ANDR_HUMAN
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 03-AUG-2022, entry version 291.
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 WILD-TYPE AND VARIANT
RP PROSTATE CANCER ALA-878 IN COMPLEX WITH DIHYDROTESTOSTERONE AND BUD31
RP PEPTIDES, INTERACTION WITH BUD31, FUNCTION, SUBCELLULAR LOCATION, AND
RP DOMAIN.
RX PubMed=25091737; DOI=10.1016/j.molonc.2014.06.009;
RA Hsu C.L., Liu J.S., Wu P.L., Guan H.H., Chen Y.L., Lin A.C., Ting H.J.,
RA Pang S.T., Yeh S.D., Ma W.L., Chen C.J., Wu W.G., Chang C.;
RT "Identification of a new androgen receptor (AR) co-regulator BUD31 and
RT related peptides to suppress wild-type and mutated AR-mediated prostate
RT cancer growth via peptide screening and X-ray structure analysis.";
RL Mol. Oncol. 8:1575-1587(2014).
RN [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 PROSTATE CANCER HIS-702 AND ALA-878.
RX PubMed=8274409; DOI=10.1016/0960-0760(93)90316-o;
RA Suzuki H., Sato N., Watabe Y., Masai M., Seino S., Shimazaki J.;
RT "Androgen receptor gene mutations in human prostate cancer.";
RL J. Steroid Biochem. Mol. Biol. 46:759-765(1993).
RN [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 PROSTATE CANCER IN POLY-GLN REGION; HIS-702 AND ARG-911.
RX PubMed=9438000; DOI=10.1093/jjco/27.6.389;
RA Watanabe M., Ushijima T., Shiraishi T., Yatani R., Shimazaki J., Kotake T.,
RA Sugimura T., Nagao M.;
RT "Genetic alterations of androgen receptor gene in Japanese human prostate
RT cancer.";
RL Jpn. J. Clin. Oncol. 27:389-393(1997).
RN [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=10.1016/s0022-5347(01)64279-4;
RA Radmayr C., Culig Z., Glatzl J., Neuschmid-Kaspar F., Bartsch G.,
RA Klocker H.;
RT "Androgen receptor point mutations as the underlying molecular defect in 2
RT patients with androgen insensitivity syndrome.";
RL J. Urol. 158:1553-1556(1997).
RN [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 VARIANTS PROSTATE CANCER IN POLY-GLN REGION AND ALA-684.
RX PubMed=10629558;
RX DOI=10.1002/(sici)1096-9896(199912)189:4<559::aid-path471>3.0.co;2-y;
RA Wallen M.J., Linja M., Kaartinen K., Schleutker J., Visakorpi T.;
RT "Androgen receptor gene mutations in hormone-refractory prostate cancer.";
RL J. Pathol. 189:559-563(1999).
RN [195]
RP VARIANTS PROSTATE CANCER HIS-702 AND ALA-878.
RX PubMed=10569618; DOI=10.1016/s0022-5347(05)68158-x;
RA Zhao X.Y., Boyle B., Krishnan A.V., Navone N.M., Peehl D.M., Feldman D.;
RT "Two mutations identified in the androgen receptor of the new human
RT prostate cancer cell line MDA PCa 2a.";
RL J. Urol. 162:2192-2199(1999).
RN [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="http://atlasgeneticsoncology.org/Genes/ARID685chXq12.html";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Androgen receptor entry;
CC URL="https://en.wikipedia.org/wiki/Androgen_receptor";
CC -!- WEB RESOURCE: Name=X-chromosome gene database, androgen receptor (AR);
CC Note=Leiden Open Variation Database (LOVD);
CC URL="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; CCDS43965.1; -. [P10275-2]
DR CCDS; CCDS87754.1; -. [P10275-3]
DR PIR; A39248; A39248.
DR RefSeq; NP_000035.2; NM_000044.4. [P10275-1]
DR RefSeq; NP_001011645.1; NM_001011645.3. [P10275-2]
DR RefSeq; NP_001334990.1; NM_001348061.1. [P10275-3]
DR RefSeq; NP_001334992.1; NM_001348063.1. [P10275-4]
DR RefSeq; NP_001334993.1; NM_001348064.1.
DR PDB; 1E3G; X-ray; 2.40 A; A=658-920.
DR PDB; 1GS4; X-ray; 1.95 A; A=671-918.
DR PDB; 1T5Z; X-ray; 2.30 A; A=670-920.
DR PDB; 1T63; X-ray; 2.07 A; A=670-919.
DR PDB; 1T65; X-ray; 1.66 A; A=670-920.
DR PDB; 1XJ7; X-ray; 2.70 A; A=664-920.
DR PDB; 1XOW; X-ray; 1.80 A; A=672-920, B=20-30.
DR PDB; 1XQ3; X-ray; 2.25 A; A=672-920.
DR PDB; 1Z95; X-ray; 1.80 A; A=673-918.
DR PDB; 2AM9; X-ray; 1.64 A; A=655-920.
DR PDB; 2AMA; X-ray; 1.90 A; A=655-920.
DR PDB; 2AMB; X-ray; 1.75 A; A=655-920.
DR PDB; 2AO6; X-ray; 1.89 A; A=672-920.
DR PDB; 2AX6; X-ray; 1.50 A; A=665-920.
DR PDB; 2AX7; X-ray; 1.90 A; A=665-920.
DR PDB; 2AX8; X-ray; 1.70 A; A=665-920.
DR PDB; 2AX9; X-ray; 1.65 A; A=665-920.
DR PDB; 2AXA; X-ray; 1.80 A; A=665-920.
DR PDB; 2HVC; X-ray; 2.10 A; A=670-919.
DR PDB; 2OZ7; X-ray; 1.80 A; A=672-920.
DR PDB; 2PIO; X-ray; 2.03 A; A=670-920.
DR PDB; 2PIP; X-ray; 1.80 A; L=670-920.
DR PDB; 2PIQ; X-ray; 2.40 A; A=670-920.
DR PDB; 2PIR; X-ray; 2.10 A; A=670-920.
DR PDB; 2PIT; X-ray; 1.76 A; A=670-920.
DR PDB; 2PIU; X-ray; 2.12 A; A=670-920.
DR PDB; 2PIV; X-ray; 1.95 A; A=670-920.
DR PDB; 2PIW; X-ray; 2.58 A; A=670-920.
DR PDB; 2PIX; X-ray; 2.40 A; A=670-920.
DR PDB; 2PKL; X-ray; 2.49 A; A=670-920.
DR PDB; 2PNU; X-ray; 1.65 A; A=655-920.
DR PDB; 2Q7I; X-ray; 1.87 A; A=664-920, B=20-30.
DR PDB; 2Q7J; X-ray; 1.90 A; A=664-920.
DR PDB; 2Q7K; X-ray; 1.80 A; A=664-920, B=20-30.
DR PDB; 2Q7L; X-ray; 1.92 A; A=664-920.
DR PDB; 2YHD; X-ray; 2.20 A; A=672-920.
DR PDB; 2YLO; X-ray; 2.50 A; A=665-920.
DR PDB; 2YLP; X-ray; 2.30 A; A=665-920.
DR PDB; 2YLQ; X-ray; 2.40 A; A=665-920.
DR PDB; 2Z4J; X-ray; 2.60 A; A=672-919.
DR PDB; 3B5R; X-ray; 1.80 A; A=672-920.
DR PDB; 3B65; X-ray; 1.80 A; A=672-920.
DR PDB; 3B66; X-ray; 1.65 A; A=672-920.
DR PDB; 3B67; X-ray; 1.90 A; A=672-920.
DR PDB; 3B68; X-ray; 1.90 A; A=672-920.
DR PDB; 3BTR; X-ray; 2.60 A; B=622-636.
DR PDB; 3L3X; X-ray; 1.55 A; A=671-919.
DR PDB; 3L3Z; X-ray; 2.00 A; A=671-919.
DR PDB; 3RLJ; X-ray; 1.90 A; A=672-918.
DR PDB; 3RLL; X-ray; 1.70 A; A=672-918.
DR PDB; 3V49; X-ray; 1.70 A; A=655-920, B=21-31.
DR PDB; 3V4A; X-ray; 1.95 A; A=672-920, B=21-31.
DR PDB; 3ZQT; X-ray; 2.29 A; A=665-920.
DR PDB; 4HLW; X-ray; 2.50 A; A=665-920.
DR PDB; 4K7A; X-ray; 2.44 A; A=671-919.
DR PDB; 4OEA; X-ray; 2.12 A; A=671-920.
DR PDB; 4OED; X-ray; 2.79 A; A=671-920.
DR PDB; 4OEY; X-ray; 1.83 A; A=671-920.
DR PDB; 4OEZ; X-ray; 1.80 A; A=671-920.
DR PDB; 4OFR; X-ray; 2.26 A; A=671-920.
DR PDB; 4OFU; X-ray; 2.12 A; A=671-920.
DR PDB; 4OGH; X-ray; 2.98 A; A=671-920.
DR PDB; 4OH5; X-ray; 2.00 A; A=671-920.
DR PDB; 4OH6; X-ray; 3.56 A; A=671-920.
DR PDB; 4OHA; X-ray; 1.42 A; A=671-920.
DR PDB; 4OIL; X-ray; 2.51 A; A=671-920.
DR PDB; 4OIU; X-ray; 3.01 A; A=671-920.
DR PDB; 4OJ9; X-ray; 3.31 A; A=671-920.
DR PDB; 4OJB; X-ray; 2.00 A; A=671-920.
DR PDB; 4OK1; X-ray; 2.09 A; A=671-920.
DR PDB; 4OKB; X-ray; 2.95 A; A=671-920.
DR PDB; 4OKT; X-ray; 2.50 A; A=671-920.
DR PDB; 4OKW; X-ray; 2.00 A; A=671-920.
DR PDB; 4OKX; X-ray; 2.10 A; A=671-920.
DR PDB; 4OLM; X-ray; 2.80 A; A=671-920.
DR PDB; 4QL8; X-ray; 2.10 A; A=663-920.
DR PDB; 5CJ6; X-ray; 2.07 A; A=642-920, B=21-30.
DR PDB; 5JJM; X-ray; 2.15 A; A/B/C/D=669-920.
DR PDB; 5T8E; X-ray; 2.71 A; A=672-920.
DR PDB; 5T8J; X-ray; 2.70 A; A=672-920.
DR PDB; 5V8Q; X-ray; 1.44 A; A=672-920.
DR PDB; 5VO4; X-ray; 2.35 A; A=671-920.
DR PDBsum; 1E3G; -.
DR PDBsum; 1GS4; -.
DR PDBsum; 1T5Z; -.
DR PDBsum; 1T63; -.
DR PDBsum; 1T65; -.
DR PDBsum; 1XJ7; -.
DR PDBsum; 1XOW; -.
DR PDBsum; 1XQ3; -.
DR PDBsum; 1Z95; -.
DR PDBsum; 2AM9; -.
DR PDBsum; 2AMA; -.
DR PDBsum; 2AMB; -.
DR PDBsum; 2AO6; -.
DR PDBsum; 2AX6; -.
DR PDBsum; 2AX7; -.
DR PDBsum; 2AX8; -.
DR PDBsum; 2AX9; -.
DR PDBsum; 2AXA; -.
DR PDBsum; 2HVC; -.
DR PDBsum; 2OZ7; -.
DR PDBsum; 2PIO; -.
DR PDBsum; 2PIP; -.
DR PDBsum; 2PIQ; -.
DR PDBsum; 2PIR; -.
DR PDBsum; 2PIT; -.
DR PDBsum; 2PIU; -.
DR PDBsum; 2PIV; -.
DR PDBsum; 2PIW; -.
DR PDBsum; 2PIX; -.
DR PDBsum; 2PKL; -.
DR PDBsum; 2PNU; -.
DR PDBsum; 2Q7I; -.
DR PDBsum; 2Q7J; -.
DR PDBsum; 2Q7K; -.
DR PDBsum; 2Q7L; -.
DR PDBsum; 2YHD; -.
DR PDBsum; 2YLO; -.
DR PDBsum; 2YLP; -.
DR PDBsum; 2YLQ; -.
DR PDBsum; 2Z4J; -.
DR PDBsum; 3B5R; -.
DR PDBsum; 3B65; -.
DR PDBsum; 3B66; -.
DR PDBsum; 3B67; -.
DR PDBsum; 3B68; -.
DR PDBsum; 3BTR; -.
DR PDBsum; 3L3X; -.
DR PDBsum; 3L3Z; -.
DR PDBsum; 3RLJ; -.
DR PDBsum; 3RLL; -.
DR PDBsum; 3V49; -.
DR PDBsum; 3V4A; -.
DR PDBsum; 3ZQT; -.
DR PDBsum; 4HLW; -.
DR PDBsum; 4K7A; -.
DR PDBsum; 4OEA; -.
DR PDBsum; 4OED; -.
DR PDBsum; 4OEY; -.
DR PDBsum; 4OEZ; -.
DR PDBsum; 4OFR; -.
DR PDBsum; 4OFU; -.
DR PDBsum; 4OGH; -.
DR PDBsum; 4OH5; -.
DR PDBsum; 4OH6; -.
DR PDBsum; 4OHA; -.
DR PDBsum; 4OIL; -.
DR PDBsum; 4OIU; -.
DR PDBsum; 4OJ9; -.
DR PDBsum; 4OJB; -.
DR PDBsum; 4OK1; -.
DR PDBsum; 4OKB; -.
DR PDBsum; 4OKT; -.
DR PDBsum; 4OKW; -.
DR PDBsum; 4OKX; -.
DR PDBsum; 4OLM; -.
DR PDBsum; 4QL8; -.
DR PDBsum; 5CJ6; -.
DR PDBsum; 5JJM; -.
DR PDBsum; 5T8E; -.
DR PDBsum; 5T8J; -.
DR PDBsum; 5V8Q; -.
DR PDBsum; 5VO4; -.
DR AlphaFoldDB; P10275; -.
DR PCDDB; P10275; -.
DR SMR; P10275; -.
DR BioGRID; 106862; 823.
DR CORUM; P10275; -.
DR DIP; DIP-125N; -.
DR ELM; P10275; -.
DR IntAct; P10275; 311.
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; 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; P10275; -.
DR PeptideAtlas; P10275; -.
DR PRIDE; P10275; -.
DR ProteomicsDB; 18721; -.
DR ProteomicsDB; 52590; -. [P10275-1]
DR ProteomicsDB; 52591; -. [P10275-2]
DR TopDownProteomics; P10275-1; -. [P10275-1]
DR Antibodypedia; 3489; 2550 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 KEGG; hsa: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 CTD; 367; -.
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; GHPESSC; -.
DR OrthoDB; 782607at2759; -.
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 723 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 178 other 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; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0005497; F:androgen binding; IDA:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; IDA:MGI.
DR GO; GO:0008013; F:beta-catenin binding; IDA:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:UniProtKB.
DR GO; GO:0070974; F:POU domain binding; IEA:Ensembl.
DR GO; GO: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:0060769; P:positive regulation of epithelial cell proliferation involved in prostate gland development; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0045726; P:positive regulation of integrin biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:BHF-UCL.
DR GO; GO:0042327; P:positive regulation of phosphorylation; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0060740; P:prostate gland epithelium morphogenesis; IEA:Ensembl.
DR GO; GO:0060736; P:prostate gland growth; IEA:Ensembl.
DR GO; GO: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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 DisProt; DP00492; -.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 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 Pfam; PF02166; Androgen_recep; 1.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00521; ANDROGENR.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Cytoplasm; Disease 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; unknown pathological significance;
FT dbSNP:rs1355285524)"
FT /evidence="ECO:0000269|PubMed:10571951"
FT /id="VAR_009228"
FT VARIANT 492
FT /note="G -> S (in AIS)"
FT /id="VAR_009719"
FT VARIANT 529
FT /note="D -> G (in prostate cancer)"
FT /id="VAR_009720"
FT VARIANT 548
FT /note="L -> F (in PAIS; dbSNP:rs139524801)"
FT /id="VAR_009721"
FT VARIANT 549
FT /note="P -> S (in AIS; dbSNP:rs137852588)"
FT /evidence="ECO:0000269|PubMed:8683794"
FT /id="VAR_009722"
FT VARIANT 560
FT /note="C -> Y (in AIS)"
FT /evidence="ECO:0000269|PubMed:1316540"
FT /id="VAR_009723"
FT VARIANT 569
FT /note="G -> V (in a patient with isolated hypospadias)"
FT /evidence="ECO:0000269|PubMed:7673412"
FT /id="VAR_009725"
FT VARIANT 569
FT /note="G -> W (in PAIS; dbSNP:rs1555982864)"
FT /evidence="ECO:0000269|PubMed:7910529"
FT /id="VAR_009726"
FT VARIANT 572
FT /note="Y -> C (in AIS)"
FT /evidence="ECO:0000269|PubMed:9544375"
FT /id="VAR_009727"
FT VARIANT 574
FT /note="A -> D (in AIS)"
FT /id="VAR_009728"
FT VARIANT 575
FT /note="L -> P (in prostate cancer)"
FT /id="VAR_009729"
FT VARIANT 576
FT /note="T -> A (in prostate cancer)"
FT /evidence="ECO:0000269|PubMed:10706109"
FT /id="VAR_009730"
FT VARIANT 577
FT /note="C -> F (in AIS)"
FT /evidence="ECO:0000269|PubMed:14756668"
FT /id="VAR_009731"
FT VARIANT 577
FT /note="C -> R (in AIS)"
FT /evidence="ECO:0000269|PubMed:1316540"
FT /id="VAR_009732"
FT VARIANT 580
FT /note="C -> F (in AIS; reduced transcription and DNA
FT binding; dbSNP:rs137852586)"
FT /evidence="ECO:0000269|PubMed:8809734"
FT /id="VAR_009733"
FT VARIANT 580
FT /note="C -> Y (in AIS; 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; associated with P-618 in a PAIS
FT patient; normal androgen binding; does not activate
FT transcription; impairs DNA binding; dbSNP:rs142280455)"
FT /evidence="ECO:0000269|PubMed:1316540"
FT /id="VAR_009744"
FT VARIANT 598
FT /note="S -> T (in a patient with severe hypospadias)"
FT /evidence="ECO:0000269|PubMed:10092153"
FT /id="VAR_009745"
FT VARIANT 602
FT /note="C -> F (in AIS)"
FT /evidence="ECO:0000269|PubMed:7981689"
FT /id="VAR_009746"
FT VARIANT 605
FT /note="D -> Y (in PAIS)"
FT /evidence="ECO:0000269|PubMed:7981687"
FT /id="VAR_009747"
FT VARIANT 608
FT /note="R -> Q (in PAIS and breast cancer;
FT dbSNP:rs137852573)"
FT /evidence="ECO:0000269|PubMed:10221692,
FT ECO:0000269|PubMed:1303262, ECO:0000269|PubMed:9039340,
FT ECO:0000269|PubMed:9543136"
FT /id="VAR_004684"
FT VARIANT 609
FT /note="R -> K (in PAIS and breast cancer; defective nuclear
FT localization; dbSNP:rs137852576)"
FT /evidence="ECO:0000269|PubMed:1424203,
FT ECO:0000269|PubMed:8281139, ECO:0000269|PubMed:9196614"
FT /id="VAR_004685"
FT VARIANT 611
FT /note="N -> T (in PAIS)"
FT /evidence="ECO:0000269|PubMed:9039340"
FT /id="VAR_009748"
FT VARIANT 612
FT /note="C -> Y (in AIS)"
FT /id="VAR_009749"
FT VARIANT 616
FT /note="R -> H (in AIS and PAIS; dbSNP:rs754201976)"
FT /evidence="ECO:0000269|PubMed:7970939,
FT ECO:0000269|PubMed:8162033, ECO:0000269|PubMed:8413310,
FT ECO:0000269|PubMed:9698822"
FT /id="VAR_009751"
FT VARIANT 616
FT /note="R -> P (in AIS)"
FT /id="VAR_009752"
FT VARIANT 616
FT /note="Missing (in AIS)"
FT /evidence="ECO:0000269|PubMed:8162033"
FT /id="VAR_009750"
FT VARIANT 617
FT /note="L -> P (in AIS; dbSNP:rs1555990488)"
FT /evidence="ECO:0000269|PubMed:8647313"
FT /id="VAR_009753"
FT VARIANT 617
FT /note="L -> R (in PAIS)"
FT /evidence="ECO:0000269|PubMed:8126121"
FT /id="VAR_009754"
FT VARIANT 618
FT /note="R -> P (in AIS and PAIS; associated with G-598 in a
FT PAIS patient; loss of DNA-binding activity)"
FT /evidence="ECO:0000269|PubMed:1316540,
FT ECO:0000269|PubMed:1999491"
FT /id="VAR_009755"
FT VARIANT 620
FT /note="C -> Y (in prostate cancer; loss of DNA binding;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:10598582,
FT ECO:0000269|PubMed:10706109"
FT /id="VAR_009756"
FT VARIANT 630
FT /note="R -> Q (in prostate cancer; dbSNP:rs868669253)"
FT /evidence="ECO:0000269|PubMed:9184448"
FT /id="VAR_009757"
FT VARIANT 631
FT /note="K -> T (in prostate cancer)"
FT /id="VAR_009758"
FT VARIANT 646
FT /note="A -> D (in dbSNP:rs1800053)"
FT /evidence="ECO:0000269|PubMed:9554755"
FT /id="VAR_004686"
FT VARIANT 648
FT /note="S -> N (in prostate cancer; dbSNP:rs137852584)"
FT /id="VAR_009760"
FT VARIANT 665
FT /note="I -> N (in AIS and PAIS)"
FT /id="VAR_004687"
FT VARIANT 671
FT /note="Q -> R (in prostate cancer)"
FT /id="VAR_009761"
FT VARIANT 672
FT /note="P -> H (in PAIS)"
FT /id="VAR_009762"
FT VARIANT 673
FT /note="I -> T (in prostate cancer)"
FT /id="VAR_009763"
FT VARIANT 678
FT /note="L -> P (in AIS; dbSNP:rs137852579)"
FT /evidence="ECO:0000269|PubMed:7537149"
FT /id="VAR_004688"
FT VARIANT 682
FT /note="E -> K (in AIS; dbSNP:rs1555995816)"
FT /evidence="ECO:0000269|PubMed:10221692,
FT ECO:0000269|PubMed:8325950"
FT /id="VAR_009764"
FT VARIANT 683
FT /note="P -> T (in PAIS)"
FT /evidence="ECO:0000269|PubMed:11587068"
FT /id="VAR_013474"
FT VARIANT 684
FT /note="G -> A (in prostate cancer)"
FT /evidence="ECO:0000269|PubMed:10629558,
FT ECO:0000269|PubMed:9000575"
FT /id="VAR_009765"
FT VARIANT 685
FT /note="V -> I (in AIS; dbSNP:rs1555995822)"
FT /id="VAR_009766"
FT VARIANT 687
FT /note="C -> R (in PAIS)"
FT /id="VAR_009767"
FT VARIANT 688
FT /note="A -> V (in PAIS)"
FT /id="VAR_009768"
FT VARIANT 689
FT /note="G -> E (in AIS)"
FT /id="VAR_009769"
FT VARIANT 691
FT /note="Missing (in PAIS)"
FT /evidence="ECO:0000269|Ref.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 (in AIS and prostate cancer;
FT dbSNP:rs864622007)"
FT /evidence="ECO:0000269|PubMed:10569618,
FT ECO:0000269|PubMed:8274409, ECO:0000269|PubMed:9438000"
FT /id="VAR_009773"
FT VARIANT 703
FT /note="S -> A (in AIS)"
FT /id="VAR_009774"
FT VARIANT 704
FT /note="S -> C (in AIS)"
FT /id="VAR_009775"
FT VARIANT 704
FT /note="S -> G (in PAIS and AIS)"
FT /evidence="ECO:0000269|PubMed:9302173"
FT /id="VAR_004693"
FT VARIANT 706
FT /note="N -> S (in AIS; 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 (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:4OHA"
FT STRAND 692..694
FT /evidence="ECO:0007829|PDB:5VO4"
FT HELIX 698..721
FT /evidence="ECO:0007829|PDB:4OHA"
FT HELIX 726..728
FT /evidence="ECO:0007829|PDB:4OHA"
FT HELIX 731..758
FT /evidence="ECO:0007829|PDB:4OHA"
FT STRAND 761..766
FT /evidence="ECO:0007829|PDB:4OHA"
FT STRAND 769..771
FT /evidence="ECO:0007829|PDB:4OHA"
FT HELIX 773..778
FT /evidence="ECO:0007829|PDB:4OHA"
FT HELIX 782..797
FT /evidence="ECO:0007829|PDB:4OHA"
FT HELIX 802..812
FT /evidence="ECO:0007829|PDB:4OHA"
FT STRAND 815..818
FT /evidence="ECO:0007829|PDB:4OHA"
FT HELIX 825..843
FT /evidence="ECO:0007829|PDB:4OHA"
FT TURN 844..846
FT /evidence="ECO:0007829|PDB:2PKL"
FT TURN 850..852
FT /evidence="ECO:0007829|PDB:2PIV"
FT HELIX 853..883
FT /evidence="ECO:0007829|PDB:4OHA"
FT HELIX 885..888
FT /evidence="ECO:0007829|PDB:4OHA"
FT HELIX 894..902
FT /evidence="ECO:0007829|PDB:4OHA"
FT HELIX 904..908
FT /evidence="ECO:0007829|PDB:4OHA"
FT STRAND 911..914
FT /evidence="ECO:0007829|PDB:4OHA"
SQ SEQUENCE 920 AA; 99188 MW; A73432C55D39AE06 CRC64;
MEVQLGLGRV YPRPPSKTYR GAFQNLFQSV REVIQNPGPR HPEAASAAPP GASLLLLQQQ
QQQQQQQQQQ QQQQQQQQQQ ETSPRQQQQQ QGEDGSPQAH RRGPTGYLVL DEEQQPSQPQ
SALECHPERG CVPEPGAAVA ASKGLPQQLP APPDEDDSAA PSTLSLLGPT FPGLSSCSAD
LKDILSEAST MQLLQQQQQE AVSEGSSSGR AREASGAPTS SKDNYLGGTS TISDNAKELC
KAVSVSMGLG VEALEHLSPG EQLRGDCMYA PLLGVPPAVR PTPCAPLAEC KGSLLDDSAG
KSTEDTAEYS PFKGGYTKGL EGESLGCSGS AAAGSSGTLE LPSTLSLYKS GALDEAAAYQ
SRDYYNFPLA LAGPPPPPPP PHPHARIKLE NPLDYGSAWA AAAAQCRYGD LASLHGAGAA
GPGSGSPSAA ASSSWHTLFT AEEGQLYGPC GGGGGGGGGG GGGGGGGGGG GGGEAGAVAP
YGYTRPPQGL AGQESDFTAP DVWYPGGMVS RVPYPSPTCV KSEMGPWMDS YSGPYGDMRL
ETARDHVLPI DYYFPPQKTC LICGDEASGC HYGALTCGSC KVFFKRAAEG KQKYLCASRN
DCTIDKFRRK NCPSCRLRKC YEAGMTLGAR KLKKLGNLKL QEEGEASSTT SPTEETTQKL
TVSHIEGYEC QPIFLNVLEA IEPGVVCAGH DNNQPDSFAA LLSSLNELGE RQLVHVVKWA
KALPGFRNLH VDDQMAVIQY SWMGLMVFAM GWRSFTNVNS RMLYFAPDLV FNEYRMHKSR
MYSQCVRMRH LSQEFGWLQI TPQEFLCMKA LLLFSIIPVD GLKNQKFFDE LRMNYIKELD
RIIACKRKNP TSCSRRFYQL TKLLDSVQPI ARELHQFTFD LLIKSHMVSV DFPEMMAEII
SVQVPKILSG KVKPIYFHTQ
