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Heat shock protein HSP 90-beta (HSP 90) (Heat shock 84 kDa) (HSP 84) (HSP84)

 HS90B_HUMAN             Reviewed;         724 AA.
P08238; B2R5P0; Q5T9W7; Q9NQW0; Q9NTK6;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
25-OCT-2017, entry version 225.
RecName: Full=Heat shock protein HSP 90-beta;
Short=HSP 90;
AltName: Full=Heat shock 84 kDa;
Short=HSP 84;
Short=HSP84;
Name=HSP90AB1; Synonyms=HSP90B, HSPC2, HSPCB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3301534; DOI=10.1016/0378-1119(87)90012-6;
Rebbe N.F., Ware J., Bertina R.M., Modrich P., Stafford D.W.;
"Nucleotide sequence of a cDNA for a member of the human 90-kDa heat-
shock protein family.";
Gene 53:235-245(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2768249;
Rebbe N.F., Hickman W.S., Ley T.J., Stafford D.W., Hickman S.;
"Nucleotide sequence and regulation of a human 90-kDa heat shock
protein gene.";
J. Biol. Chem. 264:15006-15011(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
Lu L., Huang X.Y., Yin L.L., Xu M., Li J.M., Zhou Z.M., Sha J.H.;
"Cloning a new isoform of heat shock 90kDa in testis.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Amygdala;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[9]
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.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon, Lymph, Muscle, Skin, and Testis;
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).
[11]
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).
[12]
PROTEIN SEQUENCE OF 42-107; 149-168; 181-197; 204-221; 250-265;
274-284; 292-348; 360-392; 412-427; 439-448; 450-475; 482-502;
506-526; 539-551; 584-604; 613-639 AND 653-679, PHOSPHORYLATION AT
SER-255, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryonic kidney;
Bienvenut W.V., Waridel P., Quadroni M.;
Submitted (MAR-2009) to UniProtKB.
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 50-118.
PubMed=8180474; DOI=10.1007/BF00292342;
Takahashi I., Tanuma R., Hirata M., Hashimoto K.;
"A cosmid clone at the D6S182 locus on human chromosome 6p12 contains
the 90-kDa heat shock protein beta gene (HSP90 beta).";
Mamm. Genome 5:121-122(1994).
[14]
SEQUENCE REVISION.
Takahashi I., Tanuma R., Hirata M., Hashimoto K.;
Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
[15]
PROTEIN SEQUENCE OF 54-64 AND 187-199.
TISSUE=Colon carcinoma;
PubMed=9150948; DOI=10.1002/elps.1150180344;
Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.;
"A two-dimensional gel database of human colon carcinoma proteins.";
Electrophoresis 18:605-613(1997).
[16]
NUCLEOTIDE SEQUENCE [MRNA] OF 93-724.
TISSUE=Pancreas;
Mason A., O'Connor D., Greenhalf W.;
"Novel sequence for human Hsp90 beta giving a substitution of R55T
(R147 in original sequence) and M85R (M177 in original sequence).";
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[17]
HOMODIMERIZATION.
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).
[18]
SUBCELLULAR LOCATION, AND INTERACTION WITH CDK6 AND CDC37.
PubMed=9482106; DOI=10.1038/sj.onc.1201570;
Mahony D., Parry D.A., Lees E.;
"Active cdk6 complexes are predominantly nuclear and represent only a
minority of the cdk6 in T cells.";
Oncogene 16:603-611(1998).
[19]
PHOSPHORYLATION AT SER-226 AND SER-255, MUTAGENESIS OF SER-226 AND
SER-255, AND INTERACTION WITH AHR.
PubMed=15581363; DOI=10.1021/bi048736m;
Ogiso H., Kagi N., Matsumoto E., Nishimoto M., Arai R., Shirouzu M.,
Mimura J., Fujii-Kuriyama Y., Yokoyama S.;
"Phosphorylation analysis of 90 kDa heat shock protein within the
cytosolic arylhydrocarbon receptor complex.";
Biochemistry 43:15510-15519(2004).
[20]
INTERACTION WITH TP53, AND REGION.
PubMed=15358771; DOI=10.1074/jbc.M407687200;
Mueller L., Schaupp A., Walerych D., Wegele H., Buchner J.;
"Hsp90 regulates the activity of wild type p53 under physiological and
elevated temperatures.";
J. Biol. Chem. 279:48846-48854(2004).
[21]
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).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[23]
INTERACTION WITH SGTA, AND SUBCELLULAR LOCATION.
PubMed=16580629; DOI=10.1016/j.bbrc.2006.03.090;
Yin H., Wang H., Zong H., Chen X., Wang Y., Yun X., Wu Y., Wang J.,
Gu J.;
"SGT, a Hsp90beta binding partner, is accumulated in the nucleus
during cell apoptosis.";
Biochem. Biophys. Res. Commun. 343:1153-1158(2006).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, 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).
[25]
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).
[26]
FUNCTION, AND INTERACTION WITH UNC45A.
PubMed=16478993; DOI=10.1128/MCB.26.5.1722-1730.2006;
Chadli A., Graham J.D., Abel M.G., Jackson T.A., Gordon D.F.,
Wood W.M., Felts S.J., Horwitz K.B., Toft D.;
"GCUNC-45 is a novel regulator for the progesterone receptor/hsp90
chaperoning pathway.";
Mol. Cell. Biol. 26:1722-1730(2006).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-297, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[28]
UBIQUITINATION.
PubMed=18042044; DOI=10.1042/BJ20071338;
Windheim M., Peggie M., Cohen P.;
"Two different classes of E2 ubiquitin-conjugating enzymes are
required for the mono-ubiquitination of proteins and elongation by
polyubiquitin chains with a specific topology.";
Biochem. J. 409:723-729(2008).
[29]
INTERACTION WITH DNAJC7.
PubMed=18620420; DOI=10.1021/bi800770g;
Moffatt N.S., Bruinsma E., Uhl C., Obermann W.M., Toft D.;
"Role of the cochaperone Tpr2 in Hsp90 chaperoning.";
Biochemistry 47:8203-8213(2008).
[30]
IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH BIRC2,
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=18239673; DOI=10.1038/cdd.2008.5;
Didelot C., Lanneau D., Brunet M., Bouchot A., Cartier J., Jacquel A.,
Ducoroy P., Cathelin S., Decologne N., Chiosis G., Dubrez-Daloz L.,
Solary E., Garrido C.;
"Interaction of heat-shock protein 90 beta isoform (HSP90 beta) with
cellular inhibitor of apoptosis 1 (c-IAP1) is required for cell
differentiation.";
Cell Death Differ. 15:859-866(2008).
[31]
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).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, 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).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, 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).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, 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).
[35]
FUNCTION, S-NITROSYLATION AT CYS-590, AND MUTAGENESIS OF CYS-590.
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).
[36]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-435 AND LYS-481, 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).
[37]
INTERACTION WITH TGFB1 PROCESSED FORM (LAP), AND SUBCELLULAR LOCATION.
PubMed=20599762; DOI=10.1016/j.bbrc.2010.06.112;
Suzuki S., Kulkarni A.B.;
"Extracellular heat shock protein HSP90beta secreted by MG63
osteosarcoma cells inhibits activation of latent TGF-beta1.";
Biochem. Biophys. Res. Commun. 398:525-531(2010).
[38]
INTERACTION WITH HSP90AA1; JAK2 AND PRKCE, INDUCTION, AND FUNCTION.
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).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND 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).
[40]
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).
[41]
MALONYLATION AT LYS-399.
PubMed=21908771; DOI=10.1074/mcp.M111.012658;
Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,
He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,
Dai J., Verdin E., Ye Y., Zhao Y.;
"The first identification of lysine malonylation substrates and its
regulatory enzyme.";
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
[42]
INTERACTION WITH AHSA1 AND XPO1.
PubMed=22022502; DOI=10.1371/journal.pone.0026044;
Echeverria P.C., Bernthaler A., Dupuis P., Mayer B., Picard D.;
"An interaction network predicted from public data as a discovery
tool: application to the Hsp90 molecular chaperone machine.";
PLoS ONE 6:E26044-E26044(2011).
[43]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, 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).
[44]
PHOSPHORYLATION AT SER-718 BY PLK2 AND PLK3.
PubMed=22828320; DOI=10.1016/j.bbapap.2012.07.003;
Salvi M., Trashi E., Cozza G., Franchin C., Arrigoni G., Pinna L.A.;
"Investigation on PLK2 and PLK3 substrate recognition.";
Biochim. Biophys. Acta 1824:1366-1373(2012).
[45]
INTERACTION WITH CDC25A.
PubMed=22843495; DOI=10.1093/hmg/dds303;
Giessrigl B., Krieger S., Rosner M., Huttary N., Saiko P., Alami M.,
Messaoudi S., Peyrat J.F., Maciuk A., Gollinger M., Kopf S.,
Kazlauskas E., Mazal P., Szekeres T., Hengstschlaeger M., Matulis D.,
Jaeger W., Krupitza G.;
"Hsp90 stabilizes Cdc25A and counteracts heat shock-mediated Cdc25A
degradation and cell-cycle attenuation in pancreatic carcinoma
cells.";
Hum. Mol. Genet. 21:4615-4627(2012).
[46]
PROTEIN CLEAVAGE, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=22848402; DOI=10.1371/journal.pone.0040795;
Beck R., Dejeans N., Glorieux C., Creton M., Delaive E., Dieu M.,
Raes M., Leveque P., Gallez B., Depuydt M., Collet J.F.,
Calderon P.B., Verrax J.;
"Hsp90 is cleaved by reactive oxygen species at a highly conserved N-
terminal amino acid motif.";
PLoS ONE 7:E40795-E40795(2012).
[47]
INTERACTION WITH NOS3, MUTAGENESIS OF TYR-301, AND PHOSPHORYLATION AT
TYR-301 BY SRC.
PubMed=23585225; DOI=10.1152/ajplung.00419.2012;
Barabutis N., Handa V., Dimitropoulou C., Rafikov R., Snead C.,
Kumar S., Joshi A., Thangjam G., Fulton D., Black S.M., Patel V.,
Catravas J.D.;
"LPS induces pp60c-src-mediated tyrosine phosphorylation of Hsp90 in
lung vascular endothelial cells and mouse lung.";
Am. J. Physiol. 304:L883-L893(2013).
[48]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-255; THR-297;
SER-445 AND THR-479, 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).
[49]
INTERACTION WITH MAPK7.
PubMed=23428871; DOI=10.1128/MCB.01246-12;
Erazo T., Moreno A., Ruiz-Babot G., Rodriguez-Asiain A., Morrice N.A.,
Espadamala J., Bayascas J.R., Gomez N., Lizcano J.M.;
"Canonical and kinase activity-independent mechanisms for
extracellular signal-regulated kinase 5 (ERK5) nuclear translocation
require dissociation of Hsp90 from the ERK5-Cdc37 complex.";
Mol. Cell. Biol. 33:1671-1686(2013).
[50]
INTERACTION WITH KCNQ4.
PubMed=23431407; DOI=10.1371/journal.pone.0057282;
Gao Y., Yechikov S., Vazquez A.E., Chen D., Nie L.;
"Distinct roles of molecular chaperones HSP90alpha and HSP90beta in
the biogenesis of KCNQ4 channels.";
PLoS ONE 8:E57282-E57282(2013).
[51]
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).
[52]
METHYLATION AT LYS-531 AND LYS-574 BY SMYD2, IDENTIFICATION BY MASS
SPECTROMETRY, MUTAGENESIS OF LYS-531 AND LYS-574, INTERACTION WITH
STIP1 AND CDC37, AND SUBCELLULAR LOCATION.
PubMed=24880080; DOI=10.1016/j.canlet.2014.05.014;
Hamamoto R., Toyokawa G., Nakakido M., Ueda K., Nakamura Y.;
"SMYD2-dependent HSP90 methylation promotes cancer cell proliferation
by regulating the chaperone complex formation.";
Cancer Lett. 351:126-133(2014).
[53]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-669, 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).
[54]
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).
[55]
INTERACTION WITH AHSA1; BIRC2 AND CDC37, AND REGION.
PubMed=25486457; DOI=10.1016/j.bbamcr.2014.11.026;
Synoradzki K., Bieganowski P.;
"Middle domain of human Hsp90 isoforms differentially binds Aha1 in
human cells and alters Hsp90 activity in yeast.";
Biochim. Biophys. Acta 1853:445-452(2015).
[56]
REVIEW.
PubMed=25973397; DOI=10.3389/fonc.2015.00100;
Khurana N., Bhattacharyya S.;
"Hsp90, the concertmaster: tuning transcription.";
Front. Oncol. 5:100-100(2015).
[57]
INTERACTION WITH HSF1; HIF1A; ERBB2; MET; KEAP1 AND RHOBTB2, AND
MUTAGENESIS OF GLU-42 AND ASP-88.
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).
[58]
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).
[59]
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).
[60]
REVIEW.
PubMed=26991466; DOI=10.1002/bip.22835;
Pearl L.H.;
"Review: The HSP90 molecular chaperone-an enigmatic ATPase.";
Biopolymers 105:594-607(2016).
[61]
X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 1-221 IN COMPLEX WITH PURINE
ANALOG.
PubMed=15217611; DOI=10.1016/j.chembiol.2004.03.033;
Wright L., Barril X., Dymock B., Sheridan L., Surgenor A., Beswick M.,
Drysdale M., Collier A., Massey A., Davies N., Fink A., Fromont C.,
Aherne W., Boxall K., Sharp S., Workman P., Hubbard R.E.;
"Structure-activity relationships in purine-based inhibitor binding to
HSP90 isoforms.";
Chem. Biol. 11:775-785(2004).
[62]
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 720-724 IN COMPLEX WITH
FKBP4.
PubMed=15159550; DOI=10.1073/pnas.0305969101;
Wu B., Li P., Liu Y., Lou Z., Ding Y., Shu C., Ye S., Bartlam M.,
Shen B., Rao Z.;
"3D structure of human FK506-binding protein 52: implications for the
assembly of the glucocorticoid receptor/Hsp90/immunophilin
heterocomplex.";
Proc. Natl. Acad. Sci. U.S.A. 101:8348-8353(2004).
[63]
X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 284-543.
Structural genomics consortium (SGC);
"Crystal structure of the middle domain of human hsp90-beta.";
Submitted (DEC-2010) to the PDB data bank.
-!- 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. 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:16478993, PubMed:19696785). 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). Antagonizes STUB1-mediated
inhibition of TGF-beta signaling via inhibition of STUB1-mediated
SMAD3 ubiquitination and degradation (PubMed:24613385). Promotes
cell differentiation by chaperoning BIRC2 and thereby protecting
from auto-ubiquitination and degradation by the proteasomal
machinery (PubMed:18239673). Main chaperone that is involved in
the phosphorylation/activation of the STAT1 by chaperoning both
JAK2 and PRKCE under heat shock and in turn, activates its own
transcription (PubMed:20353823). {ECO:0000269|PubMed:16478993,
ECO:0000269|PubMed:18239673, ECO:0000269|PubMed:19696785,
ECO:0000269|PubMed:20353823, ECO:0000269|PubMed:24613385,
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: Monomer (PubMed:24880080). Homodimer (PubMed:7588731,
PubMed:18400751). Forms a complex with CDK6 and CDC37
(PubMed:9482106, PubMed:25486457). Interacts with UNC45A; binding
to UNC45A involves 2 UNC45A monomers per HSP90AB1 dimer
(PubMed:16478993). Interacts with CHORDC1 (By similarity).
Interacts with DNAJC7 (PubMed:18620420). Interacts with FKBP4
(PubMed:15159550). May interact with NWD1 (PubMed:24681825).
Interacts with SGTA (PubMed:16580629). Interacts with HSF1 in an
ATP-dependent manner. 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 STUB1 and SMAD3
(PubMed:24613385). Interacts with XPO1 and AHSA1 (PubMed:22022502,
PubMed:25486457). Interacts with BIRC2 (PubMed:25486457).
Interacts with KCNQ4; promotes cell surface expression of KCNQ4
(PubMed:23431407). Interacts with BIRC2; prevents auto-
ubiquitination and degradation of its client protein BIRC2
(PubMed:18239673). Interacts with NOS3 (PubMed:23585225).
Interacts with AHR; interaction is inhibited by HSP90AB1
phosphorylation on Ser-226 and Ser-255 (PubMed:15581363).
Interacts with STIP1 and CDC37; upon SMYD2-dependent methylation
(PubMed:24880080). Interacts with JAK2 and PRKCE; promotes
functional activation in a heat shock-dependent manner
(PubMed:20353823). Interacts with HSP90AA1; interaction is
constitutive (PubMed:20353823). HSP90AB1-CDC37 chaperone complex
interacts with inactive MAPK7 (via N-terminal half) in resting
cells; the interaction is MAP2K5-independent and prevents from
ubiquitination and proteasomal degradation (PubMed:23428871).
Interacts with CDC25A; prevents heat shock-mediated CDC25A
degradation and contributes to cell cycle progression
(PubMed:22843495). Interacts with TP53 (via DNA binding domain);
suppresses TP53 aggregation and prevents from irreversible thermal
inactivation (PubMed:15358771). Interacts with TGFB1 processed
form (LAP); inhibits latent TGFB1 activation (PubMed:20599762).
Interacts with TRIM8; prevents nucleus translocation of
phosphorylated STAT3 and HSP90AB1 (By similarity).
{ECO:0000250|UniProtKB:P11499, ECO:0000269|PubMed:15159550,
ECO:0000269|PubMed:15358771, ECO:0000269|PubMed:15581363,
ECO:0000269|PubMed:16478993, ECO:0000269|PubMed:16580629,
ECO:0000269|PubMed:18239673, ECO:0000269|PubMed:18400751,
ECO:0000269|PubMed:18620420, ECO:0000269|PubMed:20353823,
ECO:0000269|PubMed:20599762, ECO:0000269|PubMed:22022502,
ECO:0000269|PubMed:22843495, ECO:0000269|PubMed:23428871,
ECO:0000269|PubMed:23431407, ECO:0000269|PubMed:23585225,
ECO:0000269|PubMed:24613385, ECO:0000269|PubMed:24681825,
ECO:0000269|PubMed:24880080, ECO:0000269|PubMed:25486457,
ECO:0000269|PubMed:26517842, ECO:0000269|PubMed:7588731,
ECO:0000269|PubMed:9482106}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-352572, EBI-352572;
P36896:ACVR1B; NbExp=2; IntAct=EBI-352572, EBI-1384128;
Q9UL18:AGO1; NbExp=3; IntAct=EBI-352572, EBI-527363;
O95433:AHSA1; NbExp=3; IntAct=EBI-352572, EBI-448610;
O00170:AIP; NbExp=6; IntAct=EBI-352572, EBI-704197;
P31751:AKT2; NbExp=2; IntAct=EBI-352572, EBI-296058;
Q9UM73:ALK; NbExp=2; IntAct=EBI-352572, EBI-357361;
Q16671:AMHR2; NbExp=2; IntAct=EBI-352572, EBI-6423788;
Q01432:AMPD3; NbExp=2; IntAct=EBI-352572, EBI-1223554;
P10398:ARAF; NbExp=6; IntAct=EBI-352572, EBI-365961;
Q96GD4:AURKB; NbExp=2; IntAct=EBI-352572, EBI-624291;
P15056:BRAF; NbExp=2; IntAct=EBI-352572, EBI-365980;
Q06187:BTK; NbExp=2; IntAct=EBI-352572, EBI-624835;
Q13555:CAMK2G; NbExp=2; IntAct=EBI-352572, EBI-1383465;
Q16543:CDC37; NbExp=11; IntAct=EBI-352572, EBI-295634;
Q7L3B6:CDC37L1; NbExp=5; IntAct=EBI-352572, EBI-2841876;
Q15131:CDK10; NbExp=2; IntAct=EBI-352572, EBI-1646959;
O94921:CDK14; NbExp=2; IntAct=EBI-352572, EBI-1043945;
Q96Q40:CDK15; NbExp=2; IntAct=EBI-352572, EBI-1051975;
P11802:CDK4; NbExp=3; IntAct=EBI-352572, EBI-295644;
Q00534:CDK6; NbExp=2; IntAct=EBI-352572, EBI-295663;
P50750:CDK9; NbExp=2; IntAct=EBI-352572, EBI-1383449;
O14757:CHEK1; NbExp=3; IntAct=EBI-352572, EBI-974488;
Q9UHD1:CHORDC1; NbExp=3; IntAct=EBI-352572, EBI-2550959;
P49674:CSNK1E; NbExp=2; IntAct=EBI-352572, EBI-749343;
Q13618:CUL3; NbExp=2; IntAct=EBI-352572, EBI-456129;
Q16832:DDR2; NbExp=2; IntAct=EBI-352572, EBI-1381484;
P00533:EGFR; NbExp=8; IntAct=EBI-352572, EBI-297353;
P29317:EPHA2; NbExp=2; IntAct=EBI-352572, EBI-702104;
P04626:ERBB2; NbExp=3; IntAct=EBI-352572, EBI-641062;
P21860:ERBB3; NbExp=3; IntAct=EBI-352572, EBI-720706;
Q15303:ERBB4; NbExp=2; IntAct=EBI-352572, EBI-80371;
Q96A26:FAM162A; NbExp=3; IntAct=EBI-352572, EBI-6123466;
Q9UKC9:FBXL2; NbExp=2; IntAct=EBI-352572, EBI-724253;
O75426:FBXO24; NbExp=2; IntAct=EBI-352572, EBI-6425658;
Q9UKT8:FBXW2; NbExp=2; IntAct=EBI-352572, EBI-914727;
P22607:FGFR3; NbExp=2; IntAct=EBI-352572, EBI-348399;
P09769:FGR; NbExp=2; IntAct=EBI-352572, EBI-1383732;
Q02790:FKBP4; NbExp=5; IntAct=EBI-352572, EBI-1047444;
Q13451:FKBP5; NbExp=4; IntAct=EBI-352572, EBI-306914;
P21333:FLNA; NbExp=2; IntAct=EBI-352572, EBI-350432;
P35916:FLT4; NbExp=2; IntAct=EBI-352572, EBI-1005467;
P06241:FYN; NbExp=2; IntAct=EBI-352572, EBI-515315;
Q8TF76:GSG2; NbExp=2; IntAct=EBI-352572, EBI-1237328;
P49840:GSK3A; NbExp=2; IntAct=EBI-352572, EBI-1044067;
Q9UPZ9:ICK; NbExp=2; IntAct=EBI-352572, EBI-6381479;
O14920:IKBKB; NbExp=2; IntAct=EBI-352572, EBI-81266;
Q14164:IKBKE; NbExp=2; IntAct=EBI-352572, EBI-307369;
Q9Y6K9:IKBKG; NbExp=3; IntAct=EBI-352572, EBI-81279;
Q2WGJ6:KLHL38; NbExp=3; IntAct=EBI-352572, EBI-6426443;
P06239:LCK; NbExp=2; IntAct=EBI-352572, EBI-1348;
P53671:LIMK2; NbExp=2; IntAct=EBI-352572, EBI-1384350;
Q99558:MAP3K14; NbExp=2; IntAct=EBI-352572, EBI-358011;
P41279:MAP3K8; NbExp=2; IntAct=EBI-352572, EBI-354900;
P80192:MAP3K9; NbExp=2; IntAct=EBI-352572, EBI-3951604;
P31152:MAPK4; NbExp=2; IntAct=EBI-352572, EBI-3906061;
P10636-8:MAPT; NbExp=4; IntAct=EBI-352572, EBI-366233;
P42679:MATK; NbExp=2; IntAct=EBI-352572, EBI-751664;
O15146:MUSK; NbExp=2; IntAct=EBI-352572, EBI-6423196;
Q8TD19:NEK9; NbExp=2; IntAct=EBI-352572, EBI-1044009;
P19838:NFKB1; NbExp=3; IntAct=EBI-352572, EBI-300010;
O75469:NR1I2; NbExp=2; IntAct=EBI-352572, EBI-3905991;
Q9P215:POGK; NbExp=2; IntAct=EBI-352572, EBI-2555775;
P53041:PPP5C; NbExp=7; IntAct=EBI-352572, EBI-716663;
Q13131:PRKAA1; NbExp=2; IntAct=EBI-352572, EBI-1181405;
P22694:PRKACB; NbExp=2; IntAct=EBI-352572, EBI-2679622;
Q02156:PRKCE; NbExp=2; IntAct=EBI-352572, EBI-706254;
Q05513:PRKCZ; NbExp=2; IntAct=EBI-352572, EBI-295351;
Q15139:PRKD1; NbExp=2; IntAct=EBI-352572, EBI-1181072;
P51817:PRKX; NbExp=2; IntAct=EBI-352572, EBI-4302903;
P11801:PSKH1; NbExp=2; IntAct=EBI-352572, EBI-3922781;
Q15185:PTGES3; NbExp=4; IntAct=EBI-352572, EBI-1049387;
P04049:RAF1; NbExp=3; IntAct=EBI-352572, EBI-365996;
P49758:RGS6; NbExp=2; IntAct=EBI-352572, EBI-6426927;
Q01974:ROR2; NbExp=2; IntAct=EBI-352572, EBI-6422642;
P62913:RPL11; NbExp=2; IntAct=EBI-352572, EBI-354380;
Q15418:RPS6KA1; NbExp=2; IntAct=EBI-352572, EBI-963034;
P31948:STIP1; NbExp=3; IntAct=EBI-352572, EBI-1054052;
Q15831:STK11; NbExp=3; IntAct=EBI-352572, EBI-306838;
Q15208:STK38; NbExp=2; IntAct=EBI-352572, EBI-458376;
Q9UNE7:STUB1; NbExp=5; IntAct=EBI-352572, EBI-357085;
Q9Y2Z0-2:SUGT1; NbExp=2; IntAct=EBI-352572, EBI-10768076;
Q9UHD2:TBK1; NbExp=2; IntAct=EBI-352572, EBI-356402;
Q96S53:TESK2; NbExp=2; IntAct=EBI-352572, EBI-1384110;
Q9BXA6:TSSK6; NbExp=3; IntAct=EBI-352572, EBI-851883;
P29597:TYK2; NbExp=2; IntAct=EBI-352572, EBI-1383454;
Q8IWX7:UNC45B; NbExp=2; IntAct=EBI-352572, EBI-9363363;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16580629,
ECO:0000269|PubMed:18239673, ECO:0000269|PubMed:24880080,
ECO:0000269|PubMed:9482106}. Melanosome
{ECO:0000269|PubMed:17081065}. Nucleus
{ECO:0000269|PubMed:18239673}. Secreted
{ECO:0000269|PubMed:20599762}. Cell membrane
{ECO:0000269|PubMed:20599762}. Note=Identified by mass
spectrometry in melanosome fractions from stage I to stage IV
(PubMed:17081065). Translocates with BIRC2 from the nucleus to the
cytoplasm during differentiation (PubMed:18239673). Secreted when
associated with TGFB1 processed form (LAP) (PubMed:20599762).
{ECO:0000269|PubMed:17081065, ECO:0000269|PubMed:18239673,
ECO:0000269|PubMed:20599762}.
-!- INDUCTION: By heat shock. {ECO:0000269|PubMed:20353823}.
-!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
repeat-containing proteins. {ECO:0000250|UniProtKB:P07900}.
-!- PTM: Ubiquitinated in the presence of STUB1-UBE2D1 complex (in
vitro). {ECO:0000269|PubMed:18042044}.
-!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
-!- PTM: S-nitrosylated; negatively regulates the ATPase activity.
{ECO:0000305|PubMed:19696785}.
-!- PTM: Phosphorylation at Tyr-301 by SRC is induced by
lipopolysaccharide (PubMed:23585225). Phosphorylation at Ser-226
and Ser-255 inhibits AHR interaction (PubMed:15581363).
{ECO:0000269|PubMed:15581363, ECO:0000269|PubMed:23585225}.
-!- PTM: Methylated by SMYD2; facilitates dimerization and chaperone
complex formation; promotes cancer cell proliferation.
{ECO:0000269|PubMed:24880080}.
-!- PTM: Cleaved following oxidative stress resulting in HSP90AB1
protein radicals formation; disrupts the chaperoning function and
the degradation of its client proteins.
{ECO:0000269|PubMed:22848402}.
-!- SIMILARITY: Belongs to the heat shock protein 90 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD14062.3; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAB66478.1; Type=Frameshift; Positions=709; Evidence={ECO:0000305};
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EMBL; M16660; AAA36025.1; -; mRNA.
EMBL; J04988; AAA36026.1; -; Genomic_DNA.
EMBL; AY359878; AAQ63401.1; -; mRNA.
EMBL; AL136543; CAB66478.1; ALT_FRAME; mRNA.
EMBL; AK312255; BAG35187.1; -; mRNA.
EMBL; DQ314872; ABC40731.1; -; Genomic_DNA.
EMBL; AL139392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471081; EAX04257.1; -; Genomic_DNA.
EMBL; BC004928; AAH04928.1; -; mRNA.
EMBL; BC009206; AAH09206.2; -; mRNA.
EMBL; BC012807; AAH12807.1; -; mRNA.
EMBL; BC014485; AAH14485.1; -; mRNA.
EMBL; BC016753; AAH16753.1; -; mRNA.
EMBL; BC068474; AAH68474.1; -; mRNA.
EMBL; AH007358; AAD14062.3; ALT_INIT; Genomic_DNA.
EMBL; AF275719; AAF82792.1; -; mRNA.
CCDS; CCDS4909.1; -.
PIR; A29461; HHHU84.
PIR; T46243; T46243.
RefSeq; NP_001258898.1; NM_001271969.1.
RefSeq; NP_001258899.1; NM_001271970.1.
RefSeq; NP_001258900.1; NM_001271971.1.
RefSeq; NP_031381.2; NM_007355.3.
UniGene; Hs.509736; -.
PDB; 1QZ2; X-ray; 3.00 A; G/H=720-724.
PDB; 1UYM; X-ray; 2.45 A; A=2-221.
PDB; 2L6J; NMR; -; B=720-724.
PDB; 3FWV; X-ray; 2.20 A; C/D=719-723.
PDB; 3NMQ; X-ray; 2.20 A; A=1-223.
PDB; 3PRY; X-ray; 2.28 A; A/B/C=284-543.
PDB; 3UQ3; X-ray; 2.60 A; B/C=720-724.
PDB; 5FWK; EM; 3.90 A; A/B=1-724.
PDB; 5FWL; EM; 9.00 A; A/B=1-724.
PDB; 5FWM; EM; 8.00 A; A/B=1-724.
PDB; 5FWP; EM; 7.20 A; A/B=1-724.
PDBsum; 1QZ2; -.
PDBsum; 1UYM; -.
PDBsum; 2L6J; -.
PDBsum; 3FWV; -.
PDBsum; 3NMQ; -.
PDBsum; 3PRY; -.
PDBsum; 3UQ3; -.
PDBsum; 5FWK; -.
PDBsum; 5FWL; -.
PDBsum; 5FWM; -.
PDBsum; 5FWP; -.
ProteinModelPortal; P08238; -.
SMR; P08238; -.
BioGrid; 109558; 330.
CORUM; P08238; -.
DIP; DIP-413N; -.
IntAct; P08238; 530.
MINT; MINT-99712; -.
STRING; 9606.ENSP00000325875; -.
BindingDB; P08238; -.
ChEMBL; CHEMBL4303; -.
DrugBank; DB05134; CNF1010.
DrugBank; DB02424; Geldanamycin.
DrugBank; DB03758; Radicicol.
DrugBank; DB06070; SNX-5422.
GuidetoPHARMACOLOGY; 2907; -.
iPTMnet; P08238; -.
PhosphoSitePlus; P08238; -.
SwissPalm; P08238; -.
DMDM; 17865718; -.
OGP; P08238; -.
EPD; P08238; -.
MaxQB; P08238; -.
PaxDb; P08238; -.
PeptideAtlas; P08238; -.
PRIDE; P08238; -.
TopDownProteomics; P08238; -.
DNASU; 3326; -.
Ensembl; ENST00000353801; ENSP00000325875; ENSG00000096384.
Ensembl; ENST00000371554; ENSP00000360609; ENSG00000096384.
Ensembl; ENST00000371646; ENSP00000360709; ENSG00000096384.
Ensembl; ENST00000620073; ENSP00000481908; ENSG00000096384.
GeneID; 3326; -.
KEGG; hsa:3326; -.
UCSC; uc003oxa.3; human.
CTD; 3326; -.
DisGeNET; 3326; -.
EuPathDB; HostDB:ENSG00000096384.19; -.
GeneCards; HSP90AB1; -.
H-InvDB; HIX0031498; -.
H-InvDB; HIX0057380; -.
HGNC; HGNC:5258; HSP90AB1.
HPA; CAB005230; -.
HPA; HPA055729; -.
MIM; 140572; gene.
neXtProt; NX_P08238; -.
OpenTargets; ENSG00000096384; -.
PharmGKB; PA29524; -.
eggNOG; KOG0019; Eukaryota.
eggNOG; KOG0020; Eukaryota.
eggNOG; COG0326; LUCA.
GeneTree; ENSGT00900000140936; -.
HOGENOM; HOG000031988; -.
HOVERGEN; HBG007374; -.
InParanoid; P08238; -.
KO; K04079; -.
OMA; LRYHSSQ; -.
OrthoDB; EOG091G0270; -.
PhylomeDB; P08238; -.
TreeFam; TF300686; -.
Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
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-399954; Sema3A PAK dependent Axon repulsion.
Reactome; R-HSA-5336415; Uptake and function of diphtheria toxin.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-844456; The NLRP3 inflammasome.
Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-HSA-8937144; Aryl hydrocarbon receptor signalling.
SIGNOR; P08238; -.
ChiTaRS; HSP90AB1; human.
EvolutionaryTrace; P08238; -.
GeneWiki; HSP90AB1; -.
GenomeRNAi; 3326; -.
PRO; PR:P08238; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000096384; -.
CleanEx; HS_HSP90AB1; -.
ExpressionAtlas; P08238; baseline and differential.
Genevisible; P08238; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0034751; C:aryl hydrocarbon receptor complex; IDA:UniProtKB.
GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
GO; GO:0031526; C:brush border membrane; IEA:Ensembl.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0016234; C:inclusion body; IEA:Ensembl.
GO; GO:0005765; C:lysosomal membrane; IEA:Ensembl.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:1990917; C:ooplasm; IEA:Ensembl.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:1990913; C:sperm head plasma membrane; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IDA:CAFA.
GO; GO:0043008; F:ATP-dependent protein binding; IPI:CAFA.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0002135; F:CTP binding; IEA:Ensembl.
GO; GO:0032564; F:dATP binding; IEA:Ensembl.
GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
GO; GO:0070182; F:DNA polymerase binding; IPI:BHF-UCL.
GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
GO; GO:0008144; F:drug binding; IEA:Ensembl.
GO; GO:0005525; F:GTP binding; IEA:Ensembl.
GO; GO:0031072; F:heat shock protein binding; IPI:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
GO; GO:1990226; F:histone methyltransferase binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0044325; F:ion channel binding; IEA:Ensembl.
GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
GO; GO:0023026; F:MHC class II protein complex binding; IDA:UniProtKB.
GO; GO:0030235; F:nitric-oxide synthase regulator activity; ISS:UniProtKB.
GO; GO:0042277; F:peptide binding; IPI:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0019887; F:protein kinase regulator activity; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0017098; F:sulfonylurea receptor binding; IEA:Ensembl.
GO; GO:0030911; F:TPR domain binding; ISS:UniProtKB.
GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
GO; GO:0002134; F:UTP binding; IEA:Ensembl.
GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0051131; P:chaperone-mediated protein complex assembly; IDA:CAFA.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0071157; P:negative regulation of cell cycle arrest; IMP:UniProtKB.
GO; GO:1903660; P:negative regulation of complement-dependent cytotoxicity; IEA:Ensembl.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:1901389; P:negative regulation of transforming growth factor beta activation; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0001890; P:placenta development; IEA:Ensembl.
GO; GO:0045597; P:positive regulation of cell differentiation; IMP:UniProtKB.
GO; GO:0045793; P:positive regulation of cell size; IEA:Ensembl.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:UniProtKB.
GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IDA:UniProtKB.
GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
GO; GO:0033160; P:positive regulation of protein import into nucleus, translocation; IEA:Ensembl.
GO; GO:2000010; P:positive regulation of protein localization to cell surface; IDA:UniProtKB.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IEA:Ensembl.
GO; GO:0051973; P:positive regulation of telomerase activity; IDA:BHF-UCL.
GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
GO; GO:0006457; P:protein folding; IEA:InterPro.
GO; GO:0050821; P:protein stabilization; TAS:Reactome.
GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
GO; GO:0060334; P:regulation of interferon-gamma-mediated signaling pathway; IMP:MGI.
GO; GO:0031396; P:regulation of protein ubiquitination; IDA:BHF-UCL.
GO; GO:0060338; P:regulation of type I interferon-mediated signaling pathway; IMP:MGI.
GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
GO; GO:0009651; P:response to salt stress; IEA:Ensembl.
GO; GO:0006986; P:response to unfolded protein; NAS:UniProtKB.
GO; GO:0097435; P:supramolecular fiber organization; IMP:CACAO.
GO; GO:1905323; P:telomerase holoenzyme complex assembly; IDA:BHF-UCL.
GO; GO:0007004; P:telomere maintenance via telomerase; IDA:BHF-UCL.
GO; GO:0019062; P:virion attachment to host cell; IMP:CACAO.
GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
CDD; cd00075; HATPase_c; 1.
Gene3D; 3.30.565.10; -; 1.
HAMAP; MF_00505; HSP90; 1.
InterPro; IPR003594; HATPase_C.
InterPro; IPR036890; HATPase_C_sf.
InterPro; IPR019805; Heat_shock_protein_90_CS.
InterPro; IPR037196; HSP90_C.
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; SSF110942; SSF110942; 1.
SUPFAM; SSF54211; SSF54211; 1.
SUPFAM; SSF55874; SSF55874; 1.
PROSITE; PS00298; HSP90; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Cell membrane; Chaperone;
Complete proteome; Cytoplasm; Direct protein sequencing; Glycoprotein;
Membrane; Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; S-nitrosylation; Secreted;
Stress response; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2492519}.
CHAIN 2 724 Heat shock protein HSP 90-beta.
/FTId=PRO_0000062917.
REGION 2 527 Interaction with TP53.
{ECO:0000269|PubMed:15358771}.
REGION 2 214 Interaction with BIRC2.
{ECO:0000269|PubMed:25486457}.
REGION 215 552 Interaction with AHSA1.
{ECO:0000269|PubMed:25486457}.
MOTIF 720 724 TPR repeat-binding.
BINDING 46 46 ATP. {ECO:0000250}.
BINDING 88 88 ATP.
BINDING 107 107 ATP. {ECO:0000250}.
BINDING 133 133 ATP; via amide nitrogen. {ECO:0000250}.
BINDING 392 392 ATP. {ECO:0000250}.
SITE 126 127 Cleaved under oxidative stress.
{ECO:0000269|PubMed:22848402}.
MOD_RES 219 219 N6-succinyllysine.
{ECO:0000250|UniProtKB:P11499}.
MOD_RES 226 226 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 255 255 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:23186163,
ECO:0000269|Ref.12}.
MOD_RES 261 261 Phosphoserine.
{ECO:0000269|PubMed:2492519}.
MOD_RES 297 297 Phosphothreonine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:23186163}.
MOD_RES 301 301 Phosphotyrosine; by SRC.
{ECO:0000269|PubMed:23585225}.
MOD_RES 305 305 Phosphotyrosine.
{ECO:0000250|UniProtKB:P11499}.
MOD_RES 307 307 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 399 399 N6-malonyllysine.
{ECO:0000269|PubMed:21908771}.
MOD_RES 435 435 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 445 445 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 452 452 Phosphoserine; alternate.
{ECO:0000269|PubMed:2492519}.
MOD_RES 479 479 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 481 481 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 484 484 Phosphotyrosine.
{ECO:0000269|PubMed:2492519}.
MOD_RES 531 531 N6-methylated lysine; alternate.
{ECO:0000269|PubMed:24880080}.
MOD_RES 531 531 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P11499}.
MOD_RES 532 532 Phosphoserine.
{ECO:0000269|PubMed:2492519}.
MOD_RES 574 574 N6-methylated lysine.
{ECO:0000269|PubMed:24880080}.
MOD_RES 577 577 N6-succinyllysine.
{ECO:0000250|UniProtKB:P11499}.
MOD_RES 590 590 S-nitrosocysteine.
{ECO:0000305|PubMed:19696785}.
MOD_RES 624 624 N6-acetyllysine.
{ECO:0000250|UniProtKB:P11499}.
MOD_RES 669 669 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 718 718 Phosphoserine; by PLK2 and PLK3.
{ECO:0000269|PubMed:22828320}.
CARBOHYD 434 434 O-linked (GlcNAc) serine. {ECO:0000250}.
CARBOHYD 452 452 O-linked (GlcNAc) serine; alternate.
{ECO:0000250}.
VARIANT 349 349 K -> E (in dbSNP:rs11538975).
/FTId=VAR_049624.
MUTAGEN 42 42 E->A: Strong ATP-binding. Strong
interaction with HSF1, HIF1A, ERBB2, MET,
KEAP1 and RHOBTB2.
{ECO:0000269|PubMed:26517842}.
MUTAGEN 88 88 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 226 226 S->A: Increases the binding affinity for
AHR; when associated with A-255.
Increases AHR transcription activity;
when associated with A-255.
{ECO:0000269|PubMed:15581363}.
MUTAGEN 226 226 S->E: No effect on the interaction with
AHR; when associated with E-255.
{ECO:0000269|PubMed:15581363}.
MUTAGEN 255 255 S->A: Increases the binding affinity for
AHR; when associated with A-226.
Increases AHR transcription activity;
when associated with A-226.
{ECO:0000269|PubMed:15581363}.
MUTAGEN 255 255 S->E: No effect on the interaction with
AHR; when associated with E-226.
{ECO:0000269|PubMed:15581363}.
MUTAGEN 301 301 Y->F: Decreases interaction with NOS3 and
SRC. impairs resists LPS-induced tyrosine
phosphorylation. Does not block LPS-
induced pp60src phosphorylation.
{ECO:0000269|PubMed:23585225}.
MUTAGEN 531 531 K->A: Highly decreases the signal of
SMYD2-dependent HSP90AB1 methylation;
when associated with A-574. Diminishes
dimerized form; when associated with A-
574. Reduces interaction with STIP1 or
CDC37; when associated with A-574.
{ECO:0000269|PubMed:24880080}.
MUTAGEN 574 574 K->A: Decreases the signal of SMYD2-
dependent HSP90AB1 methylation. Highly
decreases the signal of SMYD2-dependent
HSP90AB1 methylation; when associated
with A-531. Diminishes dimerized form;
when associated with A-531. Reduces
interaction with STIP1 or CDC37; when
associated with A-531.
{ECO:0000269|PubMed:24880080}.
MUTAGEN 590 590 C->A,N,D: Reduced ATPase activity and
client protein activation.
{ECO:0000269|PubMed:19696785}.
CONFLICT 147 147 T -> R (in Ref. 1; AAA36025).
{ECO:0000305}.
CONFLICT 177 177 R -> M (in Ref. 1; AAA36025).
{ECO:0000305}.
CONFLICT 403 403 V -> A (in Ref. 5; CAB66478).
{ECO:0000305}.
STRAND 13 16 {ECO:0000244|PDB:3NMQ}.
HELIX 19 30 {ECO:0000244|PDB:3NMQ}.
HELIX 38 60 {ECO:0000244|PDB:3NMQ}.
HELIX 62 65 {ECO:0000244|PDB:3NMQ}.
STRAND 73 78 {ECO:0000244|PDB:3NMQ}.
TURN 79 82 {ECO:0000244|PDB:3NMQ}.
STRAND 83 88 {ECO:0000244|PDB:3NMQ}.
HELIX 95 99 {ECO:0000244|PDB:3NMQ}.
HELIX 101 118 {ECO:0000244|PDB:3NMQ}.
HELIX 123 129 {ECO:0000244|PDB:3NMQ}.
HELIX 132 138 {ECO:0000244|PDB:3NMQ}.
STRAND 140 148 {ECO:0000244|PDB:3NMQ}.
STRAND 155 159 {ECO:0000244|PDB:3NMQ}.
STRAND 164 169 {ECO:0000244|PDB:3NMQ}.
STRAND 176 185 {ECO:0000244|PDB:3NMQ}.
HELIX 187 193 {ECO:0000244|PDB:3NMQ}.
HELIX 195 205 {ECO:0000244|PDB:3NMQ}.
STRAND 213 215 {ECO:0000244|PDB:3NMQ}.
HELIX 288 290 {ECO:0000244|PDB:3PRY}.
HELIX 293 295 {ECO:0000244|PDB:3PRY}.
HELIX 298 309 {ECO:0000244|PDB:3PRY}.
STRAND 316 323 {ECO:0000244|PDB:3PRY}.
STRAND 325 327 {ECO:0000244|PDB:3PRY}.
STRAND 329 335 {ECO:0000244|PDB:3PRY}.
STRAND 353 357 {ECO:0000244|PDB:3PRY}.
STRAND 360 364 {ECO:0000244|PDB:3PRY}.
HELIX 367 369 {ECO:0000244|PDB:3PRY}.
HELIX 372 374 {ECO:0000244|PDB:3PRY}.
STRAND 378 386 {ECO:0000244|PDB:3PRY}.
HELIX 395 420 {ECO:0000244|PDB:3PRY}.
HELIX 423 443 {ECO:0000244|PDB:3PRY}.
HELIX 445 447 {ECO:0000244|PDB:3PRY}.
HELIX 448 453 {ECO:0000244|PDB:3PRY}.
STRAND 456 459 {ECO:0000244|PDB:3PRY}.
TURN 460 464 {ECO:0000244|PDB:3PRY}.
HELIX 469 474 {ECO:0000244|PDB:3PRY}.
STRAND 482 486 {ECO:0000244|PDB:3PRY}.
HELIX 491 495 {ECO:0000244|PDB:3PRY}.
HELIX 498 504 {ECO:0000244|PDB:3PRY}.
TURN 505 507 {ECO:0000244|PDB:3PRY}.
STRAND 510 512 {ECO:0000244|PDB:3PRY}.
HELIX 518 525 {ECO:0000244|PDB:3PRY}.
STRAND 531 535 {ECO:0000244|PDB:3PRY}.
SEQUENCE 724 AA; 83264 MW; A93118C214D03810 CRC64;
MPEEVHHGEE EVETFAFQAE IAQLMSLIIN TFYSNKEIFL RELISNASDA LDKIRYESLT
DPSKLDSGKE LKIDIIPNPQ ERTLTLVDTG IGMTKADLIN NLGTIAKSGT KAFMEALQAG
ADISMIGQFG VGFYSAYLVA EKVVVITKHN DDEQYAWESS AGGSFTVRAD HGEPIGRGTK
VILHLKEDQT EYLEERRVKE VVKKHSQFIG YPITLYLEKE REKEISDDEA EEEKGEKEEE
DKDDEEKPKI EDVGSDEEDD SGKDKKKKTK KIKEKYIDQE ELNKTKPIWT RNPDDITQEE
YGEFYKSLTN DWEDHLAVKH FSVEGQLEFR ALLFIPRRAP FDLFENKKKK NNIKLYVRRV
FIMDSCDELI PEYLNFIRGV VDSEDLPLNI SREMLQQSKI LKVIRKNIVK KCLELFSELA
EDKENYKKFY EAFSKNLKLG IHEDSTNRRR LSELLRYHTS QSGDEMTSLS EYVSRMKETQ
KSIYYITGES KEQVANSAFV ERVRKRGFEV VYMTEPIDEY CVQQLKEFDG KSLVSVTKEG
LELPEDEEEK KKMEESKAKF ENLCKLMKEI LDKKVEKVTI SNRLVSSPCC IVTSTYGWTA
NMERIMKAQA LRDNSTMGYM MAKKHLEINP DHPIVETLRQ KAEADKNDKA VKDLVVLLFE
TALLSSGFSL EDPQTHSNRI YRMIKLGLGI DEDEVAAEEP NAAVPDEIPP LEGDEDASRM
EEVD


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18-003-42935 Heat-shock protein beta-1 - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg Protein A
18-003-43409 Heat shock protein beta-1 - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg Protein A
E0693h ELISA kit 28 kDa heat shock protein,Estrogen-regulated 24 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,Homo sapiens,HSP 27,HSP27,HSP28,HspB1,HSPB1,Human,SRP27,Stress-responsive pro 96T
E0693h ELISA 28 kDa heat shock protein,Estrogen-regulated 24 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,Homo sapiens,HSP 27,HSP27,HSP28,HspB1,HSPB1,Human,SRP27,Stress-responsive protein 96T
U0693h CLIA 28 kDa heat shock protein,Estrogen-regulated 24 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,Homo sapiens,HSP 27,HSP27,HSP28,HspB1,HSPB1,Human,SRP27,Stress-responsive protein 2 96T
10-782-55038 Heat-shock protein beta-1 - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.05 mg
10-782-55038 Heat-shock protein beta-1 - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.2 mg
27-259 HSF2 binds specifically to the heat-shock element and has homology to HSFs of other species. Heat shock transcription factors activate heat-shock response genes under conditions of heat or other stres 0.05 mg
E0693m ELISA Growth-related 25 kDa protein,Heat shock 25 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,HSP 25,HSP 27,Hsp25,Hsp27,HspB1,Hspb1,Mouse,Mus musculus,p25 96T
U0693m CLIA Growth-related 25 kDa protein,Heat shock 25 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,HSP 25,HSP 27,Hsp25,Hsp27,HspB1,Hspb1,Mouse,Mus musculus,p25 96T
E0693m ELISA kit Growth-related 25 kDa protein,Heat shock 25 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,HSP 25,HSP 27,Hsp25,Hsp27,HspB1,Hspb1,Mouse,Mus musculus,p25 96T
10-663-45494 Heat Shock Protein 27kD (HSP27) Human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 1 mg
10-663-45494 Heat Shock Protein 27kD (HSP27) Human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.05 mg
10-663-45494 Heat Shock Protein 27kD (HSP27) Human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.01 mg
E0693c ELISA kit 25 kDa IAP,Actin polymerization inhibitor,Chicken,Gallus gallus,Heat shock 25 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,HSP 25,HSP 27,HspB1,HSPB1 96T
U0693c CLIA 25 kDa IAP,Actin polymerization inhibitor,Chicken,Gallus gallus,Heat shock 25 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,HSP 25,HSP 27,HspB1,HSPB1 96T
E0693c ELISA 25 kDa IAP,Actin polymerization inhibitor,Chicken,Gallus gallus,Heat shock 25 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,HSP 25,HSP 27,HspB1,HSPB1 96T
25-272 The heat-shock response is elicited by exposure of cells to thermal and chemical stress and through the activation of HSFs (heat shock factors) results in the elevated expression of heat-shock induced 0.05 mg
hsp-091 Recombinant Human Heat Shock Protein 90kDa Beta (GRP94) Member 1 HEAT SHOCK PROTEINS 10
hsp-091 Recombinant Human Heat Shock Protein 90kDa Beta (GRP94) Member 1 HEAT SHOCK PROTEINS 2
hsp-091 Recombinant Human Heat Shock Protein 90kDa Beta (GRP94) Member 1 HEAT SHOCK PROTEINS 1mg
20-372-60095 heat shock 70kDa protein 1-like - Mouse monoclonal anti-human HSPA1L antibody; Heat shock 70 kDa protein 1-like; Heat shock 70 kDa protein 1-Hom; HSP70-Hom Monoclonal 0.1 mg
PC-084 Heat Shock Protein 90b (HSP90b or HSP84) 500 ug
PC-084 Heat Shock Protein 90b (HSP90b or HSP84) 500 ug
EIAAB11548 DnaJ homolog subfamily B member 5,DNAJB5,Heat shock protein cognate 40,Heat shock protein Hsp40-2,Heat shock protein Hsp40-3,Homo sapiens,Hsc40,HSC40,Human


 

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