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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.
02-JUN-2021, entry version 257.
RecName: Full=Heat shock protein HSP 90-beta;
Short=HSP 90;
AltName: Full=Heat shock 84 kDa;
Short=HSP 84;
Short=HSP84;
Name=HSP90AB1 {ECO:0000312|HGNC:HGNC:5258}; 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]
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Lymphoblast;
PubMed=14654843; DOI=10.1038/nature02166;
Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
"Proteomic characterization of the human centrosome by protein correlation
profiling.";
Nature 426:570-574(2003).
[20]
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).
[21]
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).
[22]
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).
[23]
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).
[24]
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).
[25]
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).
[26]
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).
[27]
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).
[28]
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).
[29]
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).
[30]
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).
[31]
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).
[32]
SUBUNIT, ACTIVITY 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).
[33]
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).
[34]
INTERACTION WITH TTC4.
PubMed=18320024; DOI=10.1371/journal.pone.0001737;
Crevel G., Bennett D., Cotterill S.;
"The human TPR protein TTC4 is a putative Hsp90 co-chaperone which
interacts with CDC6 and shows alterations in transformed cells.";
PLoS ONE 3:E0001737-E0001737(2008).
[35]
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).
[36]
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).
[37]
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).
[38]
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).
[39]
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).
[40]
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).
[41]
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).
[42]
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).
[43]
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).
[44]
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).
[45]
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).
[46]
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).
[47]
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).
[48]
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).
[49]
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).
[50]
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).
[51]
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).
[52]
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).
[53]
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).
[54]
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).
[55]
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).
[56]
INTERACTION WITH NWD1.
PubMed=24681825; DOI=10.18632/oncotarget.1850;
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).
[57]
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).
[58]
REVIEW.
PubMed=25973397; DOI=10.3389/fonc.2015.00100;
Khurana N., Bhattacharyya S.;
"Hsp90, the concertmaster: tuning transcription.";
Front. Oncol. 5:100-100(2015).
[59]
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).
[60]
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).
[61]
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).
[62]
REVIEW.
PubMed=26991466; DOI=10.1002/bip.22835;
Pearl L.H.;
"Review: The HSP90 molecular chaperone-an enigmatic ATPase.";
Biopolymers 105:594-607(2016).
[63]
FUNCTION, AND INTERACTION WITH IL1B.
PubMed=32272059; DOI=10.1016/j.cell.2020.03.031;
Zhang M., Liu L., Lin X., Wang Y., Li Y., Guo Q., Li S., Sun Y., Tao X.,
Zhang D., Lv X., Zheng L., Ge L.;
"A Translocation Pathway for Vesicle-Mediated Unconventional Protein
Secretion.";
Cell 181:637-652(2020).
[64]
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).
[65]
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).
[66]
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 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. They first 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 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). Involved in the translocation into ERGIC
(endoplasmic reticulum-Golgi intermediate compartment) of leaderless
cargos (lacking the secretion signal sequence) such as the interleukin
1/IL-1; the translocation process is mediated by the cargo receptor
TMED10 (PubMed:32272059). {ECO:0000269|PubMed:16478993,
ECO:0000269|PubMed:18239673, ECO:0000269|PubMed:19696785,
ECO:0000269|PubMed:20353823, ECO:0000269|PubMed:24613385,
ECO:0000269|PubMed:32272059, ECO:0000303|PubMed:25973397,
ECO:0000303|PubMed:26991466, ECO:0000303|PubMed:27295069}.
-!- ACTIVITY 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). Interacts with NR3C1 (via domain NR
LBD) and NR1D1 (via domain NR LBD) (By similarity). Interacts with
PDCL3 (By similarity). Interacts with TTC4 (via TPR repeats)
(PubMed:18320024). Interacts with IL1B; the interaction facilitates
cargo translocation into the ERGIC (PubMed:32272059).
{ECO:0000250|UniProtKB:P11499, ECO:0000250|UniProtKB:P34058,
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:18320024, 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:32272059,
ECO:0000269|PubMed:7588731, ECO:0000269|PubMed:9482106}.
-!- INTERACTION:
P08238; P36896: ACVR1B; NbExp=2; IntAct=EBI-352572, EBI-1384128;
P08238; Q9UL18: AGO1; NbExp=3; IntAct=EBI-352572, EBI-527363;
P08238; O95433: AHSA1; NbExp=4; IntAct=EBI-352572, EBI-448610;
P08238; O00170: AIP; NbExp=8; IntAct=EBI-352572, EBI-704197;
P08238; P31749: AKT1; NbExp=3; IntAct=EBI-352572, EBI-296087;
P08238; P31751: AKT2; NbExp=2; IntAct=EBI-352572, EBI-296058;
P08238; Q9UM73: ALK; NbExp=2; IntAct=EBI-352572, EBI-357361;
P08238; Q16671: AMHR2; NbExp=2; IntAct=EBI-352572, EBI-6423788;
P08238; Q01432: AMPD3; NbExp=2; IntAct=EBI-352572, EBI-1223554;
P08238; P10398: ARAF; NbExp=8; IntAct=EBI-352572, EBI-365961;
P08238; Q96GD4: AURKB; NbExp=4; IntAct=EBI-352572, EBI-624291;
P08238; P30530: AXL; NbExp=3; IntAct=EBI-352572, EBI-2850927;
P08238; P51451: BLK; NbExp=2; IntAct=EBI-352572, EBI-2105445;
P08238; P51813: BMX; NbExp=3; IntAct=EBI-352572, EBI-696657;
P08238; P15056: BRAF; NbExp=4; IntAct=EBI-352572, EBI-365980;
P08238; Q06187: BTK; NbExp=2; IntAct=EBI-352572, EBI-624835;
P08238; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-352572, EBI-1383687;
P08238; Q13555: CAMK2G; NbExp=2; IntAct=EBI-352572, EBI-1383465;
P08238; Q16543: CDC37; NbExp=11; IntAct=EBI-352572, EBI-295634;
P08238; Q7L3B6: CDC37L1; NbExp=5; IntAct=EBI-352572, EBI-2841876;
P08238; Q15131: CDK10; NbExp=2; IntAct=EBI-352572, EBI-1646959;
P08238; O94921: CDK14; NbExp=2; IntAct=EBI-352572, EBI-1043945;
P08238; Q96Q40: CDK15; NbExp=2; IntAct=EBI-352572, EBI-1051975;
P08238; Q00526: CDK3; NbExp=2; IntAct=EBI-352572, EBI-1245761;
P08238; P11802: CDK4; NbExp=4; IntAct=EBI-352572, EBI-295644;
P08238; Q00534: CDK6; NbExp=2; IntAct=EBI-352572, EBI-295663;
P08238; P50613: CDK7; NbExp=2; IntAct=EBI-352572, EBI-1245958;
P08238; P50750: CDK9; NbExp=2; IntAct=EBI-352572, EBI-1383449;
P08238; O14757: CHEK1; NbExp=3; IntAct=EBI-352572, EBI-974488;
P08238; Q9UHD1: CHORDC1; NbExp=6; IntAct=EBI-352572, EBI-2550959;
P08238; Q9UPZ9: CILK1; NbExp=2; IntAct=EBI-352572, EBI-6381479;
P08238; P49674: CSNK1E; NbExp=2; IntAct=EBI-352572, EBI-749343;
P08238; Q13616: CUL1; NbExp=2; IntAct=EBI-352572, EBI-359390;
P08238; Q13617: CUL2; NbExp=2; IntAct=EBI-352572, EBI-456179;
P08238; Q13618: CUL3; NbExp=3; IntAct=EBI-352572, EBI-456129;
P08238; Q13619: CUL4A; NbExp=2; IntAct=EBI-352572, EBI-456106;
P08238; Q13620: CUL4B; NbExp=2; IntAct=EBI-352572, EBI-456067;
P08238; Q16832: DDR2; NbExp=2; IntAct=EBI-352572, EBI-1381484;
P08238; P00533: EGFR; NbExp=10; IntAct=EBI-352572, EBI-297353;
P08238; P29317: EPHA2; NbExp=2; IntAct=EBI-352572, EBI-702104;
P08238; P04626: ERBB2; NbExp=4; IntAct=EBI-352572, EBI-641062;
P08238; P21860: ERBB3; NbExp=3; IntAct=EBI-352572, EBI-720706;
P08238; Q15303: ERBB4; NbExp=2; IntAct=EBI-352572, EBI-80371;
P08238; Q96A26: FAM162A; NbExp=3; IntAct=EBI-352572, EBI-6123466;
P08238; Q9UKC9: FBXL2; NbExp=2; IntAct=EBI-352572, EBI-724253;
P08238; O75426: FBXO24; NbExp=2; IntAct=EBI-352572, EBI-6425658;
P08238; Q9UKT8: FBXW2; NbExp=2; IntAct=EBI-352572, EBI-914727;
P08238; P11362: FGFR1; NbExp=2; IntAct=EBI-352572, EBI-1028277;
P08238; P22607: FGFR3; NbExp=2; IntAct=EBI-352572, EBI-348399;
P08238; P09769: FGR; NbExp=4; IntAct=EBI-352572, EBI-1383732;
P08238; Q02790: FKBP4; NbExp=6; IntAct=EBI-352572, EBI-1047444;
P08238; Q13451: FKBP5; NbExp=16; IntAct=EBI-352572, EBI-306914;
P08238; P35916: FLT4; NbExp=2; IntAct=EBI-352572, EBI-1005467;
P08238; P06241: FYN; NbExp=4; IntAct=EBI-352572, EBI-515315;
P08238; P49840: GSK3A; NbExp=3; IntAct=EBI-352572, EBI-1044067;
P08238; Q8TF76: HASPIN; NbExp=2; IntAct=EBI-352572, EBI-1237328;
P08238; P08631: HCK; NbExp=3; IntAct=EBI-352572, EBI-346340;
P08238; P08238: HSP90AB1; NbExp=4; IntAct=EBI-352572, EBI-352572;
P08238; Q14164: IKBKE; NbExp=2; IntAct=EBI-352572, EBI-307369;
P08238; Q9Y6K9: IKBKG; NbExp=3; IntAct=EBI-352572, EBI-81279;
P08238; Q08881: ITK; NbExp=2; IntAct=EBI-352572, EBI-968552;
P08238; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-352572, EBI-6426443;
P08238; P06239: LCK; NbExp=4; IntAct=EBI-352572, EBI-1348;
P08238; P53671: LIMK2; NbExp=2; IntAct=EBI-352572, EBI-1384350;
P08238; P07948: LYN; NbExp=2; IntAct=EBI-352572, EBI-79452;
P08238; Q8N7X4: MAGEB6; NbExp=3; IntAct=EBI-352572, EBI-6447163;
P08238; Q13163: MAP2K5; NbExp=3; IntAct=EBI-352572, EBI-307294;
P08238; Q99558: MAP3K14; NbExp=4; IntAct=EBI-352572, EBI-358011;
P08238; P41279: MAP3K8; NbExp=2; IntAct=EBI-352572, EBI-354900;
P08238; P80192: MAP3K9; NbExp=2; IntAct=EBI-352572, EBI-3951604;
P08238; Q92918: MAP4K1; NbExp=3; IntAct=EBI-352572, EBI-881;
P08238; P31152: MAPK4; NbExp=2; IntAct=EBI-352572, EBI-3906061;
P08238; P10636-8: MAPT; NbExp=11; IntAct=EBI-352572, EBI-366233;
P08238; P42679: MATK; NbExp=2; IntAct=EBI-352572, EBI-751664;
P08238; O15146: MUSK; NbExp=2; IntAct=EBI-352572, EBI-6423196;
P08238; Q9H1R3: MYLK2; NbExp=3; IntAct=EBI-352572, EBI-356910;
P08238; Q86YV6: MYLK4; NbExp=2; IntAct=EBI-352572, EBI-6424604;
P08238; Q8TD19: NEK9; NbExp=2; IntAct=EBI-352572, EBI-1044009;
P08238; O75469: NR1I2; NbExp=2; IntAct=EBI-352572, EBI-3905991;
P08238; Q8N165: PDIK1L; NbExp=2; IntAct=EBI-352572, EBI-6423298;
P08238; Q9P215: POGK; NbExp=2; IntAct=EBI-352572, EBI-2555775;
P08238; P53041: PPP5C; NbExp=7; IntAct=EBI-352572, EBI-716663;
P08238; Q13131: PRKAA1; NbExp=2; IntAct=EBI-352572, EBI-1181405;
P08238; P22694: PRKACB; NbExp=2; IntAct=EBI-352572, EBI-2679622;
P08238; Q02156: PRKCE; NbExp=4; IntAct=EBI-352572, EBI-706254;
P08238; P05129: PRKCG; NbExp=2; IntAct=EBI-352572, EBI-949799;
P08238; Q05513: PRKCZ; NbExp=2; IntAct=EBI-352572, EBI-295351;
P08238; Q15139: PRKD1; NbExp=2; IntAct=EBI-352572, EBI-1181072;
P08238; O60260: PRKN; NbExp=2; IntAct=EBI-352572, EBI-716346;
P08238; P51817: PRKX; NbExp=2; IntAct=EBI-352572, EBI-4302903;
P08238; P11801: PSKH1; NbExp=2; IntAct=EBI-352572, EBI-3922781;
P08238; Q96QS6: PSKH2; NbExp=2; IntAct=EBI-352572, EBI-6424813;
P08238; Q15185: PTGES3; NbExp=4; IntAct=EBI-352572, EBI-1049387;
P08238; Q13882: PTK6; NbExp=3; IntAct=EBI-352572, EBI-1383632;
P08238; P04049: RAF1; NbExp=5; IntAct=EBI-352572, EBI-365996;
P08238; P49758: RGS6; NbExp=2; IntAct=EBI-352572, EBI-6426927;
P08238; Q01974: ROR2; NbExp=2; IntAct=EBI-352572, EBI-6422642;
P08238; P62913: RPL11; NbExp=2; IntAct=EBI-352572, EBI-354380;
P08238; Q15418: RPS6KA1; NbExp=4; IntAct=EBI-352572, EBI-963034;
P08238; P51812: RPS6KA3; NbExp=3; IntAct=EBI-352572, EBI-1046616;
P08238; P31948: STIP1; NbExp=4; IntAct=EBI-352572, EBI-1054052;
P08238; Q15831: STK11; NbExp=4; IntAct=EBI-352572, EBI-306838;
P08238; Q15208: STK38; NbExp=2; IntAct=EBI-352572, EBI-458376;
P08238; Q9UNE7: STUB1; NbExp=5; IntAct=EBI-352572, EBI-357085;
P08238; Q9Y2Z0-2: SUGT1; NbExp=2; IntAct=EBI-352572, EBI-10768076;
P08238; Q9UHD2: TBK1; NbExp=2; IntAct=EBI-352572, EBI-356402;
P08238; Q96S53: TESK2; NbExp=2; IntAct=EBI-352572, EBI-1384110;
P08238; Q07912: TNK2; NbExp=3; IntAct=EBI-352572, EBI-603457;
P08238; Q9BXA6: TSSK6; NbExp=3; IntAct=EBI-352572, EBI-851883;
P08238; O95801: TTC4; NbExp=5; IntAct=EBI-352572, EBI-1050890;
P08238; P29597: TYK2; NbExp=2; IntAct=EBI-352572, EBI-1383454;
P08238; Q8IWX7: UNC45B; NbExp=2; IntAct=EBI-352572, EBI-9363363;
P08238; P07947: YES1; NbExp=3; IntAct=EBI-352572, EBI-515331;
-!- 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}. Dynein axonemal particle
{ECO:0000250|UniProtKB:Q6AZV1}. 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=Truncated N-terminus.; Evidence={ECO:0000305};
Sequence=CAB66478.1; Type=Frameshift; 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.
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.
PDB; 5UC4; X-ray; 2.05 A; A/B/C/D=1-218.
PDB; 5UCH; X-ray; 2.65 A; A/B/C/D=1-218.
PDB; 5UCI; X-ray; 2.70 A; A/B/C/D=1-218.
PDB; 5UCJ; X-ray; 1.69 A; A/B/C/D=1-218.
PDB; 6N8W; X-ray; 3.09 A; A/B/C/D=1-231.
PDB; 6N8Y; X-ray; 1.55 A; A=1-221.
PDBsum; 1QZ2; -.
PDBsum; 1UYM; -.
PDBsum; 2L6J; -.
PDBsum; 3FWV; -.
PDBsum; 3NMQ; -.
PDBsum; 3PRY; -.
PDBsum; 3UQ3; -.
PDBsum; 5FWK; -.
PDBsum; 5FWL; -.
PDBsum; 5FWM; -.
PDBsum; 5FWP; -.
PDBsum; 5UC4; -.
PDBsum; 5UCH; -.
PDBsum; 5UCI; -.
PDBsum; 5UCJ; -.
PDBsum; 6N8W; -.
PDBsum; 6N8Y; -.
SMR; P08238; -.
BioGRID; 109558; 525.
ComplexPortal; CPX-3285; HSP90B-CDC37 chaperone complex.
CORUM; P08238; -.
DIP; DIP-413N; -.
IntAct; P08238; 566.
MINT; P08238; -.
STRING; 9606.ENSP00000360609; -.
BindingDB; P08238; -.
ChEMBL; CHEMBL4303; -.
DrugBank; DB08293; (5E)-12-CHLORO-13,15-DIHYDROXY-4,7,8,9-TETRAHYDRO-2-BENZOXACYCLOTRIDECINE-1,10(3H,11H)-DIONE.
DrugBank; DB08153; (5E)-14-CHLORO-15,17-DIHYDROXY-4,7,8,9,10,11-HEXAHYDRO-2-BENZOXACYCLOPENTADECINE-1,12(3H,13H)-DIONE.
DrugBank; DB08292; (5Z)-12-CHLORO-13,15-DIHYDROXY-4,7,8,9-TETRAHYDRO-2-BENZOXACYCLOTRIDECINE-1,10(3H,11H)-DIONE.
DrugBank; DB08346; (5Z)-13-CHLORO-14,16-DIHYDROXY-3,4,7,8,9,10-HEXAHYDRO-1H-2-BENZOXACYCLOTETRADECINE-1,11(12H)-DIONE.
DrugBank; DB08465; 2-(3-AMINO-2,5,6-TRIMETHOXYPHENYL)ETHYL 5-CHLORO-2,4-DIHYDROXYBENZOATE.
DrugBank; DB08045; 4-{4-[4-(3-AMINOPROPOXY)PHENYL]-1H-PYRAZOL-5-YL}-6-CHLOROBENZENE-1,3-DIOL.
DrugBank; DB07877; 8-(6-BROMO-BENZO[1,3]DIOXOL-5-YLSULFANYL)-9-(3-ISOPROPYLAMINO-PROPYL)-ADENINE.
DrugBank; DB02754; 9-Butyl-8-(3,4,5-Trimethoxybenzyl)-9h-Purin-6-Amine.
DrugBank; DB07594; CCT-018159.
DrugBank; DB02424; Geldanamycin.
DrugBank; DB08464; METHYL 3-CHLORO-2-{3-[(2,5-DIHYDROXY-4-METHOXYPHENYL)AMINO]-3-OXOPROPYL}-4,6-DIHYDROXYBENZOATE.
DrugBank; DB09221; Polaprezinc.
DrugBank; DB03758; Radicicol.
DrugBank; DB06070; SNX-5422.
DrugBank; DB05134; Tanespimycin.
GuidetoPHARMACOLOGY; 2907; -.
MoonDB; P08238; Predicted.
CarbonylDB; P08238; -.
GlyConnect; 1302; 2 N-Linked glycans (2 sites).
GlyGen; P08238; 5 sites, 1 O-linked glycan (1 site).
iPTMnet; P08238; -.
MetOSite; P08238; -.
PhosphoSitePlus; P08238; -.
SwissPalm; P08238; -.
BioMuta; HSP90AB1; -.
DMDM; 17865718; -.
OGP; P08238; -.
EPD; P08238; -.
jPOST; P08238; -.
MassIVE; P08238; -.
MaxQB; P08238; -.
PaxDb; P08238; -.
PeptideAtlas; P08238; -.
PRIDE; P08238; -.
ProteomicsDB; 52096; -.
TopDownProteomics; P08238; -.
ABCD; P08238; 1 sequenced antibody.
Antibodypedia; 3929; 1709 antibodies.
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; -.
GeneCards; HSP90AB1; -.
HGNC; HGNC:5258; HSP90AB1.
HPA; ENSG00000096384; Low tissue specificity.
MIM; 140572; gene.
neXtProt; NX_P08238; -.
OpenTargets; ENSG00000096384; -.
PharmGKB; PA29524; -.
VEuPathDB; HostDB:ENSG00000096384.19; -.
eggNOG; KOG0019; Eukaryota.
GeneTree; ENSGT01020000230401; -.
HOGENOM; CLU_006684_1_3_1; -.
InParanoid; P08238; -.
OMA; IMDNCEQ; -.
OrthoDB; 924636at2759; -.
PhylomeDB; P08238; -.
TreeFam; TF300686; -.
BRENDA; 3.6.4.10; 2681.
PathwayCommons; P08238; -.
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.
Reactome; R-HSA-8939211; ESR-mediated signaling.
Reactome; R-HSA-9013418; RHOBTB2 GTPase cycle.
Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
Reactome; R-HSA-9613829; Chaperone Mediated Autophagy.
Reactome; R-HSA-9660826; Purinergic signaling in leishmaniasis infection.
Reactome; R-HSA-9679191; Potential therapeutics for SARS.
SIGNOR; P08238; -.
BioGRID-ORCS; 3326; 109 hits in 1017 CRISPR screens.
ChiTaRS; HSP90AB1; human.
EvolutionaryTrace; P08238; -.
GeneWiki; HSP90AB1; -.
GenomeRNAi; 3326; -.
Pharos; P08238; Tchem.
PRO; PR:P08238; -.
Proteomes; UP000005640; Chromosome 6.
RNAct; P08238; protein.
Bgee; ENSG00000096384; Expressed in hypothalamus and 252 other tissues.
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:0044295; C:axonal growth cone; ISS:ARUK-UCL.
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:0044294; C:dendritic growth cone; ISS:ARUK-UCL.
GO; GO:0120293; C:dynein axonemal particle; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:1990565; C:HSP90-CDC37 chaperone complex; IDA:ParkinsonsUK-UCL.
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; HDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; HDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; ISS:ARUK-UCL.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:1990917; C:ooplasm; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:ARUK-UCL.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0032991; C:protein-containing 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:0016887; F:ATPase activity; IEA:InterPro.
GO; GO:0045296; F:cadherin binding; HDA: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: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; HDA: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:0044183; F:protein folding chaperone; IEA:Ensembl.
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; HDA:UniProtKB.
GO; GO:0017098; F:sulfonylurea receptor binding; IEA:Ensembl.
GO; GO:0048156; F:tau protein binding; NAS:ARUK-UCL.
GO; GO:0030911; F:TPR domain binding; ISS:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ARUK-UCL.
GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
GO; GO:0002134; F:UTP binding; IEA:Ensembl.
GO; GO:0048675; P:axon extension; ISS:ARUK-UCL.
GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
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:0021955; P:central nervous system neuron axonogenesis; ISS:ARUK-UCL.
GO; GO:0051131; P:chaperone-mediated protein complex assembly; IDA:CAFA.
GO; GO:0030010; P:establishment of cell polarity; ISS:ARUK-UCL.
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:1901799; P:negative regulation of proteasomal protein catabolic process; ISS:ARUK-UCL.
GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0051248; P:negative regulation of protein metabolic process; ISS:ARUK-UCL.
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:1904031; P:positive regulation of cyclin-dependent protein kinase activity; ISS:ARUK-UCL.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:UniProtKB.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISS:ARUK-UCL.
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:0042307; P:positive regulation of protein import into nucleus; IEA:Ensembl.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:ARUK-UCL.
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:1902949; P:positive regulation of tau-protein kinase activity; IC:ARUK-UCL.
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; IBA:GO_Central.
GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
GO; GO:0035590; P:purinergic nucleotide receptor signaling pathway; TAS:Reactome.
GO; GO:1903827; P:regulation of cellular protein localization; ISS:ARUK-UCL.
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:0042493; P:response to drug; 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.
Gene3D; 1.20.120.790; -; 1.
Gene3D; 3.30.565.10; -; 1.
HAMAP; MF_00505; HSP90; 1.
IDEAL; IID00536; -.
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;
Cytoplasm; Direct protein sequencing; Glycoprotein; Membrane; Methylation;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
S-nitrosylation; Secreted; Stress response; Ubl conjugation.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000269|PubMed:2492519"
CHAIN 2..724
/note="Heat shock protein HSP 90-beta"
/id="PRO_0000062917"
REGION 2..527
/note="Interaction with TP53"
/evidence="ECO:0000269|PubMed:15358771"
REGION 2..214
/note="Interaction with BIRC2"
/evidence="ECO:0000269|PubMed:25486457"
REGION 9..231
/note="Interaction with NR3C1"
/evidence="ECO:0000250|UniProtKB:P11499"
REGION 215..552
/note="Interaction with AHSA1"
/evidence="ECO:0000269|PubMed:25486457"
REGION 222..270
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 264..608
/note="Interaction with NR3C1"
/evidence="ECO:0000250|UniProtKB:P11499"
REGION 620..723
/note="Interaction with NR1D1"
/evidence="ECO:0000250|UniProtKB:P11499"
REGION 696..724
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOTIF 720..724
/note="TPR repeat-binding"
COMPBIAS 241..270
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
BINDING 46
/note="ATP"
/evidence="ECO:0000250"
BINDING 88
/note="ATP"
BINDING 107
/note="ATP"
/evidence="ECO:0000250"
BINDING 133
/note="ATP; via amide nitrogen"
/evidence="ECO:0000250"
BINDING 392
/note="ATP"
/evidence="ECO:0000250"
SITE 126..127
/note="Cleaved under oxidative stress"
/evidence="ECO:0000269|PubMed:22848402"
MOD_RES 219
/note="N6-succinyllysine"
/evidence="ECO:0000250|UniProtKB:P11499"
MOD_RES 226
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18088087,
ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
MOD_RES 255
/note="Phosphoserine"
/evidence="ECO:0000269|Ref.12, ECO:0007744|PubMed:17081983,
ECO:0007744|PubMed:23186163"
MOD_RES 261
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P11499"
MOD_RES 297
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:17525332,
ECO:0007744|PubMed:23186163"
MOD_RES 301
/note="Phosphotyrosine; by SRC"
/evidence="ECO:0000269|PubMed:23585225"
MOD_RES 305
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:P11499"
MOD_RES 307
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648"
MOD_RES 399
/note="N6-malonyllysine"
/evidence="ECO:0000269|PubMed:21908771"
MOD_RES 435
/note="N6-acetyllysine"
/evidence="ECO:0007744|PubMed:19608861"
MOD_RES 445
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 479
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 481
/note="N6-acetyllysine"
/evidence="ECO:0007744|PubMed:19608861"
MOD_RES 484
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:P11499"
MOD_RES 531
/note="N6-methylated lysine; alternate"
/evidence="ECO:0000269|PubMed:24880080"
MOD_RES 531
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P11499"
MOD_RES 574
/note="N6-methylated lysine"
/evidence="ECO:0000269|PubMed:24880080"
MOD_RES 577
/note="N6-succinyllysine"
/evidence="ECO:0000250|UniProtKB:P11499"
MOD_RES 590
/note="S-nitrosocysteine"
/evidence="ECO:0000305|PubMed:19696785"
MOD_RES 624
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P11499"
MOD_RES 669
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:24275569"
MOD_RES 718
/note="Phosphoserine; by PLK2 and PLK3"
/evidence="ECO:0000269|PubMed:22828320"
CARBOHYD 434
/note="O-linked (GlcNAc) serine"
/evidence="ECO:0000250"
CARBOHYD 452
/note="O-linked (GlcNAc) serine"
/evidence="ECO:0000250"
VARIANT 349
/note="K -> E (in dbSNP:rs11538975)"
/id="VAR_049624"
MUTAGEN 42
/note="E->A: Strong ATP-binding. Strong interaction with
HSF1, HIF1A, ERBB2, MET, KEAP1 and RHOBTB2."
/evidence="ECO:0000269|PubMed:26517842"
MUTAGEN 88
/note="D->A: Impaired ATP-binding. Strong interaction with
HIF1A, MET, KEAP1 and RHOBTB2. Loss of interaction with
HSF1 and ERBB2."
/evidence="ECO:0000269|PubMed:26517842"
MUTAGEN 226
/note="S->A: Increases the binding affinity for AHR; when
associated with A-255. Increases AHR transcription
activity; when associated with A-255."
/evidence="ECO:0000269|PubMed:15581363"
MUTAGEN 226
/note="S->E: No effect on the interaction with AHR; when
associated with E-255."
/evidence="ECO:0000269|PubMed:15581363"
MUTAGEN 255
/note="S->A: Increases the binding affinity for AHR; when
associated with A-226. Increases AHR transcription
activity; when associated with A-226."
/evidence="ECO:0000269|PubMed:15581363"
MUTAGEN 255
/note="S->E: No effect on the interaction with AHR; when
associated with E-226."
/evidence="ECO:0000269|PubMed:15581363"
MUTAGEN 301
/note="Y->F: Decreases interaction with NOS3 and SRC.
impairs resists LPS-induced tyrosine phosphorylation. Does
not block LPS-induced pp60src phosphorylation."
/evidence="ECO:0000269|PubMed:23585225"
MUTAGEN 531
/note="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."
/evidence="ECO:0000269|PubMed:24880080"
MUTAGEN 574
/note="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."
/evidence="ECO:0000269|PubMed:24880080"
MUTAGEN 590
/note="C->A,N,D: Reduced ATPase activity and client protein
activation."
/evidence="ECO:0000269|PubMed:19696785"
CONFLICT 147
/note="T -> R (in Ref. 1; AAA36025)"
/evidence="ECO:0000305"
CONFLICT 177
/note="R -> M (in Ref. 1; AAA36025)"
/evidence="ECO:0000305"
CONFLICT 403
/note="V -> A (in Ref. 5; CAB66478)"
/evidence="ECO:0000305"
STRAND 2..6
/evidence="ECO:0007829|PDB:6N8W"
STRAND 13..16
/evidence="ECO:0007829|PDB:6N8Y"
HELIX 19..30
/evidence="ECO:0007829|PDB:6N8Y"
TURN 34..37
/evidence="ECO:0007829|PDB:5UCH"
HELIX 38..60
/evidence="ECO:0007829|PDB:6N8Y"
HELIX 62..65
/evidence="ECO:0007829|PDB:6N8Y"
STRAND 73..78
/evidence="ECO:0007829|PDB:6N8Y"
TURN 79..82
/evidence="ECO:0007829|PDB:6N8Y"
STRAND 83..88
/evidence="ECO:0007829|PDB:6N8Y"
HELIX 95..99
/evidence="ECO:0007829|PDB:6N8Y"
HELIX 101..118
/evidence="ECO:0007829|PDB:6N8Y"
HELIX 123..129
/evidence="ECO:0007829|PDB:6N8Y"
HELIX 132..138
/evidence="ECO:0007829|PDB:6N8Y"
STRAND 140..148
/evidence="ECO:0007829|PDB:6N8Y"
STRAND 155..159
/evidence="ECO:0007829|PDB:6N8Y"
STRAND 164..169
/evidence="ECO:0007829|PDB:6N8Y"
STRAND 176..185
/evidence="ECO:0007829|PDB:6N8Y"
HELIX 187..193
/evidence="ECO:0007829|PDB:6N8Y"
HELIX 195..205
/evidence="ECO:0007829|PDB:6N8Y"
STRAND 213..215
/evidence="ECO:0007829|PDB:6N8Y"
HELIX 288..290
/evidence="ECO:0007829|PDB:3PRY"
HELIX 293..295
/evidence="ECO:0007829|PDB:3PRY"
HELIX 298..309
/evidence="ECO:0007829|PDB:3PRY"
STRAND 316..323
/evidence="ECO:0007829|PDB:3PRY"
STRAND 325..327
/evidence="ECO:0007829|PDB:3PRY"
STRAND 329..335
/evidence="ECO:0007829|PDB:3PRY"
STRAND 353..357
/evidence="ECO:0007829|PDB:3PRY"
STRAND 360..364
/evidence="ECO:0007829|PDB:3PRY"
HELIX 367..369
/evidence="ECO:0007829|PDB:3PRY"
HELIX 372..374
/evidence="ECO:0007829|PDB:3PRY"
STRAND 378..386
/evidence="ECO:0007829|PDB:3PRY"
HELIX 395..420
/evidence="ECO:0007829|PDB:3PRY"
HELIX 423..443
/evidence="ECO:0007829|PDB:3PRY"
HELIX 445..447
/evidence="ECO:0007829|PDB:3PRY"
HELIX 448..453
/evidence="ECO:0007829|PDB:3PRY"
STRAND 456..459
/evidence="ECO:0007829|PDB:3PRY"
TURN 460..464
/evidence="ECO:0007829|PDB:3PRY"
HELIX 469..474
/evidence="ECO:0007829|PDB:3PRY"
STRAND 482..486
/evidence="ECO:0007829|PDB:3PRY"
HELIX 491..495
/evidence="ECO:0007829|PDB:3PRY"
HELIX 498..504
/evidence="ECO:0007829|PDB:3PRY"
TURN 505..507
/evidence="ECO:0007829|PDB:3PRY"
STRAND 510..512
/evidence="ECO:0007829|PDB:3PRY"
HELIX 518..525
/evidence="ECO:0007829|PDB:3PRY"
STRAND 531..535
/evidence="ECO:0007829|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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WP215: noncanonical wnt pathway
WP443: Beta Oxidation Meta MAPP
WP1045: TGF-beta Receptor Signaling Pathway
WP1571: EBV LMP1 signaling
WP1835: Interferon alpha/beta signaling
WP262: EBV LMP1 signaling
WP73: G Protein Signaling Pathways
WP1226: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1892: Protein folding
WP32: Translation Factors
WP809: TGF-beta Receptor Signaling Pathway
WP1269: Fatty Acid Beta Oxidation
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[Hsp90ab1 Hsp84 Hsp84-1 Hspcb] Heat shock protein HSP 90-beta (Heat shock 84 kDa) (HSP 84) (HSP84) (Tumor-specific transplantation 84 kDa antigen) (TSTA)
[HSP90AB1 HSP90B HSPC2 HSPCB] Heat shock protein HSP 90-beta (HSP 90) (Heat shock 84 kDa) (HSP 84) (HSP84)
[Hsp90ab1 Hsp84 Hspcb] Heat shock protein HSP 90-beta (Heat shock 84 kDa) (HSP 84) (HSP84)
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[Hsp90b1 Grp94 Tra-1 Tra1] Endoplasmin (94 kDa glucose-regulated protein) (GRP-94) (Endoplasmic reticulum resident protein 99) (ERp99) (Heat shock protein 90 kDa beta member 1) (Polymorphic tumor rejection antigen 1) (Tumor rejection antigen gp96)
[Hsp90aa1 Hsp86 Hspca] Heat shock protein HSP 90-alpha (EC 3.6.4.10) (Heat shock 86 kDa) (HSP 86) (HSP86)
[HSPB1 HSP27 HSP28] Heat shock protein beta-1 (HspB1) (28 kDa heat shock protein) (Estrogen-regulated 24 kDa protein) (Heat shock 27 kDa protein) (HSP 27) (Stress-responsive protein 27) (SRP27)
[HSP90AB1 HSPCB] Heat shock protein HSP 90-beta
[HSP90B1 GRP94 TRA1] Endoplasmin (94 kDa glucose-regulated protein) (GRP-94) (Heat shock protein 90 kDa beta member 1) (Tumor rejection antigen 1) (gp96 homolog)
[Hspb1 Hsp25 Hsp27] Heat shock protein beta-1 (HspB1) (Growth-related 25 kDa protein) (Heat shock 25 kDa protein) (HSP 25) (Heat shock 27 kDa protein) (HSP 27) (p25)
[HSP90B1 GRP94 TRA1] Endoplasmin (94 kDa glucose-regulated protein) (GRP-94) (Heat shock protein 90 kDa beta member 1)
[hsp90ab1 hsp90b] Heat shock protein HSP 90-beta
[HSP90-5 CR88 EMB1956 HSP88-1 At2g04030] Heat shock protein 90-5, chloroplastic (AtHSP90.5) (AtHsp90-5) (Heat shock protein 88-1) (Hsp88-1) (Hsp90C) (Protein EMBRYO DEFECTIVE 1956) (Protein chlorate-resistance 88)
[HSP90AA1 HSP90A HSPCA] Heat shock protein HSP 90-alpha (EC 3.6.4.10)
[HSPA1A HSP72 HSPA1 HSX70] Heat shock 70 kDa protein 1A (Heat shock 70 kDa protein 1) (HSP70-1) (HSP70.1)
[HSPA5 GRP78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[HSPA1B HSP72] Heat shock 70 kDa protein 1B (Heat shock 70 kDa protein 2) (HSP70-2) (HSP70.2)
[HSP90AB1 QccE-21185] Heat shock protein HSP 90-beta
[HSP90AB1 HSPCB] Heat shock protein HSP 90-beta
[Hsp90b1 Grp94 Tra1] Endoplasmin (94 kDa glucose-regulated protein) (GRP-94) (Heat shock protein 90 kDa beta member 1)
[HSP90AB1 HSPCB] Heat shock protein HSP 90-beta
[Hspa1a Hsp70-3 Hsp70A1] Heat shock 70 kDa protein 1A (Heat shock 70 kDa protein 3) (HSP70.3) (Hsp68)
[Hspa1a Hsp70-1 Hspa1] Heat shock 70 kDa protein 1A (Heat shock 70 kDa protein 2) (HSP70-2) (HSP70.2)
[Hspa1b Hsp70-2 Hspa2] Heat shock 70 kDa protein 1B (Heat shock 70 kDa protein 1) (HSP70-1) (HSP70.1)
[hsp90a.1 hsp90 hsp90a hsp90aa1 zgc:86652] Heat shock protein HSP 90-alpha 1
[HSP90AA1 HSPCA] Heat shock protein HSP 90-alpha (EC 3.6.4.10)
[Hspa1b Hcp70.1 Hsp70-1 Hsp70a1 Hspa1] Heat shock 70 kDa protein 1B (Heat shock 70 kDa protein 1) (HSP70.1)
[Hspa5 Grp78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein) (Steroidogenesis-activator polypeptide)
[HSP70-4 HSC70-4 HSP70 MED37_2 MED37C At3g12580 T16H11.7 T2E22.11] Heat shock 70 kDa protein 4 (Heat shock cognate 70 kDa protein 4) (Heat shock cognate protein 70-4) (AtHsc70-4) (Heat shock protein 70-4) (AtHsp70-4)

Bibliography :