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Database: UniProt
Entry: P07900
LinkDB: P07900
Original site: P07900 
ID   HS90A_HUMAN             Reviewed;         732 AA.
AC   P07900; A8K500; B3KPJ9; Q2PP14; Q5CAQ6; Q5CAQ7; Q9BVQ5;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 5.
DT   13-NOV-2019, entry version 252.
DE   RecName: Full=Heat shock protein HSP 90-alpha;
DE   AltName: Full=Heat shock 86 kDa;
DE            Short=HSP 86;
DE            Short=HSP86;
DE   AltName: Full=Lipopolysaccharide-associated protein 2;
DE            Short=LAP-2;
DE            Short=LPS-associated protein 2;
DE   AltName: Full=Renal carcinoma antigen NY-REN-38;
GN   Name=HSP90AA1; Synonyms=HSP90A, HSPC1, HSPCA;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Peripheral blood lymphocyte;
RX   PubMed=2780322; DOI=10.1093/nar/17.17.7108;
RA   Soeda E., Yokoyama K., Yamazaki M., Akaogi K., Miwa T., Imai T.;
RT   "Nucleotide sequence of a full-length cDNA for 90 kDa heat-shock
RT   protein from human peripheral blood lymphocytes.";
RL   Nucleic Acids Res. 17:7108-7108(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=1368637; DOI=10.1271/bbb1961.54.3163;
RA   Yamazaki M., Tashiro H., Yokoyama K., Soeda E.;
RT   "Molecular cloning of cDNA encoding a human heat-shock protein whose
RT   expression is induced by adenovirus type 12 E1A in HeLa cells.";
RL   Agric. Biol. Chem. 54:3163-3170(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Placenta;
RX   PubMed=2527334; DOI=10.1128/mcb.9.6.2615;
RA   Hickey E., Brandon S.E., Smale G., Lloyd D., Weber L.A.;
RT   "Sequence and regulation of a gene encoding a human 89-kilodalton heat
RT   shock protein.";
RL   Mol. Cell. Biol. 9:2615-2626(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND NOMENCLATURE.
RX   PubMed=16269234; DOI=10.1016/j.ygeno.2005.08.012;
RA   Chen B., Piel W.H., Gui L., Bruford E., Monteiro A.;
RT   "The HSP90 family of genes in the human genome: insights into their
RT   divergence and evolution.";
RL   Genomics 86:627-637(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   NHLBI resequencing and genotyping service (RS&G);
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Placenta, and Teratocarcinoma;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA   Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA   Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA   Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA   Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA   Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA   Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA   Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA   Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA   Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA   Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA   Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA   Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA   Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA   Quetier F., Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-312.
RX   PubMed=2469626; DOI=10.1016/0378-1119(88)90182-5;
RA   Hoffmann T., Hovemann B.;
RT   "Heat-shock proteins, Hsp84 and Hsp86, of mice and men: two related
RT   genes encode formerly identified tumour-specific transplantation
RT   antigens.";
RL   Gene 74:491-501(1988).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-312.
RX   PubMed=2591742; DOI=10.1016/0378-1119(89)90408-3;
RA   Walter T., Drabent B., Krebs H., Tomalak M., Heiss S., Benecke B.J.J.;
RT   "Cloning and analysis of a human 86-kDa heat-shock-protein-encoding
RT   gene.";
RL   Gene 83:105-115(1989).
RN   [11]
RP   PROTEIN SEQUENCE OF 101-112; 210-224; 300-314; 328-338; 346-355;
RP   387-400; 465-478 AND 633-647, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA   Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [12]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 185-732.
RC   TISSUE=Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [13]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 539-732.
RC   TISSUE=Heart;
RA   Tanaka M., Tanaka T., Mitsui Y., Yamamoto M., Wood J.N.;
RT   "The analysis of the genes reactive to monoclonal antibody, CE5.";
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [14]
RP   PROTEIN SEQUENCE OF 2-21, AND PHOSPHORYLATION AT SER-231 AND SER-263.
RX   PubMed=2492519;
RA   Lees-Miller S.P., Anderson C.W.;
RT   "Two human 90-kDa heat shock proteins are phosphorylated in vivo at
RT   conserved serines that are phosphorylated in vitro by casein kinase
RT   II.";
RL   J. Biol. Chem. 264:2431-2437(1989).
RN   [15]
RP   PROTEIN SEQUENCE OF 154-163 AND 186-191, AND INTERACTION WITH KSR1.
RX   PubMed=10409742; DOI=10.1128/mcb.19.8.5523;
RA   Stewart S., Sundaram M., Zhang Y., Lee J., Han M., Guan K.L.;
RT   "Kinase suppressor of Ras forms a multiprotein signaling complex and
RT   modulates MEK localization.";
RL   Mol. Cell. Biol. 19:5523-5534(1999).
RN   [16]
RP   PROTEIN SEQUENCE OF 592-612, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS
RP   OF CYS-598, AND S-NITROSYLATION AT CYS-598.
RX   PubMed=15937123; DOI=10.1073/pnas.0407294102;
RA   Martinez-Ruiz A., Villanueva L., Gonzalez de Orduna C.,
RA   Lopez-Ferrer D., Higueras M.A., Tarin C., Rodriguez-Crespo I.,
RA   Vazquez J., Lamas S.;
RT   "S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and
RT   endothelial nitric oxide synthase regulatory activities.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:8525-8530(2005).
RN   [17]
RP   PHOSPHORYLATION AT THR-5 AND THR-7.
RX   PubMed=2507541;
RA   Lees-Miller S.P., Anderson C.W.;
RT   "The human double-stranded DNA-activated protein kinase phosphorylates
RT   the 90-kDa heat-shock protein, hsp90 alpha at two NH2-terminal
RT   threonine residues.";
RL   J. Biol. Chem. 264:17275-17280(1989).
RN   [18]
RP   HOMODIMERIZATION.
RX   PubMed=8289821; DOI=10.1128/mcb.14.2.1459;
RA   Minami Y., Kimura Y., Kawasaki H., Suzuki K., Yahara I.;
RT   "The carboxy-terminal region of mammalian HSP90 is required for its
RT   dimerization and function in vivo.";
RL   Mol. Cell. Biol. 14:1459-1464(1994).
RN   [19]
RP   SUBUNIT.
RX   PubMed=7588731; DOI=10.1111/j.1432-1033.1995.001_1.x;
RA   Nemoto T., Ohara-Nemoto Y., Ota M., Takagi T., Yokoyama K.;
RT   "Mechanism of dimer formation of the 90-kDa heat-shock protein.";
RL   Eur. J. Biochem. 233:1-8(1995).
RN   [20]
RP   IDENTIFICATION IN A COMPLEX WITH NR3C1 AND FKBP4; PPID; PPP5C OR
RP   STIP1.
RX   PubMed=9195923; DOI=10.1074/jbc.272.26.16224;
RA   Silverstein A.M., Galigniana M.D., Chen M.S., Owens-Grillo J.K.,
RA   Chinkers M., Pratt W.B.;
RT   "Protein phosphatase 5 is a major component of glucocorticoid
RT   receptor.hsp90 complexes with properties of an FK506-binding
RT   immunophilin.";
RL   J. Biol. Chem. 272:16224-16230(1997).
RN   [21]
RP   INTERACTION WITH TOM34.
RX   PubMed=9660753; DOI=10.1074/jbc.273.29.18007;
RA   Young J.C., Obermann W.M., Hartl F.U.;
RT   "Specific binding of tetratricopeptide repeat proteins to the C-
RT   terminal 12-kDa domain of hsp90.";
RL   J. Biol. Chem. 273:18007-18010(1998).
RN   [22]
RP   IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC   TISSUE=Renal cell carcinoma;
RX   PubMed=10508479;
RX   DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA   Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA   Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA   Old L.J.;
RT   "Antigens recognized by autologous antibody in patients with renal-
RT   cell carcinoma.";
RL   Int. J. Cancer 83:456-464(1999).
RN   [23]
RP   INTERACTION WITH TERT, AND FUNCTION AS A CO-CHAPERONE IN TELOMERASE
RP   HOLOENZYME ASSEMBLY.
RX   PubMed=11274138; DOI=10.1074/jbc.c100055200;
RA   Forsythe H.L., Jarvis J.L., Turner J.W., Elmore L.W., Holt S.E.;
RT   "Stable association of hsp90 and p23, but Not hsp70, with active human
RT   telomerase.";
RL   J. Biol. Chem. 276:15571-15574(2001).
RN   [24]
RP   INTERACTION WITH HSF1.
RX   PubMed=11583998; DOI=10.1074/jbc.m105931200;
RA   Guo Y., Guettouche T., Fenna M., Boellmann F., Pratt W.B., Toft D.O.,
RA   Smith D.F., Voellmy R.;
RT   "Evidence for a mechanism of repression of heat shock factor 1
RT   transcriptional activity by a multichaperone complex.";
RL   J. Biol. Chem. 276:45791-45799(2001).
RN   [25]
RP   FUNCTION, IDENTIFICATION AS LPS RECEPTOR, INTERACTION WITH CXCR4; GDF5
RP   AND HSPA8, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=11276205; DOI=10.1038/86342;
RA   Triantafilou K., Triantafilou M., Dedrick R.L.;
RT   "A CD14-independent LPS receptor cluster.";
RL   Nat. Immunol. 2:338-345(2001).
RN   [26]
RP   INTERACTION WITH DNAJC7.
RX   PubMed=12853476; DOI=10.1093/emboj/cdg362;
RA   Brychzy A., Rein T., Winklhofer K.F., Hartl F.U., Young J.C.,
RA   Obermann W.M.;
RT   "Cofactor Tpr2 combines two TPR domains and a J domain to regulate the
RT   Hsp70/Hsp90 chaperone system.";
RL   EMBO J. 22:3613-3623(2003).
RN   [27]
RP   INTERACTION WITH AHSA1.
RX   PubMed=12604615; DOI=10.1074/jbc.m212761200;
RA   Lotz G.P., Lin H., Harst A., Obermann W.M.J.;
RT   "Aha1 binds to the middle domain of Hsp90, contributes to client
RT   protein activation, and stimulates the ATPase activity of the
RT   molecular chaperone.";
RL   J. Biol. Chem. 278:17228-17235(2003).
RN   [28]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Lymphoblast;
RX   PubMed=14654843; DOI=10.1038/nature02166;
RA   Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A.,
RA   Mann M.;
RT   "Proteomic characterization of the human centrosome by protein
RT   correlation profiling.";
RL   Nature 426:570-574(2003).
RN   [29]
RP   INTERACTION WITH SMYD3.
RX   PubMed=15235609; DOI=10.1038/ncb1151;
RA   Hamamoto R., Furukawa Y., Morita M., Iimura Y., Silva F.P., Li M.,
RA   Yagyu R., Nakamura Y.;
RT   "SMYD3 encodes a histone methyltransferase involved in the
RT   proliferation of cancer cells.";
RL   Nat. Cell Biol. 6:731-740(2004).
RN   [30]
RP   INTERACTION WITH SGTA AND TTC1.
RX   PubMed=15708368; DOI=10.1016/j.abb.2004.12.020;
RA   Liou S.T., Wang C.;
RT   "Small glutamine-rich tetratricopeptide repeat-containing protein is
RT   composed of three structural units with distinct functions.";
RL   Arch. Biochem. Biophys. 435:253-263(2005).
RN   [31]
RP   INTERACTION WITH PPP5C, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=15383005; DOI=10.1042/bj20040690;
RA   Zeke T., Morrice N., Vazquez-Martin C., Cohen P.T.;
RT   "Human protein phosphatase 5 dissociates from heat-shock proteins and
RT   is proteolytically activated in response to arachidonic acid and the
RT   microtubule-depolymerizing drug nocodazole.";
RL   Biochem. J. 385:45-56(2005).
RN   [32]
RP   FUNCTION, AND INTERACTION WITH PPP5C.
RX   PubMed=15577939; DOI=10.1038/sj.emboj.7600496;
RA   Yang J., Roe S.M., Cliff M.J., Williams M.A., Ladbury J.E.,
RA   Cohen P.T., Barford D.;
RT   "Molecular basis for TPR domain-mediated regulation of protein
RT   phosphatase 5.";
RL   EMBO J. 24:1-10(2005).
RN   [33]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 AND SER-263, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [34]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Pituitary;
RX   PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
RA   Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
RT   "Phosphoproteomic analysis of the human pituitary.";
RL   Pituitary 9:109-120(2006).
RN   [35]
RP   INTERACTION WITH PPP5C.
RX   PubMed=16531226; DOI=10.1016/j.str.2005.12.009;
RA   Cliff M.J., Harris R., Barford D., Ladbury J.E., Williams M.A.;
RT   "Conformational diversity in the TPR domain-mediated interaction of
RT   protein phosphatase 5 with Hsp90.";
RL   Structure 14:415-426(2006).
RN   [36]
RP   INTERACTION WITH NLRP12.
RX   PubMed=17947705; DOI=10.4049/jimmunol.179.9.6291;
RA   Arthur J.C., Lich J.D., Aziz R.K., Kotb M., Ting J.P.;
RT   "Heat shock protein 90 associates with monarch-1 and regulates its
RT   ability to promote degradation of NF-kappaB-inducing kinase.";
RL   J. Immunol. 179:6291-6296(2007).
RN   [37]
RP   SUBUNIT, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=18400751; DOI=10.1074/jbc.m800540200;
RA   Richter K., Soroka J., Skalniak L., Leskovar A., Hessling M.,
RA   Reinstein J., Buchner J.;
RT   "Conserved conformational changes in the ATPase cycle of human
RT   Hsp90.";
RL   J. Biol. Chem. 283:17757-17765(2008).
RN   [38]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=T-cell;
RX   PubMed=19367720; DOI=10.1021/pr800500r;
RA   Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT   "Phosphorylation analysis of primary human T lymphocytes using
RT   sequential IMAC and titanium oxide enrichment.";
RL   J. Proteome Res. 7:5167-5176(2008).
RN   [39]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252 AND SER-263, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Platelet;
RX   PubMed=18088087; DOI=10.1021/pr0704130;
RA   Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA   Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT   "Phosphoproteome of resting human platelets.";
RL   J. Proteome Res. 7:526-534(2008).
RN   [40]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [41]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [42]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 AND SER-263, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18318008; DOI=10.1002/pmic.200700884;
RA   Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA   Zou H., Gu J.;
RT   "Large-scale phosphoproteome analysis of human liver tissue by
RT   enrichment and fractionation of phosphopeptides with strong anion
RT   exchange chromatography.";
RL   Proteomics 8:1346-1361(2008).
RN   [43]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [44]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [45]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-443; LYS-458; LYS-489 AND
RP   LYS-585, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [46]
RP   INTERACTION WITH CHORDC1.
RX   PubMed=19875381; DOI=10.1074/mcp.m900261-mcp200;
RA   Gano J.J., Simon J.A.;
RT   "A proteomic investigation of ligand-dependent HSP90 complexes reveals
RT   CHORDC1 as a novel ADP-dependent HSP90-interacting protein.";
RL   Mol. Cell. Proteomics 9:255-270(2010).
RN   [47]
RP   ISGYLATION.
RX   PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA   Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA   Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT   "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT   human cells.";
RL   Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN   [48]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   TISSUE=Melanoma;
RX   PubMed=17081065; DOI=10.1021/pr060363j;
RA   Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA   Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA   Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA   Hunt D.F.;
RT   "Proteomic and bioinformatic characterization of the biogenesis and
RT   function of melanosomes.";
RL   J. Proteome Res. 5:3135-3144(2006).
RN   [49]
RP   INTERACTION WITH FNIP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=17028174; DOI=10.1073/pnas.0603781103;
RA   Baba M., Hong S.-B., Sharma N., Warren M.B., Nickerson M.L.,
RA   Iwamatsu A., Esposito D., Gillette W.K., Hopkins R.F. III,
RA   Hartley J.L., Furihata M., Oishi S., Zhen W., Burke T.R. Jr.,
RA   Linehan W.M., Schmidt L.S., Zbar B.;
RT   "Folliculin encoded by the BHD gene interacts with a binding protein,
RT   FNIP1, and AMPK, and is involved in AMPK and mTOR signaling.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15552-15557(2006).
RN   [50]
RP   MUTAGENESIS OF GLY-97.
RX   PubMed=18256191; DOI=10.1242/dev.018150;
RA   Hawkins T.A., Haramis A.P., Etard C., Prodromou C., Vaughan C.K.,
RA   Ashworth R., Ray S., Behra M., Holder N., Talbot W.S., Pearl L.H.,
RA   Strahle U., Wilson S.W.;
RT   "The ATPase-dependent chaperoning activity of Hsp90a regulates thick
RT   filament formation and integration during skeletal muscle
RT   myofibrillogenesis.";
RL   Development 135:1147-1156(2008).
RN   [51]
RP   MUTAGENESIS OF CYS-598.
RX   PubMed=19696785; DOI=10.1038/embor.2009.153;
RA   Retzlaff M., Stahl M., Eberl H.C., Lagleder S., Beck J., Kessler H.,
RA   Buchner J.;
RT   "Hsp90 is regulated by a switch point in the C-terminal domain.";
RL   EMBO Rep. 10:1147-1153(2009).
RN   [52]
RP   INTERACTION WITH HSP90AB1.
RX   PubMed=20353823; DOI=10.1016/j.cellsig.2010.03.012;
RA   Cheng M.B., Zhang Y., Zhong X., Sutter B., Cao C.Y., Chen X.S.,
RA   Cheng X.K., Zhang Y., Xiao L., Shen Y.F.;
RT   "Stat1 mediates an auto-regulation of hsp90beta gene in heat shock
RT   response.";
RL   Cell. Signal. 22:1206-1213(2010).
RN   [53]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [54]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [55]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [56]
RP   INTERACTION WITH CDC37.
RX   PubMed=23569206; DOI=10.1074/jbc.m112.439257;
RA   Eckl J.M., Rutz D.A., Haslbeck V., Zierer B.K., Reinstein J.,
RA   Richter K.;
RT   "Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein
RT   90) motility by interaction with N-terminal and middle domain binding
RT   sites.";
RL   J. Biol. Chem. 288:16032-16042(2013).
RN   [57]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231; SER-252; SER-263;
RP   SER-476 AND SER-641, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [58]
RP   FUNCTION, AND INTERACTION WITH STUB1 AND SMAD3.
RX   PubMed=24613385; DOI=10.1016/j.bbrc.2014.02.124;
RA   Shang Y., Xu X., Duan X., Guo J., Wang Y., Ren F., He D., Chang Z.;
RT   "Hsp70 and Hsp90 oppositely regulate TGF-beta signaling through
RT   CHIP/Stub1.";
RL   Biochem. Biophys. Res. Commun. 446:387-392(2014).
RN   [59]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [60]
RP   INTERACTION WITH NWD1.
RX   PubMed=24681825; DOI=10.18632/oncotarget.1850;
RA   Correa R.G., Krajewska M., Ware C.F., Gerlic M., Reed J.C.;
RT   "The NLR-related protein NWD1 is associated with prostate cancer and
RT   modulates androgen receptor signaling.";
RL   Oncotarget 5:1666-1682(2014).
RN   [61]
RP   REVIEW.
RX   PubMed=25973397; DOI=10.3389/fonc.2015.00100;
RA   Khurana N., Bhattacharyya S.;
RT   "Hsp90, the concertmaster: tuning transcription.";
RL   Front. Oncol. 5:100-100(2015).
RN   [62]
RP   INTERACTION WITH SMYD3.
RX   PubMed=25738358; DOI=10.18632/oncotarget.2970;
RA   Brown M.A., Foreman K., Harriss J., Das C., Zhu L., Edwards M.,
RA   Shaaban S., Tucker H.;
RT   "C-terminal domain of SMYD3 serves as a unique HSP90-regulated motif
RT   in oncogenesis.";
RL   Oncotarget 6:4005-4019(2015).
RN   [63]
RP   INTERACTION WITH HSF1; HIF1A; ERBB2; MET; KEAP1 AND RHOBTB2, AND
RP   MUTAGENESIS OF GLU-47 AND ASP-93.
RX   PubMed=26517842; DOI=10.1371/journal.pone.0141786;
RA   Prince T.L., Kijima T., Tatokoro M., Lee S., Tsutsumi S., Yim K.,
RA   Rivas C., Alarcon S., Schwartz H., Khamit-Kush K., Scroggins B.T.,
RA   Beebe K., Trepel J.B., Neckers L.;
RT   "Client proteins and small molecule inhibitors display distinct
RT   binding preferences for constitutive and stress-induced HSP90 isoforms
RT   and their conformationally restricted mutants.";
RL   PLoS ONE 10:E0141786-E0141786(2015).
RN   [64]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA   Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [65]
RP   REVIEW.
RX   PubMed=27295069; DOI=10.1016/j.biochi.2016.05.018;
RA   Verma S., Goyal S., Jamal S., Singh A., Grover A.;
RT   "Hsp90: Friends, clients and natural foes.";
RL   Biochimie 127:227-240(2016).
RN   [66]
RP   REVIEW.
RX   PubMed=26991466; DOI=10.1002/bip.22835;
RA   Pearl L.H.;
RT   "Review: The HSP90 molecular chaperone-an enigmatic ATPase.";
RL   Biopolymers 105:594-607(2016).
RN   [67]
RP   FUNCTION, AND INTERACTION WITH FLCN; AHSA1; HSP70; CDC37; FNIP1;
RP   FNIP2; STUB1; STIP1; PTGES3 AND PPP5C.
RX   PubMed=27353360; DOI=10.1038/ncomms12037;
RA   Woodford M.R., Dunn D.M., Blanden A.R., Capriotti D., Loiselle D.,
RA   Prodromou C., Panaretou B., Hughes P.F., Smith A., Ackerman W.,
RA   Haystead T.A., Loh S.N., Bourboulia D., Schmidt L.S.,
RA   Marston Linehan W., Bratslavsky G., Mollapour M.;
RT   "The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and
RT   enhance drug binding.";
RL   Nat. Commun. 7:12037-12037(2016).
RN   [68]
RP   INTERACTION WITH HSF1.
RX   PubMed=26754925; DOI=10.1038/srep19174;
RA   Asano Y., Kawase T., Okabe A., Tsutsumi S., Ichikawa H., Tatebe S.,
RA   Kitabayashi I., Tashiro F., Namiki H., Kondo T., Semba K.,
RA   Aburatani H., Taya Y., Nakagama H., Ohki R.;
RT   "IER5 generates a novel hypo-phosphorylated active form of HSF1 and
RT   contributes to tumorigenesis.";
RL   Sci. Rep. 6:19174-19174(2016).
RN   [69]
RP   FUNCTION, ACTIVITY REGULATION, IDENTIFICATION IN A COMPLEX WITH TSC1
RP   AND TSC2, INTERACTION WITH TSC1 AND AHSA1, SUBUNIT, AND MUTAGENESIS OF
RP   GLU-47; ASP-93; TYR-313 AND 728-MET--ASP-732.
RX   PubMed=29127155; DOI=10.15252/embj.201796700;
RA   Woodford M.R., Sager R.A., Marris E., Dunn D.M., Blanden A.R.,
RA   Murphy R.L., Rensing N., Shapiro O., Panaretou B., Prodromou C.,
RA   Loh S.N., Gutmann D.H., Bourboulia D., Bratslavsky G., Wong M.,
RA   Mollapour M.;
RT   "Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates
RT   folding of kinase and non-kinase clients.";
RL   EMBO J. 36:3650-3665(2017).
RN   [70]
RP   INTERACTION WITH NLRP12.
RX   PubMed=30559449; DOI=10.1038/s41467-018-07750-5;
RA   Normand S., Waldschmitt N., Neerincx A., Martinez-Torres R.J.,
RA   Chauvin C., Couturier-Maillard A., Boulard O., Cobret L., Awad F.,
RA   Huot L., Ribeiro-Ribeiro A., Lautz K., Ruez R., Delacre M., Bondu C.,
RA   Guilliams M., Scott C., Segal A., Amselem S., Hot D., Karabina S.,
RA   Bohn E., Ryffel B., Poulin L.F., Kufer T.A., Chamaillard M.;
RT   "Proteasomal degradation of NOD2 by NLRP12 in monocytes promotes
RT   bacterial tolerance and colonization by enteropathogens.";
RL   Nat. Commun. 9:5338-5338(2018).
RN   [71]
RP   INTERACTION WITH HERPES SIMPLEX VIRUS 1 PROTEIN US11 (MICROBIAL
RP   INFECTION).
RX   PubMed=29743370; DOI=10.1128/jvi.00402-18;
RA   Liu X., Main D., Ma Y., He B.;
RT   "Herpes Simplex Virus 1 Inhibits TANK-Binding Kinase 1 through
RT   Formation of the Us11-Hsp90 Complex.";
RL   J. Virol. 92:0-0(2018).
RN   [72]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 11-223 IN COMPLEX WITH
RP   GELDANAMYCIN.
RX   PubMed=9108479; DOI=10.1016/s0092-8674(00)80203-2;
RA   Stebbins C.E., Russo A.A., Schneider C., Rosen N., Hartl F.U.,
RA   Pavletich N.P.;
RT   "Crystal structure of an Hsp90-geldanamycin complex: targeting of a
RT   protein chaperone by an antitumor agent.";
RL   Cell 89:239-250(1997).
RN   [73]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 11-223 IN COMPLEX WITH ADP,
RP   CATALYTIC ACTIVITY, AND INTERACTION WITH PTGES3.
RX   PubMed=9817749; DOI=10.1083/jcb.143.4.901;
RA   Obermann W.M., Sondermann H., Russo A.A., Pavletich N.P., Hartl F.U.;
RT   "In vivo function of Hsp90 is dependent on ATP binding and ATP
RT   hydrolysis.";
RL   J. Cell Biol. 143:901-910(1998).
RN   [74]
RP   X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 724-732 IN COMPLEX WITH
RP   STUB1, INTERACTION WITH STUB1 AND UBE2N, AND MOTIF TPR REPEAT-BINDING.
RX   PubMed=16307917; DOI=10.1016/j.molcel.2005.09.023;
RA   Zhang M., Windheim M., Roe S.M., Peggie M., Cohen P., Prodromou C.,
RA   Pearl L.H.;
RT   "Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3
RT   ubiquitin ligase and a CHIP-Ubc13-Uev1a complex.";
RL   Mol. Cell 20:525-538(2005).
CC   -!- FUNCTION: Molecular chaperone that promotes the maturation,
CC       structural maintenance and proper regulation of specific target
CC       proteins involved for instance in cell cycle control and signal
CC       transduction. Undergoes a functional cycle that is linked to its
CC       ATPase activity which is essential for its chaperone activity.
CC       This cycle probably induces conformational changes in the client
CC       proteins, thereby causing their activation. Interacts dynamically
CC       with various co-chaperones that modulate its substrate
CC       recognition, ATPase cycle and chaperone function (PubMed:11274138,
CC       PubMed:15577939, PubMed:15937123, PubMed:27353360,
CC       PubMed:29127155). Engages with a range of client protein classes
CC       via its interaction with various co-chaperone proteins or
CC       complexes, that act as adapters, simultaneously able to interact
CC       with the specific client and the central chaperone itself
CC       (PubMed:29127155). Recruitment of ATP and co-chaperone followed by
CC       client protein forms a functional chaperone. After the completion
CC       of the chaperoning process, properly folded client protein and co-
CC       chaperone leave HSP90 in an ADP-bound partially open conformation
CC       and finally, ADP is released from HSP90 which acquires an open
CC       conformation for the next cycle (PubMed:27295069,
CC       PubMed:26991466). Apart from its chaperone activity, it also plays
CC       a role in the regulation of the transcription machinery. HSP90 and
CC       its co-chaperones modulate transcription at least at three
CC       different levels (PubMed:25973397). In the first place, they alter
CC       the steady-state levels of certain transcription factors in
CC       response to various physiological cues(PubMed:25973397). Second,
CC       they modulate the activity of certain epigenetic modifiers, such
CC       as histone deacetylases or DNA methyl transferases, and thereby
CC       respond to the change in the environment (PubMed:25973397). Third,
CC       they participate in the eviction of histones from the promoter
CC       region of certain genes and thereby turn on gene expression
CC       (PubMed:25973397). Binds bacterial lipopolysaccharide (LPS) and
CC       mediates LPS-induced inflammatory response, including TNF
CC       secretion by monocytes (PubMed:11276205). Antagonizes STUB1-
CC       mediated inhibition of TGF-beta signaling via inhibition of STUB1-
CC       mediated SMAD3 ubiquitination and degradation (PubMed:24613385).
CC       {ECO:0000269|PubMed:11274138, ECO:0000269|PubMed:11276205,
CC       ECO:0000269|PubMed:15577939, ECO:0000269|PubMed:15937123,
CC       ECO:0000269|PubMed:24613385, ECO:0000269|PubMed:27353360,
CC       ECO:0000269|PubMed:29127155, ECO:0000303|PubMed:25973397,
CC       ECO:0000303|PubMed:26991466, ECO:0000303|PubMed:27295069}.
CC   -!- ACTIVITY REGULATION: In the resting state, through the
CC       dimerization of its C-terminal domain, HSP90 forms a homodimer
CC       which is defined as the open conformation (PubMed:18400751). Upon
CC       ATP-binding, the N-terminal domain undergoes significant
CC       conformational changes and comes in contact to form an active
CC       closed conformation (PubMed:18400751). After HSP90 finishes its
CC       chaperoning tasks of assisting the proper folding, stabilization
CC       and activation of client proteins under the active state, ATP
CC       molecule is hydrolyzed to ADP which then dissociates from HSP90
CC       and directs the protein back to the resting state
CC       (PubMed:18400751). Co-chaperone TSC1 promotes ATP binding and
CC       inhibits HSP90AA1 ATPase activity (PubMed:29127155). Binding to
CC       phosphorylated AHSA1 promotes HSP90AA1 ATPase activity
CC       (PubMed:29127155). Inhibited by Ganetespib (STA-9090) and SNX-2112
CC       (PubMed:29127155). {ECO:0000269|PubMed:18400751,
CC       ECO:0000269|PubMed:29127155}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=300 uM for ATP {ECO:0000269|PubMed:18400751};
CC   -!- SUBUNIT: Homodimer (PubMed:7588731, PubMed:8289821,
CC       PubMed:18400751, PubMed:29127155). Identified in NR3C1/GCR steroid
CC       receptor-chaperone complexes formed at least by NR3C1, HSP90AA1
CC       and a variety of proteins containing TPR repeats such as FKBP4,
CC       FKBP5, PPID, PPP5C or STIP1 (PubMed:15383005, PubMed:9195923).
CC       Forms a complex containing HSP90AA1, TSC1 and TSC2; TSC1 is
CC       required to recruit TCS2 to the complex (PubMed:29127155). The
CC       closed form interacts (via the middle domain and TPR repeat-
CC       binding motif) with co-chaperone TSC1 (via C-terminus)
CC       (PubMed:29127155). Interacts with TOM34 (PubMed:9660753).
CC       Interacts with TERT; the interaction, together with PTGES3, is
CC       required for correct assembly and stabilization of the TERT
CC       holoenzyme complex (PubMed:11274138, PubMed:9817749). Interacts
CC       with CHORDC1 and DNAJC7 (PubMed:12853476, PubMed:19875381).
CC       Interacts with STUB1 and UBE2N; may couple the chaperone and
CC       ubiquitination systems (PubMed:16307917, PubMed:27353360).
CC       Interacts (via TPR repeat-binding motif) with PPP5C (via TPR
CC       repeats); the interaction is direct and activates PPP5C
CC       phosphatase activity (PubMed:15383005, PubMed:15577939,
CC       PubMed:16531226, PubMed:27353360). Following LPS binding, may form
CC       a complex with CXCR4, GDF5 and HSPA8 (PubMed:11276205). Interacts
CC       with KSR1 (PubMed:10409742). Interacts with co-chaperone CDC37
CC       (via C-terminus); the interaction inhibits HSP90AA1 ATPase
CC       activity (PubMed:23569206, PubMed:27353360). May interact with
CC       NWD1 (PubMed:24681825). Interacts with FNIP1 and FNIP2; the
CC       interaction inhibits HSP90AA1 ATPase activity (PubMed:17028174,
CC       PubMed:27353360). Interacts with co-chaperone AHSA1
CC       (phosphorylated on 'Tyr-223'); the interaction activates HSP90AA1
CC       ATPase activity and results in the dissociation of TSC1 from
CC       HSP90AA1 (PubMed:12604615, PubMed:27353360, PubMed:29127155).
CC       Interacts with FLCN in the presence of FNIP1 (PubMed:27353360).
CC       Interacts with HSP70, STIP1 and PTGES3 (PubMed:27353360).
CC       Interacts with SMYD3; this interaction enhances SMYD3 histone-
CC       lysine N-methyltransferase (PubMed:15235609, PubMed:25738358).
CC       Interacts with SGTA (via TPR repeats) (PubMed:15708368). Interacts
CC       with TTC1 (via TPR repeats) (PubMed:15708368). Interacts with HSF1
CC       in an ATP-dependent manner (PubMed:11583998. PubMed:26517842).
CC       Interacts with MET; the interaction suppresses MET kinase activity
CC       (PubMed:26517842). Interacts with ERBB2 in an ATP-dependent
CC       manner; the interaction suppresses ERBB2 kinase activity
CC       (PubMed:26517842). Interacts with HIF1A, KEAP1 and RHOBTB2
CC       (PubMed:26517842). Interacts with HSF1; this interaction is
CC       decreased in a IER5-dependent manner, promoting HSF1 accumulation
CC       in the nucleus, homotrimerization and DNA-binding activities
CC       (PubMed:26754925). Interacts with STUB1 and SMAD3
CC       (PubMed:24613385). Interacts with HSP90AB1; interaction is
CC       constitutive (PubMed:20353823). Interacts with HECTD1 (via N-
CC       terminus) (By similarity). Interacts with NR3C1 (via domain NR
CC       LBD) and NR1D1 (via domain NR LBD) (By similarity). Interacts with
CC       NLPR12 (PubMed:30559449, PubMed:17947705). Interacts with PDCL3
CC       (By similarity). {ECO:0000250|UniProtKB:P07901,
CC       ECO:0000250|UniProtKB:P82995, ECO:0000269|PubMed:10409742,
CC       ECO:0000269|PubMed:11274138, ECO:0000269|PubMed:11276205,
CC       ECO:0000269|PubMed:11583998, ECO:0000269|PubMed:12604615,
CC       ECO:0000269|PubMed:12853476, ECO:0000269|PubMed:15235609,
CC       ECO:0000269|PubMed:15383005, ECO:0000269|PubMed:15577939,
CC       ECO:0000269|PubMed:15708368, ECO:0000269|PubMed:16307917,
CC       ECO:0000269|PubMed:16531226, ECO:0000269|PubMed:17028174,
CC       ECO:0000269|PubMed:17947705, ECO:0000269|PubMed:18400751,
CC       ECO:0000269|PubMed:19875381, ECO:0000269|PubMed:20353823,
CC       ECO:0000269|PubMed:23569206, ECO:0000269|PubMed:24613385,
CC       ECO:0000269|PubMed:24681825, ECO:0000269|PubMed:25738358,
CC       ECO:0000269|PubMed:26517842, ECO:0000269|PubMed:26754925,
CC       ECO:0000269|PubMed:27353360, ECO:0000269|PubMed:29127155,
CC       ECO:0000269|PubMed:30559449, ECO:0000269|PubMed:7588731,
CC       ECO:0000269|PubMed:8289821, ECO:0000269|PubMed:9195923,
CC       ECO:0000269|PubMed:9660753, ECO:0000269|PubMed:9817749}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with herpes simplex virus
CC       1 protein US11; this interaction inhibits TBK1-induced interferon
CC       production. {ECO:0000269|PubMed:29743370}.
CC   -!- INTERACTION:
CC       Self; NbExp=6; IntAct=EBI-296047, EBI-296047;
CC       O95433:AHSA1; NbExp=4; IntAct=EBI-296047, EBI-448610;
CC       Q8IWD4:CCDC117; NbExp=5; IntAct=EBI-296047, EBI-3387963;
CC       Q16543:CDC37; NbExp=14; IntAct=EBI-296047, EBI-295634;
CC       Q7L3B6:CDC37L1; NbExp=2; IntAct=EBI-296047, EBI-2841876;
CC       P50750:CDK9; NbExp=2; IntAct=EBI-296047, EBI-1383449;
CC       Q96G23:CERS2; NbExp=2; IntAct=EBI-296047, EBI-1057080;
CC       Q9UHD1:CHORDC1; NbExp=8; IntAct=EBI-296047, EBI-2550959;
CC       O15111:CHUK; NbExp=3; IntAct=EBI-296047, EBI-81249;
CC       P00533:EGFR; NbExp=5; IntAct=EBI-296047, EBI-297353;
CC       P04626:ERBB2; NbExp=5; IntAct=EBI-296047, EBI-641062;
CC       Q02790:FKBP4; NbExp=8; IntAct=EBI-296047, EBI-1047444;
CC       Q14318:FKBP8; NbExp=7; IntAct=EBI-296047, EBI-724839;
CC       Q6PK50:HSP90AB1; NbExp=2; IntAct=EBI-296047, EBI-9356629;
CC       Q9Y6K9:IKBKG; NbExp=3; IntAct=EBI-296047, EBI-81279;
CC       Q9UHH9:IP6K2; NbExp=2; IntAct=EBI-296047, EBI-747509;
CC       P05412:JUN; NbExp=4; IntAct=EBI-296047, EBI-852823;
CC       Q6VAB6:KSR2; NbExp=5; IntAct=EBI-296047, EBI-6424389;
CC       Q99558:MAP3K14; NbExp=2; IntAct=EBI-296047, EBI-358011;
CC       O43318-2:MAP3K7; NbExp=5; IntAct=EBI-296047, EBI-358700;
CC       P04150:NR3C1; NbExp=8; IntAct=EBI-296047, EBI-493507;
CC       Q8WVJ2:NUDCD2; NbExp=4; IntAct=EBI-296047, EBI-1052153;
CC       P43034:PAFAH1B1; NbExp=5; IntAct=EBI-296047, EBI-720620;
CC       P26882:PPID (xeno); NbExp=4; IntAct=EBI-296047, EBI-6477155;
CC       P53041:PPP5C; NbExp=11; IntAct=EBI-296047, EBI-716663;
CC       Q15185:PTGES3; NbExp=6; IntAct=EBI-296047, EBI-1049387;
CC       Q9H6T3:RPAP3; NbExp=6; IntAct=EBI-296047, EBI-356928;
CC       P61247:RPS3A; NbExp=3; IntAct=EBI-296047, EBI-352378;
CC       P35467:S100a1 (xeno); NbExp=4; IntAct=EBI-296047, EBI-6477109;
CC       Q15831:STK11; NbExp=2; IntAct=EBI-296047, EBI-306838;
CC       Q9UNE7:STUB1; NbExp=9; IntAct=EBI-296047, EBI-357085;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}.
CC       Cytoplasm {ECO:0000250|UniProtKB:P07901}. Melanosome
CC       {ECO:0000269|PubMed:17081065}. Cell membrane
CC       {ECO:0000269|PubMed:11276205}. Note=Identified by mass
CC       spectrometry in melanosome fractions from stage I to stage IV.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=HSP90AA1-1, HSP90-alpha 2;
CC         IsoId=P07900-1; Sequence=Displayed;
CC       Name=2; Synonyms=HSP90AA1-2;
CC         IsoId=P07900-2; Sequence=VSP_026604;
CC         Note=Variant in position: 71:M->L (in dbSNP:rs8005905).;
CC   -!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
CC       repeat-containing proteins like the co-chaperone STUB1.
CC       {ECO:0000269|PubMed:16307917}.
CC   -!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
CC   -!- PTM: S-nitrosylated; negatively regulates the ATPase activity and
CC       the activation of eNOS by HSP90AA1. {ECO:0000269|PubMed:15937123}.
CC   -!- PTM: Ubiquitinated via 'Lys-63'-linked polyubiquitination by
CC       HECTD1. Ubiquitination promotes translocation into the cytoplasm
CC       away from the membrane and secretory pathways.
CC       {ECO:0000250|UniProtKB:P07901}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000305}.
DR   EMBL; X15183; CAA33259.1; -; mRNA.
DR   EMBL; M27024; AAA63194.1; -; Genomic_DNA.
DR   EMBL; AJ890082; CAI64495.1; -; mRNA.
DR   EMBL; AJ890083; CAI64496.1; -; mRNA.
DR   EMBL; DQ314871; ABC40730.1; -; Genomic_DNA.
DR   EMBL; AK056446; BAG51711.1; -; mRNA.
DR   EMBL; AK291115; BAF83804.1; -; mRNA.
DR   EMBL; AK291607; BAF84296.1; -; mRNA.
DR   EMBL; AL133223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471061; EAW81765.1; -; Genomic_DNA.
DR   EMBL; X07270; CAA30255.1; -; mRNA.
DR   EMBL; M30626; AAA36023.1; -; Genomic_DNA.
DR   EMBL; BC000987; AAH00987.1; -; mRNA.
DR   EMBL; BC121062; AAI21063.1; -; mRNA.
DR   EMBL; D87666; BAA13430.1; -; mRNA.
DR   EMBL; D87666; BAA13431.1; -; mRNA.
DR   CCDS; CCDS32160.1; -. [P07900-2]
DR   CCDS; CCDS9967.1; -. [P07900-1]
DR   PIR; A32319; HHHU86.
DR   RefSeq; NP_001017963.2; NM_001017963.2. [P07900-2]
DR   RefSeq; NP_005339.3; NM_005348.3. [P07900-1]
DR   PDB; 1BYQ; X-ray; 1.50 A; A=9-236.
DR   PDB; 1OSF; X-ray; 1.75 A; A=9-223.
DR   PDB; 1UY6; X-ray; 1.90 A; A=2-236.
DR   PDB; 1UY7; X-ray; 1.90 A; A=2-236.
DR   PDB; 1UY8; X-ray; 1.98 A; A=2-236.
DR   PDB; 1UY9; X-ray; 2.00 A; A=2-236.
DR   PDB; 1UYC; X-ray; 2.00 A; A=2-236.
DR   PDB; 1UYD; X-ray; 2.20 A; A=2-236.
DR   PDB; 1UYE; X-ray; 2.00 A; A=2-236.
DR   PDB; 1UYF; X-ray; 2.00 A; A=2-236.
DR   PDB; 1UYG; X-ray; 2.00 A; A=2-236.
DR   PDB; 1UYH; X-ray; 2.20 A; A=2-236.
DR   PDB; 1UYI; X-ray; 2.20 A; A=2-236.
DR   PDB; 1UYK; X-ray; 2.20 A; A=2-236.
DR   PDB; 1UYL; X-ray; 1.40 A; A=2-236.
DR   PDB; 1YC1; X-ray; 1.70 A; A=9-236.
DR   PDB; 1YC3; X-ray; 2.12 A; A=9-236.
DR   PDB; 1YC4; X-ray; 1.81 A; A=9-236.
DR   PDB; 1YER; X-ray; 1.65 A; A=9-236.
DR   PDB; 1YES; X-ray; 2.20 A; A=9-236.
DR   PDB; 1YET; X-ray; 1.90 A; A=9-236.
DR   PDB; 2BSM; X-ray; 2.05 A; A=2-236.
DR   PDB; 2BT0; X-ray; 1.90 A; A/B=2-236.
DR   PDB; 2BUG; NMR; -; B=728-732.
DR   PDB; 2BYH; X-ray; 1.90 A; A=11-236.
DR   PDB; 2BYI; X-ray; 1.60 A; A=11-236.
DR   PDB; 2BZ5; X-ray; 1.90 A; A/B=2-236.
DR   PDB; 2C2L; X-ray; 3.30 A; E/F/G/H=724-732.
DR   PDB; 2CCS; X-ray; 1.79 A; A=1-236.
DR   PDB; 2CCT; X-ray; 2.30 A; A=1-236.
DR   PDB; 2CCU; X-ray; 2.70 A; A=1-236.
DR   PDB; 2FWY; X-ray; 2.10 A; A=1-236.
DR   PDB; 2FWZ; X-ray; 2.10 A; A=1-236.
DR   PDB; 2H55; X-ray; 2.00 A; A=1-236.
DR   PDB; 2JJC; X-ray; 1.95 A; A=9-223.
DR   PDB; 2K5B; NMR; -; A=14-223.
DR   PDB; 2QF6; X-ray; 3.10 A; A/B/C/D=17-223.
DR   PDB; 2QFO; X-ray; 1.68 A; A/B=17-223.
DR   PDB; 2QG0; X-ray; 1.85 A; A/B=17-223.
DR   PDB; 2QG2; X-ray; 1.80 A; A=17-223.
DR   PDB; 2UWD; X-ray; 1.90 A; A=2-236.
DR   PDB; 2VCI; X-ray; 2.00 A; A=1-236.
DR   PDB; 2VCJ; X-ray; 2.50 A; A=1-236.
DR   PDB; 2WI1; X-ray; 2.30 A; A=1-236.
DR   PDB; 2WI2; X-ray; 2.09 A; A/B=1-236.
DR   PDB; 2WI3; X-ray; 1.90 A; A=1-236.
DR   PDB; 2WI4; X-ray; 2.40 A; A=1-236.
DR   PDB; 2WI5; X-ray; 2.10 A; A=1-236.
DR   PDB; 2WI6; X-ray; 2.18 A; A=1-236.
DR   PDB; 2WI7; X-ray; 2.50 A; A=1-236.
DR   PDB; 2XAB; X-ray; 1.90 A; A/B=9-236.
DR   PDB; 2XDK; X-ray; 1.97 A; A=9-236.
DR   PDB; 2XDL; X-ray; 1.98 A; A=9-236.
DR   PDB; 2XDS; X-ray; 1.97 A; A=9-236.
DR   PDB; 2XDU; X-ray; 1.74 A; A=14-224.
DR   PDB; 2XDX; X-ray; 2.42 A; A=9-236.
DR   PDB; 2XHR; X-ray; 2.20 A; A=9-236.
DR   PDB; 2XHT; X-ray; 2.27 A; A=9-236.
DR   PDB; 2XHX; X-ray; 2.80 A; A=9-236.
DR   PDB; 2XJG; X-ray; 2.25 A; A=9-236.
DR   PDB; 2XJJ; X-ray; 1.90 A; A/B=9-236.
DR   PDB; 2XJX; X-ray; 1.66 A; A=9-236.
DR   PDB; 2XK2; X-ray; 1.95 A; A=9-236.
DR   PDB; 2YE2; X-ray; 1.90 A; A=9-236.
DR   PDB; 2YE3; X-ray; 1.95 A; A=9-236.
DR   PDB; 2YE4; X-ray; 2.30 A; A=9-236.
DR   PDB; 2YE5; X-ray; 1.73 A; A=9-236.
DR   PDB; 2YE6; X-ray; 2.56 A; A=9-236.
DR   PDB; 2YE7; X-ray; 2.20 A; A=9-236.
DR   PDB; 2YE8; X-ray; 2.30 A; A=9-236.
DR   PDB; 2YE9; X-ray; 2.20 A; A=9-236.
DR   PDB; 2YEA; X-ray; 1.73 A; A=9-236.
DR   PDB; 2YEB; X-ray; 2.40 A; A=9-236.
DR   PDB; 2YEC; X-ray; 2.10 A; A=9-236.
DR   PDB; 2YED; X-ray; 2.10 A; A=9-236.
DR   PDB; 2YEE; X-ray; 2.30 A; A=9-236.
DR   PDB; 2YEF; X-ray; 1.55 A; A=9-236.
DR   PDB; 2YEG; X-ray; 2.50 A; A/B=9-236.
DR   PDB; 2YEH; X-ray; 2.10 A; A=9-236.
DR   PDB; 2YEI; X-ray; 2.20 A; A=9-236.
DR   PDB; 2YEJ; X-ray; 2.20 A; A=9-236.
DR   PDB; 2YI0; X-ray; 1.60 A; A=1-229.
DR   PDB; 2YI5; X-ray; 2.50 A; A=1-229.
DR   PDB; 2YI6; X-ray; 1.80 A; A=1-229.
DR   PDB; 2YI7; X-ray; 1.40 A; A=1-229.
DR   PDB; 2YJW; X-ray; 1.61 A; A=18-223.
DR   PDB; 2YJX; X-ray; 1.83 A; A=18-223.
DR   PDB; 2YK2; X-ray; 1.74 A; A=18-223.
DR   PDB; 2YK9; X-ray; 1.32 A; A=18-223.
DR   PDB; 2YKB; X-ray; 1.93 A; A=18-223.
DR   PDB; 2YKC; X-ray; 1.67 A; A=18-223.
DR   PDB; 2YKE; X-ray; 1.43 A; A=18-223.
DR   PDB; 2YKI; X-ray; 1.67 A; A=18-223.
DR   PDB; 2YKJ; X-ray; 1.46 A; A=18-223.
DR   PDB; 3B24; X-ray; 1.70 A; A/B=9-236.
DR   PDB; 3B25; X-ray; 1.75 A; A=9-236.
DR   PDB; 3B26; X-ray; 2.10 A; A/B=9-236.
DR   PDB; 3B27; X-ray; 1.50 A; A=9-236.
DR   PDB; 3B28; X-ray; 1.35 A; A/B=9-236.
DR   PDB; 3BM9; X-ray; 1.60 A; A=14-236.
DR   PDB; 3BMY; X-ray; 1.60 A; A=14-236.
DR   PDB; 3D0B; X-ray; 1.74 A; A=1-232.
DR   PDB; 3EKO; X-ray; 1.55 A; A/B=9-225.
DR   PDB; 3EKR; X-ray; 2.00 A; A/B=9-225.
DR   PDB; 3FT5; X-ray; 1.90 A; A=9-236.
DR   PDB; 3FT8; X-ray; 2.00 A; A=9-236.
DR   PDB; 3HEK; X-ray; 1.95 A; A/B=9-225.
DR   PDB; 3HHU; X-ray; 1.59 A; A/B=1-224.
DR   PDB; 3HYY; X-ray; 1.90 A; A=9-236.
DR   PDB; 3HYZ; X-ray; 2.30 A; A/B=9-236.
DR   PDB; 3HZ1; X-ray; 2.30 A; A=9-236.
DR   PDB; 3HZ5; X-ray; 1.90 A; A=9-236.
DR   PDB; 3INW; X-ray; 1.95 A; A=10-236.
DR   PDB; 3INX; X-ray; 1.75 A; A=10-236.
DR   PDB; 3K97; X-ray; 1.95 A; A=9-236.
DR   PDB; 3K98; X-ray; 2.40 A; A/B=9-225.
DR   PDB; 3K99; X-ray; 2.10 A; A/B/C/D=9-225.
DR   PDB; 3MNR; X-ray; 1.90 A; P=1-232.
DR   PDB; 3O0I; X-ray; 1.47 A; A=1-236.
DR   PDB; 3OW6; X-ray; 1.80 A; A=17-223.
DR   PDB; 3OWB; X-ray; 2.05 A; A=17-223.
DR   PDB; 3OWD; X-ray; 1.63 A; A=17-223.
DR   PDB; 3Q6M; X-ray; 3.00 A; A/B/C=293-732.
DR   PDB; 3Q6N; X-ray; 3.05 A; A/B/C/D/E/F=293-732.
DR   PDB; 3QDD; X-ray; 1.79 A; A=1-236.
DR   PDB; 3QTF; X-ray; 1.57 A; A=14-236.
DR   PDB; 3R4M; X-ray; 1.70 A; A=9-236.
DR   PDB; 3R4N; X-ray; 2.00 A; A/B=9-225.
DR   PDB; 3R4O; X-ray; 2.65 A; A/B=9-225.
DR   PDB; 3R4P; X-ray; 1.70 A; A/B=9-225.
DR   PDB; 3R91; X-ray; 1.58 A; A=14-236.
DR   PDB; 3R92; X-ray; 1.58 A; A=14-236.
DR   PDB; 3RKZ; X-ray; 1.57 A; A=14-236.
DR   PDB; 3RLP; X-ray; 1.70 A; A/B=9-225.
DR   PDB; 3RLQ; X-ray; 1.90 A; A/B=9-225.
DR   PDB; 3RLR; X-ray; 1.70 A; A/B=9-225.
DR   PDB; 3T0H; X-ray; 1.20 A; A=9-236.
DR   PDB; 3T0Z; X-ray; 2.19 A; A=9-236.
DR   PDB; 3T10; X-ray; 1.24 A; A=9-236.
DR   PDB; 3T1K; X-ray; 1.50 A; A/B=9-236.
DR   PDB; 3T2S; X-ray; 1.50 A; A/B=9-236.
DR   PDB; 3TUH; X-ray; 1.80 A; A/B=16-224.
DR   PDB; 3VHA; X-ray; 1.39 A; A=9-236.
DR   PDB; 3VHC; X-ray; 1.41 A; A=9-236.
DR   PDB; 3VHD; X-ray; 1.52 A; A/B=9-236.
DR   PDB; 3WHA; X-ray; 1.30 A; A/B=9-236.
DR   PDB; 3WQ9; X-ray; 1.80 A; A=1-236.
DR   PDB; 4AIF; X-ray; 2.01 A; D/E=726-732.
DR   PDB; 4AWO; X-ray; 1.70 A; A/B=9-236.
DR   PDB; 4AWP; X-ray; 1.82 A; A/B=9-236.
DR   PDB; 4AWQ; X-ray; 1.60 A; A/B=9-236.
DR   PDB; 4B7P; X-ray; 1.70 A; A=9-236.
DR   PDB; 4BQG; X-ray; 1.90 A; A=9-236.
DR   PDB; 4BQJ; X-ray; 2.00 A; A=9-236.
DR   PDB; 4CGQ; X-ray; 2.00 A; Q=726-732.
DR   PDB; 4CGU; X-ray; 2.11 A; C=726-732.
DR   PDB; 4CGV; X-ray; 2.54 A; E/F=726-732.
DR   PDB; 4CGW; X-ray; 3.00 A; C/D=726-732.
DR   PDB; 4CWF; X-ray; 2.00 A; A=9-236.
DR   PDB; 4CWN; X-ray; 1.80 A; A=9-236.
DR   PDB; 4CWO; X-ray; 2.31 A; A=9-236.
DR   PDB; 4CWP; X-ray; 1.95 A; A=9-236.
DR   PDB; 4CWQ; X-ray; 2.00 A; A=9-236.
DR   PDB; 4CWR; X-ray; 2.00 A; A=9-236.
DR   PDB; 4CWS; X-ray; 2.30 A; A=9-236.
DR   PDB; 4CWT; X-ray; 1.90 A; A=9-236.
DR   PDB; 4EEH; X-ray; 1.60 A; A=9-236.
DR   PDB; 4EFT; X-ray; 2.12 A; A=9-236.
DR   PDB; 4EFU; X-ray; 2.00 A; A=9-236.
DR   PDB; 4EGH; X-ray; 1.60 A; A=9-236.
DR   PDB; 4EGI; X-ray; 1.79 A; A=9-236.
DR   PDB; 4EGK; X-ray; 1.69 A; A=9-236.
DR   PDB; 4FCP; X-ray; 2.00 A; A/B=1-236.
DR   PDB; 4FCQ; X-ray; 2.15 A; A=1-236.
DR   PDB; 4FCR; X-ray; 1.70 A; A=1-236.
DR   PDB; 4HY6; X-ray; 1.65 A; A=9-236.
DR   PDB; 4JQL; X-ray; 1.72 A; A=9-236.
DR   PDB; 4L8Z; X-ray; 1.70 A; A=9-236.
DR   PDB; 4L90; X-ray; 2.00 A; A=9-236.
DR   PDB; 4L91; X-ray; 1.75 A; A=9-236.
DR   PDB; 4L93; X-ray; 1.84 A; A/B=9-236.
DR   PDB; 4L94; X-ray; 1.65 A; A=9-236.
DR   PDB; 4LWE; X-ray; 1.50 A; A=17-224.
DR   PDB; 4LWF; X-ray; 1.75 A; A=17-224.
DR   PDB; 4LWG; X-ray; 1.60 A; A=17-224.
DR   PDB; 4LWH; X-ray; 1.70 A; A=16-224.
DR   PDB; 4LWI; X-ray; 1.70 A; A=17-224.
DR   PDB; 4NH7; X-ray; 2.00 A; A/B=9-236.
DR   PDB; 4NH8; X-ray; 1.65 A; A=9-236.
DR   PDB; 4O04; X-ray; 1.82 A; A=9-236.
DR   PDB; 4O05; X-ray; 1.79 A; A=9-236.
DR   PDB; 4O07; X-ray; 1.86 A; A=9-236.
DR   PDB; 4O09; X-ray; 1.96 A; A=9-236.
DR   PDB; 4O0B; X-ray; 1.93 A; A=9-236.
DR   PDB; 4R3M; X-ray; 1.80 A; A=16-224.
DR   PDB; 4U93; X-ray; 1.55 A; A=1-236.
DR   PDB; 4W7T; X-ray; 1.80 A; A=1-236.
DR   PDB; 4XIP; X-ray; 1.70 A; A=9-236.
DR   PDB; 4XIQ; X-ray; 1.84 A; A=9-236.
DR   PDB; 4XIR; X-ray; 1.70 A; A=9-236.
DR   PDB; 4XIT; X-ray; 1.86 A; A=9-236.
DR   PDB; 4YKQ; X-ray; 1.91 A; A=2-236.
DR   PDB; 4YKR; X-ray; 1.61 A; A=2-236.
DR   PDB; 4YKT; X-ray; 1.85 A; A=2-236.
DR   PDB; 4YKU; X-ray; 1.70 A; A=2-236.
DR   PDB; 4YKW; X-ray; 1.85 A; A/B=2-236.
DR   PDB; 4YKX; X-ray; 1.80 A; A=2-236.
DR   PDB; 4YKY; X-ray; 1.78 A; A=2-236.
DR   PDB; 4YKZ; X-ray; 1.85 A; A=2-236.
DR   PDB; 5CF0; X-ray; 1.80 A; A=9-236.
DR   PDB; 5FNC; X-ray; 2.20 A; A=1-236.
DR   PDB; 5FND; X-ray; 2.00 A; A=1-236.
DR   PDB; 5FNF; X-ray; 2.10 A; A=1-236.
DR   PDB; 5GGZ; X-ray; 2.02 A; A/B/C/D=16-225.
DR   PDB; 5J20; X-ray; 1.76 A; A=17-223.
DR   PDB; 5J27; X-ray; 1.70 A; A=16-224.
DR   PDB; 5J2V; X-ray; 1.59 A; A=17-223.
DR   PDB; 5J2X; X-ray; 1.22 A; A=17-224.
DR   PDB; 5J64; X-ray; 1.38 A; A=9-236.
DR   PDB; 5J6L; X-ray; 1.75 A; A=9-236.
DR   PDB; 5J6M; X-ray; 1.64 A; A=9-234.
DR   PDB; 5J6N; X-ray; 1.90 A; A=9-234.
DR   PDB; 5J80; X-ray; 1.17 A; A=9-233.
DR   PDB; 5J82; X-ray; 2.17 A; A=9-233.
DR   PDB; 5J86; X-ray; 1.87 A; A=9-233.
DR   PDB; 5J8M; X-ray; 1.90 A; A/B=9-233.
DR   PDB; 5J8U; X-ray; 1.75 A; A/B=9-233.
DR   PDB; 5J9X; X-ray; 1.80 A; A=9-233.
DR   PDB; 5LNY; X-ray; 1.88 A; A=9-236.
DR   PDB; 5LNZ; X-ray; 1.54 A; A=9-236.
DR   PDB; 5LO0; X-ray; 2.30 A; A=9-236.
DR   PDB; 5LO1; X-ray; 2.70 A; A=9-236.
DR   PDB; 5LO5; X-ray; 1.44 A; A=9-236.
DR   PDB; 5LO6; X-ray; 2.40 A; A=9-236.
DR   PDB; 5LQ9; X-ray; 1.90 A; A=17-223.
DR   PDB; 5LR1; X-ray; 1.44 A; A=18-223.
DR   PDB; 5LR7; X-ray; 1.86 A; A=18-223.
DR   PDB; 5LRL; X-ray; 1.33 A; A=18-223.
DR   PDB; 5LRZ; X-ray; 2.00 A; A=18-223.
DR   PDB; 5LS1; X-ray; 1.85 A; A=17-223.
DR   PDB; 5M4E; X-ray; 1.90 A; A=9-236.
DR   PDB; 5M4H; X-ray; 2.00 A; A=9-236.
DR   PDB; 5NYH; X-ray; 1.65 A; A=9-236.
DR   PDB; 5NYI; X-ray; 1.44 A; A=9-235.
DR   PDB; 5OCI; X-ray; 1.62 A; A=9-236.
DR   PDB; 5OD7; X-ray; 2.00 A; A=9-236.
DR   PDB; 5ODX; X-ray; 1.82 A; A=9-236.
DR   PDB; 5T21; X-ray; 2.10 A; A=18-223.
DR   PDB; 5VYY; X-ray; 1.79 A; A=1-236.
DR   PDB; 5XQD; X-ray; 1.60 A; A=9-236.
DR   PDB; 5XQE; X-ray; 1.70 A; A=9-236.
DR   PDB; 5XR5; X-ray; 1.60 A; A=9-236.
DR   PDB; 5XR9; X-ray; 1.50 A; A=9-236.
DR   PDB; 5XRB; X-ray; 1.65 A; A=9-236.
DR   PDB; 5XRD; X-ray; 1.30 A; A=9-236.
DR   PDB; 5XRE; X-ray; 1.50 A; A=9-236.
DR   PDB; 5ZR3; X-ray; 2.50 A; A/C/E/G=1-236.
DR   PDB; 6B99; X-ray; 1.60 A; A=1-236.
DR   PDB; 6B9A; X-ray; 1.65 A; A/B=1-236.
DR   PDB; 6CEO; X-ray; 1.90 A; A=1-236.
DR   PDB; 6CYG; X-ray; 1.50 A; A/B=1-236.
DR   PDB; 6CYH; X-ray; 1.49 A; A/B=1-236.
DR   PDB; 6EI5; X-ray; 2.20 A; A=15-223.
DR   PDB; 6EL5; X-ray; 1.67 A; A=1-236.
DR   PDB; 6ELN; X-ray; 1.60 A; A=17-223.
DR   PDB; 6ELO; X-ray; 1.80 A; A=1-236.
DR   PDB; 6ELP; X-ray; 1.85 A; A=1-236.
DR   PDB; 6EY8; X-ray; 2.16 A; A=1-236.
DR   PDB; 6EY9; X-ray; 2.00 A; A=1-236.
DR   PDB; 6EYA; X-ray; 2.10 A; A=1-236.
DR   PDB; 6EYB; X-ray; 1.90 A; A=1-236.
DR   PDB; 6F1N; X-ray; 2.09 A; A=1-236.
DR   PDB; 6FCJ; X-ray; 2.49 A; A=9-236.
DR   PDB; 6FDP; NMR; -; B=724-732.
DR   PDB; 6GP4; X-ray; 1.70 A; A=1-236.
DR   PDB; 6GP8; X-ray; 1.75 A; A=1-236.
DR   PDB; 6GPF; X-ray; 1.55 A; A=1-236.
DR   PDB; 6GPH; X-ray; 1.56 A; A=1-236.
DR   PDB; 6GPO; X-ray; 1.48 A; A=1-236.
DR   PDB; 6GPP; X-ray; 1.51 A; A=1-236.
DR   PDB; 6GPR; X-ray; 2.35 A; A=1-236.
DR   PDB; 6GPT; X-ray; 2.00 A; A=1-236.
DR   PDB; 6GPW; X-ray; 1.60 A; A=1-236.
DR   PDB; 6GPY; X-ray; 2.25 A; A=1-236.
DR   PDB; 6GQ6; X-ray; 2.25 A; A=1-236.
DR   PDB; 6GQR; X-ray; 2.05 A; A=1-236.
DR   PDB; 6GQS; X-ray; 1.43 A; A=1-236.
DR   PDB; 6GQU; X-ray; 1.72 A; A=1-236.
DR   PDB; 6GR1; X-ray; 2.05 A; A=1-236.
DR   PDB; 6GR3; X-ray; 1.88 A; A=1-236.
DR   PDB; 6GR4; X-ray; 1.50 A; A=1-236.
DR   PDB; 6GR5; X-ray; 1.34 A; A=1-236.
DR   PDB; 6HHR; X-ray; 2.00 A; A=17-224.
DR   PDB; 6N8X; X-ray; 1.49 A; A=1-236.
DR   PDB; 6OLX; X-ray; 1.44 A; A=1-236.
DR   PDBsum; 1BYQ; -.
DR   PDBsum; 1OSF; -.
DR   PDBsum; 1UY6; -.
DR   PDBsum; 1UY7; -.
DR   PDBsum; 1UY8; -.
DR   PDBsum; 1UY9; -.
DR   PDBsum; 1UYC; -.
DR   PDBsum; 1UYD; -.
DR   PDBsum; 1UYE; -.
DR   PDBsum; 1UYF; -.
DR   PDBsum; 1UYG; -.
DR   PDBsum; 1UYH; -.
DR   PDBsum; 1UYI; -.
DR   PDBsum; 1UYK; -.
DR   PDBsum; 1UYL; -.
DR   PDBsum; 1YC1; -.
DR   PDBsum; 1YC3; -.
DR   PDBsum; 1YC4; -.
DR   PDBsum; 1YER; -.
DR   PDBsum; 1YES; -.
DR   PDBsum; 1YET; -.
DR   PDBsum; 2BSM; -.
DR   PDBsum; 2BT0; -.
DR   PDBsum; 2BUG; -.
DR   PDBsum; 2BYH; -.
DR   PDBsum; 2BYI; -.
DR   PDBsum; 2BZ5; -.
DR   PDBsum; 2C2L; -.
DR   PDBsum; 2CCS; -.
DR   PDBsum; 2CCT; -.
DR   PDBsum; 2CCU; -.
DR   PDBsum; 2FWY; -.
DR   PDBsum; 2FWZ; -.
DR   PDBsum; 2H55; -.
DR   PDBsum; 2JJC; -.
DR   PDBsum; 2K5B; -.
DR   PDBsum; 2QF6; -.
DR   PDBsum; 2QFO; -.
DR   PDBsum; 2QG0; -.
DR   PDBsum; 2QG2; -.
DR   PDBsum; 2UWD; -.
DR   PDBsum; 2VCI; -.
DR   PDBsum; 2VCJ; -.
DR   PDBsum; 2WI1; -.
DR   PDBsum; 2WI2; -.
DR   PDBsum; 2WI3; -.
DR   PDBsum; 2WI4; -.
DR   PDBsum; 2WI5; -.
DR   PDBsum; 2WI6; -.
DR   PDBsum; 2WI7; -.
DR   PDBsum; 2XAB; -.
DR   PDBsum; 2XDK; -.
DR   PDBsum; 2XDL; -.
DR   PDBsum; 2XDS; -.
DR   PDBsum; 2XDU; -.
DR   PDBsum; 2XDX; -.
DR   PDBsum; 2XHR; -.
DR   PDBsum; 2XHT; -.
DR   PDBsum; 2XHX; -.
DR   PDBsum; 2XJG; -.
DR   PDBsum; 2XJJ; -.
DR   PDBsum; 2XJX; -.
DR   PDBsum; 2XK2; -.
DR   PDBsum; 2YE2; -.
DR   PDBsum; 2YE3; -.
DR   PDBsum; 2YE4; -.
DR   PDBsum; 2YE5; -.
DR   PDBsum; 2YE6; -.
DR   PDBsum; 2YE7; -.
DR   PDBsum; 2YE8; -.
DR   PDBsum; 2YE9; -.
DR   PDBsum; 2YEA; -.
DR   PDBsum; 2YEB; -.
DR   PDBsum; 2YEC; -.
DR   PDBsum; 2YED; -.
DR   PDBsum; 2YEE; -.
DR   PDBsum; 2YEF; -.
DR   PDBsum; 2YEG; -.
DR   PDBsum; 2YEH; -.
DR   PDBsum; 2YEI; -.
DR   PDBsum; 2YEJ; -.
DR   PDBsum; 2YI0; -.
DR   PDBsum; 2YI5; -.
DR   PDBsum; 2YI6; -.
DR   PDBsum; 2YI7; -.
DR   PDBsum; 2YJW; -.
DR   PDBsum; 2YJX; -.
DR   PDBsum; 2YK2; -.
DR   PDBsum; 2YK9; -.
DR   PDBsum; 2YKB; -.
DR   PDBsum; 2YKC; -.
DR   PDBsum; 2YKE; -.
DR   PDBsum; 2YKI; -.
DR   PDBsum; 2YKJ; -.
DR   PDBsum; 3B24; -.
DR   PDBsum; 3B25; -.
DR   PDBsum; 3B26; -.
DR   PDBsum; 3B27; -.
DR   PDBsum; 3B28; -.
DR   PDBsum; 3BM9; -.
DR   PDBsum; 3BMY; -.
DR   PDBsum; 3D0B; -.
DR   PDBsum; 3EKO; -.
DR   PDBsum; 3EKR; -.
DR   PDBsum; 3FT5; -.
DR   PDBsum; 3FT8; -.
DR   PDBsum; 3HEK; -.
DR   PDBsum; 3HHU; -.
DR   PDBsum; 3HYY; -.
DR   PDBsum; 3HYZ; -.
DR   PDBsum; 3HZ1; -.
DR   PDBsum; 3HZ5; -.
DR   PDBsum; 3INW; -.
DR   PDBsum; 3INX; -.
DR   PDBsum; 3K97; -.
DR   PDBsum; 3K98; -.
DR   PDBsum; 3K99; -.
DR   PDBsum; 3MNR; -.
DR   PDBsum; 3O0I; -.
DR   PDBsum; 3OW6; -.
DR   PDBsum; 3OWB; -.
DR   PDBsum; 3OWD; -.
DR   PDBsum; 3Q6M; -.
DR   PDBsum; 3Q6N; -.
DR   PDBsum; 3QDD; -.
DR   PDBsum; 3QTF; -.
DR   PDBsum; 3R4M; -.
DR   PDBsum; 3R4N; -.
DR   PDBsum; 3R4O; -.
DR   PDBsum; 3R4P; -.
DR   PDBsum; 3R91; -.
DR   PDBsum; 3R92; -.
DR   PDBsum; 3RKZ; -.
DR   PDBsum; 3RLP; -.
DR   PDBsum; 3RLQ; -.
DR   PDBsum; 3RLR; -.
DR   PDBsum; 3T0H; -.
DR   PDBsum; 3T0Z; -.
DR   PDBsum; 3T10; -.
DR   PDBsum; 3T1K; -.
DR   PDBsum; 3T2S; -.
DR   PDBsum; 3TUH; -.
DR   PDBsum; 3VHA; -.
DR   PDBsum; 3VHC; -.
DR   PDBsum; 3VHD; -.
DR   PDBsum; 3WHA; -.
DR   PDBsum; 3WQ9; -.
DR   PDBsum; 4AIF; -.
DR   PDBsum; 4AWO; -.
DR   PDBsum; 4AWP; -.
DR   PDBsum; 4AWQ; -.
DR   PDBsum; 4B7P; -.
DR   PDBsum; 4BQG; -.
DR   PDBsum; 4BQJ; -.
DR   PDBsum; 4CGQ; -.
DR   PDBsum; 4CGU; -.
DR   PDBsum; 4CGV; -.
DR   PDBsum; 4CGW; -.
DR   PDBsum; 4CWF; -.
DR   PDBsum; 4CWN; -.
DR   PDBsum; 4CWO; -.
DR   PDBsum; 4CWP; -.
DR   PDBsum; 4CWQ; -.
DR   PDBsum; 4CWR; -.
DR   PDBsum; 4CWS; -.
DR   PDBsum; 4CWT; -.
DR   PDBsum; 4EEH; -.
DR   PDBsum; 4EFT; -.
DR   PDBsum; 4EFU; -.
DR   PDBsum; 4EGH; -.
DR   PDBsum; 4EGI; -.
DR   PDBsum; 4EGK; -.
DR   PDBsum; 4FCP; -.
DR   PDBsum; 4FCQ; -.
DR   PDBsum; 4FCR; -.
DR   PDBsum; 4HY6; -.
DR   PDBsum; 4JQL; -.
DR   PDBsum; 4L8Z; -.
DR   PDBsum; 4L90; -.
DR   PDBsum; 4L91; -.
DR   PDBsum; 4L93; -.
DR   PDBsum; 4L94; -.
DR   PDBsum; 4LWE; -.
DR   PDBsum; 4LWF; -.
DR   PDBsum; 4LWG; -.
DR   PDBsum; 4LWH; -.
DR   PDBsum; 4LWI; -.
DR   PDBsum; 4NH7; -.
DR   PDBsum; 4NH8; -.
DR   PDBsum; 4O04; -.
DR   PDBsum; 4O05; -.
DR   PDBsum; 4O07; -.
DR   PDBsum; 4O09; -.
DR   PDBsum; 4O0B; -.
DR   PDBsum; 4R3M; -.
DR   PDBsum; 4U93; -.
DR   PDBsum; 4W7T; -.
DR   PDBsum; 4XIP; -.
DR   PDBsum; 4XIQ; -.
DR   PDBsum; 4XIR; -.
DR   PDBsum; 4XIT; -.
DR   PDBsum; 4YKQ; -.
DR   PDBsum; 4YKR; -.
DR   PDBsum; 4YKT; -.
DR   PDBsum; 4YKU; -.
DR   PDBsum; 4YKW; -.
DR   PDBsum; 4YKX; -.
DR   PDBsum; 4YKY; -.
DR   PDBsum; 4YKZ; -.
DR   PDBsum; 5CF0; -.
DR   PDBsum; 5FNC; -.
DR   PDBsum; 5FND; -.
DR   PDBsum; 5FNF; -.
DR   PDBsum; 5GGZ; -.
DR   PDBsum; 5J20; -.
DR   PDBsum; 5J27; -.
DR   PDBsum; 5J2V; -.
DR   PDBsum; 5J2X; -.
DR   PDBsum; 5J64; -.
DR   PDBsum; 5J6L; -.
DR   PDBsum; 5J6M; -.
DR   PDBsum; 5J6N; -.
DR   PDBsum; 5J80; -.
DR   PDBsum; 5J82; -.
DR   PDBsum; 5J86; -.
DR   PDBsum; 5J8M; -.
DR   PDBsum; 5J8U; -.
DR   PDBsum; 5J9X; -.
DR   PDBsum; 5LNY; -.
DR   PDBsum; 5LNZ; -.
DR   PDBsum; 5LO0; -.
DR   PDBsum; 5LO1; -.
DR   PDBsum; 5LO5; -.
DR   PDBsum; 5LO6; -.
DR   PDBsum; 5LQ9; -.
DR   PDBsum; 5LR1; -.
DR   PDBsum; 5LR7; -.
DR   PDBsum; 5LRL; -.
DR   PDBsum; 5LRZ; -.
DR   PDBsum; 5LS1; -.
DR   PDBsum; 5M4E; -.
DR   PDBsum; 5M4H; -.
DR   PDBsum; 5NYH; -.
DR   PDBsum; 5NYI; -.
DR   PDBsum; 5OCI; -.
DR   PDBsum; 5OD7; -.
DR   PDBsum; 5ODX; -.
DR   PDBsum; 5T21; -.
DR   PDBsum; 5VYY; -.
DR   PDBsum; 5XQD; -.
DR   PDBsum; 5XQE; -.
DR   PDBsum; 5XR5; -.
DR   PDBsum; 5XR9; -.
DR   PDBsum; 5XRB; -.
DR   PDBsum; 5XRD; -.
DR   PDBsum; 5XRE; -.
DR   PDBsum; 5ZR3; -.
DR   PDBsum; 6B99; -.
DR   PDBsum; 6B9A; -.
DR   PDBsum; 6CEO; -.
DR   PDBsum; 6CYG; -.
DR   PDBsum; 6CYH; -.
DR   PDBsum; 6EI5; -.
DR   PDBsum; 6EL5; -.
DR   PDBsum; 6ELN; -.
DR   PDBsum; 6ELO; -.
DR   PDBsum; 6ELP; -.
DR   PDBsum; 6EY8; -.
DR   PDBsum; 6EY9; -.
DR   PDBsum; 6EYA; -.
DR   PDBsum; 6EYB; -.
DR   PDBsum; 6F1N; -.
DR   PDBsum; 6FCJ; -.
DR   PDBsum; 6FDP; -.
DR   PDBsum; 6GP4; -.
DR   PDBsum; 6GP8; -.
DR   PDBsum; 6GPF; -.
DR   PDBsum; 6GPH; -.
DR   PDBsum; 6GPO; -.
DR   PDBsum; 6GPP; -.
DR   PDBsum; 6GPR; -.
DR   PDBsum; 6GPT; -.
DR   PDBsum; 6GPW; -.
DR   PDBsum; 6GPY; -.
DR   PDBsum; 6GQ6; -.
DR   PDBsum; 6GQR; -.
DR   PDBsum; 6GQS; -.
DR   PDBsum; 6GQU; -.
DR   PDBsum; 6GR1; -.
DR   PDBsum; 6GR3; -.
DR   PDBsum; 6GR4; -.
DR   PDBsum; 6GR5; -.
DR   PDBsum; 6HHR; -.
DR   PDBsum; 6N8X; -.
DR   PDBsum; 6OLX; -.
DR   SMR; P07900; -.
DR   BioGrid; 109552; 888.
DR   ComplexPortal; CPX-3288; HSP90A-CDC37 chaperone complex.
DR   CORUM; P07900; -.
DR   DIP; DIP-27595N; -.
DR   IntAct; P07900; 268.
DR   MINT; P07900; -.
DR   STRING; 9606.ENSP00000335153; -.
DR   BindingDB; P07900; -.
DR   ChEMBL; CHEMBL3880; -.
DR   DrugBank; DB07317; (3E)-3-[(phenylamino)methylidene]dihydrofuran-2(3H)-one.
DR   DrugBank; DB08197; (5E,7S)-2-amino-7-(4-fluoro-2-pyridin-3-ylphenyl)-4-methyl-7,8-dihydroquinazolin-5(6H)-one oxime.
DR   DrugBank; DB08443; 2-(1H-pyrrol-1-ylcarbonyl)benzene-1,3,5-triol.
DR   DrugBank; DB08557; 2-[(2-methoxyethyl)amino]-4-(4-oxo-1,2,3,4-tetrahydro-9H-carbazol-9-yl)benzamide.
DR   DrugBank; DB08789; 2-AMINO-4-(2,4-DICHLOROPHENYL)-N-ETHYLTHIENO[2,3-D]PYRIMIDINE-6-CARBOXAMIDE.
DR   DrugBank; DB06969; 2-amino-4-[2,4-dichloro-5-(2-pyrrolidin-1-ylethoxy)phenyl]-N-ethylthieno[2,3-d]pyrimidine-6-carboxamide.
DR   DrugBank; DB08788; 3,6-DIAMINO-5-CYANO-4-(4-ETHOXYPHENYL)THIENO[2,3-B]PYRIDINE-2-CARBOXAMIDE.
DR   DrugBank; DB07324; 3-({2-[(2-AMINO-6-METHYLPYRIMIDIN-4-YL)ETHYNYL]BENZYL}AMINO)-1,3-OXAZOL-2(3H)-ONE.
DR   DrugBank; DB02840; 4-(1,3-Benzodioxol-5-Yl)-5-(5-Ethyl-2,4-Dihydroxyphenyl)-2h-Pyrazole-3-Carboxylic Acid.
DR   DrugBank; DB03749; 4-(1h-Imidazol-4-Yl)-3-(5-Ethyl-2,4-Dihydroxy-Phenyl)-1h-Pyrazole.
DR   DrugBank; DB08787; 4-(2,4-dichlorophenyl)-5-phenyldiazenyl-pyrimidin-2-amine.
DR   DrugBank; DB08786; 4-(2-methoxyethoxy)-6-methylpyrimidin-2-amine.
DR   DrugBank; DB07594; 4-[4-(2,3-DIHYDRO-1,4-BENZODIOXIN-6-YL)-3-METHYL-1H-PYRAZOL-5-YL]-6-ETHYLBENZENE-1,3-DIOL.
DR   DrugBank; DB07502; 4-bromo-6-(6-hydroxy-1,2-benzisoxazol-3-yl)benzene-1,3-diol.
DR   DrugBank; DB07100; 4-CHLORO-6-(4-PIPERAZIN-1-YL-1H-PYRAZOL-5-YL)BENZENE-1,3-DIOL.
DR   DrugBank; DB06957; 4-CHLORO-6-(4-{4-[4-(METHYLSULFONYL)BENZYL]PIPERAZIN-1-YL}-1H-PYRAZOL-5-YL)BENZENE-1,3-DIOL.
DR   DrugBank; DB07601; 4-chloro-6-{5-[(2-morpholin-4-ylethyl)amino]-1,2-benzisoxazol-3-yl}benzene-1,3-diol.
DR   DrugBank; DB08194; 4-methyl-7,8-dihydro-5H-thiopyrano[4,3-d]pyrimidin-2-amine.
DR   DrugBank; DB08442; 4-{[(2R)-2-(2-methylphenyl)pyrrolidin-1-yl]carbonyl}benzene-1,3-diol.
DR   DrugBank; DB07495; 5-(5-CHLORO-2,4-DIHYDROXYPHENYL)-N-ETHYL-4-(4-METHOXYPHENYL)-1H-PYRAZOLE-3-CARBOXAMIDE.
DR   DrugBank; DB06964; 5-(5-CHLORO-2,4-DIHYDROXYPHENYL)-N-ETHYL-4-(4-METHOXYPHENYL)ISOXAZOLE-3-CARBOXAMIDE.
DR   DrugBank; DB06961; 5-(5-chloro-2,4-dihydroxyphenyl)-N-ethyl-4-[4-(morpholin-4-ylmethyl)phenyl]isoxazole-3-carboxamide.
DR   DrugBank; DB06958; 5-(5-CHLORO-2,4-DIHYDROXYPHENYL)-N-ETHYL-4-PIPERAZIN-1-YL-1H-PYRAZOLE-3-CARBOXAMIDE.
DR   DrugBank; DB07319; 6-(3-BROMO-2-NAPHTHYL)-1,3,5-TRIAZINE-2,4-DIAMINE.
DR   DrugBank; DB03137; 8-(2,5-Dimethoxy-Benzyl)-2-Fluoro-9-Pent-9h-Purin-6-Ylamine.
DR   DrugBank; DB03093; 8-(2,5-Dimethoxy-Benzyl)-2-Fluoro-9h-Purin-6-Ylamine.
DR   DrugBank; DB02550; 8-(2-Chloro-3,4,5-Trimethoxy-Benzyl)-2-Fluoro-9-Pent-4-Ylnyl-9h-Purin-6-Ylamine.
DR   DrugBank; DB04505; 8-(2-Chloro-3,4,5-Trimethoxy-Benzyl)-9-Pent-4-Ylnyl-9h-Purin-6-Ylamine.
DR   DrugBank; DB07877; 8-(6-BROMO-BENZO[1,3]DIOXOL-5-YLSULFANYL)-9-(3-ISOPROPYLAMINO-PROPYL)-ADENINE.
DR   DrugBank; DB04254; 8-Benzo[1,3]Dioxol-,5-Ylmethyl-9-Butyl-2-Fluoro-9h-Purin-6-Ylamine.
DR   DrugBank; DB08436; 8-BENZO[1,3]DIOXOL-,5-YLMETHYL-9-BUTYL-9H-.
DR   DrugBank; DB04054; 9-Butyl-8-(2,5-Dimethoxy-Benzyl)-2-Fluoro-9h-Purin-6-Ylamine.
DR   DrugBank; DB02359; 9-Butyl-8-(2,5-Dimethoxy-Benzyl)-9h-Purin-6-Ylamine.
DR   DrugBank; DB03504; 9-Butyl-8-(2-Chloro-3,4,5-Trimethoxy-Benzyl)-9h-Purin-6-Ylamine.
DR   DrugBank; DB02754; 9-Butyl-8-(3,4,5-Trimethoxybenzyl)-9h-Purin-6-Amine.
DR   DrugBank; DB03809; 9-Butyl-8-(3-Methoxybenzyl)-9h-Purin-6-Amine.
DR   DrugBank; DB03899; 9-Butyl-8-(4-Methoxybenzyl)-9h-Purin-6-Amine.
DR   DrugBank; DB12442; Alvespimycin.
DR   DrugBank; DB09130; Copper.
DR   DrugBank; DB02424; Geldanamycin.
DR   DrugBank; DB06956; N-(4-ACETYLPHENYL)-5-(5-CHLORO-2,4-DIHYDROXYPHENYL)-1H-PYRAZOLE-4-CARBOXAMIDE.
DR   DrugBank; DB07325; N-[(2-AMINO-6-METHYLPYRIMIDIN-4-YL)METHYL]-3-{[(E)-(2-OXODIHYDROFURAN-3(2H)-YLIDENE)METHYL]AMINO}BENZENESULFONAMIDE.
DR   DrugBank; DB04588; N-[4-(AMINOSULFONYL)BENZYL]-5-(5-CHLORO-2,4-DIHYDROXYPHENYL)-1H-PYRAZOLE-4-CARBOXAMIDE.
DR   DrugBank; DB00716; Nedocromil.
DR   DrugBank; DB09221; Polaprezinc.
DR   DrugBank; DB04216; Quercetin.
DR   DrugBank; DB00615; Rifabutin.
DR   DrugBank; DB06070; SNX-5422.
DR   DrugBank; DB05134; Tanespimycin.
DR   DrugCentral; P07900; -.
DR   GuidetoPHARMACOLOGY; 2905; -.
DR   MoonDB; P07900; Predicted.
DR   CarbonylDB; P07900; -.
DR   GlyConnect; 1301; -.
DR   iPTMnet; P07900; -.
DR   PhosphoSitePlus; P07900; -.
DR   SwissPalm; P07900; -.
DR   BioMuta; HSP90AA1; -.
DR   DMDM; 92090606; -.
DR   OGP; P07900; -.
DR   REPRODUCTION-2DPAGE; IPI00784295; -.
DR   EPD; P07900; -.
DR   jPOST; P07900; -.
DR   MassIVE; P07900; -.
DR   MaxQB; P07900; -.
DR   PaxDb; P07900; -.
DR   PeptideAtlas; P07900; -.
DR   PRIDE; P07900; -.
DR   ProteomicsDB; 52031; -. [P07900-1]
DR   ProteomicsDB; 52032; -. [P07900-2]
DR   TopDownProteomics; P07900-1; -. [P07900-1]
DR   Ensembl; ENST00000216281; ENSP00000216281; ENSG00000080824. [P07900-1]
DR   Ensembl; ENST00000334701; ENSP00000335153; ENSG00000080824. [P07900-2]
DR   GeneID; 3320; -.
DR   KEGG; hsa:3320; -.
DR   UCSC; uc001yku.5; human. [P07900-1]
DR   CTD; 3320; -.
DR   DisGeNET; 3320; -.
DR   GeneCards; HSP90AA1; -.
DR   HGNC; HGNC:5253; HSP90AA1.
DR   HPA; CAB002058; -.
DR   MIM; 140571; gene.
DR   neXtProt; NX_P07900; -.
DR   OpenTargets; ENSG00000080824; -.
DR   PharmGKB; PA29519; -.
DR   eggNOG; KOG0019; Eukaryota.
DR   eggNOG; KOG0020; Eukaryota.
DR   eggNOG; COG0326; LUCA.
DR   GeneTree; ENSGT00950000182747; -.
DR   InParanoid; P07900; -.
DR   KO; K04079; -.
DR   OMA; VKRHSEF; -.
DR   OrthoDB; 188544at2759; -.
DR   PhylomeDB; P07900; -.
DR   TreeFam; TF300686; -.
DR   Reactome; R-HSA-1227986; Signaling by ERBB2.
DR   Reactome; R-HSA-1236382; Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
DR   Reactome; R-HSA-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR   Reactome; R-HSA-192905; vRNP Assembly.
DR   Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; R-HSA-203615; eNOS activation.
DR   Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR   Reactome; R-HSA-3000484; Scavenging by Class F Receptors.
DR   Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
DR   Reactome; R-HSA-3371511; HSF1 activation.
DR   Reactome; R-HSA-3371568; Attenuation phase.
DR   Reactome; R-HSA-3371571; HSF1-dependent transactivation.
DR   Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR   Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR   Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR   Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR   Reactome; R-HSA-399954; Sema3A PAK dependent Axon repulsion.
DR   Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
DR   Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability.
DR   Reactome; R-HSA-5336415; Uptake and function of diphtheria toxin.
DR   Reactome; R-HSA-5601884; PIWI-interacting RNA (piRNA) biogenesis.
DR   Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR   Reactome; R-HSA-5637810; Constitutive Signaling by EGFRvIII.
DR   Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR   Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR   Reactome; R-HSA-8863795; Downregulation of ERBB2 signaling.
DR   Reactome; R-HSA-8939211; ESR-mediated signaling.
DR   Reactome; R-HSA-9009391; Extra-nuclear estrogen signaling.
DR   Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR   Reactome; R-HSA-9613829; Chaperone Mediated Autophagy.
DR   SIGNOR; P07900; -.
DR   ChiTaRS; HSP90AA1; human.
DR   EvolutionaryTrace; P07900; -.
DR   GenomeRNAi; 3320; -.
DR   Pharos; P07900; -.
DR   PMAP-CutDB; P07900; -.
DR   PRO; PR:P07900; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   Bgee; ENSG00000080824; Expressed in 252 organ(s), highest expression level in middle temporal gyrus.
DR   ExpressionAtlas; P07900; baseline and differential.
DR   Genevisible; P07900; HS.
DR   GO; GO:0044295; C:axonal growth cone; ISS:ARUK-UCL.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0044294; C:dendritic growth cone; ISS:ARUK-UCL.
DR   GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR   GO; GO:0043202; C:lysosomal lumen; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0043209; C:myelin sheath; IBA:GO_Central.
DR   GO; GO:0043025; C:neuronal cell body; ISS:ARUK-UCL.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:ARUK-UCL.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR   GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
DR   GO; GO:0042623; F:ATPase activity, coupled; TAS:Reactome.
DR   GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR   GO; GO:0070182; F:DNA polymerase binding; IPI:BHF-UCL.
DR   GO; GO:0051020; F:GTPase binding; IPI:UniProtKB.
DR   GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
DR   GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR   GO; GO:0023026; F:MHC class II protein complex binding; HDA:UniProtKB.
DR   GO; GO:0030235; F:nitric-oxide synthase regulator activity; IDA:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; TAS:UniProtKB.
DR   GO; GO:0044183; F:protein folding chaperone; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:1990782; F:protein tyrosine kinase binding; IPI:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0097110; F:scaffold protein binding; IPI:UniProtKB.
DR   GO; GO:0048156; F:tau protein binding; IPI:ARUK-UCL.
DR   GO; GO:0030911; F:TPR domain binding; IDA:UniProtKB.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ARUK-UCL.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0048675; P:axon extension; ISS:ARUK-UCL.
DR   GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR   GO; GO:0021955; P:central nervous system neuron axonogenesis; ISS:ARUK-UCL.
DR   GO; GO:0061684; P:chaperone-mediated autophagy; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0051131; P:chaperone-mediated protein complex assembly; IDA:BHF-UCL.
DR   GO; GO:0097711; P:ciliary basal body-plasma membrane docking; TAS:Reactome.
DR   GO; GO:0051186; P:cofactor metabolic process; TAS:Reactome.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0038128; P:ERBB2 signaling pathway; TAS:Reactome.
DR   GO; GO:0030010; P:establishment of cell polarity; ISS:ARUK-UCL.
DR   GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0006839; P:mitochondrial transport; TAS:UniProtKB.
DR   GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
DR   GO; GO:1903364; P:positive regulation of cellular protein catabolic process; IGI:ARUK-UCL.
DR   GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISS:ARUK-UCL.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:ARUK-UCL.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:ARUK-UCL.
DR   GO; GO:0032273; P:positive regulation of protein polymerization; IDA:ARUK-UCL.
DR   GO; GO:1902949; P:positive regulation of tau-protein kinase activity; IDA:ARUK-UCL.
DR   GO; GO:0051973; P:positive regulation of telomerase activity; IDA:BHF-UCL.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; IDA:BHF-UCL.
DR   GO; GO:0042026; P:protein refolding; TAS:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR   GO; GO:0043335; P:protein unfolding; NAS:ParkinsonsUK-UCL.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
DR   GO; GO:1903827; P:regulation of cellular protein localization; ISS:ARUK-UCL.
DR   GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
DR   GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0050999; P:regulation of nitric-oxide synthase activity; TAS:Reactome.
DR   GO; GO:0043254; P:regulation of protein complex assembly; NAS:ParkinsonsUK-UCL.
DR   GO; GO:0031396; P:regulation of protein ubiquitination; IDA:BHF-UCL.
DR   GO; GO:0046677; P:response to antibiotic; ISS:AgBase.
DR   GO; GO:0009409; P:response to cold; ISS:AgBase.
DR   GO; GO:0009408; P:response to heat; ISS:AgBase.
DR   GO; GO:0006986; P:response to unfolded protein; NAS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR   GO; GO:1905323; P:telomerase holoenzyme complex assembly; IDA:BHF-UCL.
DR   GO; GO:0007004; P:telomere maintenance via telomerase; IDA:BHF-UCL.
DR   GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
DR   Gene3D; 1.20.120.790; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   HAMAP; MF_00505; HSP90; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR019805; Heat_shock_protein_90_CS.
DR   InterPro; IPR037196; HSP90_C.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020575; Hsp90_N.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   PANTHER; PTHR11528; PTHR11528; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF110942; SSF110942; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS00298; HSP90; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW   Cell membrane; Chaperone; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Membrane; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; S-nitrosylation; Stress response;
KW   Ubl conjugation.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:2492519}.
FT   CHAIN         2    732       Heat shock protein HSP 90-alpha.
FT                                /FTId=PRO_0000062911.
FT   REGION        9    236       Interaction with NR3C1.
FT                                {ECO:0000250|UniProtKB:P07901}.
FT   REGION      271    616       Interaction with NR3C1.
FT                                {ECO:0000250|UniProtKB:P07901}.
FT   REGION      284    732       Interaction with FLCN and FNIP1.
FT                                {ECO:0000269|PubMed:27353360}.
FT   REGION      284    620       Interaction with FNIP2 and TSC1.
FT                                {ECO:0000269|PubMed:27353360,
FT                                ECO:0000269|PubMed:29127155}.
FT   REGION      628    731       Interaction with NR1D1.
FT                                {ECO:0000250|UniProtKB:P07901}.
FT   REGION      682    732       Required for homodimerization.
FT                                {ECO:0000269|PubMed:8289821}.
FT   REGION      728    732       Essential for interaction with SMYD3,
FT                                TSC1 and STIP1/HOP.
FT                                {ECO:0000269|PubMed:25738358,
FT                                ECO:0000269|PubMed:29127155}.
FT   REGION      729    732       Essential for interaction with SGTA and
FT                                TTC1. {ECO:0000269|PubMed:15708368}.
FT   MOTIF       723    732       TPR repeat-binding.
FT                                {ECO:0000269|PubMed:16307917}.
FT   BINDING      51     51       ATP.
FT   BINDING      93     93       ATP.
FT   BINDING     112    112       ATP. {ECO:0000250}.
FT   BINDING     138    138       ATP; via amide nitrogen.
FT   BINDING     400    400       ATP. {ECO:0000250}.
FT   MOD_RES       5      5       Phosphothreonine; by PRKDC.
FT                                {ECO:0000269|PubMed:2507541}.
FT   MOD_RES       7      7       Phosphothreonine; by PRKDC.
FT                                {ECO:0000269|PubMed:2507541}.
FT   MOD_RES      58     58       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P07901}.
FT   MOD_RES      84     84       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P07901}.
FT   MOD_RES     231    231       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:18318008,
FT                                ECO:0000244|PubMed:23186163,
FT                                ECO:0000244|PubMed:24275569,
FT                                ECO:0000269|PubMed:2492519}.
FT   MOD_RES     252    252       Phosphoserine.
FT                                {ECO:0000244|PubMed:18088087,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     263    263       Phosphoserine.
FT                                {ECO:0000244|PubMed:16807684,
FT                                ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:18088087,
FT                                ECO:0000244|PubMed:18318008,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:18691976,
FT                                ECO:0000244|PubMed:19367720,
FT                                ECO:0000244|PubMed:23186163,
FT                                ECO:0000269|PubMed:2492519}.
FT   MOD_RES     313    313       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P07901}.
FT   MOD_RES     443    443       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     453    453       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P82995}.
FT   MOD_RES     458    458       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     476    476       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     489    489       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     492    492       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P07901}.
FT   MOD_RES     585    585       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     598    598       S-nitrosocysteine.
FT                                {ECO:0000269|PubMed:15937123}.
FT   MOD_RES     641    641       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   VAR_SEQ       1      1       M -> MPPCSGGDGSTPPGPSLRDRDCPAQSAEYPRDRLDP
FT                                RPGSPSEASSPPFLRSRAPVNWYQEKAQVFLWHLMVSGSTT
FT                                LLCLWKQPFHVSAFPVTASLAFRQSQGAGQHLYKDLQPFIL
FT                                LRLLM (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:16269234}.
FT                                /FTId=VSP_026604.
FT   MUTAGEN      47     47       E->A: Strong ATP-binding. Strong
FT                                interaction with HSF1, HIF1A, ERBB2, MET,
FT                                KEAP1 and RHOBTB2. No effect on
FT                                interaction with TSC1.
FT                                {ECO:0000269|PubMed:26517842,
FT                                ECO:0000269|PubMed:29127155}.
FT   MUTAGEN      93     93       D->A: Impaired ATP-binding. Strong
FT                                interaction with HIF1A, MET, KEAP1 and
FT                                RHOBTB2. Loss of interaction with HSF1
FT                                and ERBB2. Los of interaction with TSC1.
FT                                {ECO:0000269|PubMed:26517842,
FT                                ECO:0000269|PubMed:29127155}.
FT   MUTAGEN      97     97       G->D: Abolishes ATPase activity.
FT                                {ECO:0000269|PubMed:18256191}.
FT   MUTAGEN     313    313       Y->E: Loss of interaction with TSC1 and
FT                                increases interacrion with AHSA1.
FT                                {ECO:0000269|PubMed:29127155}.
FT   MUTAGEN     313    313       Y->F: No deffect on the interaction with
FT                                TSC1. {ECO:0000269|PubMed:29127155}.
FT   MUTAGEN     598    598       C->A,N,D: Reduces ATPase activity and
FT                                client protein activation.
FT                                {ECO:0000269|PubMed:15937123,
FT                                ECO:0000269|PubMed:19696785}.
FT   MUTAGEN     598    598       C->S: Loss of S-nitrosylation.
FT                                {ECO:0000269|PubMed:15937123,
FT                                ECO:0000269|PubMed:19696785}.
FT   MUTAGEN     728    732       Missing: Loss of interaction with TSC1.
FT                                {ECO:0000269|PubMed:29127155}.
FT   CONFLICT     63     63       S -> T (in Ref. 1; CAA33259).
FT                                {ECO:0000305}.
FT   CONFLICT     74     74       K -> R (in Ref. 4; CAI64495 and 6;
FT                                BAG51711). {ECO:0000305}.
FT   CONFLICT     86     86       D -> G (in Ref. 4; CAI64495 and 6;
FT                                BAG51711). {ECO:0000305}.
FT   CONFLICT    162    162       W -> D (in Ref. 15; AA sequence).
FT                                {ECO:0000305}.
FT   HELIX         2      5       {ECO:0000244|PDB:6GQS}.
FT   STRAND       18     21       {ECO:0000244|PDB:5J80}.
FT   HELIX        24     35       {ECO:0000244|PDB:5J80}.
FT   TURN         39     42       {ECO:0000244|PDB:6GPF}.
FT   HELIX        43     65       {ECO:0000244|PDB:5J80}.
FT   HELIX        67     70       {ECO:0000244|PDB:5J80}.
FT   STRAND       78     83       {ECO:0000244|PDB:5J80}.
FT   TURN         84     87       {ECO:0000244|PDB:5J80}.
FT   STRAND       88     93       {ECO:0000244|PDB:5J80}.
FT   HELIX       100    104       {ECO:0000244|PDB:5J80}.
FT   TURN        105    108       {ECO:0000244|PDB:5J80}.
FT   HELIX       111    123       {ECO:0000244|PDB:5J80}.
FT   HELIX       128    134       {ECO:0000244|PDB:5J80}.
FT   HELIX       137    143       {ECO:0000244|PDB:5J80}.
FT   STRAND      145    153       {ECO:0000244|PDB:5J80}.
FT   STRAND      155    157       {ECO:0000244|PDB:2WI6}.
FT   STRAND      160    164       {ECO:0000244|PDB:5J80}.
FT   STRAND      169    174       {ECO:0000244|PDB:5J80}.
FT   STRAND      181    190       {ECO:0000244|PDB:5J80}.
FT   HELIX       192    198       {ECO:0000244|PDB:5J80}.
FT   HELIX       200    210       {ECO:0000244|PDB:5J80}.
FT   STRAND      212    216       {ECO:0000244|PDB:3VHC}.
FT   STRAND      218    220       {ECO:0000244|PDB:5J80}.
FT   TURN        221    224       {ECO:0000244|PDB:3T1K}.
FT   STRAND      225    227       {ECO:0000244|PDB:3T1K}.
FT   HELIX       228    230       {ECO:0000244|PDB:2XJX}.
FT   HELIX       296    298       {ECO:0000244|PDB:3Q6M}.
FT   HELIX       306    317       {ECO:0000244|PDB:3Q6M}.
FT   STRAND      324    331       {ECO:0000244|PDB:3Q6M}.
FT   STRAND      333    335       {ECO:0000244|PDB:3Q6M}.
FT   STRAND      337    343       {ECO:0000244|PDB:3Q6M}.
FT   STRAND      361    365       {ECO:0000244|PDB:3Q6M}.
FT   STRAND      368    372       {ECO:0000244|PDB:3Q6M}.
FT   HELIX       380    382       {ECO:0000244|PDB:3Q6M}.
FT   STRAND      386    392       {ECO:0000244|PDB:3Q6M}.
FT   HELIX       408    427       {ECO:0000244|PDB:3Q6M}.
FT   HELIX       431    451       {ECO:0000244|PDB:3Q6M}.
FT   HELIX       453    455       {ECO:0000244|PDB:3Q6M}.
FT   HELIX       456    460       {ECO:0000244|PDB:3Q6M}.
FT   STRAND      464    467       {ECO:0000244|PDB:3Q6M}.
FT   TURN        468    472       {ECO:0000244|PDB:3Q6M}.
FT   HELIX       477    482       {ECO:0000244|PDB:3Q6M}.
FT   STRAND      490    495       {ECO:0000244|PDB:3Q6M}.
FT   HELIX       499    503       {ECO:0000244|PDB:3Q6M}.
FT   HELIX       506    508       {ECO:0000244|PDB:3Q6M}.
FT   HELIX       509    514       {ECO:0000244|PDB:3Q6M}.
FT   STRAND      518    521       {ECO:0000244|PDB:3Q6M}.
FT   HELIX       525    529       {ECO:0000244|PDB:3Q6M}.
FT   TURN        530    532       {ECO:0000244|PDB:3Q6M}.
FT   STRAND      539    543       {ECO:0000244|PDB:3Q6M}.
FT   HELIX       555    567       {ECO:0000244|PDB:3Q6M}.
FT   HELIX       569    578       {ECO:0000244|PDB:3Q6M}.
FT   HELIX       580    582       {ECO:0000244|PDB:3Q6M}.
FT   STRAND      584    588       {ECO:0000244|PDB:3Q6M}.
FT   STRAND      593    601       {ECO:0000244|PDB:3Q6M}.
FT   STRAND      603    605       {ECO:0000244|PDB:3Q6M}.
FT   HELIX       608    613       {ECO:0000244|PDB:3Q6M}.
FT   STRAND      632    636       {ECO:0000244|PDB:3Q6M}.
FT   HELIX       641    652       {ECO:0000244|PDB:3Q6M}.
FT   HELIX       657    673       {ECO:0000244|PDB:3Q6M}.
FT   HELIX       681    694       {ECO:0000244|PDB:3Q6M}.
FT   STRAND      728    730       {ECO:0000244|PDB:4CGW}.
SQ   SEQUENCE   732 AA;  84660 MW;  969F65FCC0BC86FD CRC64;
     MPEETQTQDQ PMEEEEVETF AFQAEIAQLM SLIINTFYSN KEIFLRELIS NSSDALDKIR
     YESLTDPSKL DSGKELHINL IPNKQDRTLT IVDTGIGMTK ADLINNLGTI AKSGTKAFME
     ALQAGADISM IGQFGVGFYS AYLVAEKVTV ITKHNDDEQY AWESSAGGSF TVRTDTGEPM
     GRGTKVILHL KEDQTEYLEE RRIKEIVKKH SQFIGYPITL FVEKERDKEV SDDEAEEKED
     KEEEKEKEEK ESEDKPEIED VGSDEEEEKK DGDKKKKKKI KEKYIDQEEL NKTKPIWTRN
     PDDITNEEYG EFYKSLTNDW EDHLAVKHFS VEGQLEFRAL LFVPRRAPFD LFENRKKKNN
     IKLYVRRVFI MDNCEELIPE YLNFIRGVVD SEDLPLNISR EMLQQSKILK VIRKNLVKKC
     LELFTELAED KENYKKFYEQ FSKNIKLGIH EDSQNRKKLS ELLRYYTSAS GDEMVSLKDY
     CTRMKENQKH IYYITGETKD QVANSAFVER LRKHGLEVIY MIEPIDEYCV QQLKEFEGKT
     LVSVTKEGLE LPEDEEEKKK QEEKKTKFEN LCKIMKDILE KKVEKVVVSN RLVTSPCCIV
     TSTYGWTANM ERIMKAQALR DNSTMGYMAA KKHLEINPDH SIIETLRQKA EADKNDKSVK
     DLVILLYETA LLSSGFSLED PQTHANRIYR MIKLGLGIDE DDPTADDTSA AVTEEMPPLE
     GDDDTSRMEE VD
//
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