HS90A_HUMAN
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 03-AUG-2022, entry version 266.
DE RecName: Full=Heat shock protein HSP 90-alpha {ECO:0000305};
DE EC=3.6.4.10 {ECO:0000269|PubMed:12526792};
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 {ECO:0000312|HGNC:HGNC:5253}; Synonyms=HSP90A, HSPC1, HSPCA;
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).
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 protein
RT 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.9.6.2615-2626.1989;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., 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., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA 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., 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 (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 genes
RT encode formerly identified tumour-specific transplantation 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 gene.";
RL Gene 83:105-115(1989).
RN [11]
RP PROTEIN SEQUENCE OF 101-112; 210-224; 300-314; 328-338; 346-355; 387-400;
RP 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 project:
RT 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; DOI=10.1016/s0021-9258(19)81631-9;
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 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 OF
RP 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., Lopez-Ferrer D.,
RA Higueras M.A., Tarin C., Rodriguez-Crespo I., 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; DOI=10.1016/s0021-9258(18)71488-9;
RA Lees-Miller S.P., Anderson C.W.;
RT "The human double-stranded DNA-activated protein kinase phosphorylates the
RT 90-kDa heat-shock protein, hsp90 alpha at two NH2-terminal threonine
RT residues.";
RL J. Biol. Chem. 264:17275-17280(1989).
RN [18]
RP HOMODIMERIZATION.
RX PubMed=8289821; DOI=10.1128/mcb.14.2.1459-1464.1994;
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 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-terminal
RT 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-cell
RT 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 AND
RP 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 FUNCTION, INTERACTION WITH TOMM70, AND CATALYTIC ACTIVITY.
RX PubMed=12526792; DOI=10.1016/s0092-8674(02)01250-3;
RA Young J.C., Hoogenraad N.J., Hartl F.U.;
RT "Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the
RT mitochondrial import receptor Tom70.";
RL Cell 112:41-50(2003).
RN [27]
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 [28]
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 protein
RT activation, and stimulates the ATPase activity of the molecular
RT chaperone.";
RL J. Biol. Chem. 278:17228-17235(2003).
RN [29]
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., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [30]
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 proliferation of
RT cancer cells.";
RL Nat. Cell Biol. 6:731-740(2004).
RN [31]
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 [32]
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 is
RT proteolytically activated in response to arachidonic acid and the
RT microtubule-depolymerizing drug nocodazole.";
RL Biochem. J. 385:45-56(2005).
RN [33]
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., Cohen P.T.,
RA Barford D.;
RT "Molecular basis for TPR domain-mediated regulation of protein phosphatase
RT 5.";
RL EMBO J. 24:1-10(2005).
RN [34]
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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION BY
RP 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 [36]
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 protein
RT phosphatase 5 with Hsp90.";
RL Structure 14:415-426(2006).
RN [37]
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 ability
RT to promote degradation of NF-kappaB-inducing kinase.";
RL J. Immunol. 179:6291-6296(2007).
RN [38]
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., Reinstein J.,
RA Buchner J.;
RT "Conserved conformational changes in the ATPase cycle of human Hsp90.";
RL J. Biol. Chem. 283:17757-17765(2008).
RN [39]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION BY
RP 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 sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [40]
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 [41]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION BY
RP 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 the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [42]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION BY
RP 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 [43]
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 enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [44]
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., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [45]
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 [46]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-443; LYS-458; LYS-489 AND
RP LYS-585, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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 [47]
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 [48]
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 [49]
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., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., 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 [50]
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., Iwamatsu A.,
RA Esposito D., Gillette W.K., Hopkins R.F. III, Hartley J.L., Furihata M.,
RA Oishi S., Zhen W., Burke T.R. Jr., 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 [51]
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 [52]
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 [53]
RP FUNCTION, INTERACTION WITH TOMM70; IRF3 AND TBK1, AND MUTAGENESIS OF
RP 729-GLU--ASP-732.
RX PubMed=20628368; DOI=10.1038/cr.2010.103;
RA Liu X.Y., Wei B., Shi H.X., Shan Y.F., Wang C.;
RT "Tom70 mediates activation of interferon regulatory factor 3 on
RT mitochondria.";
RL Cell Res. 20:994-1011(2010).
RN [54]
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., Cheng X.K.,
RA 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 [55]
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [56]
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., Buerckstuemmer T.,
RA 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 [57]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, 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 [58]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH N.MENINGITIDIS ADHESIN
RP A (MICROBIAL INFECTION).
RX PubMed=22066472; DOI=10.1111/j.1462-5822.2011.01722.x;
RA Montanari P., Bozza G., Capecchi B., Caproni E., Barrile R., Norais N.,
RA Capitani M., Sallese M., Cecchini P., Ciucchi L., Gao Z., Rappuoli R.,
RA Pizza M., Arico B., Merola M.;
RT "Human heat shock protein (Hsp) 90 interferes with Neisseria meningitidis
RT adhesin A (NadA)-mediated adhesion and invasion.";
RL Cell. Microbiol. 14:368-385(2012).
RN [59]
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., Richter K.;
RT "Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90)
RT motility by interaction with N-terminal and middle domain binding sites.";
RL J. Biol. Chem. 288:16032-16042(2013).
RN [60]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231; SER-252; SER-263;
RP SER-476 AND SER-641, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [61]
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 [62]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [63]
RP 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 [64]
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 [65]
RP FUNCTION, INTERACTION WITH TOMM70 AND IRF3, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 728-MET--ASP-732.
RX PubMed=25609812; DOI=10.1128/jvi.02959-14;
RA Wei B., Cui Y., Huang Y., Liu H., Li L., Li M., Ruan K.C., Zhou Q.,
RA Wang C.;
RT "Tom70 mediates Sendai virus-induced apoptosis on mitochondria.";
RL J. Virol. 89:3804-3818(2015).
RN [66]
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., Shaaban S.,
RA Tucker H.;
RT "C-terminal domain of SMYD3 serves as a unique HSP90-regulated motif in
RT oncogenesis.";
RL Oncotarget 6:4005-4019(2015).
RN [67]
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., Rivas C.,
RA Alarcon S., Schwartz H., Khamit-Kush K., Scroggins B.T., Beebe K.,
RA Trepel J.B., Neckers L.;
RT "Client proteins and small molecule inhibitors display distinct binding
RT preferences for constitutive and stress-induced HSP90 isoforms and their
RT conformationally restricted mutants.";
RL PLoS ONE 10:E0141786-E0141786(2015).
RN [68]
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., Ayoub D.,
RA 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 [69]
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 [70]
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 [71]
RP FUNCTION, AND INTERACTION WITH FLCN; AHSA1; HSP70; CDC37; FNIP1; FNIP2;
RP 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., Marston Linehan W.,
RA Bratslavsky G., Mollapour M.;
RT "The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance
RT drug binding.";
RL Nat. Commun. 7:12037-12037(2016).
RN [72]
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., Aburatani H.,
RA 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 [73]
RP FUNCTION, ACTIVITY REGULATION, IDENTIFICATION IN A COMPLEX WITH TSC1 AND
RP TSC2, INTERACTION WITH TSC1 AND AHSA1, SUBUNIT, AND MUTAGENESIS OF GLU-47;
RP 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., Murphy R.L.,
RA Rensing N., Shapiro O., Panaretou B., Prodromou C., Loh S.N., Gutmann D.H.,
RA Bourboulia D., Bratslavsky G., Wong M., Mollapour M.;
RT "Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding
RT of kinase and non-kinase clients.";
RL EMBO J. 36:3650-3665(2017).
RN [74]
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., Chauvin C.,
RA Couturier-Maillard A., Boulard O., Cobret L., Awad F., Huot L.,
RA Ribeiro-Ribeiro A., Lautz K., Ruez R., Delacre M., Bondu C., Guilliams M.,
RA Scott C., Segal A., Amselem S., Hot D., Karabina S., Bohn E., Ryffel B.,
RA Poulin L.F., Kufer T.A., Chamaillard M.;
RT "Proteasomal degradation of NOD2 by NLRP12 in monocytes promotes bacterial
RT tolerance and colonization by enteropathogens.";
RL Nat. Commun. 9:5338-5338(2018).
RN [75]
RP INTERACTION WITH HERPES SIMPLEX VIRUS 1 PROTEIN US11 (MICROBIAL 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 Formation of
RT the Us11-Hsp90 Complex.";
RL J. Virol. 92:0-0(2018).
RN [76]
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 protein
RT chaperone by an antitumor agent.";
RL Cell 89:239-250(1997).
RN [77]
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 [78]
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 724-732 IN COMPLEX WITH STUB1,
RP 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, structural
CC maintenance and proper regulation of specific target proteins involved
CC for instance in cell cycle control and signal transduction. Undergoes a
CC functional cycle that is linked to its ATPase activity which is
CC essential for its chaperone activity. This cycle probably induces
CC conformational changes in the client proteins, thereby causing their
CC activation. Interacts dynamically with various co-chaperones that
CC modulate its substrate recognition, ATPase cycle and chaperone function
CC (PubMed:11274138, PubMed:15577939, PubMed:15937123, PubMed:27353360,
CC PubMed:29127155, PubMed:12526792). Engages with a range of client
CC protein classes via its interaction with various co-chaperone proteins
CC or 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 of
CC the chaperoning process, properly folded client protein and co-
CC chaperone leave HSP90 in an ADP-bound partially open conformation and
CC finally, ADP is released from HSP90 which acquires an open conformation
CC for the next cycle (PubMed:27295069, PubMed:26991466). Plays a critical
CC role in mitochondrial import, delivers preproteins to the mitochondrial
CC import receptor TOMM70 (PubMed:12526792). Apart from its chaperone
CC activity, it also plays a role in the regulation of the transcription
CC machinery. HSP90 and its co-chaperones modulate transcription at least
CC at three different levels (PubMed:25973397). In the first place, they
CC alter the steady-state levels of certain transcription factors in
CC response to various physiological cues(PubMed:25973397). Second, they
CC modulate the activity of certain epigenetic modifiers, such as histone
CC deacetylases or DNA methyl transferases, and thereby respond to the
CC change in the environment (PubMed:25973397). Third, they participate in
CC the eviction of histones from the promoter region of certain genes and
CC thereby turn on gene expression (PubMed:25973397). Binds bacterial
CC lipopolysaccharide (LPS) and mediates LPS-induced inflammatory
CC response, including TNF secretion by monocytes (PubMed:11276205).
CC Antagonizes STUB1-mediated inhibition of TGF-beta signaling via
CC inhibition of STUB1-mediated SMAD3 ubiquitination and degradation
CC (PubMed:24613385). Mediates the association of TOMM70 with IRF3 or TBK1
CC in mitochondrial outer membrane which promotes host antiviral response
CC (PubMed:20628368, PubMed:25609812). {ECO:0000269|PubMed:11274138,
CC ECO:0000269|PubMed:11276205, ECO:0000269|PubMed:12526792,
CC ECO:0000269|PubMed:15577939, ECO:0000269|PubMed:15937123,
CC ECO:0000269|PubMed:20628368, ECO:0000269|PubMed:24613385,
CC ECO:0000269|PubMed:25609812, ECO:0000269|PubMed:27353360,
CC ECO:0000269|PubMed:29127155, ECO:0000303|PubMed:25973397,
CC ECO:0000303|PubMed:26991466, ECO:0000303|PubMed:27295069}.
CC -!- FUNCTION: (Microbial infection) Seems to interfere with N.meningitidis
CC NadA-mediated invasion of human cells. Decreasing HSP90 levels
CC increases adhesion and entry of E.coli expressing NadA into human Chang
CC cells; increasing its levels leads to decreased adhesion and invasion.
CC {ECO:0000305|PubMed:22066472}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10;
CC Evidence={ECO:0000269|PubMed:12526792};
CC -!- ACTIVITY REGULATION: In the resting state, through the dimerization of
CC its C-terminal domain, HSP90 forms a homodimer which is defined as the
CC open conformation (PubMed:18400751). Upon ATP-binding, the N-terminal
CC domain undergoes significant conformational changes and comes in
CC contact to form an active closed conformation (PubMed:18400751). After
CC HSP90 finishes its chaperoning tasks of assisting the proper folding,
CC stabilization and activation of client proteins under the active state,
CC ATP molecule is hydrolyzed to ADP which then dissociates from HSP90 and
CC directs the protein back to the resting state (PubMed:18400751). Co-
CC chaperone TSC1 promotes ATP binding and inhibits HSP90AA1 ATPase
CC activity (PubMed:29127155). Binding to phosphorylated AHSA1 promotes
CC HSP90AA1 ATPase activity (PubMed:29127155). Inhibited by geldanamycin,
CC Ganetespib (STA-9090) and SNX-2112 (PubMed:29127155, PubMed:12526792).
CC {ECO:0000269|PubMed:18400751, 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, PubMed:18400751,
CC PubMed:29127155). Identified in NR3C1/GCR steroid receptor-chaperone
CC complexes formed at least by NR3C1, HSP90AA1 and a variety of proteins
CC containing TPR repeats such as FKBP4, FKBP5, PPID, PPP5C or STIP1
CC (PubMed:15383005, PubMed:9195923). Forms a complex containing HSP90AA1,
CC TSC1 and TSC2; TSC1 is required to recruit TCS2 to the complex
CC (PubMed:29127155). The closed form interacts (via the middle domain and
CC TPR repeat-binding motif) with co-chaperone TSC1 (via C-terminus)
CC (PubMed:29127155). Interacts with TOM34 (PubMed:9660753). Interacts
CC with TERT; the interaction, together with PTGES3, is required for
CC correct assembly and stabilization of the TERT holoenzyme complex
CC (PubMed:11274138, PubMed:9817749). Interacts with CHORDC1 and DNAJC7
CC (PubMed:12853476, PubMed:19875381). Interacts with STUB1 and UBE2N; may
CC couple the chaperone and ubiquitination systems (PubMed:16307917,
CC PubMed:27353360). Interacts (via TPR repeat-binding motif) with PPP5C
CC (via TPR 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 a
CC complex with CXCR4, GDF5 and HSPA8 (PubMed:11276205). Interacts with
CC KSR1 (PubMed:10409742). Interacts with co-chaperone CDC37 (via C-
CC terminus); the interaction inhibits HSP90AA1 ATPase activity
CC (PubMed:23569206, PubMed:27353360). May interact with NWD1
CC (PubMed:24681825). Interacts with FNIP1 and FNIP2; the interaction
CC inhibits HSP90AA1 ATPase activity (PubMed:17028174, PubMed:27353360).
CC Interacts with co-chaperone AHSA1 (phosphorylated on 'Tyr-223'); the
CC interaction activates HSP90AA1 ATPase activity and results in the
CC dissociation of TSC1 from HSP90AA1 (PubMed:12604615, PubMed:27353360,
CC PubMed:29127155). Interacts with FLCN in the presence of FNIP1
CC (PubMed:27353360). Interacts with HSP70, STIP1 and PTGES3
CC (PubMed:27353360). Interacts with SMYD3; this interaction enhances
CC SMYD3 histone-lysine N-methyltransferase (PubMed:15235609,
CC PubMed:25738358). Interacts with SGTA (via TPR repeats)
CC (PubMed:15708368). Interacts with TTC1 (via TPR repeats)
CC (PubMed:15708368). Interacts with HSF1 in an ATP-dependent manner
CC (PubMed:11583998. PubMed:26517842). Interacts with MET; the interaction
CC suppresses MET kinase activity (PubMed:26517842). Interacts with ERBB2
CC in an ATP-dependent manner; the interaction suppresses ERBB2 kinase
CC activity (PubMed:26517842). Interacts with HIF1A, KEAP1 and RHOBTB2
CC (PubMed:26517842). Interacts with HSF1; this interaction is decreased
CC in a IER5-dependent manner, promoting HSF1 accumulation in the nucleus,
CC homotrimerization and DNA-binding activities (PubMed:26754925).
CC Interacts with STUB1 and SMAD3 (PubMed:24613385). Interacts with
CC HSP90AB1; interaction is constitutive (PubMed:20353823). Interacts with
CC HECTD1 (via N-terminus) (By similarity). Interacts with NR3C1 (via
CC domain NR LBD) and NR1D1 (via domain NR LBD) (By similarity). Interacts
CC with NLPR12 (PubMed:30559449, PubMed:17947705). Interacts with PDCL3
CC (By similarity). Interacts with TOMM70; the interaction is required for
CC preprotein mitochondrial import (PubMed:12526792). Interacts with
CC TOMM70, IRF3 and TBK1; the interactions are direct and mediate the
CC association of TOMM70 with IRF3 and TBK1 (PubMed:20628368). Forms a
CC complex with ASL, ASS1 and NOS2; the complex regulates cell-autonomous
CC L-arginine synthesis and citrulline recycling while channeling
CC extracellular L-arginine to nitric oxide synthesis pathway.
CC {ECO:0000250|UniProtKB:P07901, ECO:0000250|UniProtKB:P82995,
CC ECO:0000269|PubMed:10409742, ECO:0000269|PubMed:11274138,
CC ECO:0000269|PubMed:11276205, ECO:0000269|PubMed:11583998,
CC ECO:0000269|PubMed:12526792, 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:20628368, ECO:0000269|PubMed:23569206,
CC ECO:0000269|PubMed:24613385, ECO:0000269|PubMed:24681825,
CC ECO:0000269|PubMed:25738358, ECO:0000269|PubMed:26517842,
CC ECO:0000269|PubMed:26754925, ECO:0000269|PubMed:27353360,
CC ECO:0000269|PubMed:29127155, ECO:0000269|PubMed:30559449,
CC ECO:0000269|PubMed:7588731, ECO:0000269|PubMed:8289821,
CC ECO:0000269|PubMed:9195923, ECO:0000269|PubMed:9660753,
CC ECO:0000269|PubMed:9817749}.
CC -!- SUBUNIT: (Microbial infection) Interacts with herpes simplex virus 1
CC protein US11; this interaction inhibits TBK1-induced interferon
CC production. {ECO:0000269|PubMed:29743370}.
CC -!- SUBUNIT: (Microbial infection) Interacts with N.meningitidis serogroup
CC B adhesin A (nadA). Interaction is stabilized by ADP and 17-AAG (17-N-
CC allylamino-17-demethoxygeldanamycin) and inhibited by ATP. Decreasing
CC HSP90 levels increases adhesion and entry of bacterial into human Chang
CC cells; increasing its levels leads to decreased adhseion and invasion.
CC {ECO:0000269|PubMed:22066472}.
CC -!- INTERACTION:
CC P07900; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-296047, EBI-10173507;
CC P07900; O95433: AHSA1; NbExp=4; IntAct=EBI-296047, EBI-448610;
CC P07900; P05067: APP; NbExp=5; IntAct=EBI-296047, EBI-77613;
CC P07900; Q9H0C5: BTBD1; NbExp=4; IntAct=EBI-296047, EBI-935503;
CC P07900; Q9UQM7: CAMK2A; NbExp=5; IntAct=EBI-296047, EBI-1383687;
CC P07900; Q8IWD4: CCDC117; NbExp=5; IntAct=EBI-296047, EBI-3387963;
CC P07900; Q9BV29: CCDC32; NbExp=3; IntAct=EBI-296047, EBI-2874058;
CC P07900; Q16543: CDC37; NbExp=14; IntAct=EBI-296047, EBI-295634;
CC P07900; Q7L3B6: CDC37L1; NbExp=2; IntAct=EBI-296047, EBI-2841876;
CC P07900; P50750: CDK9; NbExp=3; IntAct=EBI-296047, EBI-1383449;
CC P07900; Q96G23: CERS2; NbExp=2; IntAct=EBI-296047, EBI-1057080;
CC P07900; Q9UHD1: CHORDC1; NbExp=8; IntAct=EBI-296047, EBI-2550959;
CC P07900; O15111: CHUK; NbExp=3; IntAct=EBI-296047, EBI-81249;
CC P07900; Q6QEF8-4: CORO6; NbExp=3; IntAct=EBI-296047, EBI-10699285;
CC P07900; Q14194: CRMP1; NbExp=3; IntAct=EBI-296047, EBI-473101;
CC P07900; P35222: CTNNB1; NbExp=3; IntAct=EBI-296047, EBI-491549;
CC P07900; Q15438: CYTH1; NbExp=3; IntAct=EBI-296047, EBI-997830;
CC P07900; Q9NR20: DYRK4; NbExp=2; IntAct=EBI-296047, EBI-3914009;
CC P07900; P00533: EGFR; NbExp=7; IntAct=EBI-296047, EBI-297353;
CC P07900; P04626: ERBB2; NbExp=5; IntAct=EBI-296047, EBI-641062;
CC P07900; Q02790: FKBP4; NbExp=8; IntAct=EBI-296047, EBI-1047444;
CC P07900; Q13451: FKBP5; NbExp=8; IntAct=EBI-296047, EBI-306914;
CC P07900; Q14318: FKBP8; NbExp=7; IntAct=EBI-296047, EBI-724839;
CC P07900; P06241: FYN; NbExp=6; IntAct=EBI-296047, EBI-515315;
CC P07900; Q96LI6-3: HSFY2; NbExp=3; IntAct=EBI-296047, EBI-25830912;
CC P07900; P07900: HSP90AA1; NbExp=6; IntAct=EBI-296047, EBI-296047;
CC P07900; Q6PK50: HSP90AB1; NbExp=2; IntAct=EBI-296047, EBI-9356629;
CC P07900; Q9Y6K9: IKBKG; NbExp=3; IntAct=EBI-296047, EBI-81279;
CC P07900; Q9UHH9: IP6K2; NbExp=2; IntAct=EBI-296047, EBI-747509;
CC P07900; P05412: JUN; NbExp=4; IntAct=EBI-296047, EBI-852823;
CC P07900; Q92993-2: KAT5; NbExp=3; IntAct=EBI-296047, EBI-20795332;
CC P07900; Q6VAB6: KSR2; NbExp=6; IntAct=EBI-296047, EBI-6424389;
CC P07900; P06239: LCK; NbExp=3; IntAct=EBI-296047, EBI-1348;
CC P07900; Q99558: MAP3K14; NbExp=5; IntAct=EBI-296047, EBI-358011;
CC P07900; O43318-2: MAP3K7; NbExp=5; IntAct=EBI-296047, EBI-358700;
CC P07900; P00540: MOS; NbExp=2; IntAct=EBI-296047, EBI-1757866;
CC P07900; P04150: NR3C1; NbExp=8; IntAct=EBI-296047, EBI-493507;
CC P07900; Q8WVJ2: NUDCD2; NbExp=4; IntAct=EBI-296047, EBI-1052153;
CC P07900; P43034: PAFAH1B1; NbExp=5; IntAct=EBI-296047, EBI-720620;
CC P07900; P53041: PPP5C; NbExp=12; IntAct=EBI-296047, EBI-716663;
CC P07900; P17612: PRKACA; NbExp=4; IntAct=EBI-296047, EBI-476586;
CC P07900; A0A0C4DFM3: PRUNE2; NbExp=3; IntAct=EBI-296047, EBI-25830870;
CC P07900; Q96QS6: PSKH2; NbExp=2; IntAct=EBI-296047, EBI-6424813;
CC P07900; Q15185: PTGES3; NbExp=6; IntAct=EBI-296047, EBI-1049387;
CC P07900; P04049: RAF1; NbExp=4; IntAct=EBI-296047, EBI-365996;
CC P07900; Q13127: REST; NbExp=4; IntAct=EBI-296047, EBI-926706;
CC P07900; Q9H6T3: RPAP3; NbExp=6; IntAct=EBI-296047, EBI-356928;
CC P07900; P61247: RPS3A; NbExp=3; IntAct=EBI-296047, EBI-352378;
CC P07900; P12931: SRC; NbExp=3; IntAct=EBI-296047, EBI-621482;
CC P07900; Q15831: STK11; NbExp=3; IntAct=EBI-296047, EBI-306838;
CC P07900; Q9UNE7: STUB1; NbExp=9; IntAct=EBI-296047, EBI-357085;
CC P07900; O94826: TOMM70; NbExp=4; IntAct=EBI-296047, EBI-2800236;
CC P07900; Q9BXA6: TSSK6; NbExp=2; IntAct=EBI-296047, EBI-851883;
CC P07900; P10599: TXN; NbExp=3; IntAct=EBI-296047, EBI-594644;
CC P07900; Q9H6R7-2: WDCP; NbExp=3; IntAct=EBI-296047, EBI-25833271;
CC P07900; P26882: PPID; Xeno; NbExp=4; IntAct=EBI-296047, EBI-6477155;
CC P07900; P35467: S100a1; Xeno; NbExp=4; IntAct=EBI-296047, EBI-6477109;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm
CC {ECO:0000250|UniProtKB:P07901}. Melanosome
CC {ECO:0000269|PubMed:17081065}. Cell membrane
CC {ECO:0000269|PubMed:11276205}. Mitochondrion
CC {ECO:0000269|PubMed:25609812}. Note=Identified by mass spectrometry in
CC 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 -!- 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 the
CC activation of eNOS by HSP90AA1. {ECO:0000269|PubMed:15937123}.
CC -!- PTM: Ubiquitinated via 'Lys-63'-linked polyubiquitination by HECTD1.
CC Ubiquitination promotes translocation into the cytoplasm away from the
CC membrane and secretory pathways. {ECO:0000250|UniProtKB:P07901}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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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; 6KSQ; X-ray; 2.20 A; A=293-554.
DR PDB; 6LR9; X-ray; 2.20 A; A=9-236.
DR PDB; 6LSZ; X-ray; 1.99 A; A=9-236.
DR PDB; 6LT8; X-ray; 1.59 A; A=9-236.
DR PDB; 6LTI; X-ray; 1.59 A; A=9-236.
DR PDB; 6LTK; X-ray; 2.14 A; A=9-236.
DR PDB; 6N8X; X-ray; 1.49 A; A=1-236.
DR PDB; 6OLX; X-ray; 1.44 A; A=1-236.
DR PDB; 6TN4; X-ray; 1.27 A; AAA=9-236.
DR PDB; 6TN5; X-ray; 1.17 A; AAA=9-236.
DR PDB; 6U98; X-ray; 1.50 A; A=2-236.
DR PDB; 6U99; X-ray; 1.60 A; A=2-236.
DR PDB; 6U9A; X-ray; 1.65 A; A=2-236.
DR PDB; 6U9B; X-ray; 1.75 A; A=2-236.
DR PDB; 7DMC; X-ray; 2.34 A; A=16-224.
DR PDB; 7KRJ; EM; 2.56 A; A/B=1-732.
DR PDB; 7KW7; EM; 3.57 A; A/B=1-732.
DR PDB; 7L7I; EM; 3.30 A; A/B=1-732.
DR PDB; 7L7J; EM; 3.10 A; A/B=1-732.
DR PDB; 7LSZ; X-ray; 1.70 A; A=1-293.
DR PDB; 7LT0; X-ray; 1.70 A; A=1-293.
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; 6KSQ; -.
DR PDBsum; 6LR9; -.
DR PDBsum; 6LSZ; -.
DR PDBsum; 6LT8; -.
DR PDBsum; 6LTI; -.
DR PDBsum; 6LTK; -.
DR PDBsum; 6N8X; -.
DR PDBsum; 6OLX; -.
DR PDBsum; 6TN4; -.
DR PDBsum; 6TN5; -.
DR PDBsum; 6U98; -.
DR PDBsum; 6U99; -.
DR PDBsum; 6U9A; -.
DR PDBsum; 6U9B; -.
DR PDBsum; 7DMC; -.
DR PDBsum; 7KRJ; -.
DR PDBsum; 7KW7; -.
DR PDBsum; 7L7I; -.
DR PDBsum; 7L7J; -.
DR PDBsum; 7LSZ; -.
DR PDBsum; 7LT0; -.
DR AlphaFoldDB; P07900; -.
DR BMRB; P07900; -.
DR SMR; P07900; -.
DR BioGRID; 109552; 1060.
DR ComplexPortal; CPX-3288; HSP90A-CDC37 chaperone complex.
DR CORUM; P07900; -.
DR DIP; DIP-27595N; -.
DR IntAct; P07900; 387.
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; 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; DB07594; CCT-018159.
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; 1 N-Linked glycan (1 site).
DR GlyGen; P07900; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; P07900; -.
DR MetOSite; 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 Antibodypedia; 3676; 1858 antibodies from 45 providers.
DR DNASU; 3320; -.
DR Ensembl; ENST00000216281.13; ENSP00000216281.8; ENSG00000080824.19. [P07900-1]
DR Ensembl; ENST00000334701.11; ENSP00000335153.7; ENSG00000080824.19. [P07900-2]
DR GeneID; 3320; -.
DR KEGG; hsa:3320; -.
DR MANE-Select; ENST00000216281.13; ENSP00000216281.8; NM_005348.4; NP_005339.3.
DR UCSC; uc001yku.5; human. [P07900-1]
DR CTD; 3320; -.
DR DisGeNET; 3320; -.
DR GeneCards; HSP90AA1; -.
DR HGNC; HGNC:5253; HSP90AA1.
DR HPA; ENSG00000080824; Tissue enhanced (brain).
DR MIM; 140571; gene.
DR neXtProt; NX_P07900; -.
DR OpenTargets; ENSG00000080824; -.
DR PharmGKB; PA29519; -.
DR VEuPathDB; HostDB:ENSG00000080824; -.
DR eggNOG; KOG0019; Eukaryota.
DR GeneTree; ENSGT01020000230401; -.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; P07900; -.
DR OMA; AHDQPME; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; P07900; -.
DR TreeFam; TF300686; -.
DR BRENDA; 3.6.4.10; 2681.
DR PathwayCommons; P07900; -.
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-168928; DDX58/IFIH1-mediated induction of interferon-alpha/beta.
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) in the presence of ligand.
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-5675482; Regulation of necroptotic cell death.
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-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-9613829; Chaperone Mediated Autophagy.
DR Reactome; R-HSA-9634285; Constitutive Signaling by Overexpressed ERBB2.
DR Reactome; R-HSA-9646399; Aggrephagy.
DR Reactome; R-HSA-9652282; Drug-mediated inhibition of ERBB2 signaling.
DR Reactome; R-HSA-9664565; Signaling by ERBB2 KD Mutants.
DR Reactome; R-HSA-9665233; Resistance of ERBB2 KD mutants to trastuzumab.
DR Reactome; R-HSA-9665244; Resistance of ERBB2 KD mutants to sapitinib.
DR Reactome; R-HSA-9665245; Resistance of ERBB2 KD mutants to tesevatinib.
DR Reactome; R-HSA-9665246; Resistance of ERBB2 KD mutants to neratinib.
DR Reactome; R-HSA-9665247; Resistance of ERBB2 KD mutants to osimertinib.
DR Reactome; R-HSA-9665249; Resistance of ERBB2 KD mutants to afatinib.
DR Reactome; R-HSA-9665250; Resistance of ERBB2 KD mutants to AEE788.
DR Reactome; R-HSA-9665251; Resistance of ERBB2 KD mutants to lapatinib.
DR Reactome; R-HSA-9665348; Signaling by ERBB2 ECD mutants.
DR Reactome; R-HSA-9665686; Signaling by ERBB2 TMD/JMD mutants.
DR Reactome; R-HSA-9665737; Drug resistance in ERBB2 TMD/JMD mutants.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR SignaLink; P07900; -.
DR SIGNOR; P07900; -.
DR BioGRID-ORCS; 3320; 37 hits in 1091 CRISPR screens.
DR ChiTaRS; HSP90AA1; human.
DR EvolutionaryTrace; P07900; -.
DR GenomeRNAi; 3320; -.
DR Pharos; P07900; Tchem.
DR PRO; PR:P07900; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P07900; protein.
DR Bgee; ENSG00000080824; Expressed in Brodmann (1909) area 23 and 216 other tissues.
DR ExpressionAtlas; P07900; baseline and differential.
DR Genevisible; P07900; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0044295; C:axonal growth cone; ISS:ARUK-UCL.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0031526; C:brush border membrane; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:Ensembl.
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:0005739; C:mitochondrion; IDA: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:0097226; C:sperm mitochondrial sheath; IEA:Ensembl.
DR GO; GO:0097524; C:sperm plasma membrane; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0002135; F:CTP binding; IEA:Ensembl.
DR GO; GO:0032564; F:dATP binding; IEA:Ensembl.
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:0005525; F:GTP binding; IEA:Ensembl.
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:0003729; F:mRNA binding; IEA:Ensembl.
DR GO; GO:0030235; F:nitric-oxide synthase regulator activity; IDA:UniProtKB.
DR GO; GO:0044183; F:protein folding chaperone; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IPI:UniProtKB.
DR GO; GO:0051022; F:Rho GDP-dissociation inhibitor binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0097110; F:scaffold protein binding; IPI:UniProtKB.
DR GO; GO:0017098; F:sulfonylurea receptor binding; IEA:Ensembl.
DR GO; GO:0048156; F:tau protein binding; IPI:ARUK-UCL.
DR GO; GO:0030911; F:TPR domain binding; IDA:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
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:0002134; F:UTP binding; IEA:Ensembl.
DR GO; GO:0002218; P:activation of innate immune response; IDA:UniProtKB.
DR GO; GO:0048675; P:axon extension; ISS:ARUK-UCL.
DR GO; GO:0010659; P:cardiac muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0098586; P:cellular response to virus; IDA:UniProtKB.
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:0030010; P:establishment of cell polarity; ISS:ARUK-UCL.
DR GO; GO:0006839; P:mitochondrial transport; TAS:UniProtKB.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:0060452; P:positive regulation of cardiac muscle contraction; IEA:Ensembl.
DR GO; GO:0045793; P:positive regulation of cell size; IEA:Ensembl.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IDA:UniProtKB.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; IDA:UniProtKB.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IEA:Ensembl.
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:0045732; P:positive regulation of protein catabolic process; IGI:ARUK-UCL.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IEA:Ensembl.
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:0042981; P:regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; ISS:ARUK-UCL.
DR GO; GO:0031396; P:regulation of protein ubiquitination; IDA:BHF-UCL.
DR GO; GO:0043254; P:regulation of protein-containing complex assembly; NAS:ParkinsonsUK-UCL.
DR GO; GO:0046677; P:response to antibiotic; ISS:AgBase.
DR GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
DR GO; GO:0009409; P:response to cold; ISS:AgBase.
DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR GO; GO:0009408; P:response to heat; ISS:AgBase.
DR GO; GO:0009651; P:response to salt stress; IEA:Ensembl.
DR GO; GO:0006986; P:response to unfolded protein; NAS:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0003009; P:skeletal muscle contraction; IEA:Ensembl.
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 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; Cytoplasm; Direct protein sequencing;
KW Host-virus interaction; Hydrolase; Membrane; Mitochondrion;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW S-nitrosylation; Stress response; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2492519"
FT CHAIN 2..732
FT /note="Heat shock protein HSP 90-alpha"
FT /id="PRO_0000062911"
FT REGION 9..236
FT /note="Interaction with NR3C1"
FT /evidence="ECO:0000250|UniProtKB:P07901"
FT REGION 225..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..616
FT /note="Interaction with NR3C1"
FT /evidence="ECO:0000250|UniProtKB:P07901"
FT REGION 284..732
FT /note="Interaction with FLCN and FNIP1"
FT /evidence="ECO:0000269|PubMed:27353360"
FT REGION 284..620
FT /note="Interaction with FNIP2 and TSC1"
FT /evidence="ECO:0000269|PubMed:27353360,
FT ECO:0000269|PubMed:29127155"
FT REGION 628..731
FT /note="Interaction with NR1D1"
FT /evidence="ECO:0000250|UniProtKB:P07901"
FT REGION 682..732
FT /note="Required for homodimerization"
FT /evidence="ECO:0000269|PubMed:8289821"
FT REGION 700..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..732
FT /note="Essential for interaction with SMYD3, TSC1 and
FT STIP1/HOP"
FT /evidence="ECO:0000269|PubMed:25738358,
FT ECO:0000269|PubMed:29127155"
FT REGION 729..732
FT /note="Essential for interaction with SGTA and TTC1"
FT /evidence="ECO:0000269|PubMed:15708368"
FT MOTIF 723..732
FT /note="TPR repeat-binding"
FT /evidence="ECO:0000269|PubMed:16307917"
FT COMPBIAS 243..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 400
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 5
FT /note="Phosphothreonine; by PRKDC"
FT /evidence="ECO:0000269|PubMed:2507541"
FT MOD_RES 7
FT /note="Phosphothreonine; by PRKDC"
FT /evidence="ECO:0000269|PubMed:2507541"
FT MOD_RES 58
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07901"
FT MOD_RES 84
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07901"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2492519,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2492519,
FT ECO:0007744|PubMed:16807684, ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:23186163"
FT MOD_RES 313
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P07901"
FT MOD_RES 443
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P82995"
FT MOD_RES 458
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 489
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 492
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P07901"
FT MOD_RES 585
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 598
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000269|PubMed:15937123"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1
FT /note="M -> MPPCSGGDGSTPPGPSLRDRDCPAQSAEYPRDRLDPRPGSPSEASSP
FT PFLRSRAPVNWYQEKAQVFLWHLMVSGSTTLLCLWKQPFHVSAFPVTASLAFRQSQGAG
FT QHLYKDLQPFILLRLLM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:16269234"
FT /id="VSP_026604"
FT MUTAGEN 47
FT /note="E->A: Strong ATP-binding. Strong interaction with
FT HSF1, HIF1A, ERBB2, MET, KEAP1 and RHOBTB2. No effect on
FT interaction with TSC1."
FT /evidence="ECO:0000269|PubMed:26517842,
FT ECO:0000269|PubMed:29127155"
FT MUTAGEN 93
FT /note="D->A: Impaired ATP-binding. Strong interaction with
FT HIF1A, MET, KEAP1 and RHOBTB2. Loss of interaction with
FT HSF1 and ERBB2. Los of interaction with TSC1."
FT /evidence="ECO:0000269|PubMed:26517842,
FT ECO:0000269|PubMed:29127155"
FT MUTAGEN 97
FT /note="G->D: Abolishes ATPase activity."
FT /evidence="ECO:0000269|PubMed:18256191"
FT MUTAGEN 313
FT /note="Y->E: Loss of interaction with TSC1 and increases
FT interacrion with AHSA1."
FT /evidence="ECO:0000269|PubMed:29127155"
FT MUTAGEN 313
FT /note="Y->F: No deffect on the interaction with TSC1."
FT /evidence="ECO:0000269|PubMed:29127155"
FT MUTAGEN 598
FT /note="C->A,N,D: Reduces ATPase activity and client protein
FT activation."
FT /evidence="ECO:0000269|PubMed:15937123,
FT ECO:0000269|PubMed:19696785"
FT MUTAGEN 598
FT /note="C->S: Loss of S-nitrosylation."
FT /evidence="ECO:0000269|PubMed:15937123,
FT ECO:0000269|PubMed:19696785"
FT MUTAGEN 728..732
FT /note="MEEVD->AAAA: Loss of interaction with TOMM70. No
FT effect on interaction with IRF3."
FT /evidence="ECO:0000269|PubMed:25609812"
FT MUTAGEN 728..732
FT /note="Missing: Loss of interaction with TSC1."
FT /evidence="ECO:0000269|PubMed:29127155"
FT MUTAGEN 729..732
FT /note="Missing: Loss of interaction with TOMM70."
FT /evidence="ECO:0000269|PubMed:20628368"
FT MUTAGEN 731..732
FT /note="VD->AA: Loss of interaction with TOMM70. No effect
FT on interaction with IRF3."
FT /evidence="ECO:0000269|PubMed:20628368,
FT ECO:0000269|PubMed:25609812"
FT CONFLICT 63
FT /note="S -> T (in Ref. 1; CAA33259)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="K -> R (in Ref. 4; CAI64495 and 6; BAG51711)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="D -> G (in Ref. 4; CAI64495 and 6; BAG51711)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="W -> D (in Ref. 15; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 2..5
FT /evidence="ECO:0007829|PDB:6GQS"
FT STRAND 18..21
FT /evidence="ECO:0007829|PDB:5J80"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:5J80"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:6GPF"
FT HELIX 43..65
FT /evidence="ECO:0007829|PDB:5J80"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:5J80"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:5J80"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:5J80"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:5J80"
FT HELIX 100..104
FT /evidence="ECO:0007829|PDB:5J80"
FT TURN 105..108
FT /evidence="ECO:0007829|PDB:5J80"
FT HELIX 111..123
FT /evidence="ECO:0007829|PDB:5J80"
FT HELIX 128..134
FT /evidence="ECO:0007829|PDB:5J80"
FT HELIX 137..143
FT /evidence="ECO:0007829|PDB:5J80"
FT STRAND 145..153
FT /evidence="ECO:0007829|PDB:5J80"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:2WI6"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:5J80"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:5J80"
FT STRAND 181..190
FT /evidence="ECO:0007829|PDB:5J80"
FT HELIX 192..198
FT /evidence="ECO:0007829|PDB:5J80"
FT HELIX 200..210
FT /evidence="ECO:0007829|PDB:5J80"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:3VHC"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:5J80"
FT TURN 221..224
FT /evidence="ECO:0007829|PDB:3T1K"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:3T1K"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:2XJX"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:7KRJ"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:6KSQ"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:6KSQ"
FT HELIX 306..317
FT /evidence="ECO:0007829|PDB:6KSQ"
FT STRAND 324..331
FT /evidence="ECO:0007829|PDB:6KSQ"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:6KSQ"
FT STRAND 337..343
FT /evidence="ECO:0007829|PDB:6KSQ"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:6KSQ"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:6KSQ"
FT STRAND 368..372
FT /evidence="ECO:0007829|PDB:6KSQ"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:6KSQ"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:6KSQ"
FT STRAND 386..394
FT /evidence="ECO:0007829|PDB:6KSQ"
FT HELIX 400..405
FT /evidence="ECO:0007829|PDB:6KSQ"
FT HELIX 407..428
FT /evidence="ECO:0007829|PDB:6KSQ"
FT HELIX 431..451
FT /evidence="ECO:0007829|PDB:6KSQ"
FT HELIX 453..455
FT /evidence="ECO:0007829|PDB:6KSQ"
FT HELIX 456..460
FT /evidence="ECO:0007829|PDB:6KSQ"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:7KRJ"
FT TURN 468..472
FT /evidence="ECO:0007829|PDB:6KSQ"
FT HELIX 477..482
FT /evidence="ECO:0007829|PDB:6KSQ"
FT STRAND 490..495
FT /evidence="ECO:0007829|PDB:6KSQ"
FT HELIX 499..504
FT /evidence="ECO:0007829|PDB:6KSQ"
FT HELIX 506..513
FT /evidence="ECO:0007829|PDB:6KSQ"
FT STRAND 518..521
FT /evidence="ECO:0007829|PDB:6KSQ"
FT HELIX 525..532
FT /evidence="ECO:0007829|PDB:6KSQ"
FT STRAND 539..543
FT /evidence="ECO:0007829|PDB:6KSQ"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:7L7I"
FT HELIX 555..567
FT /evidence="ECO:0007829|PDB:7KRJ"
FT HELIX 569..578
FT /evidence="ECO:0007829|PDB:7KRJ"
FT TURN 579..582
FT /evidence="ECO:0007829|PDB:7KRJ"
FT STRAND 586..588
FT /evidence="ECO:0007829|PDB:7KRJ"
FT STRAND 593..595
FT /evidence="ECO:0007829|PDB:7KRJ"
FT STRAND 598..601
FT /evidence="ECO:0007829|PDB:7KRJ"
FT STRAND 603..605
FT /evidence="ECO:0007829|PDB:7KRJ"
FT HELIX 608..614
FT /evidence="ECO:0007829|PDB:7KRJ"
FT HELIX 622..624
FT /evidence="ECO:0007829|PDB:7KRJ"
FT TURN 625..629
FT /evidence="ECO:0007829|PDB:7KRJ"
FT STRAND 632..636
FT /evidence="ECO:0007829|PDB:7KRJ"
FT HELIX 641..652
FT /evidence="ECO:0007829|PDB:7KRJ"
FT HELIX 657..673
FT /evidence="ECO:0007829|PDB:7KRJ"
FT HELIX 681..695
FT /evidence="ECO:0007829|PDB:7KRJ"
FT STRAND 728..730
FT /evidence="ECO:0007829|PDB:4CGW"
FT VARIANT P07900-2:71
FT /note="M -> L (in dbSNP:rs8005905)"
FT /evidence="ECO:0000305"
FT /id="VAR_082835"
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
