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Heat shock protein HSP 90-alpha (Heat shock 86 kDa) (HSP 86) (HSP86) (Lipopolysaccharide-associated protein 2) (LAP-2) (LPS-associated protein 2) (Renal carcinoma antigen NY-REN-38)

 HS90A_HUMAN             Reviewed;         732 AA.
P07900; A8K500; B3KPJ9; Q2PP14; Q5CAQ6; Q5CAQ7; Q9BVQ5;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 5.
27-SEP-2017, entry version 228.
RecName: Full=Heat shock protein HSP 90-alpha;
AltName: Full=Heat shock 86 kDa;
Short=HSP 86;
Short=HSP86;
AltName: Full=Lipopolysaccharide-associated protein 2;
Short=LAP-2;
Short=LPS-associated protein 2;
AltName: Full=Renal carcinoma antigen NY-REN-38;
Name=HSP90AA1; Synonyms=HSP90A, HSPC1, HSPCA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Peripheral blood lymphocyte;
PubMed=2780322; DOI=10.1093/nar/17.17.7108;
Soeda E., Yokoyama K., Yamazaki M., Akaogi K., Miwa T., Imai T.;
"Nucleotide sequence of a full-length cDNA for 90 kDa heat-shock
protein from human peripheral blood lymphocytes.";
Nucleic Acids Res. 17:7108-7108(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1368637; DOI=10.1271/bbb1961.54.3163;
Yamazaki M., Tashiro H., Yokoyama K., Soeda E.;
"Molecular cloning of cDNA encoding a human heat-shock protein whose
expression is induced by adenovirus type 12 E1A in HeLa cells.";
Agric. Biol. Chem. 54:3163-3170(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=2527334; DOI=10.1128/MCB.9.6.2615;
Hickey E., Brandon S.E., Smale G., Lloyd D., Weber L.A.;
"Sequence and regulation of a gene encoding a human 89-kilodalton heat
shock protein.";
Mol. Cell. Biol. 9:2615-2626(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND NOMENCLATURE.
PubMed=16269234; DOI=10.1016/j.ygeno.2005.08.012;
Chen B., Piel W.H., Gui L., Bruford E., Monteiro A.;
"The HSP90 family of genes in the human genome: insights into their
divergence and evolution.";
Genomics 86:627-637(2005).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Placenta, and Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-312.
PubMed=2469626; DOI=10.1016/0378-1119(88)90182-5;
Hoffmann T., Hovemann B.;
"Heat-shock proteins, Hsp84 and Hsp86, of mice and men: two related
genes encode formerly identified tumour-specific transplantation
antigens.";
Gene 74:491-501(1988).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-312.
PubMed=2591742; DOI=10.1016/0378-1119(89)90408-3;
Walter T., Drabent B., Krebs H., Tomalak M., Heiss S., Benecke B.J.J.;
"Cloning and analysis of a human 86-kDa heat-shock-protein-encoding
gene.";
Gene 83:105-115(1989).
[11]
PROTEIN SEQUENCE OF 101-112; 210-224; 300-314; 328-338; 346-355;
387-400; 465-478 AND 633-647, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 185-732.
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 539-732.
TISSUE=Heart;
Tanaka M., Tanaka T., Mitsui Y., Yamamoto M., Wood J.N.;
"The analysis of the genes reactive to monoclonal antibody, CE5.";
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
[14]
PROTEIN SEQUENCE OF 2-21, AND PHOSPHORYLATION.
PubMed=2492519;
Lees-Miller S.P., Anderson C.W.;
"Two human 90-kDa heat shock proteins are phosphorylated in vivo at
conserved serines that are phosphorylated in vitro by casein kinase
II.";
J. Biol. Chem. 264:2431-2437(1989).
[15]
PROTEIN SEQUENCE OF 154-163 AND 186-191, AND INTERACTION WITH KSR1.
PubMed=10409742; DOI=10.1128/MCB.19.8.5523;
Stewart S., Sundaram M., Zhang Y., Lee J., Han M., Guan K.L.;
"Kinase suppressor of Ras forms a multiprotein signaling complex and
modulates MEK localization.";
Mol. Cell. Biol. 19:5523-5534(1999).
[16]
PROTEIN SEQUENCE OF 592-612, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS
OF CYS-598, AND S-NITROSYLATION AT CYS-598.
PubMed=15937123; DOI=10.1073/pnas.0407294102;
Martinez-Ruiz A., Villanueva L., Gonzalez de Orduna C.,
Lopez-Ferrer D., Higueras M.A., Tarin C., Rodriguez-Crespo I.,
Vazquez J., Lamas S.;
"S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and
endothelial nitric oxide synthase regulatory activities.";
Proc. Natl. Acad. Sci. U.S.A. 102:8525-8530(2005).
[17]
PHOSPHORYLATION AT THR-5 AND THR-7.
PubMed=2507541;
Lees-Miller S.P., Anderson C.W.;
"The human double-stranded DNA-activated protein kinase phosphorylates
the 90-kDa heat-shock protein, hsp90 alpha at two NH2-terminal
threonine residues.";
J. Biol. Chem. 264:17275-17280(1989).
[18]
HOMODIMERIZATION.
PubMed=8289821; DOI=10.1128/MCB.14.2.1459;
Minami Y., Kimura Y., Kawasaki H., Suzuki K., Yahara I.;
"The carboxy-terminal region of mammalian HSP90 is required for its
dimerization and function in vivo.";
Mol. Cell. Biol. 14:1459-1464(1994).
[19]
SUBUNIT.
PubMed=7588731; DOI=10.1111/j.1432-1033.1995.001_1.x;
Nemoto T., Ohara-Nemoto Y., Ota M., Takagi T., Yokoyama K.;
"Mechanism of dimer formation of the 90-kDa heat-shock protein.";
Eur. J. Biochem. 233:1-8(1995).
[20]
IDENTIFICATION IN A COMPLEX WITH NR3C1 AND FKBP4; PPID; PPP5C OR
STIP1.
PubMed=9195923; DOI=10.1074/jbc.272.26.16224;
Silverstein A.M., Galigniana M.D., Chen M.S., Owens-Grillo J.K.,
Chinkers M., Pratt W.B.;
"Protein phosphatase 5 is a major component of glucocorticoid
receptor.hsp90 complexes with properties of an FK506-binding
immunophilin.";
J. Biol. Chem. 272:16224-16230(1997).
[21]
INTERACTION WITH TOM34.
PubMed=9660753; DOI=10.1074/jbc.273.29.18007;
Young J.C., Obermann W.M., Hartl F.U.;
"Specific binding of tetratricopeptide repeat proteins to the C-
terminal 12-kDa domain of hsp90.";
J. Biol. Chem. 273:18007-18010(1998).
[22]
IDENTIFICATION AS A RENAL CANCER ANTIGEN.
TISSUE=Renal cell carcinoma;
PubMed=10508479;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
Old L.J.;
"Antigens recognized by autologous antibody in patients with renal-
cell carcinoma.";
Int. J. Cancer 83:456-464(1999).
[23]
INTERACTION WITH TERT, AND FUNCTION AS A CO-CHAPERONE IN TELOMERASE
HOLOENZYME ASSEMBLY.
PubMed=11274138; DOI=10.1074/jbc.C100055200;
Forsythe H.L., Jarvis J.L., Turner J.W., Elmore L.W., Holt S.E.;
"Stable association of hsp90 and p23, but Not hsp70, with active human
telomerase.";
J. Biol. Chem. 276:15571-15574(2001).
[24]
INTERACTION WITH HSF1.
PubMed=11583998; DOI=10.1074/jbc.M105931200;
Guo Y., Guettouche T., Fenna M., Boellmann F., Pratt W.B., Toft D.O.,
Smith D.F., Voellmy R.;
"Evidence for a mechanism of repression of heat shock factor 1
transcriptional activity by a multichaperone complex.";
J. Biol. Chem. 276:45791-45799(2001).
[25]
FUNCTION, IDENTIFICATION AS LPS RECEPTOR, INTERACTION WITH CXCR4; GDF5
AND HSPA8, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=11276205; DOI=10.1038/86342;
Triantafilou K., Triantafilou M., Dedrick R.L.;
"A CD14-independent LPS receptor cluster.";
Nat. Immunol. 2:338-345(2001).
[26]
INTERACTION WITH DNAJC7.
PubMed=12853476; DOI=10.1093/emboj/cdg362;
Brychzy A., Rein T., Winklhofer K.F., Hartl F.U., Young J.C.,
Obermann W.M.;
"Cofactor Tpr2 combines two TPR domains and a J domain to regulate the
Hsp70/Hsp90 chaperone system.";
EMBO J. 22:3613-3623(2003).
[27]
INTERACTION WITH AHSA1.
PubMed=12604615; DOI=10.1074/jbc.M212761200;
Lotz G.P., Lin H., Harst A., Obermann W.M.J.;
"Aha1 binds to the middle domain of Hsp90, contributes to client
protein activation, and stimulates the ATPase activity of the
molecular chaperone.";
J. Biol. Chem. 278:17228-17235(2003).
[28]
INTERACTION WITH SMYD3.
PubMed=15235609; DOI=10.1038/ncb1151;
Hamamoto R., Furukawa Y., Morita M., Iimura Y., Silva F.P., Li M.,
Yagyu R., Nakamura Y.;
"SMYD3 encodes a histone methyltransferase involved in the
proliferation of cancer cells.";
Nat. Cell Biol. 6:731-740(2004).
[29]
INTERACTION WITH SGTA AND TTC1.
PubMed=15708368; DOI=10.1016/j.abb.2004.12.020;
Liou S.T., Wang C.;
"Small glutamine-rich tetratricopeptide repeat-containing protein is
composed of three structural units with distinct functions.";
Arch. Biochem. Biophys. 435:253-263(2005).
[30]
INTERACTION WITH PPP5C, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=15383005; DOI=10.1042/BJ20040690;
Zeke T., Morrice N., Vazquez-Martin C., Cohen P.T.;
"Human protein phosphatase 5 dissociates from heat-shock proteins and
is proteolytically activated in response to arachidonic acid and the
microtubule-depolymerizing drug nocodazole.";
Biochem. J. 385:45-56(2005).
[31]
FUNCTION, AND INTERACTION WITH PPP5C.
PubMed=15577939; DOI=10.1038/sj.emboj.7600496;
Yang J., Roe S.M., Cliff M.J., Williams M.A., Ladbury J.E.,
Cohen P.T., Barford D.;
"Molecular basis for TPR domain-mediated regulation of protein
phosphatase 5.";
EMBO J. 24:1-10(2005).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 AND SER-263, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Pituitary;
PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
"Phosphoproteomic analysis of the human pituitary.";
Pituitary 9:109-120(2006).
[34]
INTERACTION WITH PPP5C.
PubMed=16531226; DOI=10.1016/j.str.2005.12.009;
Cliff M.J., Harris R., Barford D., Ladbury J.E., Williams M.A.;
"Conformational diversity in the TPR domain-mediated interaction of
protein phosphatase 5 with Hsp90.";
Structure 14:415-426(2006).
[35]
SUBUNIT, ENZYME REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=18400751; DOI=10.1074/jbc.M800540200;
Richter K., Soroka J., Skalniak L., Leskovar A., Hessling M.,
Reinstein J., Buchner J.;
"Conserved conformational changes in the ATPase cycle of human
Hsp90.";
J. Biol. Chem. 283:17757-17765(2008).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252 AND SER-263, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[40]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 AND SER-263, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[41]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[42]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[43]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-443; LYS-458; LYS-489 AND
LYS-585, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[44]
INTERACTION WITH CHORDC1.
PubMed=19875381; DOI=10.1074/mcp.M900261-MCP200;
Gano J.J., Simon J.A.;
"A proteomic investigation of ligand-dependent HSP90 complexes reveals
CHORDC1 as a novel ADP-dependent HSP90-interacting protein.";
Mol. Cell. Proteomics 9:255-270(2010).
[45]
ISGYLATION.
PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
"Proteomic identification of proteins conjugated to ISG15 in mouse and
human cells.";
Biochem. Biophys. Res. Commun. 336:496-506(2005).
[46]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[47]
INTERACTION WITH FNIP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17028174; DOI=10.1073/pnas.0603781103;
Baba M., Hong S.-B., Sharma N., Warren M.B., Nickerson M.L.,
Iwamatsu A., Esposito D., Gillette W.K., Hopkins R.F. III,
Hartley J.L., Furihata M., Oishi S., Zhen W., Burke T.R. Jr.,
Linehan W.M., Schmidt L.S., Zbar B.;
"Folliculin encoded by the BHD gene interacts with a binding protein,
FNIP1, and AMPK, and is involved in AMPK and mTOR signaling.";
Proc. Natl. Acad. Sci. U.S.A. 103:15552-15557(2006).
[48]
MUTAGENESIS OF GLY-97.
PubMed=18256191; DOI=10.1242/dev.018150;
Hawkins T.A., Haramis A.P., Etard C., Prodromou C., Vaughan C.K.,
Ashworth R., Ray S., Behra M., Holder N., Talbot W.S., Pearl L.H.,
Strahle U., Wilson S.W.;
"The ATPase-dependent chaperoning activity of Hsp90a regulates thick
filament formation and integration during skeletal muscle
myofibrillogenesis.";
Development 135:1147-1156(2008).
[49]
MUTAGENESIS OF CYS-598.
PubMed=19696785; DOI=10.1038/embor.2009.153;
Retzlaff M., Stahl M., Eberl H.C., Lagleder S., Beck J., Kessler H.,
Buchner J.;
"Hsp90 is regulated by a switch point in the C-terminal domain.";
EMBO Rep. 10:1147-1153(2009).
[50]
INTERACTION WITH HSP90AB1.
PubMed=20353823; DOI=10.1016/j.cellsig.2010.03.012;
Cheng M.B., Zhang Y., Zhong X., Sutter B., Cao C.Y., Chen X.S.,
Cheng X.K., Zhang Y., Xiao L., Shen Y.F.;
"Stat1 mediates an auto-regulation of hsp90beta gene in heat shock
response.";
Cell. Signal. 22:1206-1213(2010).
[51]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[52]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[53]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[54]
INTERACTION WITH CDC37.
PubMed=23569206; DOI=10.1074/jbc.M112.439257;
Eckl J.M., Rutz D.A., Haslbeck V., Zierer B.K., Reinstein J.,
Richter K.;
"Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein
90) motility by interaction with N-terminal and middle domain binding
sites.";
J. Biol. Chem. 288:16032-16042(2013).
[55]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231; SER-252; SER-263;
SER-476 AND SER-641, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[56]
FUNCTION, AND INTERACTION WITH STUB1 AND SMAD3.
PubMed=24613385; DOI=10.1016/j.bbrc.2014.02.124;
Shang Y., Xu X., Duan X., Guo J., Wang Y., Ren F., He D., Chang Z.;
"Hsp70 and Hsp90 oppositely regulate TGF-beta signaling through
CHIP/Stub1.";
Biochem. Biophys. Res. Commun. 446:387-392(2014).
[57]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[58]
INTERACTION WITH NWD1.
PubMed=24681825;
Correa R.G., Krajewska M., Ware C.F., Gerlic M., Reed J.C.;
"The NLR-related protein NWD1 is associated with prostate cancer and
modulates androgen receptor signaling.";
Oncotarget 5:1666-1682(2014).
[59]
REVIEW.
PubMed=25973397; DOI=10.3389/fonc.2015.00100;
Khurana N., Bhattacharyya S.;
"Hsp90, the concertmaster: tuning transcription.";
Front. Oncol. 5:100-100(2015).
[60]
INTERACTION WITH SMYD3.
PubMed=25738358; DOI=10.18632/oncotarget.2970;
Brown M.A., Foreman K., Harriss J., Das C., Zhu L., Edwards M.,
Shaaban S., Tucker H.;
"C-terminal domain of SMYD3 serves as a unique HSP90-regulated motif
in oncogenesis.";
Oncotarget 6:4005-4019(2015).
[61]
INTERACTION WITH HSF1; HIF1A; ERBB2; MET; KEAP1 AND RHOBTB2, AND
MUTAGENESIS OF GLU-47 AND ASP-93.
PubMed=26517842; DOI=10.1371/journal.pone.0141786;
Prince T.L., Kijima T., Tatokoro M., Lee S., Tsutsumi S., Yim K.,
Rivas C., Alarcon S., Schwartz H., Khamit-Kush K., Scroggins B.T.,
Beebe K., Trepel J.B., Neckers L.;
"Client proteins and small molecule inhibitors display distinct
binding preferences for constitutive and stress-induced HSP90 isoforms
and their conformationally restricted mutants.";
PLoS ONE 10:E0141786-E0141786(2015).
[62]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[63]
REVIEW.
PubMed=27295069; DOI=10.1016/j.biochi.2016.05.018;
Verma S., Goyal S., Jamal S., Singh A., Grover A.;
"Hsp90: Friends, clients and natural foes.";
Biochimie 127:227-240(2016).
[64]
REVIEW.
PubMed=26991466; DOI=10.1002/bip.22835;
Pearl L.H.;
"Review: The HSP90 molecular chaperone-an enigmatic ATPase.";
Biopolymers 105:594-607(2016).
[65]
FUNCTION, AND INTERACTION WITH FLCN; AHSA1; HSP70; CDC37; FNIP1;
FNIP2; STUB1; STIP1; PTGES3 AND PPP5C.
PubMed=27353360; DOI=10.1038/ncomms12037;
Woodford M.R., Dunn D.M., Blanden A.R., Capriotti D., Loiselle D.,
Prodromou C., Panaretou B., Hughes P.F., Smith A., Ackerman W.,
Haystead T.A., Loh S.N., Bourboulia D., Schmidt L.S.,
Marston Linehan W., Bratslavsky G., Mollapour M.;
"The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and
enhance drug binding.";
Nat. Commun. 7:12037-12037(2016).
[66]
INTERACTION WITH HSF1.
PubMed=26754925; DOI=10.1038/srep19174;
Asano Y., Kawase T., Okabe A., Tsutsumi S., Ichikawa H., Tatebe S.,
Kitabayashi I., Tashiro F., Namiki H., Kondo T., Semba K.,
Aburatani H., Taya Y., Nakagama H., Ohki R.;
"IER5 generates a novel hypo-phosphorylated active form of HSF1 and
contributes to tumorigenesis.";
Sci. Rep. 6:19174-19174(2016).
[67]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 11-223 IN COMPLEX WITH
GELDANAMYCIN.
PubMed=9108479; DOI=10.1016/S0092-8674(00)80203-2;
Stebbins C.E., Russo A.A., Schneider C., Rosen N., Hartl F.U.,
Pavletich N.P.;
"Crystal structure of an Hsp90-geldanamycin complex: targeting of a
protein chaperone by an antitumor agent.";
Cell 89:239-250(1997).
[68]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 11-223 IN COMPLEX WITH ADP,
CATALYTIC ACTIVITY, AND INTERACTION WITH PTGES3.
PubMed=9817749; DOI=10.1083/jcb.143.4.901;
Obermann W.M., Sondermann H., Russo A.A., Pavletich N.P., Hartl F.U.;
"In vivo function of Hsp90 is dependent on ATP binding and ATP
hydrolysis.";
J. Cell Biol. 143:901-910(1998).
[69]
X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 724-732 IN COMPLEX WITH
STUB1, INTERACTION WITH STUB1 AND UBE2N, AND MOTIF TPR REPEAT-BINDING.
PubMed=16307917; DOI=10.1016/j.molcel.2005.09.023;
Zhang M., Windheim M., Roe S.M., Peggie M., Cohen P., Prodromou C.,
Pearl L.H.;
"Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3
ubiquitin ligase and a CHIP-Ubc13-Uev1a complex.";
Mol. Cell 20:525-538(2005).
-!- FUNCTION: Molecular chaperone that promotes the maturation,
structural maintenance and proper regulation of specific target
proteins involved for instance in cell cycle control and signal
transduction. Undergoes a functional cycle that is linked to its
ATPase activity which is essential for its chaperone activity.
This cycle probably induces conformational changes in the client
proteins, thereby causing their activation. Interacts dynamically
with various co-chaperones that modulate its substrate
recognition, ATPase cycle and chaperone function (PubMed:11274138,
PubMed:15577939, PubMed:15937123, PubMed:27353360). Engages with a
range of client protein classes via its interaction with various
co-chaperone proteins or complexes, that act as adapters,
simultaneously able to interact with the specific client and the
central chaperone itself. Recruitment of ATP and co-chaperone
followed by client protein forms a functional chaperone. After the
completion of the chaperoning process, properly folded client
protein and co-chaperone leave HSP90 in an ADP-bound partially
open conformation and finally, ADP is released from HSP90 which
acquires an open conformation for the next cycle (PubMed:27295069,
PubMed:26991466). Apart from its chaperone activity, it also plays
a role in the regulation of the transcription machinery. HSP90 and
its co-chaperones modulate transcription at least at three
different levels. In the first place, they alter the steady-state
levels of certain transcription factors in response to various
physiological cues. Second, they modulate the activity of certain
epigenetic modifiers, such as histone deacetylases or DNA methyl
transferases, and thereby respond to the change in the
environment. Third, they participate in the eviction of histones
from the promoter region of certain genes and thereby turn on gene
expression (PubMed:25973397). Binds bacterial lipopolysaccharide
(LPS) and mediates LPS-induced inflammatory response, including
TNF secretion by monocytes (PubMed:11276205). Antagonizes STUB1-
mediated inhibition of TGF-beta signaling via inhibition of STUB1-
mediated SMAD3 ubiquitination and degradation (PubMed:24613385).
{ECO:0000269|PubMed:11274138, ECO:0000269|PubMed:11276205,
ECO:0000269|PubMed:15577939, ECO:0000269|PubMed:15937123,
ECO:0000269|PubMed:24613385, ECO:0000269|PubMed:27353360,
ECO:0000303|PubMed:25973397, ECO:0000303|PubMed:26991466,
ECO:0000303|PubMed:27295069}.
-!- ENZYME REGULATION: In the resting state, through the dimerization
of its C-terminal domain, HSP90 forms a homodimer which is defined
as the open conformation. Upon ATP-binding, the N-terminal domain
undergoes significant conformational changes and comes in contact
to form an active closed conformation. After HSP90 finishes its
chaperoning tasks of assisting the proper folding, stabilization
and activation of client proteins under the active state, ATP
molecule is hydrolyzed to ADP which then dissociates from HSP90
and directs the protein back to the resting state.
{ECO:0000269|PubMed:18400751}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=300 uM for ATP {ECO:0000269|PubMed:18400751};
-!- SUBUNIT: Homodimer (PubMed:7588731, PubMed:8289821,
PubMed:18400751). Identified in NR3C1/GCR steroid receptor-
chaperone complexes formed at least by NR3C1, HSP90AA1 and a
variety of proteins containing TPR repeats such as FKBP4, FKBP5,
PPID, PPP5C or STIP1 (PubMed:15383005, PubMed:9195923). Interacts
with TOM34 (PubMed:9660753). Interacts with TERT; the interaction,
together with PTGES3, is required for correct assembly and
stabilization of the TERT holoenzyme complex (PubMed:11274138,
PubMed:9817749). Interacts with CHORDC1 and DNAJC7
(PubMed:12853476, PubMed:19875381). Interacts with STUB1 and
UBE2N; may couple the chaperone and ubiquitination systems
(PubMed:16307917, PubMed:27353360). Interacts (via TPR repeat-
binding motif) with PPP5C (via TPR repeats); the interaction is
direct and activates PPP5C phosphatase activity (PubMed:15383005,
PubMed:15577939, PubMed:16531226, PubMed:27353360). Following LPS
binding, may form a complex with CXCR4, GDF5 and HSPA8
(PubMed:11276205). Interacts with KSR1 (PubMed:10409742).
Interacts with co-chaperone CDC37 (via C-terminus); the
interaction inhibits HSP90AA1 ATPase activity (PubMed:23569206,
PubMed:27353360). May interact with NWD1 (PubMed:24681825).
Interacts with FNIP1 and FNIP2; the interaction inhibits HSP90AA1
ATPase activity (PubMed:17028174, PubMed:27353360). Interacts with
AHSA1; the interaction activates HSP90AA1 ATPase activity
(PubMed:12604615, PubMed:27353360). Interacts with FLCN in the
presence of FNIP1. Interacts with HSP70, STIP1 and PTGES3
(PubMed:27353360). Interacts with SMYD3; this interaction enhances
SMYD3 histone-lysine N-methyltransferase (PubMed:15235609,
PubMed:25738358). Interacts with SGTA (via TPR repeats)
(PubMed:15708368). Interacts with TTC1 (via TPR repeats)
(PubMed:15708368). Interacts with HSF1 in an ATP-dependent manner
(PubMed:11583998. PubMed:26517842). Interacts with MET; the
interaction suppresses MET kinase activity. Interacts with ERBB2
in an ATP-dependent manner; the interaction suppresses ERBB2
kinase activity. Interacts with HIF1A, KEAP1 and RHOBTB2
(PubMed:26517842). Interacts with HSF1; this interaction is
decreased in a IER5-dependent manner, promoting HSF1 accumulation
in the nucleus, homotrimerization and DNA-binding activities
(PubMed:26754925). Interacts with STUB1 and SMAD3
(PubMed:24613385). Interacts with HSP90AB1; interaction is
constitutive (PubMed:20353823). {ECO:0000269|PubMed:10409742,
ECO:0000269|PubMed:11274138, ECO:0000269|PubMed:11276205,
ECO:0000269|PubMed:11583998, ECO:0000269|PubMed:12604615,
ECO:0000269|PubMed:12853476, ECO:0000269|PubMed:15235609,
ECO:0000269|PubMed:15383005, ECO:0000269|PubMed:15577939,
ECO:0000269|PubMed:15708368, ECO:0000269|PubMed:16307917,
ECO:0000269|PubMed:16531226, ECO:0000269|PubMed:17028174,
ECO:0000269|PubMed:18400751, ECO:0000269|PubMed:19875381,
ECO:0000269|PubMed:20353823, ECO:0000269|PubMed:23569206,
ECO:0000269|PubMed:24613385, ECO:0000269|PubMed:24681825,
ECO:0000269|PubMed:25738358, ECO:0000269|PubMed:26517842,
ECO:0000269|PubMed:26754925, ECO:0000269|PubMed:27353360,
ECO:0000269|PubMed:7588731, ECO:0000269|PubMed:8289821,
ECO:0000269|PubMed:9195923, ECO:0000269|PubMed:9660753,
ECO:0000269|PubMed:9817749}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-296047, EBI-296047;
O95433:AHSA1; NbExp=4; IntAct=EBI-296047, EBI-448610;
Q8IWD4:CCDC117; NbExp=5; IntAct=EBI-296047, EBI-3387963;
Q16543:CDC37; NbExp=14; IntAct=EBI-296047, EBI-295634;
Q7L3B6:CDC37L1; NbExp=2; IntAct=EBI-296047, EBI-2841876;
P50750:CDK9; NbExp=2; IntAct=EBI-296047, EBI-1383449;
Q96G23:CERS2; NbExp=2; IntAct=EBI-296047, EBI-1057080;
Q9UHD1:CHORDC1; NbExp=8; IntAct=EBI-296047, EBI-2550959;
Q9D1P4:Chordc1 (xeno); NbExp=3; IntAct=EBI-296047, EBI-7448218;
O15111:CHUK; NbExp=3; IntAct=EBI-296047, EBI-81249;
P00533:EGFR; NbExp=5; IntAct=EBI-296047, EBI-297353;
P07814:EPRS; NbExp=2; IntAct=EBI-296047, EBI-355315;
P04626:ERBB2; NbExp=4; IntAct=EBI-296047, EBI-641062;
Q02790:FKBP4; NbExp=8; IntAct=EBI-296047, EBI-1047444;
Q14318:FKBP8; NbExp=7; IntAct=EBI-296047, EBI-724839;
Q6PK50:HSP90AB1; NbExp=2; IntAct=EBI-296047, EBI-9356629;
Q9Y6K9:IKBKG; NbExp=3; IntAct=EBI-296047, EBI-81279;
P05412:JUN; NbExp=4; IntAct=EBI-296047, EBI-852823;
Q6VAB6:KSR2; NbExp=5; IntAct=EBI-296047, EBI-6424389;
O43318-2:MAP3K7; NbExp=5; IntAct=EBI-296047, EBI-358700;
Q9Y239:NOD1; NbExp=2; IntAct=EBI-296047, EBI-1051262;
P04150:NR3C1; NbExp=7; IntAct=EBI-296047, EBI-493507;
P26882:PPID (xeno); NbExp=4; IntAct=EBI-296047, EBI-6477155;
P53041:PPP5C; NbExp=11; IntAct=EBI-296047, EBI-716663;
Q15185:PTGES3; NbExp=6; IntAct=EBI-296047, EBI-1049387;
Q9H6T3:RPAP3; NbExp=3; IntAct=EBI-296047, EBI-356928;
P61247:RPS3A; NbExp=3; IntAct=EBI-296047, EBI-352378;
P35467:S100a1 (xeno); NbExp=4; IntAct=EBI-296047, EBI-6477109;
Q15831:STK11; NbExp=2; IntAct=EBI-296047, EBI-306838;
Q9UNE7:STUB1; NbExp=9; IntAct=EBI-296047, EBI-357085;
Q15750:TAB1; NbExp=2; IntAct=EBI-296047, EBI-358643;
Q9NYJ8:TAB2; NbExp=2; IntAct=EBI-296047, EBI-358708;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P07901}.
Melanosome {ECO:0000269|PubMed:17081065}. Cell membrane
{ECO:0000269|PubMed:11276205}. Note=Identified by mass
spectrometry in melanosome fractions from stage I to stage IV.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=HSP90AA1-1, HSP90-alpha 2;
IsoId=P07900-1; Sequence=Displayed;
Name=2; Synonyms=HSP90AA1-2;
IsoId=P07900-2; Sequence=VSP_026604;
Note=Variant in position: 71:M->L (in dbSNP:rs8005905).;
-!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
repeat-containing proteins like the co-chaperone STUB1.
{ECO:0000269|PubMed:16307917}.
-!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
-!- PTM: S-nitrosylated; negatively regulates the ATPase activity and
the activation of eNOS by HSP90AA1. {ECO:0000269|PubMed:15937123}.
-!- SIMILARITY: Belongs to the heat shock protein 90 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X15183; CAA33259.1; -; mRNA.
EMBL; M27024; AAA63194.1; -; Genomic_DNA.
EMBL; AJ890082; CAI64495.1; -; mRNA.
EMBL; AJ890083; CAI64496.1; -; mRNA.
EMBL; DQ314871; ABC40730.1; -; Genomic_DNA.
EMBL; AK056446; BAG51711.1; -; mRNA.
EMBL; AK291115; BAF83804.1; -; mRNA.
EMBL; AK291607; BAF84296.1; -; mRNA.
EMBL; AL133223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471061; EAW81765.1; -; Genomic_DNA.
EMBL; X07270; CAA30255.1; -; mRNA.
EMBL; M30626; AAA36023.1; -; Genomic_DNA.
EMBL; BC000987; AAH00987.1; -; mRNA.
EMBL; BC121062; AAI21063.1; -; mRNA.
EMBL; D87666; BAA13430.1; -; mRNA.
EMBL; D87666; BAA13431.1; -; mRNA.
CCDS; CCDS32160.1; -. [P07900-2]
CCDS; CCDS9967.1; -. [P07900-1]
PIR; A32319; HHHU86.
RefSeq; NP_001017963.2; NM_001017963.2. [P07900-2]
RefSeq; NP_005339.3; NM_005348.3. [P07900-1]
UniGene; Hs.525600; -.
PDB; 1BYQ; X-ray; 1.50 A; A=9-236.
PDB; 1OSF; X-ray; 1.75 A; A=9-223.
PDB; 1UY6; X-ray; 1.90 A; A=2-236.
PDB; 1UY7; X-ray; 1.90 A; A=2-236.
PDB; 1UY8; X-ray; 1.98 A; A=2-236.
PDB; 1UY9; X-ray; 2.00 A; A=2-236.
PDB; 1UYC; X-ray; 2.00 A; A=2-236.
PDB; 1UYD; X-ray; 2.20 A; A=2-236.
PDB; 1UYE; X-ray; 2.00 A; A=2-236.
PDB; 1UYF; X-ray; 2.00 A; A=2-236.
PDB; 1UYG; X-ray; 2.00 A; A=2-236.
PDB; 1UYH; X-ray; 2.20 A; A=2-236.
PDB; 1UYI; X-ray; 2.20 A; A=2-236.
PDB; 1UYK; X-ray; 2.20 A; A=2-236.
PDB; 1UYL; X-ray; 1.40 A; A=2-236.
PDB; 1YC1; X-ray; 1.70 A; A=9-236.
PDB; 1YC3; X-ray; 2.12 A; A=9-236.
PDB; 1YC4; X-ray; 1.81 A; A=9-236.
PDB; 1YER; X-ray; 1.65 A; A=9-236.
PDB; 1YES; X-ray; 2.20 A; A=9-236.
PDB; 1YET; X-ray; 1.90 A; A=9-236.
PDB; 2BSM; X-ray; 2.05 A; A=2-236.
PDB; 2BT0; X-ray; 1.90 A; A/B=2-236.
PDB; 2BUG; NMR; -; B=728-732.
PDB; 2BYH; X-ray; 1.90 A; A=11-236.
PDB; 2BYI; X-ray; 1.60 A; A=11-236.
PDB; 2BZ5; X-ray; 1.90 A; A/B=2-236.
PDB; 2C2L; X-ray; 3.30 A; E/F/G/H=724-732.
PDB; 2CCS; X-ray; 1.79 A; A=1-236.
PDB; 2CCT; X-ray; 2.30 A; A=1-236.
PDB; 2CCU; X-ray; 2.70 A; A=1-236.
PDB; 2FWY; X-ray; 2.10 A; A=1-236.
PDB; 2FWZ; X-ray; 2.10 A; A=1-236.
PDB; 2H55; X-ray; 2.00 A; A=1-236.
PDB; 2JJC; X-ray; 1.95 A; A=9-223.
PDB; 2K5B; NMR; -; A=14-223.
PDB; 2QF6; X-ray; 3.10 A; A/B/C/D=17-223.
PDB; 2QFO; X-ray; 1.68 A; A/B=17-223.
PDB; 2QG0; X-ray; 1.85 A; A/B=17-223.
PDB; 2QG2; X-ray; 1.80 A; A=17-223.
PDB; 2UWD; X-ray; 1.90 A; A=2-236.
PDB; 2VCI; X-ray; 2.00 A; A=1-236.
PDB; 2VCJ; X-ray; 2.50 A; A=1-236.
PDB; 2WI1; X-ray; 2.30 A; A=1-236.
PDB; 2WI2; X-ray; 2.09 A; A/B=1-236.
PDB; 2WI3; X-ray; 1.90 A; A=1-236.
PDB; 2WI4; X-ray; 2.40 A; A=1-236.
PDB; 2WI5; X-ray; 2.10 A; A=1-236.
PDB; 2WI6; X-ray; 2.18 A; A=1-236.
PDB; 2WI7; X-ray; 2.50 A; A=1-236.
PDB; 2XAB; X-ray; 1.90 A; A/B=9-236.
PDB; 2XDK; X-ray; 1.97 A; A=9-236.
PDB; 2XDL; X-ray; 1.98 A; A=9-236.
PDB; 2XDS; X-ray; 1.97 A; A=9-236.
PDB; 2XDU; X-ray; 1.74 A; A=14-224.
PDB; 2XDX; X-ray; 2.42 A; A=9-236.
PDB; 2XHR; X-ray; 2.20 A; A=9-236.
PDB; 2XHT; X-ray; 2.27 A; A=9-236.
PDB; 2XHX; X-ray; 2.80 A; A=9-236.
PDB; 2XJG; X-ray; 2.25 A; A=9-236.
PDB; 2XJJ; X-ray; 1.90 A; A/B=9-236.
PDB; 2XJX; X-ray; 1.66 A; A=9-236.
PDB; 2XK2; X-ray; 1.95 A; A=9-236.
PDB; 2YE2; X-ray; 1.90 A; A=9-236.
PDB; 2YE3; X-ray; 1.95 A; A=9-236.
PDB; 2YE4; X-ray; 2.30 A; A=9-236.
PDB; 2YE5; X-ray; 1.73 A; A=9-236.
PDB; 2YE6; X-ray; 2.56 A; A=9-236.
PDB; 2YE7; X-ray; 2.20 A; A=9-236.
PDB; 2YE8; X-ray; 2.30 A; A=9-236.
PDB; 2YE9; X-ray; 2.20 A; A=9-236.
PDB; 2YEA; X-ray; 1.73 A; A=9-236.
PDB; 2YEB; X-ray; 2.40 A; A=9-236.
PDB; 2YEC; X-ray; 2.10 A; A=9-236.
PDB; 2YED; X-ray; 2.10 A; A=9-236.
PDB; 2YEE; X-ray; 2.30 A; A=9-236.
PDB; 2YEF; X-ray; 1.55 A; A=9-236.
PDB; 2YEG; X-ray; 2.50 A; A/B=9-236.
PDB; 2YEH; X-ray; 2.10 A; A=9-236.
PDB; 2YEI; X-ray; 2.20 A; A=9-236.
PDB; 2YEJ; X-ray; 2.20 A; A=9-236.
PDB; 2YI0; X-ray; 1.60 A; A=1-229.
PDB; 2YI5; X-ray; 2.50 A; A=1-229.
PDB; 2YI6; X-ray; 1.80 A; A=1-229.
PDB; 2YI7; X-ray; 1.40 A; A=1-229.
PDB; 2YJW; X-ray; 1.61 A; A=18-223.
PDB; 2YJX; X-ray; 1.83 A; A=18-223.
PDB; 2YK2; X-ray; 1.74 A; A=18-223.
PDB; 2YK9; X-ray; 1.32 A; A=18-223.
PDB; 2YKB; X-ray; 1.93 A; A=18-223.
PDB; 2YKC; X-ray; 1.67 A; A=18-223.
PDB; 2YKE; X-ray; 1.43 A; A=18-223.
PDB; 2YKI; X-ray; 1.67 A; A=18-223.
PDB; 2YKJ; X-ray; 1.46 A; A=18-223.
PDB; 3B24; X-ray; 1.70 A; A/B=9-236.
PDB; 3B25; X-ray; 1.75 A; A=9-236.
PDB; 3B26; X-ray; 2.10 A; A/B=9-236.
PDB; 3B27; X-ray; 1.50 A; A=9-236.
PDB; 3B28; X-ray; 1.35 A; A/B=9-236.
PDB; 3BM9; X-ray; 1.60 A; A=14-236.
PDB; 3BMY; X-ray; 1.60 A; A=14-236.
PDB; 3D0B; X-ray; 1.74 A; A=1-232.
PDB; 3EKO; X-ray; 1.55 A; A/B=9-225.
PDB; 3EKR; X-ray; 2.00 A; A/B=9-225.
PDB; 3FT5; X-ray; 1.90 A; A=9-236.
PDB; 3FT8; X-ray; 2.00 A; A=9-236.
PDB; 3HEK; X-ray; 1.95 A; A/B=9-225.
PDB; 3HHU; X-ray; 1.59 A; A/B=1-224.
PDB; 3HYY; X-ray; 1.90 A; A=9-236.
PDB; 3HYZ; X-ray; 2.30 A; A/B=9-236.
PDB; 3HZ1; X-ray; 2.30 A; A=9-236.
PDB; 3HZ5; X-ray; 1.90 A; A=9-236.
PDB; 3INW; X-ray; 1.95 A; A=10-236.
PDB; 3INX; X-ray; 1.75 A; A=10-236.
PDB; 3K97; X-ray; 1.95 A; A=9-236.
PDB; 3K98; X-ray; 2.40 A; A/B=9-225.
PDB; 3K99; X-ray; 2.10 A; A/B/C/D=9-225.
PDB; 3MNR; X-ray; 1.90 A; P=1-232.
PDB; 3O0I; X-ray; 1.47 A; A=1-236.
PDB; 3OW6; X-ray; 1.80 A; A=17-223.
PDB; 3OWB; X-ray; 2.05 A; A=17-223.
PDB; 3OWD; X-ray; 1.63 A; A=17-223.
PDB; 3Q6M; X-ray; 3.00 A; A/B/C=293-732.
PDB; 3Q6N; X-ray; 3.05 A; A/B/C/D/E/F=293-732.
PDB; 3QDD; X-ray; 1.79 A; A=1-236.
PDB; 3QTF; X-ray; 1.57 A; A=14-236.
PDB; 3R4M; X-ray; 1.70 A; A=9-236.
PDB; 3R4N; X-ray; 2.00 A; A/B=9-225.
PDB; 3R4O; X-ray; 2.65 A; A/B=9-225.
PDB; 3R4P; X-ray; 1.70 A; A/B=9-225.
PDB; 3R91; X-ray; 1.58 A; A=14-236.
PDB; 3R92; X-ray; 1.58 A; A=14-236.
PDB; 3RKZ; X-ray; 1.57 A; A=14-236.
PDB; 3RLP; X-ray; 1.70 A; A/B=9-225.
PDB; 3RLQ; X-ray; 1.90 A; A/B=9-225.
PDB; 3RLR; X-ray; 1.70 A; A/B=9-225.
PDB; 3T0H; X-ray; 1.20 A; A=9-236.
PDB; 3T0Z; X-ray; 2.19 A; A=9-236.
PDB; 3T10; X-ray; 1.24 A; A=9-236.
PDB; 3T1K; X-ray; 1.50 A; A/B=9-236.
PDB; 3T2S; X-ray; 1.50 A; A/B=9-236.
PDB; 3TUH; X-ray; 1.80 A; A/B=16-224.
PDB; 3VHA; X-ray; 1.39 A; A=9-236.
PDB; 3VHC; X-ray; 1.41 A; A=9-236.
PDB; 3VHD; X-ray; 1.52 A; A/B=9-236.
PDB; 3WHA; X-ray; 1.30 A; A/B=9-236.
PDB; 3WQ9; X-ray; 1.80 A; A=1-236.
PDB; 4AIF; X-ray; 2.01 A; D/E=726-732.
PDB; 4AWO; X-ray; 1.70 A; A/B=9-236.
PDB; 4AWP; X-ray; 1.82 A; A/B=9-236.
PDB; 4AWQ; X-ray; 1.60 A; A/B=9-236.
PDB; 4B7P; X-ray; 1.70 A; A=9-236.
PDB; 4BQG; X-ray; 1.90 A; A=9-236.
PDB; 4BQJ; X-ray; 2.00 A; A=9-236.
PDB; 4CGQ; X-ray; 2.00 A; Q=726-732.
PDB; 4CGU; X-ray; 2.11 A; C=726-732.
PDB; 4CGV; X-ray; 2.54 A; E/F=726-732.
PDB; 4CGW; X-ray; 3.00 A; C/D=726-732.
PDB; 4CWF; X-ray; 2.00 A; A=9-236.
PDB; 4CWN; X-ray; 1.80 A; A=9-236.
PDB; 4CWO; X-ray; 2.31 A; A=9-236.
PDB; 4CWP; X-ray; 1.95 A; A=9-236.
PDB; 4CWQ; X-ray; 2.00 A; A=9-236.
PDB; 4CWR; X-ray; 2.00 A; A=9-236.
PDB; 4CWS; X-ray; 2.30 A; A=9-236.
PDB; 4CWT; X-ray; 1.90 A; A=9-236.
PDB; 4EEH; X-ray; 1.60 A; A=9-236.
PDB; 4EFT; X-ray; 2.12 A; A=9-236.
PDB; 4EFU; X-ray; 2.00 A; A=9-236.
PDB; 4EGH; X-ray; 1.60 A; A=9-236.
PDB; 4EGI; X-ray; 1.79 A; A=9-236.
PDB; 4EGK; X-ray; 1.69 A; A=9-236.
PDB; 4FCP; X-ray; 2.00 A; A/B=1-236.
PDB; 4FCQ; X-ray; 2.15 A; A=1-236.
PDB; 4FCR; X-ray; 1.70 A; A=1-236.
PDB; 4HY6; X-ray; 1.65 A; A=9-236.
PDB; 4JQL; X-ray; 1.72 A; A=9-236.
PDB; 4L8Z; X-ray; 1.70 A; A=9-236.
PDB; 4L90; X-ray; 2.00 A; A=9-236.
PDB; 4L91; X-ray; 1.75 A; A=9-236.
PDB; 4L93; X-ray; 1.84 A; A/B=9-236.
PDB; 4L94; X-ray; 1.65 A; A=9-236.
PDB; 4LWE; X-ray; 1.50 A; A=17-224.
PDB; 4LWF; X-ray; 1.75 A; A=17-224.
PDB; 4LWG; X-ray; 1.60 A; A=17-224.
PDB; 4LWH; X-ray; 1.70 A; A=16-224.
PDB; 4LWI; X-ray; 1.70 A; A=17-224.
PDB; 4NH7; X-ray; 2.00 A; A/B=9-236.
PDB; 4NH8; X-ray; 1.65 A; A=9-236.
PDB; 4O04; X-ray; 1.82 A; A=9-236.
PDB; 4O05; X-ray; 1.79 A; A=9-236.
PDB; 4O07; X-ray; 1.86 A; A=9-236.
PDB; 4O09; X-ray; 1.96 A; A=9-236.
PDB; 4O0B; X-ray; 1.93 A; A=9-236.
PDB; 4R3M; X-ray; 1.80 A; A=16-224.
PDB; 4U93; X-ray; 1.55 A; A=1-236.
PDB; 4W7T; X-ray; 1.80 A; A=1-236.
PDB; 4XIP; X-ray; 1.70 A; A=9-236.
PDB; 4XIQ; X-ray; 1.84 A; A=9-236.
PDB; 4XIR; X-ray; 1.70 A; A=9-236.
PDB; 4XIT; X-ray; 1.86 A; A=9-236.
PDB; 4YKQ; X-ray; 1.91 A; A=2-236.
PDB; 4YKR; X-ray; 1.61 A; A=2-236.
PDB; 4YKT; X-ray; 1.85 A; A=2-236.
PDB; 4YKU; X-ray; 1.70 A; A=2-236.
PDB; 4YKW; X-ray; 1.85 A; A/B=2-236.
PDB; 4YKX; X-ray; 1.80 A; A=2-236.
PDB; 4YKY; X-ray; 1.78 A; A=2-236.
PDB; 4YKZ; X-ray; 1.85 A; A=2-236.
PDB; 5CF0; X-ray; 1.80 A; A=9-236.
PDB; 5FNC; X-ray; 2.20 A; A=1-236.
PDB; 5FND; X-ray; 2.00 A; A=1-236.
PDB; 5FNF; X-ray; 2.10 A; A=1-236.
PDB; 5GGZ; X-ray; 2.02 A; A/B/C/D=16-225.
PDB; 5M4E; X-ray; 1.90 A; A=9-236.
PDB; 5M4H; X-ray; 2.00 A; A=9-236.
PDBsum; 1BYQ; -.
PDBsum; 1OSF; -.
PDBsum; 1UY6; -.
PDBsum; 1UY7; -.
PDBsum; 1UY8; -.
PDBsum; 1UY9; -.
PDBsum; 1UYC; -.
PDBsum; 1UYD; -.
PDBsum; 1UYE; -.
PDBsum; 1UYF; -.
PDBsum; 1UYG; -.
PDBsum; 1UYH; -.
PDBsum; 1UYI; -.
PDBsum; 1UYK; -.
PDBsum; 1UYL; -.
PDBsum; 1YC1; -.
PDBsum; 1YC3; -.
PDBsum; 1YC4; -.
PDBsum; 1YER; -.
PDBsum; 1YES; -.
PDBsum; 1YET; -.
PDBsum; 2BSM; -.
PDBsum; 2BT0; -.
PDBsum; 2BUG; -.
PDBsum; 2BYH; -.
PDBsum; 2BYI; -.
PDBsum; 2BZ5; -.
PDBsum; 2C2L; -.
PDBsum; 2CCS; -.
PDBsum; 2CCT; -.
PDBsum; 2CCU; -.
PDBsum; 2FWY; -.
PDBsum; 2FWZ; -.
PDBsum; 2H55; -.
PDBsum; 2JJC; -.
PDBsum; 2K5B; -.
PDBsum; 2QF6; -.
PDBsum; 2QFO; -.
PDBsum; 2QG0; -.
PDBsum; 2QG2; -.
PDBsum; 2UWD; -.
PDBsum; 2VCI; -.
PDBsum; 2VCJ; -.
PDBsum; 2WI1; -.
PDBsum; 2WI2; -.
PDBsum; 2WI3; -.
PDBsum; 2WI4; -.
PDBsum; 2WI5; -.
PDBsum; 2WI6; -.
PDBsum; 2WI7; -.
PDBsum; 2XAB; -.
PDBsum; 2XDK; -.
PDBsum; 2XDL; -.
PDBsum; 2XDS; -.
PDBsum; 2XDU; -.
PDBsum; 2XDX; -.
PDBsum; 2XHR; -.
PDBsum; 2XHT; -.
PDBsum; 2XHX; -.
PDBsum; 2XJG; -.
PDBsum; 2XJJ; -.
PDBsum; 2XJX; -.
PDBsum; 2XK2; -.
PDBsum; 2YE2; -.
PDBsum; 2YE3; -.
PDBsum; 2YE4; -.
PDBsum; 2YE5; -.
PDBsum; 2YE6; -.
PDBsum; 2YE7; -.
PDBsum; 2YE8; -.
PDBsum; 2YE9; -.
PDBsum; 2YEA; -.
PDBsum; 2YEB; -.
PDBsum; 2YEC; -.
PDBsum; 2YED; -.
PDBsum; 2YEE; -.
PDBsum; 2YEF; -.
PDBsum; 2YEG; -.
PDBsum; 2YEH; -.
PDBsum; 2YEI; -.
PDBsum; 2YEJ; -.
PDBsum; 2YI0; -.
PDBsum; 2YI5; -.
PDBsum; 2YI6; -.
PDBsum; 2YI7; -.
PDBsum; 2YJW; -.
PDBsum; 2YJX; -.
PDBsum; 2YK2; -.
PDBsum; 2YK9; -.
PDBsum; 2YKB; -.
PDBsum; 2YKC; -.
PDBsum; 2YKE; -.
PDBsum; 2YKI; -.
PDBsum; 2YKJ; -.
PDBsum; 3B24; -.
PDBsum; 3B25; -.
PDBsum; 3B26; -.
PDBsum; 3B27; -.
PDBsum; 3B28; -.
PDBsum; 3BM9; -.
PDBsum; 3BMY; -.
PDBsum; 3D0B; -.
PDBsum; 3EKO; -.
PDBsum; 3EKR; -.
PDBsum; 3FT5; -.
PDBsum; 3FT8; -.
PDBsum; 3HEK; -.
PDBsum; 3HHU; -.
PDBsum; 3HYY; -.
PDBsum; 3HYZ; -.
PDBsum; 3HZ1; -.
PDBsum; 3HZ5; -.
PDBsum; 3INW; -.
PDBsum; 3INX; -.
PDBsum; 3K97; -.
PDBsum; 3K98; -.
PDBsum; 3K99; -.
PDBsum; 3MNR; -.
PDBsum; 3O0I; -.
PDBsum; 3OW6; -.
PDBsum; 3OWB; -.
PDBsum; 3OWD; -.
PDBsum; 3Q6M; -.
PDBsum; 3Q6N; -.
PDBsum; 3QDD; -.
PDBsum; 3QTF; -.
PDBsum; 3R4M; -.
PDBsum; 3R4N; -.
PDBsum; 3R4O; -.
PDBsum; 3R4P; -.
PDBsum; 3R91; -.
PDBsum; 3R92; -.
PDBsum; 3RKZ; -.
PDBsum; 3RLP; -.
PDBsum; 3RLQ; -.
PDBsum; 3RLR; -.
PDBsum; 3T0H; -.
PDBsum; 3T0Z; -.
PDBsum; 3T10; -.
PDBsum; 3T1K; -.
PDBsum; 3T2S; -.
PDBsum; 3TUH; -.
PDBsum; 3VHA; -.
PDBsum; 3VHC; -.
PDBsum; 3VHD; -.
PDBsum; 3WHA; -.
PDBsum; 3WQ9; -.
PDBsum; 4AIF; -.
PDBsum; 4AWO; -.
PDBsum; 4AWP; -.
PDBsum; 4AWQ; -.
PDBsum; 4B7P; -.
PDBsum; 4BQG; -.
PDBsum; 4BQJ; -.
PDBsum; 4CGQ; -.
PDBsum; 4CGU; -.
PDBsum; 4CGV; -.
PDBsum; 4CGW; -.
PDBsum; 4CWF; -.
PDBsum; 4CWN; -.
PDBsum; 4CWO; -.
PDBsum; 4CWP; -.
PDBsum; 4CWQ; -.
PDBsum; 4CWR; -.
PDBsum; 4CWS; -.
PDBsum; 4CWT; -.
PDBsum; 4EEH; -.
PDBsum; 4EFT; -.
PDBsum; 4EFU; -.
PDBsum; 4EGH; -.
PDBsum; 4EGI; -.
PDBsum; 4EGK; -.
PDBsum; 4FCP; -.
PDBsum; 4FCQ; -.
PDBsum; 4FCR; -.
PDBsum; 4HY6; -.
PDBsum; 4JQL; -.
PDBsum; 4L8Z; -.
PDBsum; 4L90; -.
PDBsum; 4L91; -.
PDBsum; 4L93; -.
PDBsum; 4L94; -.
PDBsum; 4LWE; -.
PDBsum; 4LWF; -.
PDBsum; 4LWG; -.
PDBsum; 4LWH; -.
PDBsum; 4LWI; -.
PDBsum; 4NH7; -.
PDBsum; 4NH8; -.
PDBsum; 4O04; -.
PDBsum; 4O05; -.
PDBsum; 4O07; -.
PDBsum; 4O09; -.
PDBsum; 4O0B; -.
PDBsum; 4R3M; -.
PDBsum; 4U93; -.
PDBsum; 4W7T; -.
PDBsum; 4XIP; -.
PDBsum; 4XIQ; -.
PDBsum; 4XIR; -.
PDBsum; 4XIT; -.
PDBsum; 4YKQ; -.
PDBsum; 4YKR; -.
PDBsum; 4YKT; -.
PDBsum; 4YKU; -.
PDBsum; 4YKW; -.
PDBsum; 4YKX; -.
PDBsum; 4YKY; -.
PDBsum; 4YKZ; -.
PDBsum; 5CF0; -.
PDBsum; 5FNC; -.
PDBsum; 5FND; -.
PDBsum; 5FNF; -.
PDBsum; 5GGZ; -.
PDBsum; 5M4E; -.
PDBsum; 5M4H; -.
ProteinModelPortal; P07900; -.
SMR; P07900; -.
BioGrid; 109552; 811.
CORUM; P07900; -.
DIP; DIP-27595N; -.
IntAct; P07900; 242.
MINT; MINT-132070; -.
STRING; 9606.ENSP00000335153; -.
BindingDB; P07900; -.
ChEMBL; CHEMBL3880; -.
DrugBank; DB07317; (3E)-3-[(phenylamino)methylidene]dihydrofuran-2(3H)-one.
DrugBank; DB03080; 17-Dmag.
DrugBank; DB08786; 4-(2-methoxyethoxy)-6-methylpyrimidin-2-amine.
DrugBank; DB03809; 9-Butyl-8-(3-Methoxybenzyl)-9h-Purin-6-Amine.
DrugBank; DB03899; 9-Butyl-8-(4-Methoxybenzyl)-9h-Purin-6-Amine.
DrugBank; DB05134; CNF1010.
DrugBank; DB02424; Geldanamycin.
DrugBank; DB07325; N-[(2-AMINO-6-METHYLPYRIMIDIN-4-YL)METHYL]-3-{[(E)-(2-OXODIHYDROFURAN-3(2H)-YLIDENE)METHYL]AMINO}BENZENESULFONAMIDE.
DrugBank; DB00716; Nedocromil.
DrugBank; DB00615; Rifabutin.
DrugBank; DB06070; SNX-5422.
GuidetoPHARMACOLOGY; 2905; -.
iPTMnet; P07900; -.
PhosphoSitePlus; P07900; -.
SwissPalm; P07900; -.
BioMuta; HSP90AA1; -.
DMDM; 92090606; -.
OGP; P07900; -.
REPRODUCTION-2DPAGE; IPI00784295; -.
EPD; P07900; -.
MaxQB; P07900; -.
PaxDb; P07900; -.
PeptideAtlas; P07900; -.
PRIDE; P07900; -.
TopDownProteomics; P07900-1; -. [P07900-1]
Ensembl; ENST00000216281; ENSP00000216281; ENSG00000080824. [P07900-1]
Ensembl; ENST00000334701; ENSP00000335153; ENSG00000080824. [P07900-2]
GeneID; 3320; -.
KEGG; hsa:3320; -.
UCSC; uc001yku.5; human. [P07900-1]
CTD; 3320; -.
DisGeNET; 3320; -.
EuPathDB; HostDB:ENSG00000080824.18; -.
GeneCards; HSP90AA1; -.
HGNC; HGNC:5253; HSP90AA1.
HPA; CAB002058; -.
MIM; 140571; gene.
neXtProt; NX_P07900; -.
OpenTargets; ENSG00000080824; -.
PharmGKB; PA29519; -.
eggNOG; KOG0019; Eukaryota.
eggNOG; KOG0020; Eukaryota.
eggNOG; COG0326; LUCA.
GeneTree; ENSGT00840000129758; -.
HOVERGEN; HBG007374; -.
InParanoid; P07900; -.
KO; K04079; -.
OMA; YESFGKN; -.
OrthoDB; EOG091G0270; -.
PhylomeDB; P07900; -.
TreeFam; TF300686; -.
Reactome; R-HSA-1227986; Signaling by ERBB2.
Reactome; R-HSA-1236382; Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
Reactome; R-HSA-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
Reactome; R-HSA-192905; vRNP Assembly.
Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-HSA-203615; eNOS activation.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-3000484; Scavenging by Class F Receptors.
Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-HSA-3371511; HSF1 activation.
Reactome; R-HSA-3371568; Attenuation phase.
Reactome; R-HSA-3371571; HSF1-dependent transactivation.
Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-HSA-3928663; EPHA-mediated growth cone collapse.
Reactome; R-HSA-399954; Sema3A PAK dependent Axon repulsion.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-HSA-5336415; Uptake and function of diphtheria toxin.
Reactome; R-HSA-5601884; PIWI-interacting RNA (piRNA) biogenesis.
Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-HSA-5637810; Constitutive Signaling by EGFRvIII.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-HSA-8854518; AURKA Activation by TPX2.
Reactome; R-HSA-8863795; Downregulation of ERBB2 signaling.
SIGNOR; P07900; -.
ChiTaRS; HSP90AA1; human.
EvolutionaryTrace; P07900; -.
GenomeRNAi; 3320; -.
PMAP-CutDB; P07900; -.
PRO; PR:P07900; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000080824; -.
CleanEx; HS_HSP90AA1; -.
ExpressionAtlas; P07900; baseline and differential.
Genevisible; P07900; HS.
GO; GO:0005737; C:cytoplasm; IDA:CAFA.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0043202; C:lysosomal lumen; TAS:ParkinsonsUK-UCL.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
GO; GO:0070182; F:DNA polymerase binding; IPI:BHF-UCL.
GO; GO:0051020; F:GTPase binding; IPI:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0023026; F:MHC class II protein complex binding; IDA:UniProtKB.
GO; GO:0030235; F:nitric-oxide synthase regulator activity; IDA:UniProtKB.
GO; GO:0000166; F:nucleotide binding; TAS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; TAS:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; EXP:Reactome.
GO; GO:1990782; F:protein tyrosine kinase binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0030911; F:TPR domain binding; IDA:UniProtKB.
GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
GO; GO:0061684; P:chaperone-mediated autophagy; TAS:ParkinsonsUK-UCL.
GO; GO:0051131; P:chaperone-mediated protein complex assembly; IDA:BHF-UCL.
GO; GO:0097711; P:ciliary basal body-plasma membrane docking; TAS:Reactome.
GO; GO:0038128; P:ERBB2 signaling pathway; TAS:Reactome.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0006839; P:mitochondrial transport; TAS:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:UniProtKB.
GO; GO:0051973; P:positive regulation of telomerase activity; IDA:BHF-UCL.
GO; GO:0045040; P:protein import into mitochondrial outer membrane; IDA:BHF-UCL.
GO; GO:0042026; P:protein refolding; TAS:UniProtKB.
GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
GO; GO:0043335; P:protein unfolding; NAS:ParkinsonsUK-UCL.
GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0050999; P:regulation of nitric-oxide synthase activity; TAS:Reactome.
GO; GO:0043254; P:regulation of protein complex assembly; NAS:ParkinsonsUK-UCL.
GO; GO:0031396; P:regulation of protein ubiquitination; IDA:BHF-UCL.
GO; GO:0046677; P:response to antibiotic; ISS:AgBase.
GO; GO:0009409; P:response to cold; ISS:AgBase.
GO; GO:0009408; P:response to heat; ISS:AgBase.
GO; GO:0006986; P:response to unfolded protein; NAS:UniProtKB.
GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
GO; GO:1905323; P:telomerase holoenzyme complex assembly; IDA:BHF-UCL.
GO; GO:0007004; P:telomere maintenance via telomerase; IDA:BHF-UCL.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
Gene3D; 3.30.565.10; -; 1.
HAMAP; MF_00505; HSP90; 1.
InterPro; IPR003594; HATPase_C.
InterPro; IPR019805; Heat_shock_protein_90_CS.
InterPro; IPR001404; Hsp90_fam.
InterPro; IPR020575; Hsp90_N.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
PANTHER; PTHR11528; PTHR11528; 1.
Pfam; PF02518; HATPase_c; 1.
Pfam; PF00183; HSP90; 1.
PIRSF; PIRSF002583; Hsp90; 1.
PRINTS; PR00775; HEATSHOCK90.
SMART; SM00387; HATPase_c; 1.
SUPFAM; SSF54211; SSF54211; 1.
SUPFAM; SSF55874; SSF55874; 1.
PROSITE; PS00298; HSP90; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Cell membrane; Chaperone; Complete proteome; Cytoplasm;
Direct protein sequencing; Membrane; Nucleotide-binding;
Phosphoprotein; Reference proteome; S-nitrosylation; Stress response;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2492519}.
CHAIN 2 732 Heat shock protein HSP 90-alpha.
/FTId=PRO_0000062911.
REGION 284 732 Interaction with FLCN and FNIP1.
{ECO:0000269|PubMed:27353360}.
REGION 284 620 Interaction with FNIP2.
{ECO:0000269|PubMed:27353360}.
REGION 682 732 Required for homodimerization.
{ECO:0000269|PubMed:8289821}.
REGION 728 732 Essential for interaction with SMYD3.
{ECO:0000269|PubMed:25738358}.
REGION 729 732 Essential for interaction with SGTA and
TTC1. {ECO:0000269|PubMed:15708368}.
MOTIF 723 732 TPR repeat-binding.
{ECO:0000269|PubMed:16307917}.
BINDING 51 51 ATP.
BINDING 93 93 ATP.
BINDING 112 112 ATP. {ECO:0000250}.
BINDING 138 138 ATP; via amide nitrogen.
BINDING 400 400 ATP. {ECO:0000250}.
MOD_RES 5 5 Phosphothreonine; by PRKDC.
{ECO:0000269|PubMed:2507541}.
MOD_RES 7 7 Phosphothreonine; by PRKDC.
{ECO:0000269|PubMed:2507541}.
MOD_RES 58 58 N6-acetyllysine.
{ECO:0000250|UniProtKB:P07901}.
MOD_RES 84 84 N6-acetyllysine.
{ECO:0000250|UniProtKB:P07901}.
MOD_RES 231 231 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 252 252 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 263 263 Phosphoserine.
{ECO:0000244|PubMed:16807684,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19367720,
ECO:0000244|PubMed:23186163}.
MOD_RES 313 313 Phosphotyrosine.
{ECO:0000250|UniProtKB:P07901}.
MOD_RES 399 399 Phosphoserine.
{ECO:0000269|PubMed:2492519}.
MOD_RES 443 443 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 453 453 Phosphoserine.
{ECO:0000250|UniProtKB:P82995}.
MOD_RES 458 458 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 476 476 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 489 489 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 492 492 Phosphotyrosine.
{ECO:0000250|UniProtKB:P07901}.
MOD_RES 585 585 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 598 598 S-nitrosocysteine.
{ECO:0000269|PubMed:15937123}.
MOD_RES 641 641 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 1 M -> MPPCSGGDGSTPPGPSLRDRDCPAQSAEYPRDRLDP
RPGSPSEASSPPFLRSRAPVNWYQEKAQVFLWHLMVSGSTT
LLCLWKQPFHVSAFPVTASLAFRQSQGAGQHLYKDLQPFIL
LRLLM (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:16269234}.
/FTId=VSP_026604.
MUTAGEN 47 47 E->A: Strong ATP-binding. Strong
interaction with HSF1, HIF1A, ERBB2, MET,
KEAP1 and RHOBTB2.
{ECO:0000269|PubMed:26517842}.
MUTAGEN 93 93 D->A: Impaired ATP-binding. Strong
interaction with HIF1A, MET, KEAP1 and
RHOBTB2. Loss of interaction with HSF1
and ERBB2. {ECO:0000269|PubMed:26517842}.
MUTAGEN 97 97 G->D: Abolishes ATPase activity.
{ECO:0000269|PubMed:18256191}.
MUTAGEN 598 598 C->A,N,D: Reduces ATPase activity and
client protein activation.
{ECO:0000269|PubMed:15937123,
ECO:0000269|PubMed:19696785}.
MUTAGEN 598 598 C->S: Loss of S-nitrosylation.
{ECO:0000269|PubMed:15937123,
ECO:0000269|PubMed:19696785}.
CONFLICT 63 63 S -> T (in Ref. 1; CAA33259).
{ECO:0000305}.
CONFLICT 74 74 K -> R (in Ref. 4; CAI64495 and 6;
BAG51711). {ECO:0000305}.
CONFLICT 86 86 D -> G (in Ref. 4; CAI64495 and 6;
BAG51711). {ECO:0000305}.
CONFLICT 162 162 W -> D (in Ref. 15; AA sequence).
{ECO:0000305}.
STRAND 18 21 {ECO:0000244|PDB:3T0H}.
HELIX 24 35 {ECO:0000244|PDB:3T0H}.
HELIX 43 63 {ECO:0000244|PDB:3T0H}.
HELIX 67 70 {ECO:0000244|PDB:3T0H}.
STRAND 78 83 {ECO:0000244|PDB:3T0H}.
TURN 84 87 {ECO:0000244|PDB:3T0H}.
STRAND 88 93 {ECO:0000244|PDB:3T0H}.
HELIX 100 104 {ECO:0000244|PDB:3T0H}.
HELIX 106 108 {ECO:0000244|PDB:3T0H}.
HELIX 111 123 {ECO:0000244|PDB:3T0H}.
HELIX 128 134 {ECO:0000244|PDB:3T0H}.
HELIX 137 143 {ECO:0000244|PDB:3T0H}.
STRAND 145 153 {ECO:0000244|PDB:3T0H}.
STRAND 155 157 {ECO:0000244|PDB:2WI6}.
STRAND 159 164 {ECO:0000244|PDB:3T0H}.
STRAND 169 174 {ECO:0000244|PDB:3T0H}.
STRAND 181 190 {ECO:0000244|PDB:3T0H}.
HELIX 192 198 {ECO:0000244|PDB:3T0H}.
HELIX 200 210 {ECO:0000244|PDB:3T0H}.
STRAND 212 216 {ECO:0000244|PDB:3VHC}.
STRAND 218 220 {ECO:0000244|PDB:3T0H}.
TURN 221 224 {ECO:0000244|PDB:3T1K}.
STRAND 225 227 {ECO:0000244|PDB:3T1K}.
HELIX 228 230 {ECO:0000244|PDB:2XJX}.
HELIX 296 298 {ECO:0000244|PDB:3Q6M}.
HELIX 306 317 {ECO:0000244|PDB:3Q6M}.
STRAND 324 331 {ECO:0000244|PDB:3Q6M}.
STRAND 333 335 {ECO:0000244|PDB:3Q6M}.
STRAND 337 343 {ECO:0000244|PDB:3Q6M}.
STRAND 361 365 {ECO:0000244|PDB:3Q6M}.
STRAND 368 372 {ECO:0000244|PDB:3Q6M}.
HELIX 380 382 {ECO:0000244|PDB:3Q6M}.
STRAND 386 392 {ECO:0000244|PDB:3Q6M}.
HELIX 408 427 {ECO:0000244|PDB:3Q6M}.
HELIX 431 451 {ECO:0000244|PDB:3Q6M}.
HELIX 453 455 {ECO:0000244|PDB:3Q6M}.
HELIX 456 460 {ECO:0000244|PDB:3Q6M}.
STRAND 464 467 {ECO:0000244|PDB:3Q6M}.
TURN 468 472 {ECO:0000244|PDB:3Q6M}.
HELIX 477 482 {ECO:0000244|PDB:3Q6M}.
STRAND 490 495 {ECO:0000244|PDB:3Q6M}.
HELIX 499 503 {ECO:0000244|PDB:3Q6M}.
HELIX 506 508 {ECO:0000244|PDB:3Q6M}.
HELIX 509 514 {ECO:0000244|PDB:3Q6M}.
STRAND 518 521 {ECO:0000244|PDB:3Q6M}.
HELIX 525 529 {ECO:0000244|PDB:3Q6M}.
TURN 530 532 {ECO:0000244|PDB:3Q6M}.
STRAND 539 543 {ECO:0000244|PDB:3Q6M}.
HELIX 555 567 {ECO:0000244|PDB:3Q6M}.
HELIX 569 578 {ECO:0000244|PDB:3Q6M}.
HELIX 580 582 {ECO:0000244|PDB:3Q6M}.
STRAND 584 588 {ECO:0000244|PDB:3Q6M}.
STRAND 593 601 {ECO:0000244|PDB:3Q6M}.
STRAND 603 605 {ECO:0000244|PDB:3Q6M}.
HELIX 608 613 {ECO:0000244|PDB:3Q6M}.
STRAND 632 636 {ECO:0000244|PDB:3Q6M}.
HELIX 641 652 {ECO:0000244|PDB:3Q6M}.
HELIX 657 673 {ECO:0000244|PDB:3Q6M}.
HELIX 681 694 {ECO:0000244|PDB:3Q6M}.
STRAND 728 730 {ECO:0000244|PDB:4CGW}.
SEQUENCE 732 AA; 84660 MW; 969F65FCC0BC86FD CRC64;
MPEETQTQDQ PMEEEEVETF AFQAEIAQLM SLIINTFYSN KEIFLRELIS NSSDALDKIR
YESLTDPSKL DSGKELHINL IPNKQDRTLT IVDTGIGMTK ADLINNLGTI AKSGTKAFME
ALQAGADISM IGQFGVGFYS AYLVAEKVTV ITKHNDDEQY AWESSAGGSF TVRTDTGEPM
GRGTKVILHL KEDQTEYLEE RRIKEIVKKH SQFIGYPITL FVEKERDKEV SDDEAEEKED
KEEEKEKEEK ESEDKPEIED VGSDEEEEKK DGDKKKKKKI KEKYIDQEEL NKTKPIWTRN
PDDITNEEYG EFYKSLTNDW EDHLAVKHFS VEGQLEFRAL LFVPRRAPFD LFENRKKKNN
IKLYVRRVFI MDNCEELIPE YLNFIRGVVD SEDLPLNISR EMLQQSKILK VIRKNLVKKC
LELFTELAED KENYKKFYEQ FSKNIKLGIH EDSQNRKKLS ELLRYYTSAS GDEMVSLKDY
CTRMKENQKH IYYITGETKD QVANSAFVER LRKHGLEVIY MIEPIDEYCV QQLKEFEGKT
LVSVTKEGLE LPEDEEEKKK QEEKKTKFEN LCKIMKDILE KKVEKVVVSN RLVTSPCCIV
TSTYGWTANM ERIMKAQALR DNSTMGYMAA KKHLEINPDH SIIETLRQKA EADKNDKSVK
DLVILLYETA LLSSGFSLED PQTHANRIYR MIKLGLGIDE DDPTADDTSA AVTEEMPPLE
GDDDTSRMEE VD


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