HS90B_HUMAN
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 03-AUG-2022, entry version 261.
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 {ECO:0000312|HGNC:HGNC:5258}; Synonyms=HSP90B, HSPC2, HSPCB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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-shock
RT protein family.";
RL Gene 53:235-245(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2768249; DOI=10.1016/s0021-9258(18)63803-7;
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 protein
RT 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 genes
RT encode formerly identified tumour-specific transplantation 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., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [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., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., 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., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [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 project:
RT 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; DOI=10.1016/s0021-9258(19)81631-9;
RA Lees-Miller S.P., Anderson C.W.;
RT "Two human 90-kDa heat shock proteins are phosphorylated in vivo at
RT conserved serines that are phosphorylated in vitro by casein kinase II.";
RL J. Biol. Chem. 264:2431-2437(1989).
RN [12]
RP PROTEIN SEQUENCE OF 42-107; 149-168; 181-197; 204-221; 250-265; 274-284;
RP 292-348; 360-392; 412-427; 439-448; 450-475; 482-502; 506-526; 539-551;
RP 584-604; 613-639 AND 653-679, PHOSPHORYLATION AT SER-255, AND
RP 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 the
RT 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 (R147 in
RT 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 IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [20]
RP PHOSPHORYLATION AT SER-226 AND SER-255, MUTAGENESIS OF SER-226 AND SER-255,
RP 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 cytosolic
RT arylhydrocarbon receptor complex.";
RL Biochemistry 43:15510-15519(2004).
RN [21]
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 [22]
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 [23]
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 cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [24]
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., Gu J.;
RT "SGT, a Hsp90beta binding partner, is accumulated in the nucleus during
RT cell apoptosis.";
RL Biochem. Biophys. Res. Commun. 343:1153-1158(2006).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [26]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [27]
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., Wood W.M.,
RA 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 [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-297, AND IDENTIFICATION BY
RP 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, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA 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 [29]
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 required for
RT the mono-ubiquitination of proteins and elongation by polyubiquitin chains
RT with a specific topology.";
RL Biochem. J. 409:723-729(2008).
RN [30]
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 [31]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH BIRC2, SUBCELLULAR
RP 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 [32]
RP SUBUNIT, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18400751; DOI=10.1074/jbc.m800540200;
RA Richter K., Soroka J., Skalniak L., Leskovar A., Hessling M., Reinstein J.,
RA Buchner J.;
RT "Conserved conformational changes in the ATPase cycle of human Hsp90.";
RL J. Biol. Chem. 283:17757-17765(2008).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND IDENTIFICATION BY
RP 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 [34]
RP INTERACTION WITH TTC4.
RX PubMed=18320024; DOI=10.1371/journal.pone.0001737;
RA Crevel G., Bennett D., Cotterill S.;
RT "The human TPR protein TTC4 is a putative Hsp90 co-chaperone which
RT interacts with CDC6 and shows alterations in transformed cells.";
RL PLoS ONE 3:E0001737-E0001737(2008).
RN [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [36]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [37]
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 [38]
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., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [39]
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 osteosarcoma
RT cells inhibits activation of latent TGF-beta1.";
RL Biochem. Biophys. Res. Commun. 398:525-531(2010).
RN [40]
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., Cheng X.K.,
RA Zhang Y., Xiao L., Shen Y.F.;
RT "Stat1 mediates an auto-regulation of hsp90beta gene in heat shock
RT response.";
RL Cell. Signal. 22:1206-1213(2010).
RN [41]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [42]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [43]
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., He W.,
RA Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J.,
RA 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 [44]
RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH N.MENINGITIDIS ADHESIN A
RP (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION.
RX PubMed=21949862; DOI=10.1371/journal.pone.0025089;
RA Cecchini P., Tavano R., Polverino de Laureto P., Franzoso S., Mazzon C.,
RA Montanari P., Papini E.;
RT "The soluble recombinant Neisseria meningitidis adhesin NadA(Delta351-405)
RT stimulates human monocytes by binding to extracellular Hsp90.";
RL PLoS ONE 6:e25089-e25089(2011).
RN [45]
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 tool:
RT application to the Hsp90 molecular chaperone machine.";
RL PLoS ONE 6:E26044-E26044(2011).
RN [46]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [47]
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 [48]
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., Kazlauskas E.,
RA Mazal P., Szekeres T., Hengstschlaeger M., Matulis D., Jaeger W.,
RA Krupitza G.;
RT "Hsp90 stabilizes Cdc25A and counteracts heat shock-mediated Cdc25A
RT degradation and cell-cycle attenuation in pancreatic carcinoma cells.";
RL Hum. Mol. Genet. 21:4615-4627(2012).
RN [49]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH N.MENINGITIDIS ADHESIN
RP A (MICROBIAL INFECTION).
RX PubMed=22066472; DOI=10.1111/j.1462-5822.2011.01722.x;
RA Montanari P., Bozza G., Capecchi B., Caproni E., Barrile R., Norais N.,
RA Capitani M., Sallese M., Cecchini P., Ciucchi L., Gao Z., Rappuoli R.,
RA Pizza M., Arico B., Merola M.;
RT "Human heat shock protein (Hsp) 90 interferes with Neisseria meningitidis
RT adhesin A (NadA)-mediated adhesion and invasion.";
RL Cell. Microbiol. 14:368-385(2012).
RN [50]
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., Raes M.,
RA Leveque P., Gallez B., Depuydt M., Collet J.F., 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 [51]
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., Kumar S.,
RA Joshi A., Thangjam G., Fulton D., Black S.M., Patel V., Catravas J.D.;
RT "LPS induces pp60c-src-mediated tyrosine phosphorylation of Hsp90 in lung
RT vascular endothelial cells and mouse lung.";
RL Am. J. Physiol. 304:L883-L893(2013).
RN [52]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-255; THR-297;
RP SER-445 AND THR-479, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [53]
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 extracellular
RT signal-regulated kinase 5 (ERK5) nuclear translocation require dissociation
RT of Hsp90 from the ERK5-Cdc37 complex.";
RL Mol. Cell. Biol. 33:1671-1686(2013).
RN [54]
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 the
RT biogenesis of KCNQ4 channels.";
RL PLoS ONE 8:E57282-E57282(2013).
RN [55]
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 [56]
RP METHYLATION AT LYS-531 AND LYS-574 BY SMYD2, IDENTIFICATION BY MASS
RP SPECTROMETRY, MUTAGENESIS OF LYS-531 AND LYS-574, INTERACTION WITH STIP1
RP 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 by
RT regulating the chaperone complex formation.";
RL Cancer Lett. 351:126-133(2014).
RN [57]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-669, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [58]
RP INTERACTION WITH NWD1.
RX PubMed=24681825; DOI=10.18632/oncotarget.1850;
RA Correa R.G., Krajewska M., Ware C.F., Gerlic M., Reed J.C.;
RT "The NLR-related protein NWD1 is associated with prostate cancer and
RT modulates androgen receptor signaling.";
RL Oncotarget 5:1666-1682(2014).
RN [59]
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 human
RT cells and alters Hsp90 activity in yeast.";
RL Biochim. Biophys. Acta 1853:445-452(2015).
RN [60]
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 [61]
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., Rivas C.,
RA Alarcon S., Schwartz H., Khamit-Kush K., Scroggins B.T., Beebe K.,
RA Trepel J.B., Neckers L.;
RT "Client proteins and small molecule inhibitors display distinct binding
RT preferences for constitutive and stress-induced HSP90 isoforms and their
RT conformationally restricted mutants.";
RL PLoS ONE 10:E0141786-E0141786(2015).
RN [62]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [63]
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 [64]
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 [65]
RP FUNCTION, AND INTERACTION WITH IL1B.
RX PubMed=32272059; DOI=10.1016/j.cell.2020.03.031;
RA Zhang M., Liu L., Lin X., Wang Y., Li Y., Guo Q., Li S., Sun Y., Tao X.,
RA Zhang D., Lv X., Zheng L., Ge L.;
RT "A Translocation Pathway for Vesicle-Mediated Unconventional Protein
RT Secretion.";
RL Cell 181:637-652(2020).
RN [66]
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 [67]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 720-724 IN COMPLEX WITH 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., Shen B.,
RA Rao Z.;
RT "3D structure of human FK506-binding protein 52: implications for the
RT assembly of the glucocorticoid receptor/Hsp90/immunophilin heterocomplex.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8348-8353(2004).
RN [68]
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, structural
CC maintenance and proper regulation of specific target proteins involved
CC for instance in cell cycle control and signal transduction. Undergoes a
CC functional cycle linked to its ATPase activity. This cycle probably
CC induces conformational changes in the client proteins, thereby causing
CC their activation. Interacts dynamically with various co-chaperones that
CC modulate its 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 proteins
CC or complexes, that act as adapters, simultaneously able to interact
CC with the specific client and the central chaperone itself. Recruitment
CC of ATP and co-chaperone followed by client protein forms a functional
CC chaperone. After the completion of the chaperoning process, properly
CC folded client protein and co-chaperone leave HSP90 in an ADP-bound
CC partially open conformation and finally, ADP is released from HSP90
CC which acquires an open conformation for the next cycle
CC (PubMed:27295069, PubMed:26991466). Apart from its chaperone activity,
CC it also plays a role in the regulation of the transcription machinery.
CC HSP90 and its co-chaperones modulate transcription at least at three
CC different levels. They first alter the steady-state levels of certain
CC transcription factors in response to various physiological cues.
CC Second, they modulate the activity of certain epigenetic modifiers,
CC such as histone deacetylases or DNA methyl transferases, and thereby
CC respond to the change in the environment. Third, they participate in
CC the eviction of histones from the promoter region of certain genes and
CC thereby turn on gene expression (PubMed:25973397). Antagonizes STUB1-
CC mediated inhibition of TGF-beta signaling via inhibition of STUB1-
CC mediated SMAD3 ubiquitination and degradation (PubMed:24613385).
CC Promotes cell differentiation by chaperoning BIRC2 and thereby
CC protecting from auto-ubiquitination and degradation by the proteasomal
CC machinery (PubMed:18239673). Main chaperone involved in the
CC phosphorylation/activation of the STAT1 by chaperoning both JAK2 and
CC PRKCE under heat shock and in turn, activates its own transcription
CC (PubMed:20353823). Involved in the translocation into ERGIC
CC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless
CC cargos (lacking the secretion signal sequence) such as the interleukin
CC 1/IL-1; the translocation process is mediated by the cargo receptor
CC TMED10 (PubMed:32272059). {ECO:0000269|PubMed:16478993,
CC ECO:0000269|PubMed:18239673, ECO:0000269|PubMed:19696785,
CC ECO:0000269|PubMed:20353823, ECO:0000269|PubMed:24613385,
CC ECO:0000269|PubMed:32272059, ECO:0000303|PubMed:25973397,
CC ECO:0000303|PubMed:26991466, ECO:0000303|PubMed:27295069}.
CC -!- FUNCTION: (Microbial infection) Binding to N.meningitidis NadA
CC stimulates monocytes (PubMed:21949862). Seems to interfere with
CC N.meningitidis NadA-mediated invasion of human cells (Probable).
CC {ECO:0000269|PubMed:21949862, ECO:0000305|PubMed:22066472}.
CC -!- ACTIVITY REGULATION: In the resting state, through the dimerization of
CC its C-terminal domain, HSP90 forms a homodimer which is defined as the
CC open conformation. Upon ATP-binding, the N-terminal domain undergoes
CC significant conformational changes and comes in contact to form an
CC active closed conformation. After HSP90 finishes its chaperoning tasks
CC of assisting the proper folding, stabilization and activation of client
CC proteins under the active state, ATP molecule is hydrolyzed to ADP
CC which then dissociates from HSP90 and directs the protein back to the
CC resting state. {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 (PubMed:9482106,
CC PubMed:25486457). Interacts with UNC45A; binding to UNC45A involves 2
CC UNC45A monomers per HSP90AB1 dimer (PubMed:16478993). Interacts with
CC CHORDC1 (By similarity). Interacts with DNAJC7 (PubMed:18620420).
CC Interacts with FKBP4 (PubMed:15159550). May interact with NWD1
CC (PubMed:24681825). Interacts with SGTA (PubMed:16580629). Interacts
CC with HSF1 in an ATP-dependent manner. Interacts with MET; the
CC interaction suppresses MET kinase activity. Interacts with ERBB2 in an
CC ATP-dependent manner; the interaction suppresses ERBB2 kinase activity.
CC Interacts with HIF1A, KEAP1 and RHOBTB2 (PubMed:26517842). Interacts
CC with STUB1 and SMAD3 (PubMed:24613385). Interacts with XPO1 and AHSA1
CC (PubMed:22022502, PubMed:25486457). Interacts with BIRC2
CC (PubMed:25486457). Interacts with KCNQ4; promotes cell surface
CC expression of KCNQ4 (PubMed:23431407). Interacts with BIRC2; prevents
CC auto-ubiquitination and degradation of its client protein BIRC2
CC (PubMed:18239673). Interacts with NOS3 (PubMed:23585225). Interacts
CC with AHR; interaction is inhibited by HSP90AB1 phosphorylation on Ser-
CC 226 and Ser-255 (PubMed:15581363). Interacts with STIP1 and CDC37; upon
CC SMYD2-dependent methylation (PubMed:24880080). Interacts with JAK2 and
CC PRKCE; promotes functional activation in a heat shock-dependent manner
CC (PubMed:20353823). Interacts with HSP90AA1; interaction is constitutive
CC (PubMed:20353823). HSP90AB1-CDC37 chaperone complex interacts with
CC inactive MAPK7 (via N-terminal half) in resting cells; the interaction
CC is MAP2K5-independent and prevents from ubiquitination and proteasomal
CC degradation (PubMed:23428871). Interacts with CDC25A; prevents heat
CC shock-mediated CDC25A degradation and contributes to cell cycle
CC progression (PubMed:22843495). Interacts with TP53 (via DNA binding
CC domain); suppresses TP53 aggregation and prevents from irreversible
CC thermal inactivation (PubMed:15358771). Interacts with TGFB1 processed
CC form (LAP); inhibits latent TGFB1 activation (PubMed:20599762).
CC Interacts with TRIM8; prevents nucleus translocation of phosphorylated
CC STAT3 and HSP90AB1 (By similarity). Interacts with NR3C1 (via domain NR
CC LBD) and NR1D1 (via domain NR LBD) (By similarity). Interacts with
CC PDCL3 (By similarity). Interacts with TTC4 (via TPR repeats)
CC (PubMed:18320024). Interacts with IL1B; the interaction facilitates
CC cargo translocation into the ERGIC (PubMed:32272059).
CC {ECO:0000250|UniProtKB:P11499, ECO:0000250|UniProtKB:P34058,
CC ECO:0000269|PubMed:15159550, ECO:0000269|PubMed:15358771,
CC ECO:0000269|PubMed:15581363, ECO:0000269|PubMed:16478993,
CC ECO:0000269|PubMed:16580629, ECO:0000269|PubMed:18239673,
CC ECO:0000269|PubMed:18320024, 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:32272059,
CC ECO:0000269|PubMed:7588731, ECO:0000269|PubMed:9482106}.
CC -!- SUBUNIT: (Microbial infection) Protein on the cell surface interacts
CC with N.meningitidis serogroup B adhesin A (nadA).
CC {ECO:0000269|PubMed:21949862, ECO:0000269|PubMed:22066472}.
CC -!- INTERACTION:
CC P08238; P36896: ACVR1B; NbExp=2; IntAct=EBI-352572, EBI-1384128;
CC P08238; Q9UL18: AGO1; NbExp=3; IntAct=EBI-352572, EBI-527363;
CC P08238; O95433: AHSA1; NbExp=4; IntAct=EBI-352572, EBI-448610;
CC P08238; O00170: AIP; NbExp=8; IntAct=EBI-352572, EBI-704197;
CC P08238; P31749: AKT1; NbExp=3; IntAct=EBI-352572, EBI-296087;
CC P08238; P31751: AKT2; NbExp=2; IntAct=EBI-352572, EBI-296058;
CC P08238; Q9UM73: ALK; NbExp=2; IntAct=EBI-352572, EBI-357361;
CC P08238; Q16671: AMHR2; NbExp=2; IntAct=EBI-352572, EBI-6423788;
CC P08238; Q01432: AMPD3; NbExp=2; IntAct=EBI-352572, EBI-1223554;
CC P08238; P10398: ARAF; NbExp=9; IntAct=EBI-352572, EBI-365961;
CC P08238; Q96GD4: AURKB; NbExp=5; IntAct=EBI-352572, EBI-624291;
CC P08238; P30530: AXL; NbExp=3; IntAct=EBI-352572, EBI-2850927;
CC P08238; P51451: BLK; NbExp=3; IntAct=EBI-352572, EBI-2105445;
CC P08238; P51813: BMX; NbExp=3; IntAct=EBI-352572, EBI-696657;
CC P08238; P15056: BRAF; NbExp=4; IntAct=EBI-352572, EBI-365980;
CC P08238; Q06187: BTK; NbExp=2; IntAct=EBI-352572, EBI-624835;
CC P08238; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-352572, EBI-1383687;
CC P08238; Q13555: CAMK2G; NbExp=2; IntAct=EBI-352572, EBI-1383465;
CC P08238; Q16543: CDC37; NbExp=11; IntAct=EBI-352572, EBI-295634;
CC P08238; Q7L3B6: CDC37L1; NbExp=5; IntAct=EBI-352572, EBI-2841876;
CC P08238; Q15131: CDK10; NbExp=3; IntAct=EBI-352572, EBI-1646959;
CC P08238; O94921: CDK14; NbExp=2; IntAct=EBI-352572, EBI-1043945;
CC P08238; Q96Q40: CDK15; NbExp=2; IntAct=EBI-352572, EBI-1051975;
CC P08238; Q00526: CDK3; NbExp=2; IntAct=EBI-352572, EBI-1245761;
CC P08238; P11802: CDK4; NbExp=5; IntAct=EBI-352572, EBI-295644;
CC P08238; Q00534: CDK6; NbExp=2; IntAct=EBI-352572, EBI-295663;
CC P08238; P50613: CDK7; NbExp=2; IntAct=EBI-352572, EBI-1245958;
CC P08238; P50750: CDK9; NbExp=3; IntAct=EBI-352572, EBI-1383449;
CC P08238; O14757: CHEK1; NbExp=3; IntAct=EBI-352572, EBI-974488;
CC P08238; Q9UHD1: CHORDC1; NbExp=6; IntAct=EBI-352572, EBI-2550959;
CC P08238; Q9UPZ9: CILK1; NbExp=3; IntAct=EBI-352572, EBI-6381479;
CC P08238; P49761: CLK3; NbExp=2; IntAct=EBI-352572, EBI-745579;
CC P08238; P48729: CSNK1A1; NbExp=2; IntAct=EBI-352572, EBI-1383726;
CC P08238; P49674: CSNK1E; NbExp=2; IntAct=EBI-352572, EBI-749343;
CC P08238; Q13616: CUL1; NbExp=2; IntAct=EBI-352572, EBI-359390;
CC P08238; Q13617: CUL2; NbExp=2; IntAct=EBI-352572, EBI-456179;
CC P08238; Q13618: CUL3; NbExp=3; IntAct=EBI-352572, EBI-456129;
CC P08238; Q13619: CUL4A; NbExp=2; IntAct=EBI-352572, EBI-456106;
CC P08238; Q13620: CUL4B; NbExp=2; IntAct=EBI-352572, EBI-456067;
CC P08238; Q16832: DDR2; NbExp=2; IntAct=EBI-352572, EBI-1381484;
CC P08238; Q9Y463: DYRK1B; NbExp=2; IntAct=EBI-352572, EBI-634187;
CC P08238; Q9NR20: DYRK4; NbExp=2; IntAct=EBI-352572, EBI-3914009;
CC P08238; P00533: EGFR; NbExp=10; IntAct=EBI-352572, EBI-297353;
CC P08238; Q9BQI3: EIF2AK1; NbExp=2; IntAct=EBI-352572, EBI-640377;
CC P08238; P29317: EPHA2; NbExp=2; IntAct=EBI-352572, EBI-702104;
CC P08238; P04626: ERBB2; NbExp=4; IntAct=EBI-352572, EBI-641062;
CC P08238; P21860: ERBB3; NbExp=3; IntAct=EBI-352572, EBI-720706;
CC P08238; Q15303: ERBB4; NbExp=2; IntAct=EBI-352572, EBI-80371;
CC P08238; Q96A26: FAM162A; NbExp=3; IntAct=EBI-352572, EBI-6123466;
CC P08238; Q9UKC9: FBXL2; NbExp=2; IntAct=EBI-352572, EBI-724253;
CC P08238; O75426: FBXO24; NbExp=2; IntAct=EBI-352572, EBI-6425658;
CC P08238; Q9UKT8: FBXW2; NbExp=2; IntAct=EBI-352572, EBI-914727;
CC P08238; P16591: FER; NbExp=2; IntAct=EBI-352572, EBI-1380661;
CC P08238; P11362: FGFR1; NbExp=2; IntAct=EBI-352572, EBI-1028277;
CC P08238; P22607: FGFR3; NbExp=2; IntAct=EBI-352572, EBI-348399;
CC P08238; P09769: FGR; NbExp=4; IntAct=EBI-352572, EBI-1383732;
CC P08238; Q02790: FKBP4; NbExp=6; IntAct=EBI-352572, EBI-1047444;
CC P08238; Q13451: FKBP5; NbExp=16; IntAct=EBI-352572, EBI-306914;
CC P08238; P35916: FLT4; NbExp=2; IntAct=EBI-352572, EBI-1005467;
CC P08238; P06241: FYN; NbExp=5; IntAct=EBI-352572, EBI-515315;
CC P08238; P43250: GRK6; NbExp=2; IntAct=EBI-352572, EBI-722747;
CC P08238; Q8WTQ7: GRK7; NbExp=2; IntAct=EBI-352572, EBI-6423032;
CC P08238; P49840: GSK3A; NbExp=3; IntAct=EBI-352572, EBI-1044067;
CC P08238; Q8TF76: HASPIN; NbExp=2; IntAct=EBI-352572, EBI-1237328;
CC P08238; P08631: HCK; NbExp=4; IntAct=EBI-352572, EBI-346340;
CC P08238; Q8NE63: HIPK4; NbExp=2; IntAct=EBI-352572, EBI-6381114;
CC P08238; P08238: HSP90AB1; NbExp=4; IntAct=EBI-352572, EBI-352572;
CC P08238; Q14164: IKBKE; NbExp=2; IntAct=EBI-352572, EBI-307369;
CC P08238; Q9Y6K9: IKBKG; NbExp=3; IntAct=EBI-352572, EBI-81279;
CC P08238; Q13418: ILK; NbExp=2; IntAct=EBI-352572, EBI-747644;
CC P08238; Q08881: ITK; NbExp=3; IntAct=EBI-352572, EBI-968552;
CC P08238; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-352572, EBI-6426443;
CC P08238; P06239: LCK; NbExp=4; IntAct=EBI-352572, EBI-1348;
CC P08238; P53671: LIMK2; NbExp=3; IntAct=EBI-352572, EBI-1384350;
CC P08238; P07948: LYN; NbExp=2; IntAct=EBI-352572, EBI-79452;
CC P08238; Q8N7X4: MAGEB6; NbExp=3; IntAct=EBI-352572, EBI-6447163;
CC P08238; Q13163: MAP2K5; NbExp=4; IntAct=EBI-352572, EBI-307294;
CC P08238; O14733: MAP2K7; NbExp=2; IntAct=EBI-352572, EBI-492605;
CC P08238; Q99558: MAP3K14; NbExp=5; IntAct=EBI-352572, EBI-358011;
CC P08238; P41279: MAP3K8; NbExp=2; IntAct=EBI-352572, EBI-354900;
CC P08238; P80192: MAP3K9; NbExp=2; IntAct=EBI-352572, EBI-3951604;
CC P08238; Q92918: MAP4K1; NbExp=4; IntAct=EBI-352572, EBI-881;
CC P08238; Q8TD08: MAPK15; NbExp=2; IntAct=EBI-352572, EBI-1383794;
CC P08238; P31152: MAPK4; NbExp=3; IntAct=EBI-352572, EBI-3906061;
CC P08238; P10636-8: MAPT; NbExp=11; IntAct=EBI-352572, EBI-366233;
CC P08238; P42679: MATK; NbExp=2; IntAct=EBI-352572, EBI-751664;
CC P08238; P00540: MOS; NbExp=2; IntAct=EBI-352572, EBI-1757866;
CC P08238; O15146: MUSK; NbExp=2; IntAct=EBI-352572, EBI-6423196;
CC P08238; Q9H1R3: MYLK2; NbExp=3; IntAct=EBI-352572, EBI-356910;
CC P08238; Q86YV6: MYLK4; NbExp=3; IntAct=EBI-352572, EBI-6424604;
CC P08238; Q8WXR4: MYO3B; NbExp=2; IntAct=EBI-352572, EBI-350672;
CC P08238; Q8NG66: NEK11; NbExp=2; IntAct=EBI-352572, EBI-633195;
CC P08238; Q86SG6: NEK8; NbExp=2; IntAct=EBI-352572, EBI-1752987;
CC P08238; Q8TD19: NEK9; NbExp=2; IntAct=EBI-352572, EBI-1044009;
CC P08238; O75469: NR1I2; NbExp=2; IntAct=EBI-352572, EBI-3905991;
CC P08238; Q8N165: PDIK1L; NbExp=3; IntAct=EBI-352572, EBI-6423298;
CC P08238; Q9P215: POGK; NbExp=2; IntAct=EBI-352572, EBI-2555775;
CC P08238; P53041: PPP5C; NbExp=8; IntAct=EBI-352572, EBI-716663;
CC P08238; Q13131: PRKAA1; NbExp=2; IntAct=EBI-352572, EBI-1181405;
CC P08238; P22694: PRKACB; NbExp=2; IntAct=EBI-352572, EBI-2679622;
CC P08238; Q02156: PRKCE; NbExp=4; IntAct=EBI-352572, EBI-706254;
CC P08238; P05129: PRKCG; NbExp=2; IntAct=EBI-352572, EBI-949799;
CC P08238; Q05513: PRKCZ; NbExp=2; IntAct=EBI-352572, EBI-295351;
CC P08238; Q15139: PRKD1; NbExp=2; IntAct=EBI-352572, EBI-1181072;
CC P08238; O60260: PRKN; NbExp=2; IntAct=EBI-352572, EBI-716346;
CC P08238; P51817: PRKX; NbExp=3; IntAct=EBI-352572, EBI-4302903;
CC P08238; P11801: PSKH1; NbExp=3; IntAct=EBI-352572, EBI-3922781;
CC P08238; Q96QS6: PSKH2; NbExp=3; IntAct=EBI-352572, EBI-6424813;
CC P08238; Q15185: PTGES3; NbExp=4; IntAct=EBI-352572, EBI-1049387;
CC P08238; Q13882: PTK6; NbExp=3; IntAct=EBI-352572, EBI-1383632;
CC P08238; P04049: RAF1; NbExp=6; IntAct=EBI-352572, EBI-365996;
CC P08238; P49758: RGS6; NbExp=2; IntAct=EBI-352572, EBI-6426927;
CC P08238; Q01974: ROR2; NbExp=2; IntAct=EBI-352572, EBI-6422642;
CC P08238; P62913: RPL11; NbExp=2; IntAct=EBI-352572, EBI-354380;
CC P08238; Q15418: RPS6KA1; NbExp=4; IntAct=EBI-352572, EBI-963034;
CC P08238; P51812: RPS6KA3; NbExp=3; IntAct=EBI-352572, EBI-1046616;
CC P08238; Q9HBY8: SGK2; NbExp=2; IntAct=EBI-352572, EBI-3914329;
CC P08238; P31948: STIP1; NbExp=4; IntAct=EBI-352572, EBI-1054052;
CC P08238; Q15831: STK11; NbExp=5; IntAct=EBI-352572, EBI-306838;
CC P08238; Q86UX6: STK32C; NbExp=2; IntAct=EBI-352572, EBI-1050045;
CC P08238; Q15208: STK38; NbExp=2; IntAct=EBI-352572, EBI-458376;
CC P08238; Q9UNE7: STUB1; NbExp=5; IntAct=EBI-352572, EBI-357085;
CC P08238; Q6J9G0: STYK1; NbExp=2; IntAct=EBI-352572, EBI-6424915;
CC P08238; Q9Y2Z0-2: SUGT1; NbExp=2; IntAct=EBI-352572, EBI-10768076;
CC P08238; Q9UHD2: TBK1; NbExp=2; IntAct=EBI-352572, EBI-356402;
CC P08238; Q96S53: TESK2; NbExp=3; IntAct=EBI-352572, EBI-1384110;
CC P08238; Q07912: TNK2; NbExp=3; IntAct=EBI-352572, EBI-603457;
CC P08238; Q9BXA7: TSSK1B; NbExp=2; IntAct=EBI-352572, EBI-6423734;
CC P08238; Q96PF2: TSSK2; NbExp=2; IntAct=EBI-352572, EBI-852089;
CC P08238; Q9BXA6: TSSK6; NbExp=4; IntAct=EBI-352572, EBI-851883;
CC P08238; O95801: TTC4; NbExp=5; IntAct=EBI-352572, EBI-1050890;
CC P08238; P29597: TYK2; NbExp=2; IntAct=EBI-352572, EBI-1383454;
CC P08238; Q8IWX7: UNC45B; NbExp=2; IntAct=EBI-352572, EBI-9363363;
CC P08238; P07947: YES1; NbExp=3; IntAct=EBI-352572, EBI-515331;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16580629,
CC ECO:0000269|PubMed:18239673, ECO:0000269|PubMed:24880080,
CC ECO:0000269|PubMed:9482106}. Melanosome {ECO:0000269|PubMed:17081065}.
CC Nucleus {ECO:0000269|PubMed:18239673}. Secreted
CC {ECO:0000269|PubMed:20599762}. Cell membrane
CC {ECO:0000269|PubMed:20599762}. Dynein axonemal particle
CC {ECO:0000250|UniProtKB:Q6AZV1}. Cell surface
CC {ECO:0000269|PubMed:21949862}. Note=Identified by mass spectrometry in
CC melanosome fractions from stage I to stage IV (PubMed:17081065).
CC Translocates with BIRC2 from the nucleus to the cytoplasm during
CC differentiation (PubMed:18239673). Secreted when associated with TGFB1
CC processed form (LAP) (PubMed:20599762). {ECO:0000269|PubMed:17081065,
CC ECO:0000269|PubMed:18239673, 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 vitro).
CC {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 lipopolysaccharide
CC (PubMed:23585225). Phosphorylation at Ser-226 and Ser-255 inhibits AHR
CC interaction (PubMed:15581363). {ECO:0000269|PubMed:15581363,
CC 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 protein
CC radicals formation; disrupts the chaperoning function and the
CC degradation of its client proteins. {ECO:0000269|PubMed:22848402}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD14062.3; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB66478.1; Type=Frameshift; Evidence={ECO:0000305};
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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; -; NOT_ANNOTATED_CDS; 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 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 PDB; 5UC4; X-ray; 2.05 A; A/B/C/D=1-218.
DR PDB; 5UCH; X-ray; 2.65 A; A/B/C/D=1-218.
DR PDB; 5UCI; X-ray; 2.70 A; A/B/C/D=1-218.
DR PDB; 5UCJ; X-ray; 1.69 A; A/B/C/D=1-218.
DR PDB; 6N8W; X-ray; 3.09 A; A/B/C/D=1-231.
DR PDB; 6N8Y; X-ray; 1.55 A; A=1-221.
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 PDBsum; 5UC4; -.
DR PDBsum; 5UCH; -.
DR PDBsum; 5UCI; -.
DR PDBsum; 5UCJ; -.
DR PDBsum; 6N8W; -.
DR PDBsum; 6N8Y; -.
DR AlphaFoldDB; P08238; -.
DR SMR; P08238; -.
DR BioGRID; 109558; 585.
DR ComplexPortal; CPX-3285; HSP90B-CDC37 chaperone complex.
DR CORUM; P08238; -.
DR DIP; DIP-413N; -.
DR IntAct; P08238; 600.
DR MINT; P08238; -.
DR STRING; 9606.ENSP00000360609; -.
DR BindingDB; P08238; -.
DR ChEMBL; CHEMBL4303; -.
DR DrugBank; DB08293; (5E)-12-CHLORO-13,15-DIHYDROXY-4,7,8,9-TETRAHYDRO-2-BENZOXACYCLOTRIDECINE-1,10(3H,11H)-DIONE.
DR DrugBank; DB08153; (5E)-14-CHLORO-15,17-DIHYDROXY-4,7,8,9,10,11-HEXAHYDRO-2-BENZOXACYCLOPENTADECINE-1,12(3H,13H)-DIONE.
DR DrugBank; DB08292; (5Z)-12-CHLORO-13,15-DIHYDROXY-4,7,8,9-TETRAHYDRO-2-BENZOXACYCLOTRIDECINE-1,10(3H,11H)-DIONE.
DR DrugBank; DB08346; (5Z)-13-CHLORO-14,16-DIHYDROXY-3,4,7,8,9,10-HEXAHYDRO-1H-2-BENZOXACYCLOTETRADECINE-1,11(12H)-DIONE.
DR DrugBank; DB08465; 2-(3-AMINO-2,5,6-TRIMETHOXYPHENYL)ETHYL 5-CHLORO-2,4-DIHYDROXYBENZOATE.
DR DrugBank; DB08045; 4-{4-[4-(3-AMINOPROPOXY)PHENYL]-1H-PYRAZOL-5-YL}-6-CHLOROBENZENE-1,3-DIOL.
DR DrugBank; DB07877; 8-(6-BROMO-BENZO[1,3]DIOXOL-5-YLSULFANYL)-9-(3-ISOPROPYLAMINO-PROPYL)-ADENINE.
DR DrugBank; DB02754; 9-Butyl-8-(3,4,5-Trimethoxybenzyl)-9h-Purin-6-Amine.
DR DrugBank; DB07594; CCT-018159.
DR DrugBank; DB02424; Geldanamycin.
DR DrugBank; DB08464; METHYL 3-CHLORO-2-{3-[(2,5-DIHYDROXY-4-METHOXYPHENYL)AMINO]-3-OXOPROPYL}-4,6-DIHYDROXYBENZOATE.
DR DrugBank; DB09221; Polaprezinc.
DR DrugBank; DB03758; Radicicol.
DR DrugBank; DB06070; SNX-5422.
DR DrugBank; DB05134; Tanespimycin.
DR GuidetoPHARMACOLOGY; 2907; -.
DR MoonDB; P08238; Predicted.
DR TCDB; 8.A.163.1.1; the hsp90/cdc37 (hsp90/cdc37) family.
DR CarbonylDB; P08238; -.
DR GlyConnect; 1302; 2 N-Linked glycans (2 sites).
DR GlyGen; P08238; 5 sites, 2 N-linked glycans (2 sites), 2 O-linked glycans (1 site).
DR iPTMnet; P08238; -.
DR MetOSite; P08238; -.
DR PhosphoSitePlus; P08238; -.
DR SwissPalm; P08238; -.
DR BioMuta; HSP90AB1; -.
DR DMDM; 17865718; -.
DR OGP; P08238; -.
DR EPD; P08238; -.
DR jPOST; P08238; -.
DR MassIVE; P08238; -.
DR MaxQB; P08238; -.
DR PaxDb; P08238; -.
DR PeptideAtlas; P08238; -.
DR PRIDE; P08238; -.
DR ProteomicsDB; 52096; -.
DR TopDownProteomics; P08238; -.
DR ABCD; P08238; 1 sequenced antibody.
DR Antibodypedia; 3929; 1743 antibodies from 48 providers.
DR DNASU; 3326; -.
DR Ensembl; ENST00000353801.7; ENSP00000325875.3; ENSG00000096384.20.
DR Ensembl; ENST00000371554.2; ENSP00000360609.1; ENSG00000096384.20.
DR Ensembl; ENST00000371646.10; ENSP00000360709.5; ENSG00000096384.20.
DR Ensembl; ENST00000620073.4; ENSP00000481908.1; ENSG00000096384.20.
DR GeneID; 3326; -.
DR KEGG; hsa:3326; -.
DR MANE-Select; ENST00000371646.10; ENSP00000360709.5; NM_007355.4; NP_031381.2.
DR UCSC; uc003oxa.3; human.
DR CTD; 3326; -.
DR DisGeNET; 3326; -.
DR GeneCards; HSP90AB1; -.
DR HGNC; HGNC:5258; HSP90AB1.
DR HPA; ENSG00000096384; Low tissue specificity.
DR MIM; 140572; gene.
DR neXtProt; NX_P08238; -.
DR OpenTargets; ENSG00000096384; -.
DR PharmGKB; PA29524; -.
DR VEuPathDB; HostDB:ENSG00000096384; -.
DR eggNOG; KOG0019; Eukaryota.
DR GeneTree; ENSGT01020000230401; -.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; P08238; -.
DR OMA; ELISNAX; -.
DR OrthoDB; 924636at2759; -.
DR PhylomeDB; P08238; -.
DR TreeFam; TF300686; -.
DR BRENDA; 3.6.4.10; 2681.
DR PathwayCommons; P08238; -.
DR Reactome; R-HSA-168928; DDX58/IFIH1-mediated induction of interferon-alpha/beta.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-HSA-3371511; HSF1 activation.
DR Reactome; R-HSA-3371568; Attenuation phase.
DR Reactome; R-HSA-3371571; HSF1-dependent transactivation.
DR Reactome; R-HSA-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 Reactome; R-HSA-8939211; ESR-mediated signaling.
DR Reactome; R-HSA-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-9613829; Chaperone Mediated Autophagy.
DR Reactome; R-HSA-9660826; Purinergic signaling in leishmaniasis infection.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR SignaLink; P08238; -.
DR SIGNOR; P08238; -.
DR BioGRID-ORCS; 3326; 113 hits in 1098 CRISPR screens.
DR ChiTaRS; HSP90AB1; human.
DR EvolutionaryTrace; P08238; -.
DR GeneWiki; HSP90AB1; -.
DR GenomeRNAi; 3326; -.
DR Pharos; P08238; Tchem.
DR PRO; PR:P08238; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P08238; protein.
DR Bgee; ENSG00000096384; Expressed in frontal pole and 210 other tissues.
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:0044295; C:axonal growth cone; ISS:ARUK-UCL.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0031526; C:brush border membrane; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0044294; C:dendritic growth cone; ISS:ARUK-UCL.
DR GO; GO:0120293; C:dynein axonemal particle; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA: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:1990565; C:HSP90-CDC37 chaperone complex; IDA:ParkinsonsUK-UCL.
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; HDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:ARUK-UCL.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1990917; C:ooplasm; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:1990913; C:sperm head plasma membrane; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IDA:CAFA.
DR GO; GO:0016887; F:ATP hydrolysis activity; TAS:Reactome.
DR GO; GO:0043008; F:ATP-dependent protein binding; IPI:CAFA.
DR GO; GO:0045296; F:cadherin binding; HDA: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: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:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0023026; F:MHC class II protein complex binding; HDA: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:0044183; F:protein folding chaperone; IEA:Ensembl.
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; HDA:UniProtKB.
DR GO; GO:0017098; F:sulfonylurea receptor binding; IEA:Ensembl.
DR GO; GO:0048156; F:tau protein binding; NAS:ARUK-UCL.
DR GO; GO:0030911; F:TPR domain binding; ISS:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ARUK-UCL.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0002134; F:UTP binding; IEA:Ensembl.
DR GO; GO:0048675; P:axon extension; ISS:ARUK-UCL.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
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:0021955; P:central nervous system neuron axonogenesis; ISS:ARUK-UCL.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IDA:CAFA.
DR GO; GO:0030010; P:establishment of cell polarity; ISS:ARUK-UCL.
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:1901799; P:negative regulation of proteasomal protein catabolic process; ISS:ARUK-UCL.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0051248; P:negative regulation of protein metabolic process; ISS:ARUK-UCL.
DR GO; GO:1901389; P:negative regulation of transforming growth factor beta activation; IDA:UniProtKB.
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:1904031; P:positive regulation of cyclin-dependent protein kinase activity; ISS:ARUK-UCL.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISS:ARUK-UCL.
DR GO; GO: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:0042307; P:positive regulation of protein import into nucleus; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:ARUK-UCL.
DR GO; GO: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:1902949; P:positive regulation of tau-protein kinase activity; IC:ARUK-UCL.
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; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; ISS:ARUK-UCL.
DR GO; GO:0031396; P:regulation of protein ubiquitination; IDA:BHF-UCL.
DR GO; GO: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:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
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 Gene3D; 1.20.120.790; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR IDEAL; IID00536; -.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cell membrane; Chaperone;
KW Cytoplasm; Direct protein sequencing; Glycoprotein; Membrane; Methylation;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW S-nitrosylation; Secreted; Stress response; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2492519"
FT CHAIN 2..724
FT /note="Heat shock protein HSP 90-beta"
FT /id="PRO_0000062917"
FT REGION 2..527
FT /note="Interaction with TP53"
FT /evidence="ECO:0000269|PubMed:15358771"
FT REGION 2..214
FT /note="Interaction with BIRC2"
FT /evidence="ECO:0000269|PubMed:25486457"
FT REGION 9..231
FT /note="Interaction with NR3C1"
FT /evidence="ECO:0000250|UniProtKB:P11499"
FT REGION 215..552
FT /note="Interaction with AHSA1"
FT /evidence="ECO:0000269|PubMed:25486457"
FT REGION 222..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..608
FT /note="Interaction with NR3C1"
FT /evidence="ECO:0000250|UniProtKB:P11499"
FT REGION 620..723
FT /note="Interaction with NR1D1"
FT /evidence="ECO:0000250|UniProtKB:P11499"
FT REGION 696..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 720..724
FT /note="TPR repeat-binding"
FT COMPBIAS 241..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 126..127
FT /note="Cleaved under oxidative stress"
FT /evidence="ECO:0000269|PubMed:22848402"
FT MOD_RES 219
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11499"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.12, ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11499"
FT MOD_RES 297
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 301
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000269|PubMed:23585225"
FT MOD_RES 305
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P11499"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 399
FT /note="N6-malonyllysine"
FT /evidence="ECO:0000269|PubMed:21908771"
FT MOD_RES 435
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 479
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 481
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 484
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P11499"
FT MOD_RES 531
FT /note="N6-methylated lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24880080"
FT MOD_RES 531
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11499"
FT MOD_RES 574
FT /note="N6-methylated lysine"
FT /evidence="ECO:0000269|PubMed:24880080"
FT MOD_RES 577
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11499"
FT MOD_RES 590
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000305|PubMed:19696785"
FT MOD_RES 624
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11499"
FT MOD_RES 669
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 718
FT /note="Phosphoserine; by PLK2 and PLK3"
FT /evidence="ECO:0000269|PubMed:22828320"
FT CARBOHYD 434
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 452
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT VARIANT 349
FT /note="K -> E (in dbSNP:rs11538975)"
FT /id="VAR_049624"
FT MUTAGEN 42
FT /note="E->A: Strong ATP-binding. Strong interaction with
FT HSF1, HIF1A, ERBB2, MET, KEAP1 and RHOBTB2."
FT /evidence="ECO:0000269|PubMed:26517842"
FT MUTAGEN 88
FT /note="D->A: Impaired ATP-binding. Strong interaction with
FT HIF1A, MET, KEAP1 and RHOBTB2. Loss of interaction with
FT HSF1 and ERBB2."
FT /evidence="ECO:0000269|PubMed:26517842"
FT MUTAGEN 226
FT /note="S->A: Increases the binding affinity for AHR; when
FT associated with A-255. Increases AHR transcription
FT activity; when associated with A-255."
FT /evidence="ECO:0000269|PubMed:15581363"
FT MUTAGEN 226
FT /note="S->E: No effect on the interaction with AHR; when
FT associated with E-255."
FT /evidence="ECO:0000269|PubMed:15581363"
FT MUTAGEN 255
FT /note="S->A: Increases the binding affinity for AHR; when
FT associated with A-226. Increases AHR transcription
FT activity; when associated with A-226."
FT /evidence="ECO:0000269|PubMed:15581363"
FT MUTAGEN 255
FT /note="S->E: No effect on the interaction with AHR; when
FT associated with E-226."
FT /evidence="ECO:0000269|PubMed:15581363"
FT MUTAGEN 301
FT /note="Y->F: Decreases interaction with NOS3 and SRC.
FT impairs resists LPS-induced tyrosine phosphorylation. Does
FT not block LPS-induced pp60src phosphorylation."
FT /evidence="ECO:0000269|PubMed:23585225"
FT MUTAGEN 531
FT /note="K->A: Highly decreases the signal of SMYD2-dependent
FT HSP90AB1 methylation; when associated with A-574.
FT Diminishes dimerized form; when associated with A-574.
FT Reduces interaction with STIP1 or CDC37; when associated
FT with A-574."
FT /evidence="ECO:0000269|PubMed:24880080"
FT MUTAGEN 574
FT /note="K->A: Decreases the signal of SMYD2-dependent
FT HSP90AB1 methylation. Highly decreases the signal of SMYD2-
FT dependent HSP90AB1 methylation; when associated with A-531.
FT Diminishes dimerized form; when associated with A-531.
FT Reduces interaction with STIP1 or CDC37; when associated
FT with A-531."
FT /evidence="ECO:0000269|PubMed:24880080"
FT MUTAGEN 590
FT /note="C->A,N,D: Reduced ATPase activity and client protein
FT activation."
FT /evidence="ECO:0000269|PubMed:19696785"
FT CONFLICT 147
FT /note="T -> R (in Ref. 1; AAA36025)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="R -> M (in Ref. 1; AAA36025)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="V -> A (in Ref. 5; CAB66478)"
FT /evidence="ECO:0000305"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:6N8W"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:6N8Y"
FT HELIX 19..30
FT /evidence="ECO:0007829|PDB:6N8Y"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:5UCH"
FT HELIX 38..60
FT /evidence="ECO:0007829|PDB:6N8Y"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:6N8Y"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:6N8Y"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:6N8Y"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:6N8Y"
FT HELIX 95..99
FT /evidence="ECO:0007829|PDB:6N8Y"
FT HELIX 101..118
FT /evidence="ECO:0007829|PDB:6N8Y"
FT HELIX 123..129
FT /evidence="ECO:0007829|PDB:6N8Y"
FT HELIX 132..138
FT /evidence="ECO:0007829|PDB:6N8Y"
FT STRAND 140..148
FT /evidence="ECO:0007829|PDB:6N8Y"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:6N8Y"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:6N8Y"
FT STRAND 176..185
FT /evidence="ECO:0007829|PDB:6N8Y"
FT HELIX 187..193
FT /evidence="ECO:0007829|PDB:6N8Y"
FT HELIX 195..205
FT /evidence="ECO:0007829|PDB:6N8Y"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:6N8Y"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:3PRY"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:3PRY"
FT HELIX 298..309
FT /evidence="ECO:0007829|PDB:3PRY"
FT STRAND 316..323
FT /evidence="ECO:0007829|PDB:3PRY"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:3PRY"
FT STRAND 329..335
FT /evidence="ECO:0007829|PDB:3PRY"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:3PRY"
FT STRAND 360..364
FT /evidence="ECO:0007829|PDB:3PRY"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:3PRY"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:3PRY"
FT STRAND 378..386
FT /evidence="ECO:0007829|PDB:3PRY"
FT HELIX 395..420
FT /evidence="ECO:0007829|PDB:3PRY"
FT HELIX 423..443
FT /evidence="ECO:0007829|PDB:3PRY"
FT HELIX 445..447
FT /evidence="ECO:0007829|PDB:3PRY"
FT HELIX 448..453
FT /evidence="ECO:0007829|PDB:3PRY"
FT STRAND 456..459
FT /evidence="ECO:0007829|PDB:3PRY"
FT TURN 460..464
FT /evidence="ECO:0007829|PDB:3PRY"
FT HELIX 469..474
FT /evidence="ECO:0007829|PDB:3PRY"
FT STRAND 482..486
FT /evidence="ECO:0007829|PDB:3PRY"
FT HELIX 491..495
FT /evidence="ECO:0007829|PDB:3PRY"
FT HELIX 498..504
FT /evidence="ECO:0007829|PDB:3PRY"
FT TURN 505..507
FT /evidence="ECO:0007829|PDB:3PRY"
FT STRAND 510..512
FT /evidence="ECO:0007829|PDB:3PRY"
FT HELIX 518..525
FT /evidence="ECO:0007829|PDB:3PRY"
FT STRAND 531..535
FT /evidence="ECO:0007829|PDB:3PRY"
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
