ID HS90B_HUMAN Reviewed; 724 AA.
AC P08238; B2R5P0; Q5T9W7; Q9NQW0; Q9NTK6;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 10-MAY-2017, entry version 220.
DE RecName: Full=Heat shock protein HSP 90-beta;
DE Short=HSP 90;
DE AltName: Full=Heat shock 84 kDa;
DE Short=HSP 84;
DE Short=HSP84;
GN Name=HSP90AB1; Synonyms=HSP90B, HSPC2, HSPCB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3301534; DOI=10.1016/0378-1119(87)90012-6;
RA Rebbe N.F., Ware J., Bertina R.M., Modrich P., Stafford D.W.;
RT "Nucleotide sequence of a cDNA for a member of the human 90-kDa heat-
RT shock protein family.";
RL Gene 53:235-245(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2768249;
RA Rebbe N.F., Hickman W.S., Ley T.J., Stafford D.W., Hickman S.;
RT "Nucleotide sequence and regulation of a human 90-kDa heat shock
RT protein gene.";
RL J. Biol. Chem. 264:15006-15011(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2469626; DOI=10.1016/0378-1119(88)90182-5;
RA Hoffmann T., Hovemann B.;
RT "Heat-shock proteins, Hsp84 and Hsp86, of mice and men: two related
RT genes encode formerly identified tumour-specific transplantation
RT antigens.";
RL Gene 74:491-501(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Lu L., Huang X.Y., Yin L.L., Xu M., Li J.M., Zhou Z.M., Sha J.H.;
RT "Cloning a new isoform of heat shock 90kDa in testis.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, Lymph, Muscle, Skin, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP PROTEIN SEQUENCE OF 2-21, AND PHOSPHORYLATION.
RX PubMed=2492519;
RA Lees-Miller S.P., Anderson C.W.;
RT "Two human 90-kDa heat shock proteins are phosphorylated in vivo at
RT conserved serines that are phosphorylated in vitro by casein kinase
RT II.";
RL J. Biol. Chem. 264:2431-2437(1989).
RN [12]
RP PROTEIN SEQUENCE OF 42-107; 149-168; 181-197; 204-221; 250-265;
RP 274-284; 292-348; 360-392; 412-427; 439-448; 450-475; 482-502;
RP 506-526; 539-551; 584-604; 613-639 AND 653-679, PHOSPHORYLATION AT
RP SER-255, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 50-118.
RX PubMed=8180474; DOI=10.1007/BF00292342;
RA Takahashi I., Tanuma R., Hirata M., Hashimoto K.;
RT "A cosmid clone at the D6S182 locus on human chromosome 6p12 contains
RT the 90-kDa heat shock protein beta gene (HSP90 beta).";
RL Mamm. Genome 5:121-122(1994).
RN [14]
RP SEQUENCE REVISION.
RA Takahashi I., Tanuma R., Hirata M., Hashimoto K.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN [15]
RP PROTEIN SEQUENCE OF 54-64 AND 187-199.
RC TISSUE=Colon carcinoma;
RX PubMed=9150948; DOI=10.1002/elps.1150180344;
RA Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.;
RT "A two-dimensional gel database of human colon carcinoma proteins.";
RL Electrophoresis 18:605-613(1997).
RN [16]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 93-724.
RC TISSUE=Pancreas;
RA Mason A., O'Connor D., Greenhalf W.;
RT "Novel sequence for human Hsp90 beta giving a substitution of R55T
RT (R147 in original sequence) and M85R (M177 in original sequence).";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [17]
RP HOMODIMERIZATION.
RX PubMed=7588731; DOI=10.1111/j.1432-1033.1995.001_1.x;
RA Nemoto T., Ohara-Nemoto Y., Ota M., Takagi T., Yokoyama K.;
RT "Mechanism of dimer formation of the 90-kDa heat-shock protein.";
RL Eur. J. Biochem. 233:1-8(1995).
RN [18]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CDK6 AND CDC37.
RX PubMed=9482106; DOI=10.1038/sj.onc.1201570;
RA Mahony D., Parry D.A., Lees E.;
RT "Active cdk6 complexes are predominantly nuclear and represent only a
RT minority of the cdk6 in T cells.";
RL Oncogene 16:603-611(1998).
RN [19]
RP PHOSPHORYLATION AT SER-226 AND SER-255, MUTAGENESIS OF SER-226 AND
RP SER-255, AND INTERACTION WITH AHR.
RX PubMed=15581363; DOI=10.1021/bi048736m;
RA Ogiso H., Kagi N., Matsumoto E., Nishimoto M., Arai R., Shirouzu M.,
RA Mimura J., Fujii-Kuriyama Y., Yokoyama S.;
RT "Phosphorylation analysis of 90 kDa heat shock protein within the
RT cytosolic arylhydrocarbon receptor complex.";
RL Biochemistry 43:15510-15519(2004).
RN [20]
RP INTERACTION WITH TP53, AND REGION.
RX PubMed=15358771; DOI=10.1074/jbc.M407687200;
RA Mueller L., Schaupp A., Walerych D., Wegele H., Buchner J.;
RT "Hsp90 regulates the activity of wild type p53 under physiological and
RT elevated temperatures.";
RL J. Biol. Chem. 279:48846-48854(2004).
RN [21]
RP ISGYLATION.
RX PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT human cells.";
RL Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [23]
RP INTERACTION WITH SGTA, AND SUBCELLULAR LOCATION.
RX PubMed=16580629; DOI=10.1016/j.bbrc.2006.03.090;
RA Yin H., Wang H., Zong H., Chen X., Wang Y., Yun X., Wu Y., Wang J.,
RA Gu J.;
RT "SGT, a Hsp90beta binding partner, is accumulated in the nucleus
RT during cell apoptosis.";
RL Biochem. Biophys. Res. Commun. 343:1153-1158(2006).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [25]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [26]
RP FUNCTION, AND INTERACTION WITH UNC45A.
RX PubMed=16478993; DOI=10.1128/MCB.26.5.1722-1730.2006;
RA Chadli A., Graham J.D., Abel M.G., Jackson T.A., Gordon D.F.,
RA Wood W.M., Felts S.J., Horwitz K.B., Toft D.;
RT "GCUNC-45 is a novel regulator for the progesterone receptor/hsp90
RT chaperoning pathway.";
RL Mol. Cell. Biol. 26:1722-1730(2006).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-297, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [28]
RP UBIQUITINATION.
RX PubMed=18042044; DOI=10.1042/BJ20071338;
RA Windheim M., Peggie M., Cohen P.;
RT "Two different classes of E2 ubiquitin-conjugating enzymes are
RT required for the mono-ubiquitination of proteins and elongation by
RT polyubiquitin chains with a specific topology.";
RL Biochem. J. 409:723-729(2008).
RN [29]
RP INTERACTION WITH DNAJC7.
RX PubMed=18620420; DOI=10.1021/bi800770g;
RA Moffatt N.S., Bruinsma E., Uhl C., Obermann W.M., Toft D.;
RT "Role of the cochaperone Tpr2 in Hsp90 chaperoning.";
RL Biochemistry 47:8203-8213(2008).
RN [30]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH BIRC2,
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=18239673; DOI=10.1038/cdd.2008.5;
RA Didelot C., Lanneau D., Brunet M., Bouchot A., Cartier J., Jacquel A.,
RA Ducoroy P., Cathelin S., Decologne N., Chiosis G., Dubrez-Daloz L.,
RA Solary E., Garrido C.;
RT "Interaction of heat-shock protein 90 beta isoform (HSP90 beta) with
RT cellular inhibitor of apoptosis 1 (c-IAP1) is required for cell
RT differentiation.";
RL Cell Death Differ. 15:859-866(2008).
RN [31]
RP SUBUNIT, ENZYME REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18400751; DOI=10.1074/jbc.M800540200;
RA Richter K., Soroka J., Skalniak L., Leskovar A., Hessling M.,
RA Reinstein J., Buchner J.;
RT "Conserved conformational changes in the ATPase cycle of human
RT Hsp90.";
RL J. Biol. Chem. 283:17757-17765(2008).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [35]
RP FUNCTION, S-NITROSYLATION AT CYS-590, AND MUTAGENESIS OF CYS-590.
RX PubMed=19696785; DOI=10.1038/embor.2009.153;
RA Retzlaff M., Stahl M., Eberl H.C., Lagleder S., Beck J., Kessler H.,
RA Buchner J.;
RT "Hsp90 is regulated by a switch point in the C-terminal domain.";
RL EMBO Rep. 10:1147-1153(2009).
RN [36]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-435 AND LYS-481, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [37]
RP INTERACTION WITH TGFB1 PROCESSED FORM (LAP), AND SUBCELLULAR LOCATION.
RX PubMed=20599762; DOI=10.1016/j.bbrc.2010.06.112;
RA Suzuki S., Kulkarni A.B.;
RT "Extracellular heat shock protein HSP90beta secreted by MG63
RT osteosarcoma cells inhibits activation of latent TGF-beta1.";
RL Biochem. Biophys. Res. Commun. 398:525-531(2010).
RN [38]
RP INTERACTION WITH HSP90AA1; JAK2 AND PRKCE, INDUCTION, AND FUNCTION.
RX PubMed=20353823; DOI=10.1016/j.cellsig.2010.03.012;
RA Cheng M.B., Zhang Y., Zhong X., Sutter B., Cao C.Y., Chen X.S.,
RA Cheng X.K., Zhang Y., Xiao L., Shen Y.F.;
RT "Stat1 mediates an auto-regulation of hsp90beta gene in heat shock
RT response.";
RL Cell. Signal. 22:1206-1213(2010).
RN [39]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [40]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [41]
RP MALONYLATION AT LYS-399.
RX PubMed=21908771; DOI=10.1074/mcp.M111.012658;
RA Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,
RA He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,
RA Dai J., Verdin E., Ye Y., Zhao Y.;
RT "The first identification of lysine malonylation substrates and its
RT regulatory enzyme.";
RL Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
RN [42]
RP INTERACTION WITH AHSA1 AND XPO1.
RX PubMed=22022502; DOI=10.1371/journal.pone.0026044;
RA Echeverria P.C., Bernthaler A., Dupuis P., Mayer B., Picard D.;
RT "An interaction network predicted from public data as a discovery
RT tool: application to the Hsp90 molecular chaperone machine.";
RL PLoS ONE 6:E26044-E26044(2011).
RN [43]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [44]
RP PHOSPHORYLATION AT SER-718 BY PLK2 AND PLK3.
RX PubMed=22828320; DOI=10.1016/j.bbapap.2012.07.003;
RA Salvi M., Trashi E., Cozza G., Franchin C., Arrigoni G., Pinna L.A.;
RT "Investigation on PLK2 and PLK3 substrate recognition.";
RL Biochim. Biophys. Acta 1824:1366-1373(2012).
RN [45]
RP INTERACTION WITH CDC25A.
RX PubMed=22843495; DOI=10.1093/hmg/dds303;
RA Giessrigl B., Krieger S., Rosner M., Huttary N., Saiko P., Alami M.,
RA Messaoudi S., Peyrat J.F., Maciuk A., Gollinger M., Kopf S.,
RA Kazlauskas E., Mazal P., Szekeres T., Hengstschlaeger M., Matulis D.,
RA Jaeger W., Krupitza G.;
RT "Hsp90 stabilizes Cdc25A and counteracts heat shock-mediated Cdc25A
RT degradation and cell-cycle attenuation in pancreatic carcinoma
RT cells.";
RL Hum. Mol. Genet. 21:4615-4627(2012).
RN [46]
RP PROTEIN CLEAVAGE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=22848402; DOI=10.1371/journal.pone.0040795;
RA Beck R., Dejeans N., Glorieux C., Creton M., Delaive E., Dieu M.,
RA Raes M., Leveque P., Gallez B., Depuydt M., Collet J.F.,
RA Calderon P.B., Verrax J.;
RT "Hsp90 is cleaved by reactive oxygen species at a highly conserved N-
RT terminal amino acid motif.";
RL PLoS ONE 7:E40795-E40795(2012).
RN [47]
RP INTERACTION WITH NOS3, MUTAGENESIS OF TYR-301, AND PHOSPHORYLATION AT
RP TYR-301 BY SRC.
RX PubMed=23585225; DOI=10.1152/ajplung.00419.2012;
RA Barabutis N., Handa V., Dimitropoulou C., Rafikov R., Snead C.,
RA Kumar S., Joshi A., Thangjam G., Fulton D., Black S.M., Patel V.,
RA Catravas J.D.;
RT "LPS induces pp60c-src-mediated tyrosine phosphorylation of Hsp90 in
RT lung vascular endothelial cells and mouse lung.";
RL Am. J. Physiol. 304:L883-L893(2013).
RN [48]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-255; THR-297;
RP SER-445 AND THR-479, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [49]
RP INTERACTION WITH MAPK7.
RX PubMed=23428871; DOI=10.1128/MCB.01246-12;
RA Erazo T., Moreno A., Ruiz-Babot G., Rodriguez-Asiain A., Morrice N.A.,
RA Espadamala J., Bayascas J.R., Gomez N., Lizcano J.M.;
RT "Canonical and kinase activity-independent mechanisms for
RT extracellular signal-regulated kinase 5 (ERK5) nuclear translocation
RT require dissociation of Hsp90 from the ERK5-Cdc37 complex.";
RL Mol. Cell. Biol. 33:1671-1686(2013).
RN [50]
RP INTERACTION WITH KCNQ4.
RX PubMed=23431407; DOI=10.1371/journal.pone.0057282;
RA Gao Y., Yechikov S., Vazquez A.E., Chen D., Nie L.;
RT "Distinct roles of molecular chaperones HSP90alpha and HSP90beta in
RT the biogenesis of KCNQ4 channels.";
RL PLoS ONE 8:E57282-E57282(2013).
RN [51]
RP FUNCTION, AND INTERACTION WITH STUB1 AND SMAD3.
RX PubMed=24613385; DOI=10.1016/j.bbrc.2014.02.124;
RA Shang Y., Xu X., Duan X., Guo J., Wang Y., Ren F., He D., Chang Z.;
RT "Hsp70 and Hsp90 oppositely regulate TGF-beta signaling through
RT CHIP/Stub1.";
RL Biochem. Biophys. Res. Commun. 446:387-392(2014).
RN [52]
RP METHYLATION AT LYS-531 AND LYS-574 BY SMYD2, IDENTIFICATION BY MASS
RP SPECTROMETRY, MUTAGENESIS OF LYS-531 AND LYS-574, INTERACTION WITH
RP STIP1 AND CDC37, AND SUBCELLULAR LOCATION.
RX PubMed=24880080; DOI=10.1016/j.canlet.2014.05.014;
RA Hamamoto R., Toyokawa G., Nakakido M., Ueda K., Nakamura Y.;
RT "SMYD2-dependent HSP90 methylation promotes cancer cell proliferation
RT by regulating the chaperone complex formation.";
RL Cancer Lett. 351:126-133(2014).
RN [53]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-669, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA Wang L., Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT liver phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [54]
RP INTERACTION WITH NWD1.
RX PubMed=24681825;
RA Correa R.G., Krajewska M., Ware C.F., Gerlic M., Reed J.C.;
RT "The NLR-related protein NWD1 is associated with prostate cancer and
RT modulates androgen receptor signaling.";
RL Oncotarget 5:1666-1682(2014).
RN [55]
RP INTERACTION WITH AHSA1; BIRC2 AND CDC37, AND REGION.
RX PubMed=25486457; DOI=10.1016/j.bbamcr.2014.11.026;
RA Synoradzki K., Bieganowski P.;
RT "Middle domain of human Hsp90 isoforms differentially binds Aha1 in
RT human cells and alters Hsp90 activity in yeast.";
RL Biochim. Biophys. Acta 1853:445-452(2015).
RN [56]
RP REVIEW.
RX PubMed=25973397; DOI=10.3389/fonc.2015.00100;
RA Khurana N., Bhattacharyya S.;
RT "Hsp90, the concertmaster: tuning transcription.";
RL Front. Oncol. 5:100-100(2015).
RN [57]
RP INTERACTION WITH HSF1; HIF1A; ERBB2; MET; KEAP1 AND RHOBTB2, AND
RP MUTAGENESIS OF GLU-42 AND ASP-88.
RX PubMed=26517842; DOI=10.1371/journal.pone.0141786;
RA Prince T.L., Kijima T., Tatokoro M., Lee S., Tsutsumi S., Yim K.,
RA Rivas C., Alarcon S., Schwartz H., Khamit-Kush K., Scroggins B.T.,
RA Beebe K., Trepel J.B., Neckers L.;
RT "Client proteins and small molecule inhibitors display distinct
RT binding preferences for constitutive and stress-induced HSP90 isoforms
RT and their conformationally restricted mutants.";
RL PLoS ONE 10:E0141786-E0141786(2015).
RN [58]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [59]
RP REVIEW.
RX PubMed=27295069; DOI=10.1016/j.biochi.2016.05.018;
RA Verma S., Goyal S., Jamal S., Singh A., Grover A.;
RT "Hsp90: Friends, clients and natural foes.";
RL Biochimie 127:227-240(2016).
RN [60]
RP REVIEW.
RX PubMed=26991466; DOI=10.1002/bip.22835;
RA Pearl L.H.;
RT "Review: The HSP90 molecular chaperone-an enigmatic ATPase.";
RL Biopolymers 105:594-607(2016).
RN [61]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 1-221 IN COMPLEX WITH PURINE
RP ANALOG.
RX PubMed=15217611; DOI=10.1016/j.chembiol.2004.03.033;
RA Wright L., Barril X., Dymock B., Sheridan L., Surgenor A., Beswick M.,
RA Drysdale M., Collier A., Massey A., Davies N., Fink A., Fromont C.,
RA Aherne W., Boxall K., Sharp S., Workman P., Hubbard R.E.;
RT "Structure-activity relationships in purine-based inhibitor binding to
RT HSP90 isoforms.";
RL Chem. Biol. 11:775-785(2004).
RN [62]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 720-724 IN COMPLEX WITH
RP FKBP4.
RX PubMed=15159550; DOI=10.1073/pnas.0305969101;
RA Wu B., Li P., Liu Y., Lou Z., Ding Y., Shu C., Ye S., Bartlam M.,
RA Shen B., Rao Z.;
RT "3D structure of human FK506-binding protein 52: implications for the
RT assembly of the glucocorticoid receptor/Hsp90/immunophilin
RT heterocomplex.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8348-8353(2004).
RN [63]
RP X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 284-543.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the middle domain of human hsp90-beta.";
RL Submitted (DEC-2010) to the PDB data bank.
CC -!- FUNCTION: Molecular chaperone that promotes the maturation,
CC structural maintenance and proper regulation of specific target
CC proteins involved for instance in cell cycle control and signal
CC transduction. Undergoes a functional cycle that is linked to its
CC ATPase activity. This cycle probably induces conformational
CC changes in the client proteins, thereby causing their activation.
CC Interacts dynamically with various co-chaperones that modulate its
CC substrate recognition, ATPase cycle and chaperone function
CC (PubMed:16478993, PubMed:19696785). Engages with a range of client
CC protein classes via its interaction with various co-chaperone
CC proteins or complexes, that act as adapters, simultaneously able
CC to interact with the specific client and the central chaperone
CC itself. Recruitment of ATP and co-chaperone followed by client
CC protein forms a functional chaperone. After the completion of the
CC chaperoning process, properly folded client protein and co-
CC chaperone leave HSP90 in an ADP-bound partially open conformation
CC and finally, ADP is released from HSP90 which acquires an open
CC conformation for the next cycle (PubMed:27295069,
CC PubMed:26991466). Apart from its chaperone activity, it also plays
CC a role in the regulation of the transcription machinery. HSP90 and
CC its co-chaperones modulate transcription at least at three
CC different levels. In the first place, they alter the steady-state
CC levels of certain transcription factors in response to various
CC physiological cues. Second, they modulate the activity of certain
CC epigenetic modifiers, such as histone deacetylases or DNA methyl
CC transferases, and thereby respond to the change in the
CC environment. Third, they participate in the eviction of histones
CC from the promoter region of certain genes and thereby turn on gene
CC expression (PubMed:25973397). Antagonizes STUB1-mediated
CC inhibition of TGF-beta signaling via inhibition of STUB1-mediated
CC SMAD3 ubiquitination and degradation (PubMed:24613385). Promotes
CC cell differentiation by chaperoning BIRC2 and thereby protecting
CC from auto-ubiquitination and degradation by the proteasomal
CC machinery (PubMed:18239673). Main chaperone that is involved in
CC the phosphorylation/activation of the STAT1 by chaperoning both
CC JAK2 and PRKCE under heat shock and in turn, activates its own
CC transcription (PubMed:20353823). {ECO:0000269|PubMed:16478993,
CC ECO:0000269|PubMed:18239673, ECO:0000269|PubMed:19696785,
CC ECO:0000269|PubMed:20353823, ECO:0000269|PubMed:24613385,
CC ECO:0000303|PubMed:25973397, ECO:0000303|PubMed:26991466,
CC ECO:0000303|PubMed:27295069}.
CC -!- ENZYME REGULATION: In the resting state, through the dimerization
CC of its C-terminal domain, HSP90 forms a homodimer which is defined
CC as the open conformation. Upon ATP-binding, the N-terminal domain
CC undergoes significant conformational changes and comes in contact
CC to form an active closed conformation. After HSP90 finishes its
CC chaperoning tasks of assisting the proper folding, stabilization
CC and activation of client proteins under the active state, ATP
CC molecule is hydrolyzed to ADP which then dissociates from HSP90
CC and directs the protein back to the resting state.
CC {ECO:0000269|PubMed:18400751}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=300 uM for ATP {ECO:0000269|PubMed:18400751};
CC -!- SUBUNIT: Monomer (PubMed:24880080). Homodimer (PubMed:7588731,
CC PubMed:18400751). Forms a complex with CDK6 and CDC37
CC (PubMed:9482106, PubMed:25486457). Interacts with UNC45A; binding
CC to UNC45A involves 2 UNC45A monomers per HSP90AB1 dimer
CC (PubMed:16478993). Interacts with CHORDC1 (By similarity).
CC Interacts with DNAJC7 (PubMed:18620420). Interacts with FKBP4
CC (PubMed:15159550). May interact with NWD1 (PubMed:24681825).
CC Interacts with SGTA (PubMed:16580629). Interacts with HSF1 in an
CC ATP-dependent manner. Interacts with MET; the interaction
CC suppresses MET kinase activity. Interacts with ERBB2 in an ATP-
CC dependent manner; the interaction suppresses ERBB2 kinase
CC activity. Interacts with HIF1A, KEAP1 and RHOBTB2
CC (PubMed:26517842). Interacts with STUB1 and SMAD3
CC (PubMed:24613385). Interacts with XPO1 and AHSA1 (PubMed:22022502,
CC PubMed:25486457). Interacts with BIRC2 (PubMed:25486457).
CC Interacts with KCNQ4; promotes cell surface expression of KCNQ4
CC (PubMed:23431407). Interacts with BIRC2; prevents auto-
CC ubiquitination and degradation of its client protein BIRC2
CC (PubMed:18239673). Interacts with NOS3 (PubMed:23585225).
CC Interacts with AHR; interaction is inhibited by HSP90AB1
CC phosphorylation on Ser-226 and Ser-255 (PubMed:15581363).
CC Interacts with STIP1 and CDC37; upon SMYD2-dependent methylation
CC (PubMed:24880080). Interacts with JAK2 and PRKCE; promotes
CC functional activation in a heat shock-dependent manner
CC (PubMed:20353823). Interacts with HSP90AA1; interaction is
CC constitutive (PubMed:20353823). HSP90AB1-CDC37 chaperone complex
CC interacts with inactive MAPK7 (via N-terminal half) in resting
CC cells; the interaction is MAP2K5-independent and prevents from
CC ubiquitination and proteasomal degradation (PubMed:23428871).
CC Interacts with CDC25A; prevents heat shock-mediated CDC25A
CC degradation and contributes to cell cycle progression
CC (PubMed:22843495). Interacts with TP53 (via DNA binding domain);
CC suppresses TP53 aggregation and prevents from irreversible thermal
CC inactivation (PubMed:15358771). Interacts with TGFB1 processed
CC form (LAP); inhibits latent TGFB1 activation (PubMed:20599762).
CC Interacts with TRIM8; prevents nucleus translocation of
CC phosphorylated STAT3 and HSP90AB1 (By similarity).
CC {ECO:0000250|UniProtKB:P11499, ECO:0000269|PubMed:15159550,
CC ECO:0000269|PubMed:15358771, ECO:0000269|PubMed:15581363,
CC ECO:0000269|PubMed:16478993, ECO:0000269|PubMed:16580629,
CC ECO:0000269|PubMed:18239673, ECO:0000269|PubMed:18400751,
CC ECO:0000269|PubMed:18620420, ECO:0000269|PubMed:20353823,
CC ECO:0000269|PubMed:20599762, ECO:0000269|PubMed:22022502,
CC ECO:0000269|PubMed:22843495, ECO:0000269|PubMed:23428871,
CC ECO:0000269|PubMed:23431407, ECO:0000269|PubMed:23585225,
CC ECO:0000269|PubMed:24613385, ECO:0000269|PubMed:24681825,
CC ECO:0000269|PubMed:24880080, ECO:0000269|PubMed:25486457,
CC ECO:0000269|PubMed:26517842, ECO:0000269|PubMed:7588731,
CC ECO:0000269|PubMed:9482106}.
CC -!- INTERACTION:
CC P36896:ACVR1B; NbExp=2; IntAct=EBI-352572, EBI-1384128;
CC Q9UL18:AGO1; NbExp=3; IntAct=EBI-352572, EBI-527363;
CC O95433:AHSA1; NbExp=3; IntAct=EBI-352572, EBI-448610;
CC O00170:AIP; NbExp=3; IntAct=EBI-352572, EBI-704197;
CC P31751:AKT2; NbExp=2; IntAct=EBI-352572, EBI-296058;
CC Q9UM73:ALK; NbExp=2; IntAct=EBI-352572, EBI-357361;
CC Q16671:AMHR2; NbExp=2; IntAct=EBI-352572, EBI-6423788;
CC Q01432:AMPD3; NbExp=2; IntAct=EBI-352572, EBI-1223554;
CC P10398:ARAF; NbExp=6; IntAct=EBI-352572, EBI-365961;
CC Q96GD4:AURKB; NbExp=2; IntAct=EBI-352572, EBI-624291;
CC P15056:BRAF; NbExp=2; IntAct=EBI-352572, EBI-365980;
CC Q06187:BTK; NbExp=2; IntAct=EBI-352572, EBI-624835;
CC Q13555:CAMK2G; NbExp=2; IntAct=EBI-352572, EBI-1383465;
CC Q16543:CDC37; NbExp=7; IntAct=EBI-352572, EBI-295634;
CC Q7L3B6:CDC37L1; NbExp=5; IntAct=EBI-352572, EBI-2841876;
CC Q15131:CDK10; NbExp=2; IntAct=EBI-352572, EBI-1646959;
CC O94921:CDK14; NbExp=2; IntAct=EBI-352572, EBI-1043945;
CC Q96Q40:CDK15; NbExp=2; IntAct=EBI-352572, EBI-1051975;
CC P11802:CDK4; NbExp=3; IntAct=EBI-352572, EBI-295644;
CC Q00534:CDK6; NbExp=2; IntAct=EBI-352572, EBI-295663;
CC P50750:CDK9; NbExp=2; IntAct=EBI-352572, EBI-1383449;
CC O14757:CHEK1; NbExp=3; IntAct=EBI-352572, EBI-974488;
CC Q9UHD1:CHORDC1; NbExp=3; IntAct=EBI-352572, EBI-2550959;
CC P49674:CSNK1E; NbExp=2; IntAct=EBI-352572, EBI-749343;
CC Q13618:CUL3; NbExp=2; IntAct=EBI-352572, EBI-456129;
CC Q16832:DDR2; NbExp=2; IntAct=EBI-352572, EBI-1381484;
CC P00533:EGFR; NbExp=8; IntAct=EBI-352572, EBI-297353;
CC P29317:EPHA2; NbExp=2; IntAct=EBI-352572, EBI-702104;
CC P04626:ERBB2; NbExp=3; IntAct=EBI-352572, EBI-641062;
CC P21860:ERBB3; NbExp=3; IntAct=EBI-352572, EBI-720706;
CC Q15303:ERBB4; NbExp=2; IntAct=EBI-352572, EBI-80371;
CC Q96A26:FAM162A; NbExp=3; IntAct=EBI-352572, EBI-6123466;
CC Q9UKC9:FBXL2; NbExp=2; IntAct=EBI-352572, EBI-724253;
CC O75426:FBXO24; NbExp=2; IntAct=EBI-352572, EBI-6425658;
CC Q9UKT8:FBXW2; NbExp=2; IntAct=EBI-352572, EBI-914727;
CC P22607:FGFR3; NbExp=2; IntAct=EBI-352572, EBI-348399;
CC P09769:FGR; NbExp=2; IntAct=EBI-352572, EBI-1383732;
CC P21333:FLNA; NbExp=2; IntAct=EBI-352572, EBI-350432;
CC P35916:FLT4; NbExp=2; IntAct=EBI-352572, EBI-1005467;
CC P06241:FYN; NbExp=2; IntAct=EBI-352572, EBI-515315;
CC Q8TF76:GSG2; NbExp=2; IntAct=EBI-352572, EBI-1237328;
CC P49840:GSK3A; NbExp=2; IntAct=EBI-352572, EBI-1044067;
CC Q9UPZ9:ICK; NbExp=2; IntAct=EBI-352572, EBI-6381479;
CC O14920:IKBKB; NbExp=2; IntAct=EBI-352572, EBI-81266;
CC Q14164:IKBKE; NbExp=2; IntAct=EBI-352572, EBI-307369;
CC Q9Y6K9:IKBKG; NbExp=3; IntAct=EBI-352572, EBI-81279;
CC Q2WGJ6:KLHL38; NbExp=3; IntAct=EBI-352572, EBI-6426443;
CC P06239:LCK; NbExp=2; IntAct=EBI-352572, EBI-1348;
CC P53671:LIMK2; NbExp=2; IntAct=EBI-352572, EBI-1384350;
CC Q99558:MAP3K14; NbExp=2; IntAct=EBI-352572, EBI-358011;
CC P41279:MAP3K8; NbExp=2; IntAct=EBI-352572, EBI-354900;
CC P80192:MAP3K9; NbExp=2; IntAct=EBI-352572, EBI-3951604;
CC P31152:MAPK4; NbExp=2; IntAct=EBI-352572, EBI-3906061;
CC P10636-8:MAPT; NbExp=4; IntAct=EBI-352572, EBI-366233;
CC P42679:MATK; NbExp=2; IntAct=EBI-352572, EBI-751664;
CC O15146:MUSK; NbExp=2; IntAct=EBI-352572, EBI-6423196;
CC Q8TD19:NEK9; NbExp=2; IntAct=EBI-352572, EBI-1044009;
CC P19838:NFKB1; NbExp=3; IntAct=EBI-352572, EBI-300010;
CC O75469:NR1I2; NbExp=2; IntAct=EBI-352572, EBI-3905991;
CC Q9P215:POGK; NbExp=2; IntAct=EBI-352572, EBI-2555775;
CC Q13131:PRKAA1; NbExp=2; IntAct=EBI-352572, EBI-1181405;
CC P22694:PRKACB; NbExp=2; IntAct=EBI-352572, EBI-2679622;
CC Q02156:PRKCE; NbExp=2; IntAct=EBI-352572, EBI-706254;
CC Q05513:PRKCZ; NbExp=2; IntAct=EBI-352572, EBI-295351;
CC Q15139:PRKD1; NbExp=2; IntAct=EBI-352572, EBI-1181072;
CC P51817:PRKX; NbExp=2; IntAct=EBI-352572, EBI-4302903;
CC P11801:PSKH1; NbExp=2; IntAct=EBI-352572, EBI-3922781;
CC P04049:RAF1; NbExp=3; IntAct=EBI-352572, EBI-365996;
CC P49758:RGS6; NbExp=2; IntAct=EBI-352572, EBI-6426927;
CC Q01974:ROR2; NbExp=2; IntAct=EBI-352572, EBI-6422642;
CC P62913:RPL11; NbExp=2; IntAct=EBI-352572, EBI-354380;
CC Q15418:RPS6KA1; NbExp=2; IntAct=EBI-352572, EBI-963034;
CC Q15831:STK11; NbExp=3; IntAct=EBI-352572, EBI-306838;
CC Q15208:STK38; NbExp=2; IntAct=EBI-352572, EBI-458376;
CC Q9UNE7:STUB1; NbExp=5; IntAct=EBI-352572, EBI-357085;
CC Q9Y2Z0-2:SUGT1; NbExp=2; IntAct=EBI-352572, EBI-10768076;
CC Q9UHD2:TBK1; NbExp=2; IntAct=EBI-352572, EBI-356402;
CC Q96S53:TESK2; NbExp=2; IntAct=EBI-352572, EBI-1384110;
CC Q9BXA6:TSSK6; NbExp=3; IntAct=EBI-352572, EBI-851883;
CC P29597:TYK2; NbExp=2; IntAct=EBI-352572, EBI-1383454;
CC Q8IWX7:UNC45B; NbExp=2; IntAct=EBI-352572, EBI-9363363;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16580629,
CC ECO:0000269|PubMed:18239673, ECO:0000269|PubMed:24880080,
CC ECO:0000269|PubMed:9482106}. Melanosome
CC {ECO:0000269|PubMed:17081065}. Nucleus
CC {ECO:0000269|PubMed:18239673}. Secreted
CC {ECO:0000269|PubMed:20599762}. Cell membrane
CC {ECO:0000269|PubMed:20599762}. Note=Identified by mass
CC spectrometry in melanosome fractions from stage I to stage IV
CC (PubMed:17081065). Translocates with BIRC2 from the nucleus to the
CC cytoplasm during differentiation (PubMed:18239673). Secreted when
CC associated with TGFB1 processed form (LAP) (PubMed:20599762).
CC {ECO:0000269|PubMed:17081065, ECO:0000269|PubMed:18239673,
CC ECO:0000269|PubMed:20599762}.
CC -!- INDUCTION: By heat shock. {ECO:0000269|PubMed:20353823}.
CC -!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
CC repeat-containing proteins. {ECO:0000250|UniProtKB:P07900}.
CC -!- PTM: Ubiquitinated in the presence of STUB1-UBE2D1 complex (in
CC vitro). {ECO:0000269|PubMed:18042044}.
CC -!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
CC -!- PTM: S-nitrosylated; negatively regulates the ATPase activity.
CC {ECO:0000305|PubMed:19696785}.
CC -!- PTM: Phosphorylation at Tyr-301 by SRC is induced by
CC lipopolysaccharide (PubMed:23585225). Phosphorylation at Ser-226
CC and Ser-255 inhibits AHR interaction (PubMed:15581363).
CC {ECO:0000269|PubMed:15581363, ECO:0000269|PubMed:23585225}.
CC -!- PTM: Methylated by SMYD2; facilitates dimerization and chaperone
CC complex formation; promotes cancer cell proliferation.
CC {ECO:0000269|PubMed:24880080}.
CC -!- PTM: Cleaved following oxidative stress resulting in HSP90AB1
CC protein radicals formation; disrupts the chaperoning function and
CC the degradation of its client proteins.
CC {ECO:0000269|PubMed:22848402}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD14062.3; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC Sequence=CAB66478.1; Type=Frameshift; Positions=709; Evidence={ECO:0000305};
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M16660; AAA36025.1; -; mRNA.
DR EMBL; J04988; AAA36026.1; -; Genomic_DNA.
DR EMBL; AY359878; AAQ63401.1; -; mRNA.
DR EMBL; AL136543; CAB66478.1; ALT_FRAME; mRNA.
DR EMBL; AK312255; BAG35187.1; -; mRNA.
DR EMBL; DQ314872; ABC40731.1; -; Genomic_DNA.
DR EMBL; AL139392; CAI20095.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX04257.1; -; Genomic_DNA.
DR EMBL; BC004928; AAH04928.1; -; mRNA.
DR EMBL; BC009206; AAH09206.2; -; mRNA.
DR EMBL; BC012807; AAH12807.1; -; mRNA.
DR EMBL; BC014485; AAH14485.1; -; mRNA.
DR EMBL; BC016753; AAH16753.1; -; mRNA.
DR EMBL; BC068474; AAH68474.1; -; mRNA.
DR EMBL; AH007358; AAD14062.3; ALT_INIT; Genomic_DNA.
DR EMBL; AF275719; AAF82792.1; -; mRNA.
DR CCDS; CCDS4909.1; -.
DR PIR; A29461; HHHU84.
DR PIR; T46243; T46243.
DR RefSeq; NP_001258898.1; NM_001271969.1.
DR RefSeq; NP_001258899.1; NM_001271970.1.
DR RefSeq; NP_001258900.1; NM_001271971.1.
DR RefSeq; NP_031381.2; NM_007355.3.
DR UniGene; Hs.509736; -.
DR PDB; 1QZ2; X-ray; 3.00 A; G/H=720-724.
DR PDB; 1UYM; X-ray; 2.45 A; A=2-221.
DR PDB; 2L6J; NMR; -; B=720-724.
DR PDB; 3FWV; X-ray; 2.20 A; C/D=719-723.
DR PDB; 3NMQ; X-ray; 2.20 A; A=1-223.
DR PDB; 3PRY; X-ray; 2.28 A; A/B/C=284-543.
DR PDB; 3UQ3; X-ray; 2.60 A; B/C=720-724.
DR PDB; 5FWK; EM; 3.90 A; A/B=1-724.
DR PDB; 5FWL; EM; 9.00 A; A/B=1-724.
DR PDB; 5FWM; EM; 8.00 A; A/B=1-724.
DR PDB; 5FWP; EM; 7.20 A; A/B=1-724.
DR PDBsum; 1QZ2; -.
DR PDBsum; 1UYM; -.
DR PDBsum; 2L6J; -.
DR PDBsum; 3FWV; -.
DR PDBsum; 3NMQ; -.
DR PDBsum; 3PRY; -.
DR PDBsum; 3UQ3; -.
DR PDBsum; 5FWK; -.
DR PDBsum; 5FWL; -.
DR PDBsum; 5FWM; -.
DR PDBsum; 5FWP; -.
DR ProteinModelPortal; P08238; -.
DR SMR; P08238; -.
DR BioGrid; 109558; 314.
DR DIP; DIP-413N; -.
DR IntAct; P08238; 522.
DR MINT; MINT-99712; -.
DR STRING; 9606.ENSP00000325875; -.
DR BindingDB; P08238; -.
DR ChEMBL; CHEMBL4303; -.
DR DrugBank; DB05134; CNF1010.
DR DrugBank; DB02424; Geldanamycin.
DR DrugBank; DB03758; Radicicol.
DR DrugBank; DB06070; SNX-5422.
DR GuidetoPHARMACOLOGY; 2907; -.
DR iPTMnet; P08238; -.
DR PhosphoSitePlus; P08238; -.
DR SwissPalm; P08238; -.
DR DMDM; 17865718; -.
DR OGP; P08238; -.
DR EPD; P08238; -.
DR MaxQB; P08238; -.
DR PaxDb; P08238; -.
DR PeptideAtlas; P08238; -.
DR PRIDE; P08238; -.
DR TopDownProteomics; P08238; -.
DR DNASU; 3326; -.
DR Ensembl; ENST00000353801; ENSP00000325875; ENSG00000096384.
DR Ensembl; ENST00000371554; ENSP00000360609; ENSG00000096384.
DR Ensembl; ENST00000371646; ENSP00000360709; ENSG00000096384.
DR Ensembl; ENST00000620073; ENSP00000481908; ENSG00000096384.
DR GeneID; 3326; -.
DR KEGG; hsa:3326; -.
DR UCSC; uc003oxa.3; human.
DR CTD; 3326; -.
DR DisGeNET; 3326; -.
DR GeneCards; HSP90AB1; -.
DR H-InvDB; HIX0031498; -.
DR H-InvDB; HIX0057380; -.
DR HGNC; HGNC:5258; HSP90AB1.
DR HPA; CAB005230; -.
DR HPA; HPA055729; -.
DR MIM; 140572; gene.
DR neXtProt; NX_P08238; -.
DR OpenTargets; ENSG00000096384; -.
DR PharmGKB; PA29524; -.
DR eggNOG; KOG0019; Eukaryota.
DR eggNOG; KOG0020; Eukaryota.
DR eggNOG; COG0326; LUCA.
DR GeneTree; ENSGT00840000129758; -.
DR HOGENOM; HOG000031988; -.
DR HOVERGEN; HBG007374; -.
DR InParanoid; P08238; -.
DR KO; K04079; -.
DR OMA; AFANDIC; -.
DR OrthoDB; EOG091G0270; -.
DR PhylomeDB; P08238; -.
DR TreeFam; TF300686; -.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-3371511; HSF1 activation.
DR Reactome; R-HSA-3371568; Attenuation phase.
DR Reactome; R-HSA-3371571; HSF1-dependent transactivation.
DR Reactome; R-HSA-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-HSA-5336415; Uptake and function of diphtheria toxin.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-844456; The NLRP3 inflammasome.
DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-HSA-8937144; Aryl hydrocarbon receptor signalling.
DR SIGNOR; P08238; -.
DR ChiTaRS; HSP90AB1; human.
DR EvolutionaryTrace; P08238; -.
DR GeneWiki; HSP90AB1; -.
DR GenomeRNAi; 3326; -.
DR PRO; PR:P08238; -.
DR Proteomes; UP000005640; Chromosome 6.
DR Bgee; ENSG00000096384; -.
DR CleanEx; HS_HSP90AB1; -.
DR ExpressionAtlas; P08238; baseline and differential.
DR Genevisible; P08238; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0034751; C:aryl hydrocarbon receptor complex; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0031526; C:brush border membrane; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0016234; C:inclusion body; IEA:Ensembl.
DR GO; GO:0005765; C:lysosomal membrane; IEA:Ensembl.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1990917; C:ooplasm; IEA:Ensembl.
DR GO; GO:0043234; C:protein complex; IDA:CAFA.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:1990913; C:sperm head plasma membrane; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IDA:CAFA.
DR GO; GO:0043008; F:ATP-dependent protein binding; IPI:CAFA.
DR GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
DR GO; GO:0002135; F:CTP binding; IEA:Ensembl.
DR GO; GO:0032564; F:dATP binding; IEA:Ensembl.
DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR GO; GO:0070182; F:DNA polymerase binding; IPI:BHF-UCL.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0008144; F:drug binding; IEA:Ensembl.
DR GO; GO:0001948; F:glycoprotein binding; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IEA:Ensembl.
DR GO; GO:0031072; F:heat shock protein binding; IPI:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
DR GO; GO:1990226; F:histone methyltransferase binding; IPI:UniProtKB.
DR GO; GO:0044325; F:ion channel binding; IEA:Ensembl.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0023026; F:MHC class II protein complex binding; IDA:UniProtKB.
DR GO; GO:0030235; F:nitric-oxide synthase regulator activity; ISS:UniProtKB.
DR GO; GO:0042277; F:peptide binding; IPI:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0019887; F:protein kinase regulator activity; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0017098; F:sulfonylurea receptor binding; IEA:Ensembl.
DR GO; GO:0030911; F:TPR domain binding; ISS:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0002134; F:UTP binding; IEA:Ensembl.
DR GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
DR GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IDA:CAFA.
DR GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
DR GO; GO:0071157; P:negative regulation of cell cycle arrest; IMP:UniProtKB.
DR GO; GO:1903660; P:negative regulation of complement-dependent cytotoxicity; IEA:Ensembl.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:1901389; P:negative regulation of transforming growth factor beta activation; IDA:UniProtKB.
DR GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
DR GO; GO:0001890; P:placenta development; IEA:Ensembl.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IMP:UniProtKB.
DR GO; GO:0045793; P:positive regulation of cell size; IEA:Ensembl.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IDA:UniProtKB.
DR GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
DR GO; GO:0033160; P:positive regulation of protein import into nucleus, translocation; IEA:Ensembl.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; IDA:UniProtKB.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IEA:Ensembl.
DR GO; GO:0051973; P:positive regulation of telomerase activity; IDA:BHF-UCL.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0050821; P:protein stabilization; TAS:Reactome.
DR GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
DR GO; GO:0060334; P:regulation of interferon-gamma-mediated signaling pathway; IMP:MGI.
DR GO; GO:0031396; P:regulation of protein ubiquitination; IDA:BHF-UCL.
DR GO; GO:0060338; P:regulation of type I interferon-mediated signaling pathway; IMP:MGI.
DR GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
DR GO; GO:0009651; P:response to salt stress; IEA:Ensembl.
DR GO; GO:0006986; P:response to unfolded protein; NAS:UniProtKB.
DR GO; GO:0097435; P:supramolecular fiber organization; IMP:CACAO.
DR GO; GO:1905323; P:telomerase holoenzyme complex assembly; IDA:BHF-UCL.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IDA:BHF-UCL.
DR GO; GO:0019062; P:virion attachment to host cell; IMP:CACAO.
DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
DR Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cell membrane; Chaperone;
KW Complete proteome; Cytoplasm; Direct protein sequencing; Glycoprotein;
KW Membrane; Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Polymorphism; Reference proteome; S-nitrosylation; Secreted;
KW Stress response; Ubl conjugation.
FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2492519}.
FT CHAIN 2 724 Heat shock protein HSP 90-beta.
FT /FTId=PRO_0000062917.
FT REGION 2 527 Interaction with TP53.
FT {ECO:0000269|PubMed:15358771}.
FT REGION 2 214 Interaction with BIRC2.
FT {ECO:0000269|PubMed:25486457}.
FT REGION 215 552 Interaction with AHSA1.
FT {ECO:0000269|PubMed:25486457}.
FT MOTIF 720 724 TPR repeat-binding.
FT BINDING 46 46 ATP. {ECO:0000250}.
FT BINDING 88 88 ATP.
FT BINDING 107 107 ATP. {ECO:0000250}.
FT BINDING 133 133 ATP; via amide nitrogen. {ECO:0000250}.
FT BINDING 392 392 ATP. {ECO:0000250}.
FT SITE 126 127 Cleaved under oxidative stress.
FT {ECO:0000269|PubMed:22848402}.
FT MOD_RES 219 219 N6-succinyllysine.
FT {ECO:0000250|UniProtKB:P11499}.
FT MOD_RES 226 226 Phosphoserine.
FT {ECO:0000244|PubMed:18088087,
FT ECO:0000244|PubMed:18318008,
FT ECO:0000244|PubMed:20068231,
FT ECO:0000244|PubMed:21406692,
FT ECO:0000244|PubMed:23186163}.
FT MOD_RES 255 255 Phosphoserine.
FT {ECO:0000244|PubMed:17081983,
FT ECO:0000244|PubMed:23186163,
FT ECO:0000269|Ref.12}.
FT MOD_RES 261 261 Phosphoserine.
FT {ECO:0000269|PubMed:2492519}.
FT MOD_RES 297 297 Phosphothreonine.
FT {ECO:0000244|PubMed:17525332,
FT ECO:0000244|PubMed:23186163}.
FT MOD_RES 301 301 Phosphotyrosine; by SRC.
FT {ECO:0000269|PubMed:23585225}.
FT MOD_RES 305 305 Phosphotyrosine.
FT {ECO:0000250|UniProtKB:P11499}.
FT MOD_RES 307 307 Phosphoserine.
FT {ECO:0000244|PubMed:18669648}.
FT MOD_RES 399 399 N6-malonyllysine.
FT {ECO:0000269|PubMed:21908771}.
FT MOD_RES 435 435 N6-acetyllysine.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 445 445 Phosphoserine.
FT {ECO:0000244|PubMed:23186163}.
FT MOD_RES 452 452 Phosphoserine; alternate.
FT {ECO:0000269|PubMed:2492519}.
FT MOD_RES 479 479 Phosphothreonine.
FT {ECO:0000244|PubMed:23186163}.
FT MOD_RES 481 481 N6-acetyllysine.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 484 484 Phosphotyrosine.
FT {ECO:0000269|PubMed:2492519}.
FT MOD_RES 531 531 N6-methylated lysine.
FT {ECO:0000269|PubMed:24880080}.
FT MOD_RES 531 531 N6-succinyllysine.
FT {ECO:0000250|UniProtKB:P11499}.
FT MOD_RES 532 532 Phosphoserine.
FT {ECO:0000269|PubMed:2492519}.
FT MOD_RES 574 574 N6-methylated lysine.
FT {ECO:0000269|PubMed:24880080}.
FT MOD_RES 577 577 N6-succinyllysine.
FT {ECO:0000250|UniProtKB:P11499}.
FT MOD_RES 590 590 S-nitrosocysteine.
FT {ECO:0000305|PubMed:19696785}.
FT MOD_RES 624 624 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P11499}.
FT MOD_RES 669 669 Phosphoserine.
FT {ECO:0000244|PubMed:24275569}.
FT MOD_RES 718 718 Phosphoserine; by PLK2 and PLK3.
FT {ECO:0000269|PubMed:22828320}.
FT CARBOHYD 434 434 O-linked (GlcNAc) serine. {ECO:0000250}.
FT CARBOHYD 452 452 O-linked (GlcNAc) serine; alternate.
FT {ECO:0000250}.
FT VARIANT 349 349 K -> E (in dbSNP:rs11538975).
FT /FTId=VAR_049624.
FT MUTAGEN 42 42 E->A: Strong ATP-binding. Strong
FT interaction with HSF1, HIF1A, ERBB2, MET,
FT KEAP1 and RHOBTB2.
FT {ECO:0000269|PubMed:26517842}.
FT MUTAGEN 88 88 D->A: Impaired ATP-binding. Strong
FT interaction with HIF1A, MET, KEAP1 and
FT RHOBTB2. Loss of interaction with HSF1
FT and ERBB2. {ECO:0000269|PubMed:26517842}.
FT MUTAGEN 226 226 S->A: Increases the binding affinity for
FT AHR; when associated with A-255.
FT Increases AHR transcription activity;
FT when associated with A-255.
FT {ECO:0000269|PubMed:15581363}.
FT MUTAGEN 226 226 S->E: No effect on the interaction with
FT AHR; when associated with E-255.
FT {ECO:0000269|PubMed:15581363}.
FT MUTAGEN 255 255 S->A: Increases the binding affinity for
FT AHR; when associated with A-226.
FT Increases AHR transcription activity;
FT when associated with A-226.
FT {ECO:0000269|PubMed:15581363}.
FT MUTAGEN 255 255 S->E: No effect on the interaction with
FT AHR; when associated with E-226.
FT {ECO:0000269|PubMed:15581363}.
FT MUTAGEN 301 301 Y->F: Decreases interaction with NOS3 and
FT SRC. impairs resists LPS-induced tyrosine
FT phosphorylation. Does not block LPS-
FT induced pp60src phosphorylation.
FT {ECO:0000269|PubMed:23585225}.
FT MUTAGEN 531 531 K->A: Highly decreases the signal of
FT SMYD2-dependent HSP90AB1 methylation;
FT when associated with A-574. Diminishes
FT dimerized form; when associated with A-
FT 574. Reduces interaction with STIP1 or
FT CDC37; when associated with A-574.
FT {ECO:0000269|PubMed:24880080}.
FT MUTAGEN 574 574 K->A: Decreases the signal of SMYD2-
FT dependent HSP90AB1 methylation. Highly
FT decreases the signal of SMYD2-dependent
FT HSP90AB1 methylation; when associated
FT with A-531. Diminishes dimerized form;
FT when associated with A-531. Reduces
FT interaction with STIP1 or CDC37; when
FT associated with A-531.
FT {ECO:0000269|PubMed:24880080}.
FT MUTAGEN 590 590 C->A,N,D: Reduced ATPase activity and
FT client protein activation.
FT {ECO:0000269|PubMed:19696785}.
FT CONFLICT 147 147 T -> R (in Ref. 1; AAA36025).
FT {ECO:0000305}.
FT CONFLICT 177 177 R -> M (in Ref. 1; AAA36025).
FT {ECO:0000305}.
FT CONFLICT 403 403 V -> A (in Ref. 5; CAB66478).
FT {ECO:0000305}.
FT STRAND 13 16 {ECO:0000244|PDB:3NMQ}.
FT HELIX 19 30 {ECO:0000244|PDB:3NMQ}.
FT HELIX 38 60 {ECO:0000244|PDB:3NMQ}.
FT HELIX 62 65 {ECO:0000244|PDB:3NMQ}.
FT STRAND 73 78 {ECO:0000244|PDB:3NMQ}.
FT TURN 79 82 {ECO:0000244|PDB:3NMQ}.
FT STRAND 83 88 {ECO:0000244|PDB:3NMQ}.
FT HELIX 95 99 {ECO:0000244|PDB:3NMQ}.
FT HELIX 101 118 {ECO:0000244|PDB:3NMQ}.
FT HELIX 123 129 {ECO:0000244|PDB:3NMQ}.
FT HELIX 132 138 {ECO:0000244|PDB:3NMQ}.
FT STRAND 140 148 {ECO:0000244|PDB:3NMQ}.
FT STRAND 155 159 {ECO:0000244|PDB:3NMQ}.
FT STRAND 164 169 {ECO:0000244|PDB:3NMQ}.
FT STRAND 176 185 {ECO:0000244|PDB:3NMQ}.
FT HELIX 187 193 {ECO:0000244|PDB:3NMQ}.
FT HELIX 195 205 {ECO:0000244|PDB:3NMQ}.
FT STRAND 213 215 {ECO:0000244|PDB:3NMQ}.
FT HELIX 288 290 {ECO:0000244|PDB:3PRY}.
FT HELIX 293 295 {ECO:0000244|PDB:3PRY}.
FT HELIX 298 309 {ECO:0000244|PDB:3PRY}.
FT STRAND 316 323 {ECO:0000244|PDB:3PRY}.
FT STRAND 325 327 {ECO:0000244|PDB:3PRY}.
FT STRAND 329 335 {ECO:0000244|PDB:3PRY}.
FT STRAND 353 357 {ECO:0000244|PDB:3PRY}.
FT STRAND 360 364 {ECO:0000244|PDB:3PRY}.
FT HELIX 367 369 {ECO:0000244|PDB:3PRY}.
FT HELIX 372 374 {ECO:0000244|PDB:3PRY}.
FT STRAND 378 386 {ECO:0000244|PDB:3PRY}.
FT HELIX 395 420 {ECO:0000244|PDB:3PRY}.
FT HELIX 423 443 {ECO:0000244|PDB:3PRY}.
FT HELIX 445 447 {ECO:0000244|PDB:3PRY}.
FT HELIX 448 453 {ECO:0000244|PDB:3PRY}.
FT STRAND 456 459 {ECO:0000244|PDB:3PRY}.
FT TURN 460 464 {ECO:0000244|PDB:3PRY}.
FT HELIX 469 474 {ECO:0000244|PDB:3PRY}.
FT STRAND 482 486 {ECO:0000244|PDB:3PRY}.
FT HELIX 491 495 {ECO:0000244|PDB:3PRY}.
FT HELIX 498 504 {ECO:0000244|PDB:3PRY}.
FT TURN 505 507 {ECO:0000244|PDB:3PRY}.
FT STRAND 510 512 {ECO:0000244|PDB:3PRY}.
FT HELIX 518 525 {ECO:0000244|PDB:3PRY}.
FT STRAND 531 535 {ECO:0000244|PDB:3PRY}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 35 188 ipfam:HATPase_c [T]
FT MYHIT 35 189 ismart:HATPase_c [T]
FT MYHIT 33 42 ipat:HSP90 [T]
FT MYHIT 10 685 ihamap:HSP90 [T]
FT MYHIT 191 703 ipfam:HSP90 [T]
SQ 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
//
|
