [191] 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 [192] RP VARIANT AIS LEU-893. RX PubMed=10404311; DOI=10.1046/j.1442-2042.1999.00065.x; RA Kanayama H., Naroda T., Inoue Y., Kurokawa Y., Kagawa S.; RT "A case of complete testicular feminization: laparoscopic orchiectomy and RT analysis of androgen receptor gene mutation."; RL Int. J. Urol. 6:327-330(1999). RN [193] RP VARIANT PAIS ALA-773, AND VARIANT AIS GLY-872. RX PubMed=10022458; DOI=10.1210/jcem.84.2.5453; RA Shkolny D.L., Beitel L.K., Ginsberg J., Pekeles G., Arbour L., Pinsky L., RA Trifiro M.A.; RT "Discordant measures of androgen-binding kinetics in two mutant androgen RT receptors causing mild or partial androgen insensitivity, respectively."; RL J. Clin. Endocrinol. Metab. 84:805-810(1999). RN [194] RP VARIANT ALA-684. RX PubMed=10629558; RX DOI=10.1002/(sici)1096-9896(199912)189:4<559::aid-path471>3.0.co;2-y; RA Wallen M.J., Linja M., Kaartinen K., Schleutker J., Visakorpi T.; RT "Androgen receptor gene mutations in hormone-refractory prostate cancer."; RL J. Pathol. 189:559-563(1999). RN [195] RP VARIANTS HIS-702 AND ALA-878. RX PubMed=10569618; DOI=10.1016/s0022-5347(05)68158-x; RA Zhao X.Y., Boyle B., Krishnan A.V., Navone N.M., Peehl D.M., Feldman D.; RT "Two mutations identified in the androgen receptor of the new human RT prostate cancer cell line MDA PCa 2a."; RL J. Urol. 162:2192-2199(1999). RN [196] RP VARIANT PAIS THR-808. RX PubMed=10543676; DOI=10.1016/s0140-6736(99)03205-5; RA Ong Y.C., Wong H.B., Adaikan G., Yong E.L.; RT "Directed pharmacological therapy of ambiguous genitalia due to an androgen RT receptor gene mutation."; RL Lancet 354:1444-1445(1999). RN [197] RP VARIANT AIS LEU-893. RX PubMed=10221770; DOI=10.1016/s0303-7207(98)00237-8; RA Peters I., Weidemann W., Romalo G., Knorr D., Schweikert H.-U., RA Spindler K.D.; RT "An androgen receptor mutation in the direct vicinity of the proposed C- RT terminal alpha-helix of the ligand binding domain containing the AF-2 RT transcriptional activating function core is associated with complete RT androgen insensitivity."; RL Mol. Cell. Endocrinol. 148:47-53(1999). RN [198] RP VARIANT PROSTATE CANCER TYR-620. RX PubMed=10598582; DOI=10.1210/mend.13.12.0382; RA Nazareth L.V., Stenoien D.L., Bingman W.E. III, James A.J., Wu C., RA Zhang Y., Edwards D.P., Mancini M., Marcelli M., Lamb D.J., Weigel N.L.; RT "A C619Y mutation in the human androgen receptor causes inactivation and RT mislocalization of the receptor with concomitant sequestration of SRC-1."; RL Mol. Endocrinol. 13:2065-2075(1999). RN [199] RP ERRATUM OF PUBMED:10598582. RA Nazareth L.V., Stenoien D.L., Bingman W.E. III, James A.J., Wu C., RA Zhang Y., Edwards D.P., Mancini M., Marcelli M., Lamb D.J., Weigel N.L.; RL Mol. Endocrinol. 14:544-544(2000). RN [200] RP VARIANT AIS THR-597. RX PubMed=10590024; DOI=10.1203/00006450-199912000-00009; RA Holterhus P.M., Wiebel J., Sinnecker G.H., Bruggenwirth H.T., Sippell W.G., RA Brinkmann A.O., Kruse K., Hiort O.; RT "Clinical and molecular spectrum of somatic mosaicism in androgen RT insensitivity syndrome."; RL Pediatr. Res. 46:684-690(1999). RN [201] RP VARIANTS AIS PHE-813 AND GLN-832. RX PubMed=10458483; DOI=10.1620/tjem.187.263; RA Yaegashi N., Uehara S., Senoo M., Sato J., Fujiwara J., Funato T., RA Sasaki T., Yajima A.; RT "Point mutations in the steroid-binding domain of the androgen receptor RT gene of five Japanese patients with androgen insensitivity syndrome."; RL Tohoku J. Exp. Med. 187:263-272(1999). RN [202] 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 [203] RP VARIANTS PROSTATE CANCER ALA-576; ARG-581; VAL-587; TYR-620; ALA-758 AND RP GLY-847. RX PubMed=10706109; RA Marcelli M., Ittmann M., Mariani S., Sutherland R.W., Nigam R., Murthy L., RA Zhao Y., DiConcini D., Puxeddu E., Esen A., Eastham J., Weigel N.L., RA Lamb D.J.; RT "Androgen receptor mutations in prostate cancer."; RL Cancer Res. 60:944-949(2000). RN [204] RP VARIANTS AIS AND PAIS. RX PubMed=10690872; DOI=10.1210/jcem.85.2.6337; RA Ahmed S.F., Cheng A., Dovey L., Hawkins J.R., Martin H., Rowland J., RA Shimura N., Tait A.D., Hughes I.A.; RT "Phenotypic features, androgen receptor binding, and mutational analysis in RT 278 clinical cases reported as androgen insensitivity syndrome."; RL J. Clin. Endocrinol. Metab. 85:658-665(2000). RN [205] 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 [206] RP INVOLVEMENT IN ANDROGENETIC ALOPECIA, AND POLYMORPHISM OF POLY-GLY REGION. RX PubMed=11231320; DOI=10.1046/j.1523-1747.2001.01261.x; RA Ellis J.A., Stebbing M., Harrap S.B.; RT "Polymorphism of the androgen receptor gene is associated with male pattern RT baldness."; RL J. Invest. Dermatol. 116:452-455(2001). RN [207] RP VARIANT AIS TYR-706. RX PubMed=11744994; RA Sills E.S., Sholes T.E., Perloe M., Kaplan C.R., Davis J.G., Tucker M.J.; RT "Characterization of a novel receptor mutation A->T at exon 4 in complete RT androgen insensitivity syndrome and a carrier sibling via bidirectional RT polymorphism sequence analysis."; RL Int. J. Mol. Med. 9:45-48(2002). RN [208] RP INVOLVEMENT IN ANDROGENETIC ALOPECIA, AND POLYMORPHISM OF POLY-GLY REGION. RX PubMed=15902657; DOI=10.1086/431425; RA Hillmer A.M., Hanneken S., Ritzmann S., Becker T., Freudenberg J., RA Brockschmidt F.F., Flaquer A., Freudenberg-Hua Y., Jamra R.A., Metzen C., RA Heyn U., Schweiger N., Betz R.C., Blaumeiser B., Hampe J., Schreiber S., RA Schulze T.G., Hennies H.C., Schumacher J., Propping P., Ruzicka T., RA Cichon S., Wienker T.F., Kruse R., Noethen M.M.; RT "Genetic variation in the human androgen receptor gene is the major RT determinant of common early-onset androgenetic alopecia."; RL Am. J. Hum. Genet. 77:140-148(2005). RN [209] 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 [210] RP VARIANT AIS PHE-577. RX PubMed=14756668; DOI=10.1111/j.0009-9163.2004.00197.x; RA Hooper H.T., Figueiredo B.C., Pavan-Senn C.C., De Lacerda L., Sandrini R., RA Mengarelli J.K., Japp K., Karaviti L.P.; RT "Concordance of phenotypic expression and gender identity in a large RT kindred with a mutation in the androgen receptor."; RL Clin. Genet. 65:183-190(2004). RN [211] RP CHARACTERIZATION OF VARIANTS AIS ASN-696; CYS-764; HIS-775; GLU-799; RP HIS-856 AND PHE-908. RX PubMed=16595706; DOI=10.1677/jme.1.01885; RA Jaeaeskelaeinen J., Deeb A., Schwabe J.W., Mongan N.P., Martin H., RA Hughes I.A.; RT "Human androgen receptor gene ligand-binding-domain mutations leading to RT disrupted interaction between the N- and C-terminal domains."; RL J. Mol. Endocrinol. 36:361-368(2006). RN [212] RP VARIANT ARG-216. RX PubMed=27535533; DOI=10.1038/nature19057; RG Exome Aggregation Consortium; RA Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E., Fennell T., RA O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B., Tukiainen T., RA Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K., Zhao F., Zou J., RA Pierce-Hoffman E., Berghout J., Cooper D.N., Deflaux N., DePristo M., RA Do R., Flannick J., Fromer M., Gauthier L., Goldstein J., Gupta N., RA Howrigan D., Kiezun A., Kurki M.I., Moonshine A.L., Natarajan P., RA Orozco L., Peloso G.M., Poplin R., Rivas M.A., Ruano-Rubio V., Rose S.A., RA Ruderfer D.M., Shakir K., Stenson P.D., Stevens C., Thomas B.P., Tiao G., RA Tusie-Luna M.T., Weisburd B., Won H.H., Yu D., Altshuler D.M., RA Ardissino D., Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C., RA Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S., Laakso M., RA McCarroll S., McCarthy M.I., McGovern D., McPherson R., Neale B.M., RA Palotie A., Purcell S.M., Saleheen D., Scharf J.M., Sklar P., RA Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C., Wilson J.G., RA Daly M.J., MacArthur D.G.; RT "Analysis of protein-coding genetic variation in 60,706 humans."; RL Nature 536:285-291(2016). RN [213] RP POLYMORPHISM. RX PubMed=33647767; DOI=10.1016/j.ebiom.2021.103246; RG Spanish Covid HGE, GEN-COVID Multicenter Study; RA Baldassarri M., Picchiotti N., Fava F., Fallerini C., Benetti E., Daga S., RA Valentino F., Doddato G., Furini S., Giliberti A., Tita R., Amitrano S., RA Bruttini M., Croci S., Meloni I., Pinto A.M., Iuso N., Gabbi C., RA Sciarra F., Venneri M.A., Gori M., Sanarico M., Crawley F.P., Pagotto U., RA Fanelli F., Mezzullo M., Dominguez-Garrido E., Planas-Serra L., RA Schlueter A., Colobran R., Soler-Palacin P., Lapunzina P., Tenorio J., RA Pujol A., Castagna M.G., Marcelli M., Isidori A.M., Renieri A., RA Frullanti E., Mari F.; RT "Shorter androgen receptor polyQ alleles protect against life-threatening RT COVID-19 disease in European males."; RL EBioMedicine 65:103246-103246(2021). CC -!- FUNCTION: Steroid hormone receptors are ligand-activated transcription CC factors that regulate eukaryotic gene expression and affect cellular CC proliferation and differentiation in target tissues (PubMed:19022849). CC Transcription factor activity is modulated by bound coactivator and CC corepressor proteins like ZBTB7A that recruits NCOR1 and NCOR2 to the CC androgen response elements/ARE on target genes, negatively regulating CC androgen receptor signaling and androgen-induced cell proliferation CC (PubMed:20812024). Transcription activation is also down-regulated by CC NR0B2. Activated, but not phosphorylated, by HIPK3 and ZIPK/DAPK3. CC {ECO:0000269|PubMed:14664718, ECO:0000269|PubMed:15563469, CC ECO:0000269|PubMed:17591767, ECO:0000269|PubMed:17911242, CC ECO:0000269|PubMed:18084323, ECO:0000269|PubMed:19022849, CC ECO:0000269|PubMed:19345326, ECO:0000269|PubMed:20812024, CC ECO:0000269|PubMed:20980437, ECO:0000269|PubMed:25091737}. CC -!- FUNCTION: [Isoform 3]: Lacks the C-terminal ligand-binding domain and CC may therefore constitutively activate the transcription of a specific CC set of genes independently of steroid hormones. CC {ECO:0000269|PubMed:19244107}. CC -!- FUNCTION: [Isoform 4]: Lacks the C-terminal ligand-binding domain and CC may therefore constitutively activate the transcription of a specific CC set of genes independently of steroid hormones. CC {ECO:0000269|PubMed:19244107}. CC -!- ACTIVITY REGULATION: AIM-100 (4-amino-5,6-biaryl-furo[2,3-d]pyrimidine) CC suppresses TNK2-mediated phosphorylation at Tyr-269. Inhibits the CC binding of the Tyr-269 phosphorylated form to androgen-responsive CC enhancers (AREs) and its transcriptional activity. CC {ECO:0000269|PubMed:20623637}. CC -!- SUBUNIT: Binds DNA as a homodimer. Part of a ternary complex containing CC AR, EFCAB6/DJBP and PARK7. Interacts with HIPK3 and NR0B2 in the CC presence of androgen. The ligand binding domain interacts with CC KAT7/HBO1 in the presence of dihydrotestosterone. Interacts with CC EFCAB6/DJBP, PQBP1, RANBP9, RBAK, SPDEF, SRA1, TGFB1I1 and RREB1. CC Interacts with ZMIZ1/ZIMP10 and ZMIZ2/ZMIP7 which both enhance its CC transactivation activity. Interacts with SLC30A9 and RAD54L2/ARIP4. CC Interacts with MACROD1 (via macro domain) (PubMed:19022849). Interacts CC via the 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. Ran- CC binding decreases as the poly-Gln length increases. Interacts with HIP1 CC (via coiled coil domain). Interacts (via ligand-binding domain) with CC TRIM68. Interacts with TNK2. Interacts with USP26. Interacts with RNF6. CC Interacts (regulated by RNF6 probably through polyubiquitination) with CC RNF14; regulates AR transcriptional activity. Interacts with PRMT2 and CC TRIM24. Interacts with RACK1. Interacts with RANBP10; this interaction CC enhances dihydrotestosterone-induced AR transcriptional activity. CC Interacts with PRPF6 in a hormone-independent way; this interaction CC enhances dihydrotestosterone-induced AR transcriptional activity. CC Interacts with STK4/MST1. Interacts with ZIPK/DAPK3. Interacts with CC LPXN. Interacts with MAK. Part of a complex containing AR, MAK and CC NCOA3. Interacts with CRY1. Interacts with CCAR1 and GATA2. Interacts CC with ZNF318 (By similarity). Interacts with BUD31 (PubMed:25091737). CC Interacts with ARID4A (PubMed:23487765). Interacts with ARID4B (By CC similarity). Interacts (via NR LBD domain) with ZBTB7A; the interaction CC is direct and androgen-dependent (PubMed:20812024). Interacts with CC NCOR1 (PubMed:20812024). Interacts with NCOR2 (PubMed:20812024). CC Interacts with CRY2 in a ligand-dependent manner (By similarity). CC {ECO:0000250|UniProtKB:P15207, ECO:0000250|UniProtKB:P19091, CC ECO:0000269|PubMed:10075738, ECO:0000269|PubMed:10332029, CC ECO:0000269|PubMed:10383460, ECO:0000269|PubMed:10400640, CC ECO:0000269|PubMed:10625666, ECO:0000269|PubMed:10930412, CC ECO:0000269|PubMed:12039962, ECO:0000269|PubMed:12361945, CC ECO:0000269|PubMed: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:19022849, CC ECO:0000269|PubMed:19345326, ECO:0000269|PubMed:19909775, CC ECO:0000269|PubMed:20501646, ECO:0000269|PubMed:20812024, CC ECO:0000269|PubMed:20980437, ECO:0000269|PubMed:21512132, CC ECO:0000269|PubMed:22170608, ECO:0000269|PubMed:23487765, CC ECO:0000269|PubMed:23887938, ECO:0000269|PubMed:25091737}. CC -!- INTERACTION: CC P10275; P00519: ABL1; NbExp=2; IntAct=EBI-608057, EBI-375543; CC P10275; Q9UBL3: ASH2L; NbExp=3; IntAct=EBI-608057, EBI-540797; CC P10275; P51451: BLK; NbExp=3; IntAct=EBI-608057, EBI-2105445; CC P10275; Q8WV28: BLNK; NbExp=2; IntAct=EBI-608057, EBI-2623522; CC P10275; O60885-1: BRD4; NbExp=6; IntAct=EBI-608057, EBI-9345088; CC P10275; P78543: BTG2; NbExp=4; IntAct=EBI-608057, EBI-1047576; CC P10275; Q14790: CASP8; NbExp=3; IntAct=EBI-608057, EBI-78060; CC P10275; P24385: CCND1; NbExp=4; IntAct=EBI-608057, EBI-375001; CC P10275; Q92793: CREBBP; NbExp=3; IntAct=EBI-608057, EBI-81215; CC P10275; O14595: CTDSP2; NbExp=3; IntAct=EBI-608057, EBI-2802973; CC P10275; P35222: CTNNB1; NbExp=11; IntAct=EBI-608057, EBI-491549; CC P10275; Q9UER7: DAXX; NbExp=5; IntAct=EBI-608057, EBI-77321; CC P10275; P20711: DDC; NbExp=2; IntAct=EBI-608057, EBI-1632155; CC P10275; P11308: ERG; NbExp=4; IntAct=EBI-608057, EBI-79704; CC P10275; P07332: FES; NbExp=3; IntAct=EBI-608057, EBI-1055635; CC P10275; P09769: FGR; NbExp=3; IntAct=EBI-608057, EBI-1383732; CC P10275; Q02790: FKBP4; NbExp=2; IntAct=EBI-608057, EBI-1047444; CC P10275; P55317: FOXA1; NbExp=4; IntAct=EBI-608057, EBI-3918034; CC P10275; O75593: FOXH1; NbExp=3; IntAct=EBI-608057, EBI-1759806; CC P10275; Q14451: GRB7; NbExp=3; IntAct=EBI-608057, EBI-970191; CC P10275; P06396: GSN; NbExp=2; IntAct=EBI-608057, EBI-351506; CC P10275; P56524: HDAC4; NbExp=4; IntAct=EBI-608057, EBI-308629; CC P10275; Q16665: HIF1A; NbExp=2; IntAct=EBI-608057, EBI-447269; CC P10275; Q16666: IFI16; NbExp=3; IntAct=EBI-608057, EBI-2867186; CC P10275; O15357: INPPL1; NbExp=3; IntAct=EBI-608057, EBI-1384248; CC P10275; Q15652: JMJD1C; NbExp=4; IntAct=EBI-608057, EBI-1224969; CC P10275; O95251: KAT7; NbExp=5; IntAct=EBI-608057, EBI-473199; CC P10275; Q9BY66: KDM5D; NbExp=2; IntAct=EBI-608057, EBI-1246860; CC P10275; Q9BY66-3: KDM5D; NbExp=2; IntAct=EBI-608057, EBI-12559887; CC P10275; Q03164: KMT2A; NbExp=4; IntAct=EBI-608057, EBI-591370; CC P10275; O14686: KMT2D; NbExp=3; IntAct=EBI-608057, EBI-996065; CC P10275; P06239: LCK; NbExp=7; IntAct=EBI-608057, EBI-1348; CC P10275; P07948: LYN; NbExp=5; IntAct=EBI-608057, EBI-79452; CC P10275; P20794: MAK; NbExp=5; IntAct=EBI-608057, EBI-3911321; CC P10275; P42679: MATK; NbExp=4; IntAct=EBI-608057, EBI-751664; CC P10275; Q00987: MDM2; NbExp=2; IntAct=EBI-608057, EBI-389668; CC P10275; Q15596: NCOA2; NbExp=3; IntAct=EBI-608057, EBI-81236; CC P10275; Q14686: NCOA6; NbExp=3; IntAct=EBI-608057, EBI-78670; CC P10275; O96028: NSD2; NbExp=5; IntAct=EBI-608057, EBI-2693298; CC P10275; Q99497: PARK7; NbExp=6; IntAct=EBI-608057, EBI-1164361; CC P10275; P27986: PIK3R1; NbExp=5; IntAct=EBI-608057, EBI-79464; CC P10275; O00459: PIK3R2; NbExp=14; IntAct=EBI-608057, EBI-346930; CC P10275; Q92569: PIK3R3; NbExp=37; IntAct=EBI-608057, EBI-79893; CC P10275; P19174: PLCG1; NbExp=22; IntAct=EBI-608057, EBI-79387; CC P10275; P16885: PLCG2; NbExp=6; IntAct=EBI-608057, EBI-617403; CC P10275; Q06830: PRDX1; NbExp=3; IntAct=EBI-608057, EBI-353193; CC P10275; P78527: PRKDC; NbExp=3; IntAct=EBI-608057, EBI-352053; CC P10275; Q06124: PTPN11; NbExp=12; IntAct=EBI-608057, EBI-297779; CC P10275; P20936: RASA1; NbExp=16; IntAct=EBI-608057, EBI-1026476; CC P10275; Q9UBS8: RNF14; NbExp=2; IntAct=EBI-608057, EBI-2130308; CC P10275; Q9Y252: RNF6; NbExp=10; IntAct=EBI-608057, EBI-2341483; CC P10275; O14796: SH2D1B; NbExp=3; IntAct=EBI-608057, EBI-3923013; CC P10275; Q9NP31: SH2D2A; NbExp=6; IntAct=EBI-608057, EBI-490630; CC P10275; P29353: SHC1; NbExp=14; IntAct=EBI-608057, EBI-78835; CC P10275; Q6S5L8: SHC4; NbExp=3; IntAct=EBI-608057, EBI-9453524; CC P10275; Q5VZ18: SHE; NbExp=3; IntAct=EBI-608057, EBI-3956977; CC P10275; Q15797: SMAD1; NbExp=6; IntAct=EBI-608057, EBI-1567153; CC P10275; O14544: SOCS6; NbExp=4; IntAct=EBI-608057, EBI-3929549; CC P10275; P12931: SRC; NbExp=7; IntAct=EBI-608057, EBI-621482; CC P10275; Q9ULZ2: STAP1; NbExp=2; IntAct=EBI-608057, EBI-6083058; CC P10275; P63165: SUMO1; NbExp=7; IntAct=EBI-608057, EBI-80140; CC P10275; Q9HBL0: TNS1; NbExp=3; IntAct=EBI-608057, EBI-3389814; CC P10275; P07947: YES1; NbExp=5; IntAct=EBI-608057, EBI-515331; CC P10275; Q9R1E0: Foxo1; Xeno; NbExp=4; IntAct=EBI-608057, EBI-1371343; CC P10275; Q06986: Siah2; Xeno; NbExp=6; IntAct=EBI-608057, EBI-957413; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12958311, CC ECO:0000269|PubMed:15634333, ECO:0000269|PubMed:17587566, CC ECO:0000269|PubMed:19244107, ECO:0000269|PubMed:19345326, CC ECO:0000269|PubMed:25091737}. Cytoplasm {ECO:0000269|PubMed:12958311, CC ECO:0000269|PubMed:17587566, ECO:0000269|PubMed:19244107}. CC Note=Detected at the promoter of target genes (PubMed:25091737). CC Predominantly cytoplasmic in unligated form but translocates to the CC nucleus upon ligand-binding. Can also translocate to the nucleus in CC unligated form in the presence of RACK1. {ECO:0000269|PubMed:12958311, CC ECO:0000269|PubMed:17587566, ECO:0000269|PubMed:25091737}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=AR-B; CC IsoId=P10275-1; Sequence=Displayed; CC Name=2; Synonyms=AR-A, Variant AR45; CC IsoId=P10275-2; Sequence=VSP_036889, VSP_036890; CC Name=3; Synonyms=AR3; CC IsoId=P10275-3; Sequence=VSP_058166, VSP_058168; CC Name=4; Synonyms=AR4; CC IsoId=P10275-4; Sequence=VSP_058167, VSP_058169; CC -!- TISSUE SPECIFICITY: [Isoform 2]: Mainly expressed in heart and skeletal CC muscle. {ECO:0000269|PubMed:15634333}. CC -!- TISSUE SPECIFICITY: [Isoform 3]: Expressed in basal and stromal cells CC of the prostate (at protein level). {ECO:0000269|PubMed:19244107}. CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a CC DNA-binding domain and a C-terminal ligand-binding domain. In the CC presence of bound steroid the ligand-binding domain interacts with the CC N-terminal modulating domain, and thereby activates AR transcription CC factor activity. Agonist binding is required for dimerization and CC binding to target DNA. The transcription factor activity of the complex CC formed by ligand-activated AR and DNA is modulated by interactions with CC coactivator and corepressor proteins (PubMed:25091737). Interaction CC with RANBP9 is mediated by both the N-terminal domain and the DNA- CC binding domain. Interaction with EFCAB6/DJBP is mediated by the DNA- CC binding domain. {ECO:0000269|PubMed:25091737}. CC -!- PTM: Sumoylated on Lys-388 (major) and Lys-521. Ubiquitinated. CC Deubiquitinated by USP26. 'Lys-6' and 'Lys-27'-linked CC polyubiquitination by RNF6 modulates AR transcriptional activity and CC specificity. {ECO:0000269|PubMed:11121022, ECO:0000269|PubMed:19345326, CC ECO:0000269|PubMed:20501646}. CC -!- PTM: Phosphorylated in prostate cancer cells in response to several CC growth factors including EGF. Phosphorylation is induced by c-Src CC kinase (CSK). Tyr-535 is one of the major phosphorylation sites and an CC increase in phosphorylation and Src kinase activity is associated with CC prostate cancer progression. Phosphorylation by TNK2 enhances the DNA- CC binding and transcriptional activity and may be responsible for CC androgen-independent progression of prostate cancer. Phosphorylation at CC Ser-83 by CDK9 regulates AR promoter selectivity and cell growth. CC Phosphorylation by PAK6 leads to AR-mediated transcription inhibition. CC {ECO:0000269|PubMed:14573606, ECO:0000269|PubMed:17045208, CC ECO:0000269|PubMed:17494760, ECO:0000269|PubMed:20623637, CC ECO:0000269|PubMed:20980437, ECO:0000269|PubMed:21512132}. CC -!- PTM: Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is required CC for plasma membrane targeting and for rapid intracellular signaling via CC ERK and AKT kinases and cAMP generation. {ECO:0000269|PubMed:22031296}. CC -!- POLYMORPHISM: The poly-Gln region of AR is highly polymorphic and the CC number of Gln varies in the population (from 17 to 26). A smaller size CC of the poly-Gln region may be associated with the development of CC prostate cancer. Long poly-Gln alleles (>23) may be associated with CC higher testosterone levels and severe clinical outcome in COVID-19 CC disease (PubMed:33647767). {ECO:0000269|PubMed:1561105, CC ECO:0000269|PubMed:2062380, ECO:0000269|PubMed:33647767, CC ECO:0000269|PubMed:8292051, ECO:0000269|PubMed:9096391}. CC -!- POLYMORPHISM: The poly-Gly region of AR is polymorphic and ranges from CC 24 to 31 Gly. A poly-Gly region shorter or equal to 23 may be CC associated with the development of androgenetic alopecia. CC {ECO:0000269|PubMed:11231320, ECO:0000269|PubMed:15902657}. CC -!- DISEASE: Androgen insensitivity syndrome (AIS) [MIM:300068]: An X- CC linked recessive form of pseudohermaphroditism due end-organ resistance CC to androgen. Affected males have female external genitalia, female CC breast development, blind vagina, absent uterus and female adnexa, and CC abdominal or inguinal testes, despite a normal 46,XY karyotype. CC {ECO:0000269|PubMed:10022458, ECO:0000269|PubMed:10221692, CC ECO:0000269|PubMed:10221770, ECO:0000269|PubMed:10404311, CC ECO:0000269|PubMed:10458483, ECO:0000269|PubMed:10571951, CC ECO:0000269|PubMed:10590024, ECO:0000269|PubMed:10690872, CC ECO:0000269|PubMed:11587068, ECO:0000269|PubMed:11744994, CC ECO:0000269|PubMed:1307250, ECO:0000269|PubMed:1316540, CC ECO:0000269|PubMed:1426313, ECO:0000269|PubMed:1430233, CC ECO:0000269|PubMed:1464650, ECO:0000269|PubMed:14756668, CC ECO:0000269|PubMed:1480178, ECO:0000269|PubMed:1487249, CC ECO:0000269|PubMed:1569163, ECO:0000269|PubMed:1609793, CC ECO:0000269|PubMed:16129672, ECO:0000269|PubMed:16595706, CC ECO:0000269|PubMed:1775137, ECO:0000269|PubMed:1999491, CC ECO:0000269|PubMed:2082179, ECO:0000269|PubMed:2594783, CC ECO:0000269|PubMed:7537149, ECO:0000269|PubMed:7581399, CC ECO:0000269|PubMed:7633398, ECO:0000269|PubMed:7641413, CC ECO:0000269|PubMed:7671849, ECO:0000269|PubMed:7929841, CC ECO:0000269|PubMed:7962294, ECO:0000269|PubMed:7970939, CC ECO:0000269|PubMed:7981687, ECO:0000269|PubMed:7981689, CC ECO:0000269|PubMed:7993455, ECO:0000269|PubMed:8040309, CC ECO:0000269|PubMed:8096390, ECO:0000269|PubMed:8103398, CC ECO:0000269|PubMed:8162033, ECO:0000269|PubMed:8224266, CC ECO:0000269|PubMed:8281140, ECO:0000269|PubMed:8325950, CC ECO:0000269|PubMed:8339746, ECO:0000269|PubMed:8413310, CC ECO:0000269|PubMed:8446106, ECO:0000269|PubMed:8626869, CC ECO:0000269|PubMed:8647313, ECO:0000269|PubMed:8683794, CC ECO:0000269|PubMed:8723113, ECO:0000269|PubMed:8768864, CC ECO:0000269|PubMed:8809734, ECO:0000269|PubMed:8830623, CC ECO:0000269|PubMed:8918984, ECO:0000269|PubMed:8990010, CC ECO:0000269|PubMed:9001799, ECO:0000269|PubMed:9007482, CC ECO:0000269|PubMed:9039340, ECO:0000269|PubMed:9106550, CC ECO:0000269|PubMed:9160185, ECO:0000269|PubMed:9252933, CC ECO:0000269|PubMed:9255042, ECO:0000269|PubMed:9302173, CC ECO:0000269|PubMed:9328206, ECO:0000269|PubMed:9544375, CC ECO:0000269|PubMed:9554754, ECO:0000269|PubMed:9610419, CC ECO:0000269|PubMed:9627582, ECO:0000269|PubMed:9698822, CC ECO:0000269|PubMed:9851768, ECO:0000269|PubMed:9856504, CC ECO:0000269|Ref.115, ECO:0000269|Ref.181}. Note=The disease is caused CC by variants affecting the gene represented in this entry. CC -!- DISEASE: Spinal and bulbar muscular atrophy X-linked 1 (SMAX1) CC [MIM:313200]: An X-linked recessive form of spinal muscular atrophy. CC Spinal muscular atrophy refers to a group of neuromuscular disorders CC characterized by degeneration of the anterior horn cells of the spinal CC cord, leading to symmetrical muscle weakness and atrophy. SMAX1 occurs CC only in men. Age at onset is usually in the third to fifth decade of CC life, but earlier involvement has been reported. It is characterized by CC slowly progressive limb and bulbar muscle weakness with fasciculations, CC muscle atrophy, and gynecomastia. The disorder is clinically similar to CC classic forms of autosomal spinal muscular atrophy. CC {ECO:0000269|PubMed:15851746}. Note=The disease is caused by variants CC affecting the gene represented in this entry. Caused by trinucleotide CC CAG repeat expansion. In SMAX1 patients the number of Gln ranges from CC 38 to 62. Longer expansions result in earlier onset and more severe CC clinical manifestations of the disease. CC -!- DISEASE: Note=Defects in AR may play a role in metastatic prostate CC cancer. The mutated receptor stimulates prostate growth and metastases CC development despite of androgen ablation. This treatment can reduce CC primary and metastatic lesions probably by inducing apoptosis of tumor CC cells when they express the wild-type receptor. CC {ECO:0000269|PubMed:10363963, ECO:0000269|PubMed:10569618, CC ECO:0000269|PubMed:1562539, ECO:0000269|PubMed:16129672, CC ECO:0000269|PubMed:17311914, ECO:0000269|PubMed:2260966, CC ECO:0000269|PubMed:25091737, ECO:0000269|PubMed:8187068, CC ECO:0000269|PubMed:8274409, ECO:0000269|PubMed:8827083}. CC -!- DISEASE: Androgen insensitivity, partial (PAIS) [MIM:312300]: A CC disorder that is characterized by hypospadias, hypogonadism, CC gynecomastia, genital ambiguity, normal XY karyotype, and a pedigree CC pattern consistent with X-linked recessive inheritance. Some patients CC present azoospermia or severe oligospermia without other clinical CC manifestations. {ECO:0000269|PubMed:10022458, CC ECO:0000269|PubMed:10221692, ECO:0000269|PubMed:10470409, CC ECO:0000269|PubMed:10502786, ECO:0000269|PubMed:10543676, CC ECO:0000269|PubMed:11587068, ECO:0000269|PubMed:1303262, CC ECO:0000269|PubMed:1307250, ECO:0000269|PubMed:1316540, CC ECO:0000269|PubMed:1424203, ECO:0000269|PubMed:1430233, CC ECO:0000269|PubMed:14756668, ECO:0000269|PubMed:2010552, CC ECO:0000269|PubMed:7581399, ECO:0000269|PubMed:7649358, CC ECO:0000269|PubMed:7671849, ECO:0000269|PubMed:7909256, CC ECO:0000269|PubMed:7910529, ECO:0000269|PubMed:7929841, CC ECO:0000269|PubMed:7970939, ECO:0000269|PubMed:7981687, CC ECO:0000269|PubMed:8033918, ECO:0000269|PubMed:8097257, CC ECO:0000269|PubMed:8126121, ECO:0000269|PubMed:8205256, CC ECO:0000269|PubMed:8281139, ECO:0000269|PubMed:8325932, CC ECO:0000269|PubMed:8325950, ECO:0000269|PubMed:8446106, CC ECO:0000269|PubMed:8550758, ECO:0000269|PubMed:8809734, CC ECO:0000269|PubMed:8823308, ECO:0000269|PubMed:8824883, CC ECO:0000269|PubMed:9039340, ECO:0000269|PubMed:9196614, CC ECO:0000269|PubMed:9302173, ECO:0000269|PubMed:9329414, CC ECO:0000269|PubMed:9543136, ECO:0000269|PubMed:9607727, CC ECO:0000269|PubMed:9768671, ECO:0000269|PubMed:9856504, CC ECO:0000269|Ref.123}. Note=The disease is caused by variants affecting CC the gene represented in this entry. CC -!- DISEASE: Hypospadias 1, X-linked (HYSP1) [MIM:300633]: A common CC malformation in which the urethra opens on the ventral side of the CC penis, due to developmental arrest of urethral fusion. The opening can CC be located glandular, penile, or even more posterior in the scrotum or CC perineum. Hypospadias is a feature of several syndromic disorders, CC including the androgen insensitivity syndrome and Opitz syndrome. CC {ECO:0000269|PubMed:8097257}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: In the absence of ligand, steroid hormone receptors are CC thought to be weakly associated with nuclear components; hormone CC binding greatly increases receptor affinity. The hormone-receptor CC complex appears to recognize discrete DNA sequences upstream of CC transcriptional start sites. CC -!- MISCELLANEOUS: Transcriptional activity is enhanced by binding to CC RANBP9. CC -!- MISCELLANEOUS: The level of tyrosine phosphorylation may serve as a CC diagnostic tool to predict patient outcome in response to hormone- CC ablation therapy. Inhibition of tyrosine phosphorylation may be an CC effective intervention target for hormone-refractory prostate cancer. CC -!- MISCELLANEOUS: [Isoform 3]: Minor isoform up-regulated in prostate CC cancer cells. {ECO:0000269|PubMed:19244107}. CC -!- MISCELLANEOUS: [Isoform 4]: Minor isoform identified in prostate cancer CC cells. {ECO:0000269|PubMed:19244107}. CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3 CC subfamily. {ECO:0000305}. CC -!- CAUTION: Had previously been shown to interact with PELP1. However this CC paper was retracted as cell-based data was viewed as unreliable. CC {ECO:0000305|PubMed:12415108, ECO:0000305|PubMed:19666546}. CC -!- WEB RESOURCE: Name=Androgen receptor gene mutations database; CC URL="http://androgendb.mcgill.ca"; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/685/AR"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Androgen receptor entry; CC URL="https://en.wikipedia.org/wiki/Androgen_receptor"; CC -!- WEB RESOURCE: Name=X-chromosome gene database, androgen receptor (AR); CC Note=Leiden Open Variation Database (LOVD); CC URL="https://databases.lovd.nl/shared/genes/AR"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms 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; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL158016; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL356358; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471132; EAX05380.1; -; Genomic_DNA. DR EMBL; BC132975; AAI32976.1; -; mRNA. DR EMBL; L29496; AAA51770.1; -; mRNA. DR EMBL; U16371; AAB60346.1; -; Genomic_DNA. DR EMBL; M20260; AAA51774.1; -; mRNA. DR EMBL; S79366; AAB21256.2; -; Genomic_DNA. DR EMBL; S79368; AAB21257.2; -; Genomic_DNA. DR CCDS; CCDS14387.1; -. [P10275-1] DR CCDS; CCDS87754.1; -. [P10275-3] DR PIR; A39248; A39248. DR RefSeq; NP_000035.2; NM_000044.4. [P10275-1] DR RefSeq; NP_001011645.1; NM_001011645.3. [P10275-2] DR RefSeq; NP_001334990.1; NM_001348061.1. [P10275-3] DR RefSeq; NP_001334992.1; NM_001348063.1. [P10275-4] DR RefSeq; NP_001334993.1; NM_001348064.1. DR PDB; 1E3G; X-ray; 2.40 A; A=658-920. DR PDB; 1GS4; X-ray; 1.95 A; A=671-918. DR PDB; 1T5Z; X-ray; 2.30 A; A=670-920. DR PDB; 1T63; X-ray; 2.07 A; A=670-919. DR PDB; 1T65; X-ray; 1.66 A; A=670-920. DR PDB; 1XJ7; X-ray; 2.70 A; A=664-920. DR PDB; 1XOW; X-ray; 1.80 A; A=672-920, B=20-30. DR PDB; 1XQ3; X-ray; 2.25 A; A=672-920. DR PDB; 1Z95; X-ray; 1.80 A; A=673-918. DR PDB; 2AM9; X-ray; 1.64 A; A=655-920. DR PDB; 2AMA; X-ray; 1.90 A; A=655-920. DR PDB; 2AMB; X-ray; 1.75 A; A=655-920. DR PDB; 2AO6; X-ray; 1.89 A; A=672-920. DR PDB; 2AX6; X-ray; 1.50 A; A=665-920. DR PDB; 2AX7; X-ray; 1.90 A; A=665-920. DR PDB; 2AX8; X-ray; 1.70 A; A=665-920. DR PDB; 2AX9; X-ray; 1.65 A; A=665-920. DR PDB; 2AXA; X-ray; 1.80 A; A=665-920. DR PDB; 2HVC; X-ray; 2.10 A; A=670-919. DR PDB; 2OZ7; X-ray; 1.80 A; A=672-920. DR PDB; 2PIO; X-ray; 2.03 A; A=670-920. DR PDB; 2PIP; X-ray; 1.80 A; L=670-920. DR PDB; 2PIQ; X-ray; 2.40 A; A=670-920. DR PDB; 2PIR; X-ray; 2.10 A; A=670-920. DR PDB; 2PIT; X-ray; 1.76 A; A=670-920. DR PDB; 2PIU; X-ray; 2.12 A; A=670-920. DR PDB; 2PIV; X-ray; 1.95 A; A=670-920. DR PDB; 2PIW; X-ray; 2.58 A; A=670-920. DR PDB; 2PIX; X-ray; 2.40 A; A=670-920. DR PDB; 2PKL; X-ray; 2.49 A; A=670-920. DR PDB; 2PNU; X-ray; 1.65 A; A=655-920. DR PDB; 2Q7I; X-ray; 1.87 A; A=664-920, B=20-30. DR PDB; 2Q7J; X-ray; 1.90 A; A=664-920. DR PDB; 2Q7K; X-ray; 1.80 A; A=664-920, B=20-30. DR PDB; 2Q7L; X-ray; 1.92 A; A=664-920. DR PDB; 2YHD; X-ray; 2.20 A; A=672-920. DR PDB; 2YLO; X-ray; 2.50 A; A=665-920. DR PDB; 2YLP; X-ray; 2.30 A; A=665-920. DR PDB; 2YLQ; X-ray; 2.40 A; A=665-920. DR PDB; 2Z4J; X-ray; 2.60 A; A=672-919. DR PDB; 3B5R; X-ray; 1.80 A; A=672-920. DR PDB; 3B65; X-ray; 1.80 A; A=672-920. DR PDB; 3B66; X-ray; 1.65 A; A=672-920. DR PDB; 3B67; X-ray; 1.90 A; A=672-920. DR PDB; 3B68; X-ray; 1.90 A; A=672-920. DR PDB; 3BTR; X-ray; 2.60 A; B=622-636. DR PDB; 3L3X; X-ray; 1.55 A; A=671-919. DR PDB; 3L3Z; X-ray; 2.00 A; A=671-919. DR PDB; 3RLJ; X-ray; 1.90 A; A=672-918. DR PDB; 3RLL; X-ray; 1.70 A; A=672-918. DR PDB; 3V49; X-ray; 1.70 A; A=655-920, B=21-31. DR PDB; 3V4A; X-ray; 1.95 A; A=672-920, B=21-31. DR PDB; 3ZQT; X-ray; 2.29 A; A=665-920. DR PDB; 4HLW; X-ray; 2.50 A; A=665-920. DR PDB; 4K7A; X-ray; 2.44 A; A=671-919. DR PDB; 4OEA; X-ray; 2.12 A; A=671-920. DR PDB; 4OED; X-ray; 2.79 A; A=671-920. DR PDB; 4OEY; X-ray; 1.83 A; A=671-920. DR PDB; 4OEZ; X-ray; 1.80 A; A=671-920. DR PDB; 4OFR; X-ray; 2.26 A; A=671-920. DR PDB; 4OFU; X-ray; 2.12 A; A=671-920. DR PDB; 4OGH; X-ray; 2.98 A; A=671-920. DR PDB; 4OH5; X-ray; 2.00 A; A=671-920. DR PDB; 4OH6; X-ray; 3.56 A; A=671-920. DR PDB; 4OHA; X-ray; 1.42 A; A=671-920. DR PDB; 4OIL; X-ray; 2.51 A; A=671-920. DR PDB; 4OIU; X-ray; 3.01 A; A=671-920. DR PDB; 4OJ9; X-ray; 3.31 A; A=671-920. DR PDB; 4OJB; X-ray; 2.00 A; A=671-920. DR PDB; 4OK1; X-ray; 2.09 A; A=671-920. DR PDB; 4OKB; X-ray; 2.95 A; A=671-920. DR PDB; 4OKT; X-ray; 2.50 A; A=671-920. DR PDB; 4OKW; X-ray; 2.00 A; A=671-920. DR PDB; 4OKX; X-ray; 2.10 A; A=671-920. DR PDB; 4OLM; X-ray; 2.80 A; A=671-920. DR PDB; 4QL8; X-ray; 2.10 A; A=663-920. DR PDB; 5CJ6; X-ray; 2.07 A; A=642-920, B=21-30. DR PDB; 5JJM; X-ray; 2.15 A; A/B/C/D=669-920. DR PDB; 5T8E; X-ray; 2.71 A; A=672-920. DR PDB; 5T8J; X-ray; 2.70 A; A=672-920. DR PDB; 5V8Q; X-ray; 1.44 A; A=672-920. DR PDB; 5VO4; X-ray; 2.35 A; A=671-920. DR PDB; 7ZTX; X-ray; 1.89 A; A=672-920. DR PDB; 7ZTZ; X-ray; 1.40 A; A=672-920. DR PDB; 7ZU1; X-ray; 1.68 A; A=672-920. DR PDB; 7ZU2; X-ray; 1.74 A; A=672-920. DR PDB; 8E1A; X-ray; 1.20 A; A=665-920. DR PDB; 8FGY; X-ray; 2.20 A; A=663-920. DR PDB; 8FGZ; X-ray; 1.61 A; A=663-920. DR PDB; 8FH0; X-ray; 1.59 A; A=663-920. DR PDB; 8FH1; X-ray; 1.69 A; A=663-920. DR PDB; 8FH2; X-ray; 1.59 A; A=663-920. DR PDBsum; 1E3G; -. DR PDBsum; 1GS4; -. DR PDBsum; 1T5Z; -. DR PDBsum; 1T63; -. DR PDBsum; 1T65; -. DR PDBsum; 1XJ7; -. DR PDBsum; 1XOW; -. DR PDBsum; 1XQ3; -. DR PDBsum; 1Z95; -. DR PDBsum; 2AM9; -. DR PDBsum; 2AMA; -. DR PDBsum; 2AMB; -. DR PDBsum; 2AO6; -. DR PDBsum; 2AX6; -. DR PDBsum; 2AX7; -. DR PDBsum; 2AX8; -. DR PDBsum; 2AX9; -. DR PDBsum; 2AXA; -. DR PDBsum; 2HVC; -. DR PDBsum; 2OZ7; -. DR PDBsum; 2PIO; -. DR PDBsum; 2PIP; -. DR PDBsum; 2PIQ; -. DR PDBsum; 2PIR; -. DR PDBsum; 2PIT; -. DR PDBsum; 2PIU; -. DR PDBsum; 2PIV; -. DR PDBsum; 2PIW; -. DR PDBsum; 2PIX; -. DR PDBsum; 2PKL; -. DR PDBsum; 2PNU; -. DR PDBsum; 2Q7I; -. DR PDBsum; 2Q7J; -. DR PDBsum; 2Q7K; -. DR PDBsum; 2Q7L; -. DR PDBsum; 2YHD; -. DR PDBsum; 2YLO; -. DR PDBsum; 2YLP; -. DR PDBsum; 2YLQ; -. DR PDBsum; 2Z4J; -. DR PDBsum; 3B5R; -. DR PDBsum; 3B65; -. DR PDBsum; 3B66; -. DR PDBsum; 3B67; -. DR PDBsum; 3B68; -. DR PDBsum; 3BTR; -. DR PDBsum; 3L3X; -. DR PDBsum; 3L3Z; -. DR PDBsum; 3RLJ; -. DR PDBsum; 3RLL; -. DR PDBsum; 3V49; -. DR PDBsum; 3V4A; -. DR PDBsum; 3ZQT; -. DR PDBsum; 4HLW; -. DR PDBsum; 4K7A; -. DR PDBsum; 4OEA; -. DR PDBsum; 4OED; -. DR PDBsum; 4OEY; -. DR PDBsum; 4OEZ; -. DR PDBsum; 4OFR; -. DR PDBsum; 4OFU; -. DR PDBsum; 4OGH; -. DR PDBsum; 4OH5; -. DR PDBsum; 4OH6; -. DR PDBsum; 4OHA; -. DR PDBsum; 4OIL; -. DR PDBsum; 4OIU; -. DR PDBsum; 4OJ9; -. DR PDBsum; 4OJB; -. DR PDBsum; 4OK1; -. DR PDBsum; 4OKB; -. DR PDBsum; 4OKT; -. DR PDBsum; 4OKW; -. DR PDBsum; 4OKX; -. DR PDBsum; 4OLM; -. DR PDBsum; 4QL8; -. DR PDBsum; 5CJ6; -. DR PDBsum; 5JJM; -. DR PDBsum; 5T8E; -. DR PDBsum; 5T8J; -. DR PDBsum; 5V8Q; -. DR PDBsum; 5VO4; -. DR PDBsum; 7ZTX; -. DR PDBsum; 7ZTZ; -. DR PDBsum; 7ZU1; -. DR PDBsum; 7ZU2; -. DR PDBsum; 8E1A; -. DR PDBsum; 8FGY; -. DR PDBsum; 8FGZ; -. DR PDBsum; 8FH0; -. DR PDBsum; 8FH1; -. DR PDBsum; 8FH2; -. DR AlphaFoldDB; P10275; -. DR PCDDB; P10275; -. DR SMR; P10275; -. DR BioGRID; 106862; 952. DR CORUM; P10275; -. DR DIP; DIP-125N; -. DR ELM; P10275; -. DR IntAct; P10275; 310. DR MINT; P10275; -. DR STRING; 9606.ENSP00000363822; -. DR BindingDB; P10275; -. DR ChEMBL; CHEMBL1871; -. DR DrugBank; DB07422; (2S)-2-hydroxy-2-methyl-N-[4-nitro-3-(trifluoromethyl)phenyl]-3-(pentafluorophenoxy)propanamide. DR DrugBank; DB07039; (2S)-N-(4-cyano-3-iodophenyl)-3-(4-cyanophenoxy)-2-hydroxy-2-methylpropanamide. DR DrugBank; DB04709; (3AALPHA,4ALPHA,7ALPHA,7AALPHA)- 3A,4,7,7A-TETRAHYDRO-2-(4-NITRO-1-NAPHTHALENYL)-4,7-ETHANO-1H-ISOINDOLE-1,3(2H)-DIONE. DR DrugBank; DB07717; (5S,8R,9S,10S,13R,14S,17S)-13-{2-[(3,5-DIFLUOROBENZYL)OXY]ETHYL}-17-HYDROXY-10-METHYLHEXADECAHYDRO-3H-CYCLOPENTA[A]PHENANTHREN-3-ONE. DR DrugBank; DB07454; (R)-3-BROMO-2-HYDROXY-2-METHYL-N-[4-NITRO-3-(TRIFLUOROMETHYL)PHENYL]PROPANAMIDE. DR DrugBank; DB02932; (R)-Bicalutamide. DR DrugBank; DB08035; 1-TERT-BUTYL-3-(2,5-DIMETHYLBENZYL)-1H-PYRAZOLO[3,4-D]PYRIMIDIN-4-AMINE. DR DrugBank; DB01481; 1-Testosterone. DR DrugBank; DB08088; 2-chloro-4-{[(1R,3Z,7S,7aS)-7-hydroxy-1-(trifluoromethyl)tetrahydro-1H-pyrrolo[1,2-c][1,3]oxazol-3-ylidene]amino}-3-methylbenzonitrile. DR DrugBank; DB08461; 3-[(4-AMINO-1-TERT-BUTYL-1H-PYRAZOLO[3,4-D]PYRIMIDIN-3-YL)METHYL]PHENOL. DR DrugBank; DB08087; 4-[(7R,7AS)-7-HYDROXY-1,3-DIOXOTETRAHYDRO-1H-PYRROLO[1,2-C]IMIDAZOL-2(3H)-YL]-1-NAPHTHONITRILE. DR DrugBank; DB07421; 4-{[(1R,2S)-1,2-dihydroxy-2-methyl-3-(4-nitrophenoxy)propyl]amino}-2-(trifluoromethyl)benzonitrile. DR DrugBank; DB01063; Acetophenazine. DR DrugBank; DB07423; Andarine. DR DrugBank; DB11901; Apalutamide. DR DrugBank; DB01128; Bicalutamide. DR DrugBank; DB07286; BMS-564929. DR DrugBank; DB01541; Boldenone. DR DrugBank; DB14639; Boldenone undecylenate. DR DrugBank; DB01564; Calusterone. DR DrugBank; DB12499; Clascoterone. DR DrugBank; DB04839; Cyproterone acetate. DR DrugBank; DB01406; Danazol. DR DrugBank; DB12941; Darolutamide. DR DrugBank; DB09123; Dienogest. DR DrugBank; DB00255; Diethylstilbestrol. DR DrugBank; DB06133; Dimethylcurcumin. DR DrugBank; DB01395; Drospirenone. DR DrugBank; DB00858; Drostanolone. DR DrugBank; DB15488; Echinacoside. DR DrugBank; DB11219; Enzacamene. DR DrugBank; DB08899; Enzalutamide. DR DrugBank; DB13155; Esculin. DR DrugBank; DB00655; Estrone. DR DrugBank; DB09086; Eugenol. DR DrugBank; DB02266; Flufenamic acid. DR DrugBank; DB01185; Fluoxymesterone. DR DrugBank; DB00623; Fluphenazine. DR DrugBank; DB00499; Flutamide. DR DrugBank; DB11619; Gestrinone. DR DrugBank; DB11064; Homosalate. DR DrugBank; DB01026; Ketoconazole. DR DrugBank; DB15647; Ketodarolutamide. DR DrugBank; DB00367; Levonorgestrel. DR DrugBank; DB08089; LGD-2226. DR DrugBank; DB05234; LGD2941. DR DrugBank; DB13934; Ligandrol. DR DrugBank; DB11425; Luprostiol. DR DrugBank; DB06710; Methyltestosterone. DR DrugBank; DB02998; Metribolone. DR DrugBank; DB11429; Mibolerone. DR DrugBank; DB00648; Mitotane. DR DrugBank; DB08804; Nandrolone decanoate. DR DrugBank; DB00984; Nandrolone phenpropionate. DR DrugBank; DB00665; Nilutamide. DR DrugBank; DB06713; Norelgestromin. DR DrugBank; DB00717; Norethisterone. DR DrugBank; DB09371; Norethynodrel. DR DrugBank; DB00957; Norgestimate. DR DrugBank; DB09389; Norgestrel. DR DrugBank; DB00621; Oxandrolone. DR DrugBank; DB01428; Oxybenzone. DR DrugBank; DB06412; Oxymetholone. DR DrugBank; DB01608; Periciazine. DR DrugBank; DB11447; Phenothiazine. DR DrugBank; DB01708; Prasterone. DR DrugBank; DB00396; Progesterone. DR DrugBank; DB07419; S-23. DR DrugBank; DB07769; S-3-(4-FLUOROPHENOXY)-2-HYDROXY-2-METHYL-N-[4-NITRO-3-(TRIFLUOROMETHYL)PHENYL]PROPANAMIDE. DR DrugBank; DB14583; Segesterone acetate. DR DrugBank; DB00421; Spironolactone. DR DrugBank; DB02901; Stanolone. DR DrugBank; DB13951; Stanolone acetate. DR DrugBank; DB06718; Stanozolol. DR DrugBank; DB00675; Tamoxifen. DR DrugBank; DB00624; Testosterone. DR DrugBank; DB13943; Testosterone cypionate. DR DrugBank; DB13944; Testosterone enanthate. DR DrugBank; DB01420; Testosterone propionate. DR DrugBank; DB13946; Testosterone undecanoate. DR DrugBank; DB06870; Tetrahydrogestrinone. DR DrugBank; DB08604; Triclosan. DR DrugBank; DB08867; Ulipristal. DR DrugCentral; P10275; -. DR GuidetoPHARMACOLOGY; 628; -. DR SwissLipids; SLP:000001553; -. DR MoonDB; P10275; Predicted. DR iPTMnet; P10275; -. DR PhosphoSitePlus; P10275; -. DR SwissPalm; P10275; -. DR BioMuta; AR; -. DR DMDM; 113830; -. DR MassIVE; P10275; -. DR MaxQB; P10275; -. DR PaxDb; 9606-ENSP00000363822; -. DR PeptideAtlas; P10275; -. DR ProteomicsDB; 18721; -. DR ProteomicsDB; 52590; -. [P10275-1] DR ProteomicsDB; 52591; -. [P10275-2] DR TopDownProteomics; P10275-1; -. [P10275-1] DR Antibodypedia; 3489; 2929 antibodies from 51 providers. DR DNASU; 367; -. DR Ensembl; ENST00000374690.9; ENSP00000363822.3; ENSG00000169083.18. [P10275-1] DR Ensembl; ENST00000504326.5; ENSP00000421155.1; ENSG00000169083.18. [P10275-3] DR Ensembl; ENST00000612452.5; ENSP00000484033.2; ENSG00000169083.18. [P10275-1] DR GeneID; 367; -. DR MANE-Select; ENST00000374690.9; ENSP00000363822.3; NM_000044.6; NP_000035.2. DR UCSC; uc004dwv.3; human. [P10275-1] DR UCSC; uc011mpf.2; human. DR AGR; HGNC:644; -. DR DisGeNET; 367; -. DR GeneCards; AR; -. DR GeneReviews; AR; -. DR HGNC; HGNC:644; AR. DR HPA; ENSG00000169083; Tissue enhanced (liver). DR MalaCards; AR; -. DR MIM; 300068; phenotype. DR MIM; 300633; phenotype. DR MIM; 312300; phenotype. DR MIM; 313200; phenotype. DR MIM; 313700; gene. DR neXtProt; NX_P10275; -. DR OpenTargets; ENSG00000169083; -. DR Orphanet; 99429; Complete androgen insensitivity syndrome. DR Orphanet; 481; Kennedy disease. DR Orphanet; 95706; Non-syndromic posterior hypospadias. DR Orphanet; 90797; Partial androgen insensitivity syndrome. DR PharmGKB; PA57; -. DR VEuPathDB; HostDB:ENSG00000169083; -. DR eggNOG; KOG3575; Eukaryota. DR GeneTree; ENSGT00940000155516; -. DR HOGENOM; CLU_007368_15_0_1; -. DR InParanoid; P10275; -. DR OMA; FGEMRLE; -. DR OrthoDB; 5351241at2759; -. DR PhylomeDB; P10275; -. DR TreeFam; TF350286; -. DR PathwayCommons; P10275; -. DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand. DR Reactome; R-HSA-383280; Nuclear Receptor transcription pathway. DR Reactome; R-HSA-4090294; SUMOylation of intracellular receptors. DR Reactome; R-HSA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3. DR Reactome; R-HSA-5689880; Ub-specific processing proteases. DR Reactome; R-HSA-8940973; RUNX2 regulates osteoblast differentiation. DR SignaLink; P10275; -. DR SIGNOR; P10275; -. DR BioGRID-ORCS; 367; 14 hits in 805 CRISPR screens. DR ChiTaRS; AR; human. DR EvolutionaryTrace; P10275; -. DR GeneWiki; Androgen_receptor; -. DR GenomeRNAi; 367; -. DR Pharos; P10275; Tclin. DR PRO; PR:P10275; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; P10275; Protein. DR Bgee; ENSG00000169083; Expressed in seminal vesicle and 180 other cell types or tissues. DR ExpressionAtlas; P10275; baseline and differential. DR Genevisible; P10275; HS. DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. 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; IMP:UniProt. DR GO; GO:0032991; C:protein-containing complex; IDA:MGI. DR GO; GO:0005497; F:androgen binding; IDA:UniProtKB. DR GO; GO:0051117; F:ATPase binding; IDA:MGI. DR GO; GO:0008013; F:beta-catenin binding; IDA:BHF-UCL. DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0034056; F:estrogen response element binding; IBA:GO_Central. DR GO; GO:0004930; F:G protein-coupled receptor activity; IC:UniProt. DR GO; GO:0060090; F:molecular adaptor activity; IDA:DisProt. DR GO; GO:0004879; F:nuclear receptor activity; IDA:UniProtKB. DR GO; GO:0070974; F:POU domain binding; IEA:Ensembl. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB. DR GO; GO:0001091; F:RNA polymerase II general transcription initiation factor binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL. DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB. DR GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB. DR GO; GO:0001223; F:transcription coactivator binding; IDA:ARUK-UCL. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0060520; P:activation of prostate induction by androgen receptor signaling pathway; IEA:Ensembl. DR GO; GO:0030521; P:androgen receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0048645; P:animal organ formation; IEA:Ensembl. DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc. DR GO; GO:0071391; P:cellular response to estrogen stimulus; IDA:ARUK-UCL. DR GO; GO:0071383; P:cellular response to steroid hormone stimulus; IMP:CAFA. DR GO; GO:0071394; P:cellular response to testosterone stimulus; IDA:ARUK-UCL. 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:0050673; P:epithelial cell proliferation; IEA:Ensembl. DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl. DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IEA:Ensembl. DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IDA:ARUK-UCL. DR GO; GO:0030522; P:intracellular receptor signaling pathway; IDA:BHF-UCL. DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IBA:GO_Central. 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:0008584; P:male gonad development; IBA:GO_Central. 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:0000165; P:MAPK cascade; IEA:Ensembl. DR GO; GO:0060571; P:morphogenesis of an epithelial fold; IEA:Ensembl. DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB. DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl. DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IDA:BHF-UCL. DR GO; GO:0045720; P:negative regulation of integrin biosynthetic process; IDA:BHF-UCL. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:CAFA. DR GO; GO:0045597; P:positive regulation of cell differentiation; IMP:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0060769; P:positive regulation of epithelial cell proliferation involved in prostate gland development; IEA:Ensembl. DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB. DR GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; IEA:Ensembl. DR GO; GO:0045726; P:positive regulation of integrin biosynthetic process; IDA:BHF-UCL. DR GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IEA:Ensembl. DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl. DR GO; GO:1902895; P:positive regulation of miRNA transcription; IDA:BHF-UCL. DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:BHF-UCL. DR GO; GO:0042327; P:positive regulation of phosphorylation; IMP:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IDA:BHF-UCL. DR GO; GO:0060740; P:prostate gland epithelium morphogenesis; IEA:Ensembl. DR GO; GO:0060736; P:prostate gland growth; 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: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:0006366; P:transcription by RNA polymerase II; IEA:Ensembl. DR CDD; cd07173; NR_DBD_AR; 1. DR CDD; cd07073; NR_LBD_AR; 1. DR DisProt; DP00492; -. DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1. DR Gene3D; 1.10.565.10; Retinoid X Receptor; 1. DR IDEAL; IID00020; -. 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 PANTHER; PTHR48092:SF13; ANDROGEN RECEPTOR; 1. DR PANTHER; PTHR48092; KNIRPS-RELATED PROTEIN-RELATED; 1. 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; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1. DR SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 1. DR PROSITE; PS51843; NR_LBD; 1. DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1. DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Activator; Alternative splicing; Cytoplasm; Disease variant; KW DNA-binding; Isopeptide bond; Lipid-binding; Lipoprotein; Metal-binding; KW Neurodegeneration; Nucleus; Palmitate; Phosphoprotein; KW Pseudohermaphroditism; Receptor; Reference proteome; Steroid-binding; KW Transcription; Transcription regulation; Triplet repeat expansion; KW Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..920 FT /note="Androgen receptor" FT /id="PRO_0000053704" FT DOMAIN 669..900 FT /note="NR LBD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189" FT DNA_BIND 560..632 FT /note="Nuclear receptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT ZN_FING 560..580 FT /note="NR C4-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT ZN_FING 596..620 FT /note="NR C4-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT REGION 1..587 FT /note="Interaction with ZNF318" FT /evidence="ECO:0000250|UniProtKB:P19091" FT REGION 1..559 FT /note="Modulating" FT REGION 36..167 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 195..228 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 552..919 FT /note="Interaction with LPXN" FT /evidence="ECO:0000269|PubMed:18451096" FT REGION 572..662 FT /note="Interaction with HIPK3" FT /evidence="ECO:0000250|UniProtKB:P15207" FT REGION 592..919 FT /note="Interaction with CCAR1" FT /evidence="ECO:0000269|PubMed:23887938" FT REGION 625..919 FT /note="Interaction with KAT7" FT /evidence="ECO:0000269|PubMed:10930412" FT COMPBIAS 53..96 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 706 FT /ligand="17beta-hydroxy-5alpha-androstan-3-one" FT /ligand_id="ChEBI:CHEBI:16330" FT /evidence="ECO:0000269|PubMed:15563469, FT ECO:0000269|PubMed:16641486, ECO:0000269|PubMed:17591767, FT ECO:0000269|PubMed:25091737, ECO:0007744|PDB:1T5Z, FT ECO:0007744|PDB:1T63, ECO:0007744|PDB:1T65, FT ECO:0007744|PDB:1XJ7, ECO:0007744|PDB:2AM9, FT ECO:0007744|PDB:2AMA, ECO:0007744|PDB:2AMB, FT ECO:0007744|PDB:2PIO, ECO:0007744|PDB:2PIP, FT ECO:0007744|PDB:2PIR, ECO:0007744|PDB:2PIT, FT ECO:0007744|PDB:2PIU, ECO:0007744|PDB:2PIV, FT ECO:0007744|PDB:2PIW, ECO:0007744|PDB:2PIX, FT ECO:0007744|PDB:2PKL, ECO:0007744|PDB:2PNU, FT ECO:0007744|PDB:2Q7I, ECO:0007744|PDB:2Q7J, FT ECO:0007744|PDB:2Q7K, ECO:0007744|PDB:2Q7L, FT ECO:0007744|PDB:2YHD, ECO:0007744|PDB:2YLO, FT ECO:0007744|PDB:2YLP, ECO:0007744|PDB:2YLQ, FT ECO:0007744|PDB:3L3X, ECO:0007744|PDB:3L3Z, FT ECO:0007744|PDB:3ZQT, ECO:0007744|PDB:4HLW, FT ECO:0007744|PDB:4K7A, ECO:0007744|PDB:4OEA, FT ECO:0007744|PDB:4OED, ECO:0007744|PDB:4OEY, FT ECO:0007744|PDB:4OEZ, ECO:0007744|PDB:4OFR, FT ECO:0007744|PDB:4OFU, ECO:0007744|PDB:5JJM" FT BINDING 753 FT /ligand="17beta-hydroxy-5alpha-androstan-3-one" FT /ligand_id="ChEBI:CHEBI:16330" FT /evidence="ECO:0000269|PubMed:15563469, FT ECO:0000269|PubMed:16641486, ECO:0000269|PubMed:17591767, FT ECO:0000269|PubMed:25091737, ECO:0007744|PDB:1T5Z, FT ECO:0007744|PDB:1T63, ECO:0007744|PDB:1T65, FT ECO:0007744|PDB:1XJ7, ECO:0007744|PDB:2AM9, FT ECO:0007744|PDB:2AMA, ECO:0007744|PDB:2PIO, FT ECO:0007744|PDB:2PIP, ECO:0007744|PDB:2PIQ, FT ECO:0007744|PDB:2PIR, ECO:0007744|PDB:2PIT, FT ECO:0007744|PDB:2PIU, ECO:0007744|PDB:2PIV, FT ECO:0007744|PDB:2PIW, ECO:0007744|PDB:2PIX, FT ECO:0007744|PDB:2PKL, ECO:0007744|PDB:2Q7I, FT ECO:0007744|PDB:2Q7J, ECO:0007744|PDB:2Q7K, FT ECO:0007744|PDB:2Q7L, ECO:0007744|PDB:2YHD, FT ECO:0007744|PDB:2YLO, ECO:0007744|PDB:2YLP, FT ECO:0007744|PDB:2YLQ, ECO:0007744|PDB:2Z4J, FT ECO:0007744|PDB:3L3X, ECO:0007744|PDB:3L3Z, FT ECO:0007744|PDB:3ZQT, ECO:0007744|PDB:4HLW, FT ECO:0007744|PDB:4K7A, ECO:0007744|PDB:4OEA, FT ECO:0007744|PDB:4OED, ECO:0007744|PDB:4OEY, FT ECO:0007744|PDB:4OEZ, ECO:0007744|PDB:4OFR, FT ECO:0007744|PDB:4OFU, ECO:0007744|PDB:5JJM" FT BINDING 878 FT /ligand="17beta-hydroxy-5alpha-androstan-3-one" FT /ligand_id="ChEBI:CHEBI:16330" FT /evidence="ECO:0000269|PubMed:15563469, FT ECO:0000269|PubMed:16641486, ECO:0000269|PubMed:17591767, FT ECO:0000269|PubMed:25091737, ECO:0007744|PDB:1T5Z, FT ECO:0007744|PDB:1T63, ECO:0007744|PDB:1T65, FT ECO:0007744|PDB:1XJ7, ECO:0007744|PDB:2AM9, FT ECO:0007744|PDB:2AMA, ECO:0007744|PDB:2PIO, FT ECO:0007744|PDB:2PIP, ECO:0007744|PDB:2PIQ, FT ECO:0007744|PDB:2PIR, ECO:0007744|PDB:2PIT, FT ECO:0007744|PDB:2PIU, ECO:0007744|PDB:2PIV, FT ECO:0007744|PDB:2PIW, ECO:0007744|PDB:2PIX, FT ECO:0007744|PDB:2PKL, ECO:0007744|PDB:2Q7I, FT ECO:0007744|PDB:2Q7J, ECO:0007744|PDB:2Q7K, FT ECO:0007744|PDB:2Q7L, ECO:0007744|PDB:2YHD, FT ECO:0007744|PDB:2YLO, ECO:0007744|PDB:2YLP, FT ECO:0007744|PDB:2YLQ, ECO:0007744|PDB:2Z4J, FT ECO:0007744|PDB:3L3X, ECO:0007744|PDB:3L3Z, FT ECO:0007744|PDB:3ZQT, ECO:0007744|PDB:4HLW, FT ECO:0007744|PDB:4K7A, ECO:0007744|PDB:4OEA, FT ECO:0007744|PDB:4OED, ECO:0007744|PDB:4OEY, FT ECO:0007744|PDB:4OEZ, ECO:0007744|PDB:4OFR, FT ECO:0007744|PDB:4OFU, ECO:0007744|PDB:5JJM" FT SITE 721 FT /note="Interaction with coactivator LXXL and FXXFY motifs" FT /evidence="ECO:0000269|PubMed:25091737" FT SITE 898 FT /note="Interaction with coactivator FXXLF and FXXFY motifs" FT /evidence="ECO:0000269|PubMed:25091737" FT MOD_RES 83 FT /note="Phosphoserine; by CDK9" FT /evidence="ECO:0000269|PubMed:20980437" FT MOD_RES 96 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:24275569" FT MOD_RES 225 FT /note="Phosphotyrosine; by CSK" FT /evidence="ECO:0000269|PubMed:17045208" FT MOD_RES 258 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 269 FT /note="Phosphotyrosine; by CSK and TNK2" FT /evidence="ECO:0000269|PubMed:17045208, FT ECO:0000269|PubMed:17494760, ECO:0000269|PubMed:20623637" FT MOD_RES 309 FT /note="Phosphotyrosine; by CSK" FT /evidence="ECO:0000269|PubMed:17045208" FT MOD_RES 348 FT /note="Phosphotyrosine; by CSK" FT /evidence="ECO:0000269|PubMed:17045208" FT MOD_RES 359 FT /note="Phosphotyrosine; by CSK" FT /evidence="ECO:0000269|PubMed:17045208" FT MOD_RES 364 FT /note="Phosphotyrosine; by CSK" FT /evidence="ECO:0000269|PubMed:17045208" FT MOD_RES 365 FT /note="Phosphotyrosine; by CSK and TNK2" FT /evidence="ECO:0000269|PubMed:17045208, FT ECO:0000269|PubMed:17494760" FT MOD_RES 395 FT /note="Phosphotyrosine; by CSK" FT /evidence="ECO:0000269|PubMed:17045208" FT MOD_RES 535 FT /note="Phosphotyrosine; by CSK" FT /evidence="ECO:0000269|PubMed:17045208" FT MOD_RES 552 FT /note="Phosphotyrosine; by CSK" FT /evidence="ECO:0000269|PubMed:17045208" FT MOD_RES 651 FT /note="Phosphoserine; by STK4/MST1" FT /evidence="ECO:0000269|PubMed:21512132" FT MOD_RES 916 FT /note="Phosphotyrosine; by CSK" FT /evidence="ECO:0000269|PubMed:17045208" FT CROSSLNK 388 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000269|PubMed:11121022" FT CROSSLNK 521 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000269|PubMed:11121022" FT CROSSLNK 846 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:19345326" FT CROSSLNK 848 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:19345326" FT VAR_SEQ 1..532 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_036889" FT VAR_SEQ 533..539 FT /note="GPYGDMR -> MILWLHS (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_036890" FT VAR_SEQ 629..644 FT /note="ARKLKKLGNLKLQEEG -> EKFRVGNCKHLKMTRP (in isoform 3)" FT /id="VSP_058166" FT VAR_SEQ 630..648 FT /note="RKLKKLGNLKLQEEGEASS -> AVVVSERILRVFGVSEWLP (in FT isoform 4)" FT /id="VSP_058167" FT VAR_SEQ 645..920 FT /note="Missing (in isoform 3)" FT /id="VSP_058168" FT VAR_SEQ 649..920 FT /note="Missing (in isoform 4)" FT /id="VSP_058169" FT VARIANT 2 FT /note="E -> K (in PAIS; dbSNP:rs104894742)" FT /evidence="ECO:0000269|PubMed:8823308" FT /id="VAR_004679" FT VARIANT 54 FT /note="L -> S (in prostate cancer)" FT /id="VAR_004680" FT VARIANT 57 FT /note="L -> Q (in prostate cancer; dbSNP:rs78686797)" FT /evidence="ECO:0000269|PubMed:19244107" FT /id="VAR_004681" FT VARIANT 64 FT /note="Q -> R (in prostate cancer)" FT /id="VAR_009711" FT VARIANT 114 FT /note="Q -> H (in prostate cancer)" FT /id="VAR_009712" FT VARIANT 182 FT /note="K -> R (in prostate cancer)" FT /id="VAR_009713" FT VARIANT 196 FT /note="Q -> R (in AIS)" FT /evidence="ECO:0000269|PubMed:9255042" FT /id="VAR_009224" FT VARIANT 207 FT /note="S -> R (in dbSNP:rs374549047)" FT /evidence="ECO:0000269|PubMed:8213813" FT /id="VAR_009714" FT VARIANT 216 FT /note="G -> R (20% lower transactivation capacity; FT dbSNP:rs199554641)" FT /evidence="ECO:0000269|PubMed:27535533, FT ECO:0000269|PubMed:9788719" FT /id="VAR_009715" FT VARIANT 257 FT /note="L -> P (in AIS)" FT /evidence="ECO:0000269|PubMed:9610419" FT /id="VAR_009225" FT VARIANT 268 FT /note="M -> T (in prostate cancer)" FT /id="VAR_009716" FT VARIANT 271 FT /note="P -> S (in prostate cancer)" FT /id="VAR_009717" FT VARIANT 342 FT /note="P -> L (in prostate cancer; dbSNP:rs138454018)" FT /evidence="ECO:0000269|PubMed:7511268" FT /id="VAR_009718" FT VARIANT 392 FT /note="P -> R (in AIS; dbSNP:rs773996740)" FT /evidence="ECO:0000269|PubMed:10571951" FT /id="VAR_009226" FT VARIANT 392 FT /note="P -> S (in AIS; dbSNP:rs201934623)" FT /id="VAR_009227" FT VARIANT 445 FT /note="Q -> R (in AIS; uncertain significance; FT dbSNP:rs1355285524)" FT /evidence="ECO:0000269|PubMed:10571951" FT /id="VAR_009228" FT VARIANT 492 FT /note="G -> S (in AIS)" FT /id="VAR_009719" FT VARIANT 529 FT /note="D -> G (in prostate cancer)" FT /id="VAR_009720" FT VARIANT 548 FT /note="L -> F (in PAIS; dbSNP:rs139524801)" FT /id="VAR_009721" FT VARIANT 549 FT /note="P -> S (in AIS; dbSNP:rs137852588)" FT /evidence="ECO:0000269|PubMed:8683794" FT /id="VAR_009722" FT VARIANT 560 FT /note="C -> Y (in AIS)" FT /evidence="ECO:0000269|PubMed:1316540" FT /id="VAR_009723" FT VARIANT 569 FT /note="G -> V (in a patient with isolated hypospadias)" FT /evidence="ECO:0000269|PubMed:7673412" FT /id="VAR_009725" FT VARIANT 569 FT /note="G -> W (in PAIS; dbSNP:rs1555982864)" FT /evidence="ECO:0000269|PubMed:7910529" FT /id="VAR_009726" FT VARIANT 572 FT /note="Y -> C (in AIS)" FT /evidence="ECO:0000269|PubMed:9544375" FT /id="VAR_009727" FT VARIANT 574 FT /note="A -> D (in AIS)" FT /id="VAR_009728" FT VARIANT 575 FT /note="L -> P (in prostate cancer)" FT /id="VAR_009729" FT VARIANT 576 FT /note="T -> A (in prostate cancer)" FT /evidence="ECO:0000269|PubMed:10706109" FT /id="VAR_009730" FT VARIANT 577 FT /note="C -> F (in AIS)" FT /evidence="ECO:0000269|PubMed:14756668" FT /id="VAR_009731" FT VARIANT 577 FT /note="C -> R (in AIS)" FT /evidence="ECO:0000269|PubMed:1316540" FT /id="VAR_009732" FT VARIANT 580 FT /note="C -> F (in AIS; reduced transcription and DNA FT binding; dbSNP:rs137852586)" FT /evidence="ECO:0000269|PubMed:8809734" FT /id="VAR_009733" FT VARIANT 580 FT /note="C -> Y (in AIS; dbSNP:rs137852586)" FT /id="VAR_009734" FT VARIANT 581 FT /note="K -> R (in prostate cancer)" FT /evidence="ECO:0000269|PubMed:10706109" FT /id="VAR_009735" FT VARIANT 582 FT /note="V -> F (in AIS)" FT /evidence="ECO:0000269|PubMed:8224266, ECO:0000269|Ref.115" FT /id="VAR_009736" FT VARIANT 583 FT /note="F -> S (in PAIS)" FT /evidence="ECO:0000269|PubMed:7981687" FT /id="VAR_009737" FT VARIANT 583 FT /note="F -> Y (in PAIS; dbSNP:rs137852587)" FT /evidence="ECO:0000269|PubMed:8809734" FT /id="VAR_009738" FT VARIANT 583 FT /note="Missing (in AIS)" FT /evidence="ECO:0000269|PubMed:8162033" FT /id="VAR_009739" FT VARIANT 586 FT /note="R -> K (in AIS)" FT /id="VAR_009740" FT VARIANT 587 FT /note="A -> V (in prostate cancer; somatic mutation)" FT /evidence="ECO:0000269|PubMed:10706109" FT /id="VAR_009741" FT VARIANT 588 FT /note="A -> S (in prostate cancer; somatic mutation)" FT /id="VAR_009742" FT VARIANT 597 FT /note="A -> T (in AIS; abolishes dimerization; FT dbSNP:rs137852569)" FT /evidence="ECO:0000269|PubMed:10590024, FT ECO:0000269|PubMed:7649358" FT /id="VAR_009743" FT VARIANT 598 FT /note="S -> G (in PAIS; normal androgen binding; does not FT activate transcription; impairs DNA binding; FT dbSNP:rs142280455)" FT /evidence="ECO:0000269|PubMed:1316540" FT /id="VAR_009744" FT VARIANT 598 FT /note="S -> T (in a patient with severe hypospadias)" FT /evidence="ECO:0000269|PubMed:10092153" FT /id="VAR_009745" FT VARIANT 602 FT /note="C -> F (in AIS)" FT /evidence="ECO:0000269|PubMed:7981689" FT /id="VAR_009746" FT VARIANT 605 FT /note="D -> Y (in PAIS)" FT /evidence="ECO:0000269|PubMed:7981687" FT /id="VAR_009747" FT VARIANT 608 FT /note="R -> Q (in PAIS and breast cancer; FT dbSNP:rs137852573)" FT /evidence="ECO:0000269|PubMed:10221692, FT ECO:0000269|PubMed:1303262, ECO:0000269|PubMed:9039340, FT ECO:0000269|PubMed:9543136" FT /id="VAR_004684" FT VARIANT 609 FT /note="R -> K (in PAIS and breast cancer; defective nuclear FT localization; dbSNP:rs137852576)" FT /evidence="ECO:0000269|PubMed:1424203, FT ECO:0000269|PubMed:8281139, ECO:0000269|PubMed:9196614" FT /id="VAR_004685" FT VARIANT 611 FT /note="N -> T (in PAIS)" FT /evidence="ECO:0000269|PubMed:9039340" FT /id="VAR_009748" FT VARIANT 612 FT /note="C -> Y (in AIS)" FT /id="VAR_009749" FT VARIANT 616 FT /note="R -> H (in AIS and PAIS; dbSNP:rs754201976)" FT /evidence="ECO:0000269|PubMed:7970939, FT ECO:0000269|PubMed:8162033, ECO:0000269|PubMed:8413310, FT ECO:0000269|PubMed:9698822" FT /id="VAR_009751" FT VARIANT 616 FT /note="R -> P (in AIS)" FT /id="VAR_009752" FT VARIANT 616 FT /note="Missing (in AIS)" FT /evidence="ECO:0000269|PubMed:8162033" FT /id="VAR_009750" FT VARIANT 617 FT /note="L -> P (in AIS; dbSNP:rs1555990488)" FT /evidence="ECO:0000269|PubMed:8647313" FT /id="VAR_009753" FT VARIANT 617 FT /note="L -> R (in PAIS)" FT /evidence="ECO:0000269|PubMed:8126121" FT /id="VAR_009754" FT VARIANT 618 FT /note="R -> P (in AIS and PAIS; loss of DNA-binding FT activity)" FT /evidence="ECO:0000269|PubMed:1316540, FT ECO:0000269|PubMed:1999491" FT /id="VAR_009755" FT VARIANT 620 FT /note="C -> Y (in prostate cancer; loss of DNA binding; FT somatic mutation)" FT /evidence="ECO:0000269|PubMed:10598582, FT ECO:0000269|PubMed:10706109" FT /id="VAR_009756" FT VARIANT 630 FT /note="R -> Q (in prostate cancer; dbSNP:rs868669253)" FT /evidence="ECO:0000269|PubMed:9184448" FT /id="VAR_009757" FT VARIANT 631 FT /note="K -> T (in prostate cancer)" FT /id="VAR_009758" FT VARIANT 646 FT /note="A -> D (in dbSNP:rs1800053)" FT /evidence="ECO:0000269|PubMed:9554755" FT /id="VAR_004686" FT VARIANT 648 FT /note="S -> N (in prostate cancer; dbSNP:rs137852584)" FT /id="VAR_009760" FT VARIANT 665 FT /note="I -> N (in AIS and PAIS)" FT /id="VAR_004687" FT VARIANT 671 FT /note="Q -> R (in prostate cancer)" FT /id="VAR_009761" FT VARIANT 672 FT /note="P -> H (in PAIS)" FT /id="VAR_009762" FT VARIANT 673 FT /note="I -> T (in prostate cancer)" FT /id="VAR_009763" FT VARIANT 678 FT /note="L -> P (in AIS; dbSNP:rs137852579)" FT /evidence="ECO:0000269|PubMed:7537149" FT /id="VAR_004688" FT VARIANT 682 FT /note="E -> K (in AIS; dbSNP:rs1555995816)" FT /evidence="ECO:0000269|PubMed:10221692, FT ECO:0000269|PubMed:8325950" FT /id="VAR_009764" FT VARIANT 683 FT /note="P -> T (in PAIS)" FT /evidence="ECO:0000269|PubMed:11587068" FT /id="VAR_013474" FT VARIANT 684 FT /note="G -> A (found in prostate cancer)" FT /evidence="ECO:0000269|PubMed:10629558, FT ECO:0000269|PubMed:9000575" FT /id="VAR_009765" FT VARIANT 685 FT /note="V -> I (in AIS; dbSNP:rs1555995822)" FT /id="VAR_009766" FT VARIANT 687 FT /note="C -> R (in PAIS)" FT /id="VAR_009767" FT VARIANT 688 FT /note="A -> V (in PAIS)" FT /id="VAR_009768" FT VARIANT 689 FT /note="G -> E (in AIS)" FT /id="VAR_009769" FT VARIANT 691 FT /note="Missing (in PAIS)" FT /evidence="ECO:0000269|Ref.123" FT /id="VAR_009770" FT VARIANT 693 FT /note="Missing (in AIS)" FT /id="VAR_004689" FT VARIANT 696 FT /note="D -> H (in AIS)" FT /evidence="ECO:0000269|PubMed:1775137" FT /id="VAR_004690" FT VARIANT 696 FT /note="D -> N (in AIS; almost complete loss of androgen FT binding and transcription activation; dbSNP:rs1555995840)" FT /evidence="ECO:0000269|PubMed:16595706, FT ECO:0000269|PubMed:1775137" FT /id="VAR_004691" FT VARIANT 696 FT /note="D -> V (in AIS)" FT /evidence="ECO:0000269|PubMed:9554754" FT /id="VAR_004692" FT VARIANT 701 FT /note="L -> M (in AIS)" FT /id="VAR_009771" FT VARIANT 702 FT /note="L -> F (in AIS; dbSNP:rs1555995851)" FT /id="VAR_009772" FT VARIANT 702 FT /note="L -> H (found in prostate cancer; FT dbSNP:rs864622007)" FT /evidence="ECO:0000269|PubMed:10569618, FT ECO:0000269|PubMed:8274409, ECO:0000269|PubMed:9438000" FT /id="VAR_009773" FT VARIANT 703 FT /note="S -> A (in AIS)" FT /id="VAR_009774" FT VARIANT 704 FT /note="S -> C (in AIS)" FT /id="VAR_009775" FT VARIANT 704 FT /note="S -> G (in PAIS and AIS)" FT /evidence="ECO:0000269|PubMed:9302173" FT /id="VAR_004693" FT VARIANT 706 FT /note="N -> S (in AIS; dbSNP:rs925822435)" FT /evidence="ECO:0000269|PubMed:1480178, FT ECO:0000269|PubMed:7671849" FT /id="VAR_009776" FT VARIANT 706 FT /note="N -> Y (in AIS)" FT /evidence="ECO:0000269|PubMed:11744994" FT /id="VAR_013475" FT VARIANT 708 FT /note="L -> R (in AIS; dbSNP:rs137852585)" FT /evidence="ECO:0000269|PubMed:8626869" FT /id="VAR_004694" FT VARIANT 709 FT /note="G -> A (in PAIS)" FT /evidence="ECO:0000269|PubMed:7981687, FT ECO:0000269|PubMed:9329414" FT /id="VAR_009777" FT VARIANT 709 FT /note="G -> V (in AIS)" FT /id="VAR_009778" FT VARIANT 711 FT /note="R -> T (in AIS)" FT /id="VAR_009779" FT VARIANT 712 FT /note="Q -> E (in PAIS)" FT /evidence="ECO:0000269|PubMed:11587068" FT /id="VAR_013476" FT VARIANT 713 FT /note="L -> F (in PAIS; dbSNP:rs137852595)" FT /id="VAR_009780" FT VARIANT 716 FT /note="V -> M (in prostate cancer; gain in function; FT dbSNP:rs1340026226)" FT /evidence="ECO:0000269|PubMed:8145761" FT /id="VAR_009781" FT VARIANT 718 FT /note="K -> E (in prostate cancer)" FT /id="VAR_009782" FT VARIANT 721 FT /note="K -> E (in prostate cancer; found in bone FT metastases)" FT /id="VAR_009783" FT VARIANT 722 FT /note="A -> T (in prostate cancer; somatic mutation; FT dbSNP:rs137852583)" FT /id="VAR_009784" FT VARIANT 723 FT /note="L -> F (in AIS)" FT /id="VAR_009785" FT VARIANT 724 FT /note="P -> S (in AIS)" FT /id="VAR_009786" FT VARIANT 725 FT /note="G -> D (in AIS and prostate cancer)" FT /id="VAR_009787" FT VARIANT 726 FT /note="F -> L (in a patient with severe hypospadias; FT dbSNP:rs1555996810)" FT /evidence="ECO:0000269|PubMed:10092153, FT ECO:0000269|PubMed:7671849" FT /id="VAR_009788" FT VARIANT 727 FT /note="R -> L (in prostate cancer; dbSNP:rs137852593)" FT /evidence="ECO:0000269|PubMed:8530589" FT /id="VAR_009789" FT VARIANT 728 FT /note="N -> K (in AIS; dbSNP:rs768869912)" FT /evidence="ECO:0000269|PubMed:7993455" FT /id="VAR_009790" FT VARIANT 729 FT /note="L -> S (in PAIS)" FT /id="VAR_009791" FT VARIANT 731 FT /note="V -> M (in prostate cancer; increases transcription FT activation; dbSNP:rs137852571)" FT /evidence="ECO:0000269|PubMed:15525515, FT ECO:0000269|PubMed:1631125, ECO:0000269|PubMed:7591265" FT /id="VAR_004695" FT VARIANT 733 FT /note="D -> N (in AIS)" FT /evidence="ECO:0000269|PubMed:9252933" FT /id="VAR_004696" FT VARIANT 733 FT /note="D -> Y (in AIS)" FT /id="VAR_004697" FT VARIANT 734 FT /note="Q -> H (in PAIS)" FT /id="VAR_009792" FT VARIANT 738 FT /note="I -> T (in PAIS)" FT /evidence="ECO:0000269|PubMed:7671849" FT /id="VAR_009793" FT VARIANT 742 FT /note="W -> R (in AIS)" FT /evidence="ECO:0000269|PubMed:1464650" FT /id="VAR_009794" FT VARIANT 743 FT /note="M -> I (in PAIS)" FT /evidence="ECO:0000269|PubMed:8824883" FT /id="VAR_004698" FT VARIANT 743 FT /note="M -> V (in PAIS)" FT /evidence="ECO:0000269|PubMed:7970939" FT /id="VAR_009795" FT VARIANT 744 FT /note="G -> E (in AIS; dbSNP:rs137852600)" FT /evidence="ECO:0000269|PubMed:11587068" FT /id="VAR_013477" FT VARIANT 744 FT /note="G -> V (in PAIS and AIS; dbSNP:rs137852600)" FT /evidence="ECO:0000269|PubMed:8096390, FT ECO:0000269|PubMed:8325932, ECO:0000269|PubMed:9768671, FT ECO:0000269|Ref.115" FT /id="VAR_004699" FT VARIANT 745 FT /note="L -> F (in AIS and prostate cancer)" FT /id="VAR_009796" FT VARIANT 746 FT /note="M -> T (in PAIS)" FT /evidence="ECO:0000269|PubMed:7970939" FT /id="VAR_009797" FT VARIANT 747 FT /note="V -> M (in PAIS)" FT /id="VAR_009798" FT VARIANT 749 FT /note="A -> D (in PAIS)" FT /id="VAR_009799" FT VARIANT 749 FT /note="A -> T (in prostate cancer)" FT /id="VAR_009800" FT VARIANT 749 FT /note="A -> V (in prostate cancer)" FT /id="VAR_009801" FT VARIANT 750 FT /note="M -> I (in prostate cancer)" FT /id="VAR_009802" FT VARIANT 750 FT /note="M -> V (in PAIS and AIS; dbSNP:rs1085307685)" FT /evidence="ECO:0000269|PubMed:1480178, FT ECO:0000269|PubMed:1487249, ECO:0000269|PubMed:8990010" FT /id="VAR_004700" FT VARIANT 751 FT /note="G -> D (in AIS; loss of androgen binding)" FT /evidence="ECO:0000269|PubMed:9328206" FT /id="VAR_004701" FT VARIANT 751 FT /note="G -> S (in prostate cancer)" FT /id="VAR_009803" FT VARIANT 752 FT /note="W -> R (in AIS)" FT /id="VAR_009804" FT VARIANT 753 FT /note="R -> Q (in AIS; dbSNP:rs1057523747)" FT /evidence="ECO:0000269|PubMed:9544375, FT ECO:0000269|PubMed:9698822" FT /id="VAR_004702" FT VARIANT 755 FT /note="F -> L (in PAIS and prostate cancer)" FT /evidence="ECO:0000269|PubMed:7981687, FT ECO:0000269|PubMed:9039340" FT /id="VAR_009805" FT VARIANT 755 FT /note="F -> V (in AIS)" FT /evidence="ECO:0000269|PubMed:8103398, ECO:0000269|Ref.115" FT /id="VAR_004703" FT VARIANT 756 FT /note="T -> A (in prostate cancer)" FT /id="VAR_009806" FT VARIANT 757 FT /note="N -> S (in PAIS; dbSNP:rs141425171)" FT /id="VAR_009807" FT VARIANT 758 FT /note="V -> A (in prostate cancer)" FT /evidence="ECO:0000269|PubMed:10706109" FT /id="VAR_009808" FT VARIANT 759 FT /note="N -> T (in PAIS; 50% reduction in transactivation)" FT /evidence="ECO:0000269|PubMed:9607727" FT /id="VAR_009809" FT VARIANT 760 FT /note="S -> F (in AIS)" FT /evidence="ECO:0000269|PubMed:1480178" FT /id="VAR_009810" FT VARIANT 760 FT /note="S -> P (in prostate cancer)" FT /id="VAR_009811" FT VARIANT 763 FT /note="L -> F (in AIS; loss of androgen binding)" FT /evidence="ECO:0000269|PubMed:9328206" FT /id="VAR_004704" FT VARIANT 764 FT /note="Y -> C (in PAIS and prostate cancer; partial loss of FT androgen binding; dbSNP:rs137852567)" FT /evidence="ECO:0000269|PubMed:16595706, FT ECO:0000269|PubMed:2010552, ECO:0000269|PubMed:7581399" FT /id="VAR_004705" FT VARIANT 764 FT /note="Y -> H (in AIS)" FT /evidence="ECO:0000269|PubMed:7671849" FT /id="VAR_009812" FT VARIANT 765 FT /note="F -> L (in AIS)" FT /evidence="ECO:0000269|PubMed:7970939" FT /id="VAR_009813" FT VARIANT 766 FT /note="A -> T (in AIS; loss of androgen binding; FT dbSNP:rs1555996863)" FT /evidence="ECO:0000269|PubMed:1426313, FT ECO:0000269|PubMed:9252933, ECO:0000269|PubMed:9328206, FT ECO:0000269|PubMed:9856504" FT /id="VAR_004707" FT VARIANT 766 FT /note="A -> V (in AIS)" FT /id="VAR_009814" FT VARIANT 767 FT /note="P -> S (in AIS)" FT /id="VAR_009815" FT VARIANT 768 FT /note="D -> E (in AIS)" FT /evidence="ECO:0000269|Ref.115" FT /id="VAR_009816" FT VARIANT 769 FT /note="L -> P (in AIS)" FT /id="VAR_009817" FT VARIANT 772 FT /note="N -> H (in PAIS; dbSNP:rs886041352)" FT /evidence="ECO:0000269|PubMed:7981687" FT /id="VAR_009818" FT VARIANT 773 FT /note="E -> A (in PAIS)" FT /evidence="ECO:0000269|PubMed:10022458" FT /id="VAR_009819" FT VARIANT 773 FT /note="E -> G (in PAIS)" FT /evidence="ECO:0000269|PubMed:9196614" FT /id="VAR_009820" FT VARIANT 775 FT /note="R -> C (in AIS; frequent mutation; loss of androgen FT binding; dbSNP:rs137852562)" FT /evidence="ECO:0000269|PubMed:1609793, FT ECO:0000269|PubMed:1856263, ECO:0000269|PubMed:2082179, FT ECO:0000269|PubMed:8990010, ECO:0000269|PubMed:9544375" FT /id="VAR_004709" FT VARIANT 775 FT /note="R -> H (in AIS and PAIS; almost complete loss of FT androgen binding; dbSNP:rs137852572)" FT /evidence="ECO:0000269|PubMed:1480178, FT ECO:0000269|PubMed:1609793, ECO:0000269|PubMed:16595706, FT ECO:0000269|PubMed:7671849" FT /id="VAR_004708" FT VARIANT 780 FT /note="R -> W (in AIS)" FT /evidence="ECO:0000269|PubMed:7581399, FT ECO:0000269|PubMed:7981687, ECO:0000269|PubMed:9007482" FT /id="VAR_004710" FT VARIANT 781 FT /note="M -> I (in PAIS and AIS; dbSNP:rs137852589)" FT /evidence="ECO:0000269|PubMed:8768864, FT ECO:0000269|PubMed:8824883, ECO:0000269|PubMed:8990010" FT /id="VAR_004711" FT VARIANT 783 FT /note="S -> N (in prostate cancer; somatic mutation)" FT /id="VAR_009821" FT VARIANT 785 FT /note="C -> Y (in AIS; loss of androgen binding and of FT transactivation)" FT /evidence="ECO:0000269|PubMed:9856504" FT /id="VAR_004712" FT VARIANT 788 FT /note="M -> V (in AIS; dbSNP:rs137852570)" FT /evidence="ECO:0000269|PubMed:1569163" FT /id="VAR_004713" FT VARIANT 789 FT /note="R -> S (in AIS; dbSNP:rs1254203917)" FT /id="VAR_009822" FT VARIANT 791 FT /note="L -> F (in AIS)" FT /evidence="ECO:0000269|PubMed:7962294" FT /id="VAR_009823" FT VARIANT 792 FT /note="S -> P (in prostate cancer)" FT /id="VAR_009824" FT VARIANT 794 FT /note="E -> D (in dbSNP:rs1414341563)" FT /evidence="ECO:0000269|PubMed:8213813" FT /id="VAR_009825" FT VARIANT 795 FT /note="F -> S (in AIS)" FT /evidence="ECO:0000269|PubMed:8990010" FT /id="VAR_004714" FT VARIANT 799 FT /note="Q -> E (in PAIS, AIS and prostate cancer; reduced FT transcription activation; dbSNP:rs137852591)" FT /evidence="ECO:0000269|PubMed:16595706, FT ECO:0000269|PubMed:7511268, ECO:0000269|PubMed:7671849, FT ECO:0000269|PubMed:8628719, ECO:0000269|PubMed:8824883, FT ECO:0000269|PubMed:9851768" FT /id="VAR_004715" FT VARIANT 807 FT /note="C -> Y (in PAIS; dbSNP:rs1064793480)" FT /id="VAR_009826" FT VARIANT 808 FT /note="M -> R (in AIS; loss of transactivation)" FT /evidence="ECO:0000269|PubMed:8281140" FT /id="VAR_004716" FT VARIANT 808 FT /note="M -> T (in PAIS; dbSNP:rs137852592)" FT /evidence="ECO:0000269|PubMed:10543676" FT /id="VAR_009827" FT VARIANT 808 FT /note="M -> V (in AIS; 25% androgen binding)" FT /evidence="ECO:0000269|PubMed:7581399" FT /id="VAR_004717" FT VARIANT 813 FT /note="L -> F (in AIS; dbSNP:rs1555997625)" FT /evidence="ECO:0000269|PubMed:10458483" FT /id="VAR_009828" FT VARIANT 815 FT /note="S -> N (in AIS and PAIS)" FT /id="VAR_004718" FT VARIANT 821 FT /note="G -> A (in AIS)" FT /evidence="ECO:0000269|PubMed:9610419" FT /id="VAR_009829" FT VARIANT 822 FT /note="L -> V (in PAIS)" FT /id="VAR_009830" FT VARIANT 828 FT /note="F -> V (in PAIS)" FT /evidence="ECO:0000269|PubMed:11587068" FT /id="VAR_013478" FT VARIANT 831 FT /note="L -> P (in prostate cancer)" FT /id="VAR_009831" FT VARIANT 832 FT /note="R -> L (in AIS)" FT /evidence="ECO:0000269|PubMed:7633398" FT /id="VAR_004719" FT VARIANT 832 FT /note="R -> Q (in AIS; loss of androgen binding; FT dbSNP:rs1386577803)" FT /evidence="ECO:0000269|PubMed:10458483, FT ECO:0000269|PubMed:2082179, ECO:0000269|PubMed:7633398" FT /id="VAR_004720" FT VARIANT 835 FT /note="Y -> C (in AIS; loss of androgen binding; FT dbSNP:rs1057521122)" FT /evidence="ECO:0000269|PubMed:1464650" FT /id="VAR_009832" FT VARIANT 841 FT /note="R -> C (in AIS; dbSNP:rs137852577)" FT /evidence="ECO:0000269|PubMed:8040309, FT ECO:0000269|PubMed:8824883, ECO:0000269|PubMed:9768671" FT /id="VAR_004721" FT VARIANT 841 FT /note="R -> G (in PAIS)" FT /evidence="ECO:0000269|PubMed:9856504" FT /id="VAR_004722" FT VARIANT 841 FT /note="R -> H (in AIS; dbSNP:rs9332969)" FT /evidence="ECO:0000269|PubMed:7909256, FT ECO:0000269|PubMed:8040309, ECO:0000269|PubMed:8126121, FT ECO:0000269|PubMed:8205256, ECO:0000269|PubMed:8325950, FT ECO:0000269|PubMed:8830623, ECO:0000269|PubMed:9039340" FT /id="VAR_004723" FT VARIANT 841 FT /note="R -> S (in PAIS)" FT /evidence="ECO:0000269|PubMed:10502786" FT /id="VAR_009229" FT VARIANT 842 FT /note="I -> S (in PAIS)" FT /id="VAR_009833" FT VARIANT 843 FT /note="I -> T (in AIS; dbSNP:rs9332970)" FT /evidence="ECO:0000269|PubMed:8325950, FT ECO:0000269|PubMed:9039340" FT /id="VAR_004724" FT VARIANT 847 FT /note="R -> G (in prostate cancer)" FT /evidence="ECO:0000269|PubMed:10706109" FT /id="VAR_009834" FT VARIANT 855 FT /note="R -> K (in PAIS)" FT /id="VAR_009835" FT VARIANT 856 FT /note="R -> C (in AIS; dbSNP:rs886041132)" FT /evidence="ECO:0000269|PubMed:1480178, FT ECO:0000269|PubMed:7581399, ECO:0000269|PubMed:9001799, FT ECO:0000269|PubMed:9255042, ECO:0000269|Ref.115" FT /id="VAR_004725" FT VARIANT 856 FT /note="R -> H (in AIS; strongly reduced transcription FT activation; dbSNP:rs9332971)" FT /evidence="ECO:0000269|PubMed:16595706, FT ECO:0000269|PubMed:8097257, ECO:0000269|PubMed:8824883, FT ECO:0000269|PubMed:9039340, ECO:0000269|PubMed:9106550" FT /id="VAR_004726" FT VARIANT 857 FT /note="F -> L (in AIS; dbSNP:rs137852598)" FT /id="VAR_009836" FT VARIANT 864 FT /note="L -> R (in AIS)" FT /id="VAR_009837" FT VARIANT 865 FT /note="D -> G (in AIS)" FT /evidence="ECO:0000269|PubMed:1480178" FT /id="VAR_009838" FT VARIANT 865 FT /note="D -> N (in AIS; loss of androgen binding; FT dbSNP:rs1555997810)" FT /evidence="ECO:0000269|PubMed:9328206" FT /id="VAR_004727" FT VARIANT 866 FT /note="S -> P (in AIS; dbSNP:rs137852597)" FT /id="VAR_009839" FT VARIANT 867 FT /note="V -> E (in AIS)" FT /id="VAR_004728" FT VARIANT 867 FT /note="V -> L (in PAIS; dbSNP:rs137852564)" FT /evidence="ECO:0000269|PubMed:1424203, FT ECO:0000269|PubMed:8325950, ECO:0000269|PubMed:8446106" FT /id="VAR_004729" FT VARIANT 867 FT /note="V -> M (in AIS and prostate cancer; FT dbSNP:rs137852564)" FT /evidence="ECO:0000269|PubMed:2082179, FT ECO:0000269|PubMed:2594783, ECO:0000269|PubMed:8446106, FT ECO:0000269|PubMed:9039340" FT /id="VAR_004730" FT VARIANT 870 FT /note="I -> M (in PAIS; dbSNP:rs137852574)" FT /evidence="ECO:0000269|PubMed:8097257, FT ECO:0000269|PubMed:8824883" FT /id="VAR_004731" FT VARIANT 871 FT /note="A -> G (in PAIS)" FT /evidence="ECO:0000269|PubMed:9329414" FT /id="VAR_009840" FT VARIANT 871 FT /note="A -> V (in PAIS; dbSNP:rs143040492)" FT /evidence="ECO:0000269|PubMed:8033918" FT /id="VAR_009841" FT VARIANT 872 FT /note="R -> G (in AIS)" FT /evidence="ECO:0000269|PubMed:10022458" FT /id="VAR_009842" FT VARIANT 875 FT /note="H -> R (in AIS)" FT /evidence="ECO:0000269|PubMed:11587068" FT /id="VAR_013479" FT VARIANT 875 FT /note="H -> Y (in prostate cancer; increases affinity for FT testosterone and androgen sensitivity; increased FT transcription activation; dbSNP:rs137852581)" FT /evidence="ECO:0000269|PubMed:17591767" FT /id="VAR_009843" FT VARIANT 878 FT /note="T -> A (found in prostate cancer; found in bone FT metastases; alters receptor specificity so that FT transcription is activated by antiandrogens such as FT cyproterone acetate; dbSNP:rs137852578)" FT /evidence="ECO:0000269|PubMed:10363963, FT ECO:0000269|PubMed:10569618, ECO:0000269|PubMed:1562539, FT ECO:0000269|PubMed:16129672, ECO:0000269|PubMed:17311914, FT ECO:0000269|PubMed:2260966, ECO:0000269|PubMed:25091737, FT ECO:0000269|PubMed:8187068, ECO:0000269|PubMed:8274409, FT ECO:0000269|PubMed:8827083" FT /id="VAR_004732" FT VARIANT 878 FT /note="T -> S (in prostate cancer; dbSNP:rs137852580)" FT /id="VAR_009844" FT VARIANT 880 FT /note="D -> Y (in AIS)" FT /evidence="ECO:0000269|PubMed:11587068" FT /id="VAR_013480" FT VARIANT 881 FT /note="L -> Q (in prostate cancer)" FT /id="VAR_009845" FT VARIANT 882 FT /note="L -> V (in AIS)" FT /evidence="ECO:0000269|PubMed:7641413" FT /id="VAR_009846" FT VARIANT 887 FT /note="M -> V (in AIS; dbSNP:rs755226547)" FT /id="VAR_009847" FT VARIANT 890 FT /note="V -> M (in AIS and PAIS; dbSNP:rs886041133)" FT /evidence="ECO:0000269|PubMed:8126121, FT ECO:0000269|PubMed:9160185" FT /id="VAR_009848" FT VARIANT 891 FT /note="D -> N (in prostate cancer)" FT /evidence="ECO:0000269|PubMed:10363963" FT /id="VAR_009849" FT VARIANT 892 FT /note="F -> L (in prostate cancer)" FT /id="VAR_009850" FT VARIANT 893 FT /note="P -> L (in AIS)" FT /evidence="ECO:0000269|PubMed:10221770, FT ECO:0000269|PubMed:10404311, ECO:0000269|Ref.181" FT /id="VAR_004733" FT VARIANT 896 FT /note="M -> T (in AIS; low androgen binding and FT transactivation)" FT /evidence="ECO:0000269|PubMed:16129672, FT ECO:0000269|PubMed:9856504" FT /id="VAR_004734" FT VARIANT 897 FT /note="A -> T (in prostate cancer)" FT /id="VAR_009851" FT VARIANT 899 FT /note="I -> T (in AIS; dbSNP:rs1555998105)" FT /id="VAR_009852" FT VARIANT 903 FT /note="Q -> R (in prostate cancer; dbSNP:rs137852582)" FT /id="VAR_009853" FT VARIANT 904 FT /note="V -> M (in PAIS)" FT /id="VAR_009854" FT VARIANT 905 FT /note="P -> H (in AIS)" FT /id="VAR_009855" FT VARIANT 905 FT /note="P -> S (in AIS)" FT /id="VAR_009856" FT VARIANT 908 FT /note="L -> F (in AIS; almost complete loss of FT transcription activation)" FT /evidence="ECO:0000269|PubMed:16595706, FT ECO:0000269|PubMed:9328206" FT /id="VAR_004735" FT VARIANT 910 FT /note="G -> E (in prostate cancer)" FT /id="VAR_009857" FT VARIANT 910 FT /note="G -> R (in PAIS)" FT /evidence="ECO:0000269|PubMed:8550758" FT /id="VAR_009858" FT VARIANT 911 FT /note="K -> R (in prostate cancer)" FT /evidence="ECO:0000269|PubMed:9438000" FT /id="VAR_009859" FT VARIANT 912 FT /note="V -> L (in PAIS)" FT /evidence="ECO:0000269|PubMed:10470409" FT /id="VAR_009860" FT VARIANT 914 FT /note="P -> S (in PAIS)" FT /id="VAR_004736" FT VARIANT 917 FT /note="F -> L (in AIS)" FT /evidence="ECO:0000269|PubMed:9302173" FT /id="VAR_009861" FT VARIANT 918 FT /note="H -> R (in AIS)" FT /id="VAR_009862" FT VARIANT 920 FT /note="Q -> R (in prostate cancer)" FT /id="VAR_009863" FT MUTAGEN 83 FT /note="S->A: Reduced cell growth." FT /evidence="ECO:0000269|PubMed:20980437" FT MUTAGEN 225 FT /note="Y->F: Decrease of CSK-induced phosphorylation." FT /evidence="ECO:0000269|PubMed:17045208" FT MUTAGEN 269 FT /note="Y->F: Decrease of CSK-induced phosphorylation and FT phosphorylation by TNK2. Complete loss of TNK2-dependent FT phosphorylation; when associated with F-365." FT /evidence="ECO:0000269|PubMed:17045208, FT ECO:0000269|PubMed:17494760" FT MUTAGEN 309 FT /note="Y->F: Decrease of CSK-induced phosphorylation." FT /evidence="ECO:0000269|PubMed:17045208" FT MUTAGEN 348 FT /note="Y->F: Decrease of CSK-induced phosphorylation." FT /evidence="ECO:0000269|PubMed:17045208" FT MUTAGEN 359 FT /note="Y->F: Decrease of CSK-induced phosphorylation." FT /evidence="ECO:0000269|PubMed:17045208" FT MUTAGEN 364 FT /note="Y->F: Decrease of CSK-induced phosphorylation." FT /evidence="ECO:0000269|PubMed:17045208" FT MUTAGEN 365 FT /note="Y->F: Decrease of CSK-induced phosphorylation and FT phosphorylation by TNK2. Complete loss of TNK2-dependent FT phosphorylation; when associated with F-269." FT /evidence="ECO:0000269|PubMed:17045208, FT ECO:0000269|PubMed:17494760" FT MUTAGEN 395 FT /note="Y->F: Decrease of CSK-induced phosphorylation." FT /evidence="ECO:0000269|PubMed:17045208" FT MUTAGEN 535 FT /note="Y->F: Greatest decrease of CSK-induced FT phosphorylation and inhibition of transcriptional activity FT induced by EGF." FT /evidence="ECO:0000269|PubMed:17045208" FT MUTAGEN 552 FT /note="Y->F: Decrease in CSK-induced phosphorylation." FT /evidence="ECO:0000269|PubMed:17045208" FT MUTAGEN 702 FT /note="L->A: Alters receptor specificity, so that FT transcription is activated by the antiandrogen cyproterone FT acetate." FT /evidence="ECO:0000269|PubMed:17311914" FT MUTAGEN 721 FT /note="K->A: Loss of transcription activation in the FT presence of androgen and of interaction with NCOA2." FT /evidence="ECO:0000269|PubMed:15563469, FT ECO:0000269|PubMed:17591767" FT MUTAGEN 742 FT /note="W->L: Strongly decreased transcription activation in FT the presence of androgen." FT /evidence="ECO:0000269|PubMed:16129672" FT MUTAGEN 846 FT /note="K->R: Prevents ubiquitination by RNF6. Prevents AR FT transcriptional activation by RNF14 in absence of hormone." FT /evidence="ECO:0000269|PubMed:19345326" FT MUTAGEN 848 FT /note="K->R: Partially prevents ubiquitination by RNF6." FT /evidence="ECO:0000269|PubMed:19345326" FT MUTAGEN 898 FT /note="E->A,Q: Reduced transcription activation in the FT presence of androgen." FT /evidence="ECO:0000269|PubMed:15563469, FT ECO:0000269|PubMed:17591767" FT MUTAGEN 898 FT /note="E->K,R: Loss of transcription activation in the FT presence of androgen." FT /evidence="ECO:0000269|PubMed:15563469, FT ECO:0000269|PubMed:17591767" FT MUTAGEN 916 FT /note="Y->F: Decrease in CSK-induced phosphorylation." FT /evidence="ECO:0000269|PubMed:17045208" FT CONFLICT 168 FT /note="G -> A (in Ref. 5; AAA51780)" FT /evidence="ECO:0000305" FT CONFLICT 214 FT /note="A -> R (in Ref. 3 and 6; AAA51771/AAA51772)" FT /evidence="ECO:0000305" FT CONFLICT 476 FT /note="G -> E (in Ref. 2; AAA51775 and 13; AAA51770)" FT /evidence="ECO:0000305" FT CONFLICT 566 FT /note="E -> K (in Ref. 15; AAA51774)" FT /evidence="ECO:0000305" FT CONFLICT 635 FT /note="L -> P (in Ref. 19; AAB21256/AAB21257)" FT /evidence="ECO:0000305" FT CONFLICT 676 FT /note="N -> I (in Ref. 19; AAB21256/AAB21257)" FT /evidence="ECO:0000305" FT CONFLICT 811 FT /note="L -> M (in Ref. 5; AAA51780)" FT /evidence="ECO:0000305" FT HELIX 22..29 FT /evidence="ECO:0007829|PDB:3V49" FT STRAND 667..669 FT /evidence="ECO:0007829|PDB:1XJ7" FT HELIX 673..681 FT /evidence="ECO:0007829|PDB:8E1A" FT STRAND 692..694 FT /evidence="ECO:0007829|PDB:5VO4" FT HELIX 698..721 FT /evidence="ECO:0007829|PDB:8E1A" FT HELIX 726..728 FT /evidence="ECO:0007829|PDB:8E1A" FT HELIX 731..758 FT /evidence="ECO:0007829|PDB:8E1A" FT STRAND 761..766 FT /evidence="ECO:0007829|PDB:8E1A" FT STRAND 769..771 FT /evidence="ECO:0007829|PDB:8E1A" FT HELIX 773..778 FT /evidence="ECO:0007829|PDB:8E1A" FT HELIX 782..797 FT /evidence="ECO:0007829|PDB:8E1A" FT HELIX 802..813 FT /evidence="ECO:0007829|PDB:8E1A" FT STRAND 815..818 FT /evidence="ECO:0007829|PDB:8E1A" FT HELIX 825..844 FT /evidence="ECO:0007829|PDB:8E1A" FT HELIX 850..883 FT /evidence="ECO:0007829|PDB:8E1A" FT HELIX 885..888 FT /evidence="ECO:0007829|PDB:8E1A" FT HELIX 894..902 FT /evidence="ECO:0007829|PDB:8E1A" FT HELIX 904..908 FT /evidence="ECO:0007829|PDB:8E1A" FT STRAND 911..914 FT /evidence="ECO:0007829|PDB:8E1A" 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 //