Full text data of HSP90AB1
HSP90AB1
(HSP90B, HSPC2, HSPCB)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Heat shock protein HSP 90-beta; HSP 90 (Heat shock 84 kDa; HSP 84; HSP84)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Heat shock protein HSP 90-beta; HSP 90 (Heat shock 84 kDa; HSP 84; HSP84)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00334775
IPI00334775 Hypothetical protein DKFZp761K0511 Hypothetical protein DKFZp761K0511 membrane n/a n/a n/a n/a n/a n/a n/a n/a 32 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
IPI00334775 Hypothetical protein DKFZp761K0511 Hypothetical protein DKFZp761K0511 membrane n/a n/a n/a n/a n/a n/a n/a n/a 32 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
UniProt
P08238
ID HS90B_HUMAN Reviewed; 724 AA.
AC P08238; B2R5P0; Q5T9W7; Q9NQW0; Q9NTK6;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 182.
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 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 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 [18]
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 [19]
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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND MASS
RP SPECTROMETRY.
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 [21]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
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 [22]
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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-297, AND MASS
RP SPECTROMETRY.
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 [24]
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 [25]
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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND MASS
RP SPECTROMETRY.
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 [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND MASS
RP SPECTROMETRY.
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 [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND MASS
RP SPECTROMETRY.
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 [29]
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 [30]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-435 AND LYS-481, AND MASS
RP SPECTROMETRY.
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 [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND MASS
RP SPECTROMETRY.
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 [32]
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 [33]
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 [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND MASS
RP SPECTROMETRY.
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 [35]
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 [36]
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 [37]
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 -!- SUBUNIT: Homodimer. Interacts with p53/TP53 (By similarity). Forms
CC a complex with CDK6 and Hsp90/HSP90AB1. Interacts with UNC45A.
CC Binding to UNC45A involves 2 UNC45A monomers per HSP90AB1 dimer.
CC Interacts with CHORDC1 and DNAJC7 (By similarity). Interacts with
CC FKBP4.
CC -!- INTERACTION:
CC P36896:ACVR1B; NbExp=2; IntAct=EBI-352572, EBI-1384128;
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 P10398:ARAF; NbExp=3; 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=4; IntAct=EBI-352572, EBI-295634;
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 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 O95905:ECD; NbExp=2; IntAct=EBI-352572, EBI-2557598;
CC P00533:EGFR; NbExp=5; 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 P22607:FGFR3; NbExp=2; IntAct=EBI-352572, EBI-348399;
CC P09769:FGR; NbExp=2; IntAct=EBI-352572, EBI-1383732;
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 Q2WGJ6:KLHL38; NbExp=2; 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 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 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 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 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=4; IntAct=EBI-352572, EBI-357085;
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 -!- SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Note=Identified by
CC mass spectrometry in melanosome fractions from stage I to stage
CC IV.
CC -!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
CC repeat-containing proteins (By similarity).
CC -!- PTM: Ubiquitinated in the presence of STUB1-UBE2D1 complex (in
CC vitro).
CC -!- PTM: ISGylated.
CC -!- PTM: S-nitrosylated; negatively regulates the ATPase activity
CC (Probable).
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD14062.3; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=CAB66478.1; Type=Frameshift; Positions=709;
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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; 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 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 RefSeq; XP_005249132.1; XM_005249075.1.
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; 3NMQ; X-ray; 2.20 A; A=1-223.
DR PDB; 3PRY; X-ray; 2.28 A; A/B/C=284-543.
DR PDBsum; 1QZ2; -.
DR PDBsum; 1UYM; -.
DR PDBsum; 3NMQ; -.
DR PDBsum; 3PRY; -.
DR ProteinModelPortal; P08238; -.
DR SMR; P08238; 8-691.
DR DIP; DIP-413N; -.
DR IntAct; P08238; 445.
DR MINT; MINT-99712; -.
DR STRING; 9606.ENSP00000325875; -.
DR BindingDB; P08238; -.
DR ChEMBL; CHEMBL4303; -.
DR PhosphoSite; P08238; -.
DR DMDM; 17865718; -.
DR OGP; P08238; -.
DR PaxDb; P08238; -.
DR PeptideAtlas; P08238; -.
DR PRIDE; P08238; -.
DR DNASU; 3326; -.
DR Ensembl; ENST00000353801; ENSP00000325875; ENSG00000096384.
DR Ensembl; ENST00000371554; ENSP00000360609; ENSG00000096384.
DR Ensembl; ENST00000371646; ENSP00000360709; ENSG00000096384.
DR GeneID; 3326; -.
DR KEGG; hsa:3326; -.
DR UCSC; uc003oxa.2; human.
DR CTD; 3326; -.
DR GeneCards; GC06P044214; -.
DR H-InvDB; HIX0031498; -.
DR H-InvDB; HIX0057380; -.
DR HGNC; HGNC:5258; HSP90AB1.
DR HPA; CAB005230; -.
DR MIM; 140572; gene.
DR neXtProt; NX_P08238; -.
DR PharmGKB; PA29524; -.
DR eggNOG; COG0326; -.
DR HOGENOM; HOG000031988; -.
DR HOVERGEN; HBG007374; -.
DR InParanoid; P08238; -.
DR KO; K04079; -.
DR OMA; FAPKRAP; -.
DR OrthoDB; EOG780RM0; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; HSP90AB1; human.
DR EvolutionaryTrace; P08238; -.
DR GeneWiki; HSP90AB1; -.
DR GenomeRNAi; 3326; -.
DR NextBio; 13182; -.
DR PRO; PR:P08238; -.
DR ArrayExpress; P08238; -.
DR Bgee; P08238; -.
DR CleanEx; HS_HSP90AB1; -.
DR Genevestigator; P08238; -.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
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:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016234; C:inclusion body; IEA:Ensembl.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0002135; F:CTP binding; IEA:Ensembl.
DR GO; GO:0032564; F:dATP binding; IEA:Ensembl.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:Ensembl.
DR GO; GO:0030235; F:nitric-oxide synthase regulator activity; ISS:UniProtKB.
DR GO; GO:0030911; F:TPR domain binding; ISS:UniProtKB.
DR GO; GO:0002134; F:UTP binding; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
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:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
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; IMP:MGI.
DR GO; GO:0035872; P:nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway; TAS:Reactome.
DR GO; GO:0001890; P:placenta development; IEA:Ensembl.
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: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:0071902; P:positive regulation of protein serine/threonine kinase activity; IEA:Ensembl.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0060334; P:regulation of interferon-gamma-mediated signaling pathway; IMP:MGI.
DR GO; GO:0060338; P:regulation of type I interferon-mediated signaling pathway; IMP:MGI.
DR GO; GO:0009651; P:response to salt stress; IEA:Ensembl.
DR GO; GO:0006986; P:response to unfolded protein; NAS:UniProtKB.
DR Gene3D; 3.30.565.10; -; 2.
DR InterPro; IPR003594; HATPase_ATP-bd.
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; Chaperone; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Glycoprotein;
KW Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
KW S-nitrosylation; Stress response; Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 724 Heat shock protein HSP 90-beta.
FT /FTId=PRO_0000062917.
FT MOTIF 720 724 TPR repeat-binding.
FT BINDING 46 46 ATP (By similarity).
FT BINDING 88 88 ATP.
FT BINDING 107 107 ATP (By similarity).
FT BINDING 133 133 ATP; via amide nitrogen (By similarity).
FT BINDING 392 392 ATP (By similarity).
FT MOD_RES 226 226 Phosphoserine.
FT MOD_RES 255 255 Phosphoserine.
FT MOD_RES 261 261 Phosphoserine.
FT MOD_RES 275 275 N6-acetyllysine.
FT MOD_RES 284 284 N6-acetyllysine.
FT MOD_RES 297 297 Phosphothreonine.
FT MOD_RES 305 305 Phosphotyrosine (By similarity).
FT MOD_RES 307 307 Phosphoserine.
FT MOD_RES 354 354 N6-acetyllysine.
FT MOD_RES 399 399 N6-acetyllysine; alternate.
FT MOD_RES 399 399 N6-malonyllysine; alternate.
FT MOD_RES 402 402 N6-acetyllysine.
FT MOD_RES 435 435 N6-acetyllysine.
FT MOD_RES 452 452 Phosphoserine; alternate.
FT MOD_RES 481 481 N6-acetyllysine.
FT MOD_RES 484 484 Phosphotyrosine.
FT MOD_RES 532 532 Phosphoserine.
FT MOD_RES 568 568 N6-acetyllysine.
FT MOD_RES 590 590 S-nitrosocysteine (Probable).
FT MOD_RES 624 624 N6-acetyllysine.
FT MOD_RES 718 718 Phosphoserine.
FT CARBOHYD 434 434 O-linked (GlcNAc) (By similarity).
FT CARBOHYD 452 452 O-linked (GlcNAc); alternate (By
FT similarity).
FT VARIANT 349 349 K -> E (in dbSNP:rs11538975).
FT /FTId=VAR_049624.
FT MUTAGEN 590 590 C->A,N,D: Reduced ATPase activity and
FT client protein activation.
FT CONFLICT 147 147 T -> R (in Ref. 1; AAA36025).
FT CONFLICT 177 177 R -> M (in Ref. 1; AAA36025).
FT CONFLICT 403 403 V -> A (in Ref. 5; CAB66478).
FT STRAND 13 16
FT HELIX 19 30
FT HELIX 38 60
FT HELIX 62 65
FT STRAND 73 78
FT TURN 79 82
FT STRAND 83 88
FT HELIX 95 99
FT HELIX 101 118
FT HELIX 123 129
FT HELIX 132 138
FT STRAND 140 148
FT STRAND 155 159
FT STRAND 164 169
FT STRAND 176 185
FT HELIX 187 193
FT HELIX 195 205
FT STRAND 213 215
FT HELIX 288 290
FT HELIX 293 295
FT HELIX 298 309
FT STRAND 316 323
FT STRAND 325 327
FT STRAND 329 335
FT STRAND 353 357
FT STRAND 360 364
FT HELIX 367 369
FT HELIX 372 374
FT STRAND 378 386
FT HELIX 395 420
FT HELIX 423 443
FT HELIX 445 447
FT HELIX 448 453
FT STRAND 456 459
FT TURN 460 464
FT HELIX 469 474
FT STRAND 482 486
FT HELIX 491 495
FT HELIX 498 504
FT TURN 505 507
FT STRAND 510 512
FT HELIX 518 525
FT STRAND 531 535
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
//
ID HS90B_HUMAN Reviewed; 724 AA.
AC P08238; B2R5P0; Q5T9W7; Q9NQW0; Q9NTK6;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 182.
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 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 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 [18]
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 [19]
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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND MASS
RP SPECTROMETRY.
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 [21]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
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 [22]
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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-297, AND MASS
RP SPECTROMETRY.
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 [24]
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 [25]
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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND MASS
RP SPECTROMETRY.
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 [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND MASS
RP SPECTROMETRY.
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 [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND MASS
RP SPECTROMETRY.
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 [29]
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 [30]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-435 AND LYS-481, AND MASS
RP SPECTROMETRY.
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 [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND MASS
RP SPECTROMETRY.
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 [32]
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 [33]
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 [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND MASS
RP SPECTROMETRY.
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 [35]
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 [36]
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 [37]
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 -!- SUBUNIT: Homodimer. Interacts with p53/TP53 (By similarity). Forms
CC a complex with CDK6 and Hsp90/HSP90AB1. Interacts with UNC45A.
CC Binding to UNC45A involves 2 UNC45A monomers per HSP90AB1 dimer.
CC Interacts with CHORDC1 and DNAJC7 (By similarity). Interacts with
CC FKBP4.
CC -!- INTERACTION:
CC P36896:ACVR1B; NbExp=2; IntAct=EBI-352572, EBI-1384128;
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 P10398:ARAF; NbExp=3; 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=4; IntAct=EBI-352572, EBI-295634;
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 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 O95905:ECD; NbExp=2; IntAct=EBI-352572, EBI-2557598;
CC P00533:EGFR; NbExp=5; 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 P22607:FGFR3; NbExp=2; IntAct=EBI-352572, EBI-348399;
CC P09769:FGR; NbExp=2; IntAct=EBI-352572, EBI-1383732;
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 Q2WGJ6:KLHL38; NbExp=2; 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 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 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 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 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=4; IntAct=EBI-352572, EBI-357085;
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 -!- SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Note=Identified by
CC mass spectrometry in melanosome fractions from stage I to stage
CC IV.
CC -!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
CC repeat-containing proteins (By similarity).
CC -!- PTM: Ubiquitinated in the presence of STUB1-UBE2D1 complex (in
CC vitro).
CC -!- PTM: ISGylated.
CC -!- PTM: S-nitrosylated; negatively regulates the ATPase activity
CC (Probable).
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD14062.3; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=CAB66478.1; Type=Frameshift; Positions=709;
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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; 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 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 RefSeq; XP_005249132.1; XM_005249075.1.
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; 3NMQ; X-ray; 2.20 A; A=1-223.
DR PDB; 3PRY; X-ray; 2.28 A; A/B/C=284-543.
DR PDBsum; 1QZ2; -.
DR PDBsum; 1UYM; -.
DR PDBsum; 3NMQ; -.
DR PDBsum; 3PRY; -.
DR ProteinModelPortal; P08238; -.
DR SMR; P08238; 8-691.
DR DIP; DIP-413N; -.
DR IntAct; P08238; 445.
DR MINT; MINT-99712; -.
DR STRING; 9606.ENSP00000325875; -.
DR BindingDB; P08238; -.
DR ChEMBL; CHEMBL4303; -.
DR PhosphoSite; P08238; -.
DR DMDM; 17865718; -.
DR OGP; P08238; -.
DR PaxDb; P08238; -.
DR PeptideAtlas; P08238; -.
DR PRIDE; P08238; -.
DR DNASU; 3326; -.
DR Ensembl; ENST00000353801; ENSP00000325875; ENSG00000096384.
DR Ensembl; ENST00000371554; ENSP00000360609; ENSG00000096384.
DR Ensembl; ENST00000371646; ENSP00000360709; ENSG00000096384.
DR GeneID; 3326; -.
DR KEGG; hsa:3326; -.
DR UCSC; uc003oxa.2; human.
DR CTD; 3326; -.
DR GeneCards; GC06P044214; -.
DR H-InvDB; HIX0031498; -.
DR H-InvDB; HIX0057380; -.
DR HGNC; HGNC:5258; HSP90AB1.
DR HPA; CAB005230; -.
DR MIM; 140572; gene.
DR neXtProt; NX_P08238; -.
DR PharmGKB; PA29524; -.
DR eggNOG; COG0326; -.
DR HOGENOM; HOG000031988; -.
DR HOVERGEN; HBG007374; -.
DR InParanoid; P08238; -.
DR KO; K04079; -.
DR OMA; FAPKRAP; -.
DR OrthoDB; EOG780RM0; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; HSP90AB1; human.
DR EvolutionaryTrace; P08238; -.
DR GeneWiki; HSP90AB1; -.
DR GenomeRNAi; 3326; -.
DR NextBio; 13182; -.
DR PRO; PR:P08238; -.
DR ArrayExpress; P08238; -.
DR Bgee; P08238; -.
DR CleanEx; HS_HSP90AB1; -.
DR Genevestigator; P08238; -.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
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:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016234; C:inclusion body; IEA:Ensembl.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0002135; F:CTP binding; IEA:Ensembl.
DR GO; GO:0032564; F:dATP binding; IEA:Ensembl.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:Ensembl.
DR GO; GO:0030235; F:nitric-oxide synthase regulator activity; ISS:UniProtKB.
DR GO; GO:0030911; F:TPR domain binding; ISS:UniProtKB.
DR GO; GO:0002134; F:UTP binding; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
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:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
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; IMP:MGI.
DR GO; GO:0035872; P:nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway; TAS:Reactome.
DR GO; GO:0001890; P:placenta development; IEA:Ensembl.
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: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:0071902; P:positive regulation of protein serine/threonine kinase activity; IEA:Ensembl.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0060334; P:regulation of interferon-gamma-mediated signaling pathway; IMP:MGI.
DR GO; GO:0060338; P:regulation of type I interferon-mediated signaling pathway; IMP:MGI.
DR GO; GO:0009651; P:response to salt stress; IEA:Ensembl.
DR GO; GO:0006986; P:response to unfolded protein; NAS:UniProtKB.
DR Gene3D; 3.30.565.10; -; 2.
DR InterPro; IPR003594; HATPase_ATP-bd.
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; Chaperone; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Glycoprotein;
KW Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
KW S-nitrosylation; Stress response; Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 724 Heat shock protein HSP 90-beta.
FT /FTId=PRO_0000062917.
FT MOTIF 720 724 TPR repeat-binding.
FT BINDING 46 46 ATP (By similarity).
FT BINDING 88 88 ATP.
FT BINDING 107 107 ATP (By similarity).
FT BINDING 133 133 ATP; via amide nitrogen (By similarity).
FT BINDING 392 392 ATP (By similarity).
FT MOD_RES 226 226 Phosphoserine.
FT MOD_RES 255 255 Phosphoserine.
FT MOD_RES 261 261 Phosphoserine.
FT MOD_RES 275 275 N6-acetyllysine.
FT MOD_RES 284 284 N6-acetyllysine.
FT MOD_RES 297 297 Phosphothreonine.
FT MOD_RES 305 305 Phosphotyrosine (By similarity).
FT MOD_RES 307 307 Phosphoserine.
FT MOD_RES 354 354 N6-acetyllysine.
FT MOD_RES 399 399 N6-acetyllysine; alternate.
FT MOD_RES 399 399 N6-malonyllysine; alternate.
FT MOD_RES 402 402 N6-acetyllysine.
FT MOD_RES 435 435 N6-acetyllysine.
FT MOD_RES 452 452 Phosphoserine; alternate.
FT MOD_RES 481 481 N6-acetyllysine.
FT MOD_RES 484 484 Phosphotyrosine.
FT MOD_RES 532 532 Phosphoserine.
FT MOD_RES 568 568 N6-acetyllysine.
FT MOD_RES 590 590 S-nitrosocysteine (Probable).
FT MOD_RES 624 624 N6-acetyllysine.
FT MOD_RES 718 718 Phosphoserine.
FT CARBOHYD 434 434 O-linked (GlcNAc) (By similarity).
FT CARBOHYD 452 452 O-linked (GlcNAc); alternate (By
FT similarity).
FT VARIANT 349 349 K -> E (in dbSNP:rs11538975).
FT /FTId=VAR_049624.
FT MUTAGEN 590 590 C->A,N,D: Reduced ATPase activity and
FT client protein activation.
FT CONFLICT 147 147 T -> R (in Ref. 1; AAA36025).
FT CONFLICT 177 177 R -> M (in Ref. 1; AAA36025).
FT CONFLICT 403 403 V -> A (in Ref. 5; CAB66478).
FT STRAND 13 16
FT HELIX 19 30
FT HELIX 38 60
FT HELIX 62 65
FT STRAND 73 78
FT TURN 79 82
FT STRAND 83 88
FT HELIX 95 99
FT HELIX 101 118
FT HELIX 123 129
FT HELIX 132 138
FT STRAND 140 148
FT STRAND 155 159
FT STRAND 164 169
FT STRAND 176 185
FT HELIX 187 193
FT HELIX 195 205
FT STRAND 213 215
FT HELIX 288 290
FT HELIX 293 295
FT HELIX 298 309
FT STRAND 316 323
FT STRAND 325 327
FT STRAND 329 335
FT STRAND 353 357
FT STRAND 360 364
FT HELIX 367 369
FT HELIX 372 374
FT STRAND 378 386
FT HELIX 395 420
FT HELIX 423 443
FT HELIX 445 447
FT HELIX 448 453
FT STRAND 456 459
FT TURN 460 464
FT HELIX 469 474
FT STRAND 482 486
FT HELIX 491 495
FT HELIX 498 504
FT TURN 505 507
FT STRAND 510 512
FT HELIX 518 525
FT STRAND 531 535
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
//
MIM
140572
*RECORD*
*FIELD* NO
140572
*FIELD* TI
*140572 HEAT-SHOCK PROTEIN, 90-KD, ALPHA, CLASS B, MEMBER 1; HSP90AB1
;;HEAT-SHOCK 90-KD PROTEIN 1, BETA, FORMERLY; HSPCB, FORMERLY;;
read moreHSPC2;;
HSP90B
*FIELD* TX
DESCRIPTION
HSP90 proteins are highly conserved molecular chaperones that have key
roles in signal transduction, protein folding, protein degradation, and
morphologic evolution. HSP90 proteins normally associate with other
cochaperones and play important roles in folding newly synthesized
proteins or stabilizing and refolding denatured proteins after stress.
There are 2 major cytosolic HSP90 proteins, HSP90AA1 (140571), an
inducible form, and HSP90AB1, a constitutive form. Other HSP90 proteins
are found in endoplasmic reticulum (HSP90B1; 191175) and mitochondria
(TRAP1; 606219) (Chen et al., 2005).
CLONING
By database analysis, Chen et al. (2005) identified several HSP90AB1
variants encoding proteins of 571, 632, 724, and 737 amino acids. Like
other HSP90 proteins, the 724-amino acid HSP90AB1 protein has a highly
conserved N-terminal domain, a charged domain, a middle domain involved
in ATPase activity, a second charged domain, and a C-terminal domain. It
also has a 4-helical cytokine motif, a gln-rich region, and a C-terminal
MEEVD motif characteristic of cytosolic HSP90 proteins. The 737-amino
acid HSP90AB1 isoform is identical to the 724-amino acid isoform except
for a short C-terminal extension.
GENE STRUCTURE
Rebbe et al. (1989) determined the complete genomic sequence of the
HSP90B gene, including 1,102 bp upstream of the transcription initiation
site. The gene consists of 12 exons and 11 introns. The exons range in
size from 99 to 396 bp and the introns from 91 to 1,433 bp. Chen et al.
(2005) also determined that the HSP90AB1 gene contains 12 exons.
MAPPING
By PCR amplification from a panel of hybrid cell lines, Durkin et al.
(1993) mapped the HSPCB gene to chromosome 6 near the TCTE1 gene
(186975) at 6p21. They were able to differentiate the structural gene
from pseudogenes by designing primers from intronic sequences. By
designing primers that bracket an intron, they were able to map 2 HSPCB
pseudogenes, one to chromosome 4 and the other to chromosome 15. Saito
et al. (1992) isolated 68 new RFLP markers on human chromosome 6, of
which 64 were localized on chromosomal bands by fluorescence in situ
hybridization. Takahashi et al. (1994) found that one of these markers,
cloned into a cosmid vector and located at the D6S182 locus, contained
the sequence corresponding to the 5-prime upstream region of the HSP90B
gene. This strongly suggested that the gene is located at 6p12 inasmuch
as the cosmid clone had been mapped to that band by Saito et al. (1992).
By genomic sequence analysis, Chen et al. (2005) mapped the HSP90AB1
gene to chromosome 6p21.1. They identified HSP90AB pseudogenes on
chromosomes 4p15.33 (HSP90AB2P), 4q22.1 (HSP90AB3P), 15q21.3
(HSP90AB4P), 3p12.3 (HSP90AB5P), and 13q32.1 (HSP90AB6P).
NOMENCLATURE
Chen et al. (2005) provided a revised nomenclature system for the HSP90
gene family. Under this system, the root HSP90A indicates cytosolic
HSP90, HSP90B indicates endoplasmic reticulum HSP90, and TRAP indicates
mitochondrial HSP90. HSP90A was divided into 2 classes, with HSP90AA
representing conventional HSP90-alpha, and HSP90AB representing
HSP90-beta. The number following the root/class represents the gene in
that class, and a 'P' at the end indicates a putative pseudogene.
*FIELD* RF
1. Chen, B.; Piel, W. H.; Gui, L.; Bruford, E.; Monteiro, A.: The
HSP90 family of genes in the human genome: insights into their divergence
and evolution. Genomics 86: 627-637, 2005.
2. Durkin, A. S.; Maglott, D. R.; Vamvakopoulos, N. C.; Zoghbi, H.
Y.; Nierman, W. C.: Assignment of an intron-containing human heat-shock
protein gene (hsp90-beta, HSPCB) to chromosome 6 near TCTE1 (6p21)
and two intronless pseudogenes to chromosomes 4 and 15 by polymerase
chain reaction amplification from a panel of hybrid cell lines. Genomics 18:
452-454, 1993.
3. Rebbe, N. F.; Hickman, W. S.; Ley, T. J.; Stafford, D. W.; Hickman,
S.: Nucleotide sequence and regulation of a human 90-kDa heat shock
protein gene. J. Biol. Chem. 264: 15006-15011, 1989.
4. Saito, S.; Okui, K.; Tokino, T.; Oshimura, M.; Nakamura, Y.: Isolation
and mapping of 68 RFLP markers on human chromosome 6. Am. J. Hum.
Genet. 50: 65-70, 1992.
5. Takahashi, I.; Tanuma, R.; Hirata, M.; Hashimoto, K.: A cosmid
clone at the D6S182 locus on human chromosome 6p12 contains the 90-kDa
heat shock protein beta-gene (HSP90-beta). Mammalian Genome 5: 121-122,
1994.
*FIELD* CN
Matthew B. Gross - updated: 08/12/2008
*FIELD* CD
Victor A. McKusick: 12/29/1989
*FIELD* ED
mgross: 08/12/2008
jlewis: 7/28/1999
terry: 7/24/1998
dkim: 7/21/1998
mark: 12/21/1996
carol: 2/25/1994
carol: 11/29/1993
carol: 11/18/1993
supermim: 3/16/1992
carol: 11/8/1991
supermim: 3/20/1990
*RECORD*
*FIELD* NO
140572
*FIELD* TI
*140572 HEAT-SHOCK PROTEIN, 90-KD, ALPHA, CLASS B, MEMBER 1; HSP90AB1
;;HEAT-SHOCK 90-KD PROTEIN 1, BETA, FORMERLY; HSPCB, FORMERLY;;
read moreHSPC2;;
HSP90B
*FIELD* TX
DESCRIPTION
HSP90 proteins are highly conserved molecular chaperones that have key
roles in signal transduction, protein folding, protein degradation, and
morphologic evolution. HSP90 proteins normally associate with other
cochaperones and play important roles in folding newly synthesized
proteins or stabilizing and refolding denatured proteins after stress.
There are 2 major cytosolic HSP90 proteins, HSP90AA1 (140571), an
inducible form, and HSP90AB1, a constitutive form. Other HSP90 proteins
are found in endoplasmic reticulum (HSP90B1; 191175) and mitochondria
(TRAP1; 606219) (Chen et al., 2005).
CLONING
By database analysis, Chen et al. (2005) identified several HSP90AB1
variants encoding proteins of 571, 632, 724, and 737 amino acids. Like
other HSP90 proteins, the 724-amino acid HSP90AB1 protein has a highly
conserved N-terminal domain, a charged domain, a middle domain involved
in ATPase activity, a second charged domain, and a C-terminal domain. It
also has a 4-helical cytokine motif, a gln-rich region, and a C-terminal
MEEVD motif characteristic of cytosolic HSP90 proteins. The 737-amino
acid HSP90AB1 isoform is identical to the 724-amino acid isoform except
for a short C-terminal extension.
GENE STRUCTURE
Rebbe et al. (1989) determined the complete genomic sequence of the
HSP90B gene, including 1,102 bp upstream of the transcription initiation
site. The gene consists of 12 exons and 11 introns. The exons range in
size from 99 to 396 bp and the introns from 91 to 1,433 bp. Chen et al.
(2005) also determined that the HSP90AB1 gene contains 12 exons.
MAPPING
By PCR amplification from a panel of hybrid cell lines, Durkin et al.
(1993) mapped the HSPCB gene to chromosome 6 near the TCTE1 gene
(186975) at 6p21. They were able to differentiate the structural gene
from pseudogenes by designing primers from intronic sequences. By
designing primers that bracket an intron, they were able to map 2 HSPCB
pseudogenes, one to chromosome 4 and the other to chromosome 15. Saito
et al. (1992) isolated 68 new RFLP markers on human chromosome 6, of
which 64 were localized on chromosomal bands by fluorescence in situ
hybridization. Takahashi et al. (1994) found that one of these markers,
cloned into a cosmid vector and located at the D6S182 locus, contained
the sequence corresponding to the 5-prime upstream region of the HSP90B
gene. This strongly suggested that the gene is located at 6p12 inasmuch
as the cosmid clone had been mapped to that band by Saito et al. (1992).
By genomic sequence analysis, Chen et al. (2005) mapped the HSP90AB1
gene to chromosome 6p21.1. They identified HSP90AB pseudogenes on
chromosomes 4p15.33 (HSP90AB2P), 4q22.1 (HSP90AB3P), 15q21.3
(HSP90AB4P), 3p12.3 (HSP90AB5P), and 13q32.1 (HSP90AB6P).
NOMENCLATURE
Chen et al. (2005) provided a revised nomenclature system for the HSP90
gene family. Under this system, the root HSP90A indicates cytosolic
HSP90, HSP90B indicates endoplasmic reticulum HSP90, and TRAP indicates
mitochondrial HSP90. HSP90A was divided into 2 classes, with HSP90AA
representing conventional HSP90-alpha, and HSP90AB representing
HSP90-beta. The number following the root/class represents the gene in
that class, and a 'P' at the end indicates a putative pseudogene.
*FIELD* RF
1. Chen, B.; Piel, W. H.; Gui, L.; Bruford, E.; Monteiro, A.: The
HSP90 family of genes in the human genome: insights into their divergence
and evolution. Genomics 86: 627-637, 2005.
2. Durkin, A. S.; Maglott, D. R.; Vamvakopoulos, N. C.; Zoghbi, H.
Y.; Nierman, W. C.: Assignment of an intron-containing human heat-shock
protein gene (hsp90-beta, HSPCB) to chromosome 6 near TCTE1 (6p21)
and two intronless pseudogenes to chromosomes 4 and 15 by polymerase
chain reaction amplification from a panel of hybrid cell lines. Genomics 18:
452-454, 1993.
3. Rebbe, N. F.; Hickman, W. S.; Ley, T. J.; Stafford, D. W.; Hickman,
S.: Nucleotide sequence and regulation of a human 90-kDa heat shock
protein gene. J. Biol. Chem. 264: 15006-15011, 1989.
4. Saito, S.; Okui, K.; Tokino, T.; Oshimura, M.; Nakamura, Y.: Isolation
and mapping of 68 RFLP markers on human chromosome 6. Am. J. Hum.
Genet. 50: 65-70, 1992.
5. Takahashi, I.; Tanuma, R.; Hirata, M.; Hashimoto, K.: A cosmid
clone at the D6S182 locus on human chromosome 6p12 contains the 90-kDa
heat shock protein beta-gene (HSP90-beta). Mammalian Genome 5: 121-122,
1994.
*FIELD* CN
Matthew B. Gross - updated: 08/12/2008
*FIELD* CD
Victor A. McKusick: 12/29/1989
*FIELD* ED
mgross: 08/12/2008
jlewis: 7/28/1999
terry: 7/24/1998
dkim: 7/21/1998
mark: 12/21/1996
carol: 2/25/1994
carol: 11/29/1993
carol: 11/18/1993
supermim: 3/16/1992
carol: 11/8/1991
supermim: 3/20/1990