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ATP-dependent molecular chaperone HSP82 (82 kDa heat shock protein) (Heat shock protein Hsp90 heat-inducible isoform)

 HSP82_YEAST             Reviewed;         709 AA.
P02829; D6W3D1;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
27-SEP-2017, entry version 202.
RecName: Full=ATP-dependent molecular chaperone HSP82;
AltName: Full=82 kDa heat shock protein;
AltName: Full=Heat shock protein Hsp90 heat-inducible isoform;
Name=HSP82; Synonyms=HSP90; OrderedLocusNames=YPL240C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE.
PubMed=6325446;
Farrelly F.W., Finkelstein D.B.;
"Complete sequence of the heat shock-inducible HSP90 gene of
Saccharomyces cerevisiae.";
J. Biol. Chem. 259:5745-5751(1984).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169875;
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V.,
Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V.,
Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
Zollner A., Vo D.H., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
INDUCTION.
PubMed=2674684; DOI=10.1128/MCB.9.9.3919;
Borkovich K.A., Farrelly F.W., Finkelstein D.B., Taulien J.,
Lindquist S.;
"hsp82 is an essential protein that is required in higher
concentrations for growth of cells at higher temperatures.";
Mol. Cell. Biol. 9:3919-3930(1989).
[5]
ATPASE ACTIVITY.
PubMed=8419347;
Nadeau K., Das A., Walsh C.T.;
"Hsp90 chaperonins possess ATPase activity and bind heat shock
transcription factors and peptidyl prolyl isomerases.";
J. Biol. Chem. 268:1479-1487(1993).
[6]
MUTAGENESIS OF GLY-313; GLU-431; THR-525; ALA-576 AND ARG-579.
PubMed=8248264; DOI=10.1073/pnas.90.23.11424;
Bohen S.P., Yamamoto K.R.;
"Isolation of Hsp90 mutants by screening for decreased steroid
receptor function.";
Proc. Natl. Acad. Sci. U.S.A. 90:11424-11428(1993).
[7]
INTERACTION WITH STI1 AND CPR6.
PubMed=7929182;
Chang H.-C.J., Lindquist S.;
"Conservation of Hsp90 macromolecular complexes in Saccharomyces
cerevisiae.";
J. Biol. Chem. 269:24983-24988(1994).
[8]
MUTAGENESIS OF THR-22; ALA-41; GLY-81; THR-101; GLY-170; GLY-313;
GLU-381 AND ALA-587.
PubMed=7791797; DOI=10.1128/MCB.15.7.3917;
Nathan D.F., Lindquist S.;
"Mutational analysis of Hsp90 function: interactions with a steroid
receptor and a protein kinase.";
Mol. Cell. Biol. 15:3917-3925(1995).
[9]
INTERACTION WITH CPR6 AND CPR7.
PubMed=8939862; DOI=10.1126/science.274.5293.1713;
Duina A.A., Chang H.-C.J., Marsh J.A., Lindquist S., Gaber R.F.;
"A cyclophilin function in Hsp90-dependent signal transduction.";
Science 274:1713-1715(1996).
[10]
INDUCTION.
PubMed=9296388;
Zarzov P., Boucherie H., Mann C.;
"A yeast heat shock transcription factor (Hsf1) mutant is defective in
both Hsc82/Hsp82 synthesis and spindle pole body duplication.";
J. Cell Sci. 110:1879-1891(1997).
[11]
INTERACTION WITH SBA1.
PubMed=9817749; DOI=10.1083/jcb.143.4.901;
Obermann W.M., Sondermann H., Russo A.A., Pavletich N.P., Hartl F.U.;
"In vivo function of Hsp90 is dependent on ATP binding and ATP
hydrolysis.";
J. Cell Biol. 143:901-910(1998).
[12]
INTERACTION WITH SBA1, AND MUTAGENESIS OF ALA-97 AND SER-485.
PubMed=9632755; DOI=10.1128/MCB.18.7.3727;
Fang Y., Fliss A.E., Rao J., Caplan A.J.;
"SBA1 encodes a yeast hsp90 cochaperone that is homologous to
vertebrate p23 proteins.";
Mol. Cell. Biol. 18:3727-3734(1998).
[13]
INTERACTION WITH HAP1.
PubMed=9632766; DOI=10.1128/MCB.18.7.3819;
Zhang L., Hach A., Wang C.;
"Molecular mechanism governing heme signaling in yeast: a higher-order
complex mediates heme regulation of the transcriptional activator
HAP1.";
Mol. Cell. Biol. 18:3819-3828(1998).
[14]
INTERACTION WITH CNS1.
PubMed=9819421; DOI=10.1128/MCB.18.12.7344;
Dolinski K.J., Cardenas M.E., Heitman J.;
"CNS1 encodes an essential p60/Sti1 homolog in Saccharomyces
cerevisiae that suppresses cyclophilin 40 mutations and interacts with
Hsp90.";
Mol. Cell. Biol. 18:7344-7352(1998).
[15]
INTERACTION WITH SSE1.
PubMed=10480867; DOI=10.1074/jbc.274.38.26654;
Liu X.-D., Morano K.A., Thiele D.J.;
"The yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone.";
J. Biol. Chem. 274:26654-26660(1999).
[16]
INTERACTION WITH GCN2.
PubMed=10567567; DOI=10.1128/MCB.19.12.8422;
Donze O., Picard D.;
"Hsp90 binds and regulates Gcn2, the ligand-inducible kinase of the
alpha subunit of eukaryotic translation initiation factor 2.";
Mol. Cell. Biol. 19:8422-8432(1999).
[17]
BINDING TO TPR REPEATS.
PubMed=10786835; DOI=10.1016/S0092-8674(00)80830-2;
Scheufler C., Brinker A., Bourenkov G., Pegoraro S., Moroder L.,
Bartunik H., Hartl F.U., Moarefi I.;
"Structure of TPR domain-peptide complexes: critical elements in the
assembly of the Hsp70-Hsp90 multichaperone machine.";
Cell 101:199-210(2000).
[18]
ATPASE ACTIVITY, AND MUTAGENESIS OF ALA-107.
PubMed=10944121; DOI=10.1093/emboj/19.16.4383;
Prodromou C., Panaretou B., Chohan S., Siligardi G., O'Brien R.,
Ladbury J.E., Roe S.M., Piper P.W., Pearl L.H.;
"The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient
dimerization of the N-terminal domains.";
EMBO J. 19:4383-4392(2000).
[19]
INTERACTION WITH CDC37 AND STE11.
PubMed=10664467; DOI=10.1016/S0014-5793(00)01134-0;
Abbas-Terki T., Donze O., Picard D.;
"The molecular chaperone Cdc37 is required for Ste11 function and
pheromone-induced cell cycle arrest.";
FEBS Lett. 467:111-116(2000).
[20]
INTERACTION WITH AHA1 AND HCH1.
PubMed=12504007; DOI=10.1016/S1097-2765(02)00785-2;
Panaretou B., Siligardi G., Meyer P., Maloney A., Sullivan J.K.,
Singh S., Millson S.H., Clarke P.A., Naaby-Hansen S., Stein R.,
Cramer R., Mollapour M., Workman P., Piper P.W., Pearl L.H.,
Prodromou C.;
"Activation of the ATPase activity of hsp90 by the stress-regulated
cochaperone aha1.";
Mol. Cell 10:1307-1318(2002).
[21]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[22]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[23]
MUTAGENESIS OF GLY-83.
PubMed=18256191; DOI=10.1242/dev.018150;
Hawkins T.A., Haramis A.P., Etard C., Prodromou C., Vaughan C.K.,
Ashworth R., Ray S., Behra M., Holder N., Talbot W.S., Pearl L.H.,
Strahle U., Wilson S.W.;
"The ATPase-dependent chaperoning activity of Hsp90a regulates thick
filament formation and integration during skeletal muscle
myofibrillogenesis.";
Development 135:1147-1156(2008).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[25]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
PubMed=9187656; DOI=10.1038/nsb0697-477;
Prodromou C., Roe S.M., Piper P.W., Pearl L.H.;
"A molecular clamp in the crystal structure of the N-terminal domain
of the yeast Hsp90 chaperone.";
Nat. Struct. Biol. 4:477-482(1997).
[26]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2-214 IN COMPLEX WITH ADP
AND GELDANAMYCIN.
PubMed=9230303; DOI=10.1016/S0092-8674(00)80314-1;
Prodromou C., Roe S.M., O'Brien R., Ladbury J.E., Piper P.W.,
Pearl L.H.;
"Identification and structural characterization of the ATP/ADP-binding
site in the Hsp90 molecular chaperone.";
Cell 90:65-75(1997).
[27]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 273-560, AND MUTAGENESIS OF
PHE-349; ARG-380 AND GLN-384.
PubMed=12667448; DOI=10.1016/S1097-2765(03)00065-0;
Meyer P., Prodromou C., Hu B., Vaughan C.K., Roe S.M., Panaretou B.,
Piper P.W., Pearl L.H.;
"Structural and functional analysis of the middle segment of hsp90:
implications for ATP hydrolysis and client protein and cochaperone
interactions.";
Mol. Cell 11:647-658(2003).
[28]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-214 IN COMPLEX WITH HUMAN
CDC37.
PubMed=14718169; DOI=10.1016/S0092-8674(03)01027-4;
Roe S.M., Ali M.M., Meyer P., Vaughan C.K., Panaretou B., Piper P.W.,
Prodromou C., Pearl L.H.;
"The Mechanism of Hsp90 regulation by the protein kinase-specific
cochaperone p50(cdc37).";
Cell 116:87-98(2004).
[29]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 272-530 IN COMPLEX WITH
AHA1, AND MUTAGENESIS OF LYS-387.
PubMed=14739935; DOI=10.1038/sj.emboj.7600060;
Meyer P.;
"Structural basis for recruitment of the ATPase activator Aha1 to the
Hsp90 chaperone machinery.";
EMBO J. 23:511-519(2004).
[30]
ERRATUM.
PubMed=15039704; DOI=10.1038/sj.emboj.7600141;
Meyer P., Prodromou C., Liao C., Hu B., Mark Roe S., Vaughan C.K.,
Vlasic I., Panaretou B., Piper P.W., Pearl L.H.;
EMBO J. 23:1402-1410(2004).
[31]
MUTAGENESIS OF ALA-577.
PubMed=19696785; DOI=10.1038/embor.2009.153;
Retzlaff M., Stahl M., Eberl H.C., Lagleder S., Beck J., Kessler H.,
Buchner J.;
"Hsp90 is regulated by a switch point in the C-terminal domain.";
EMBO Rep. 10:1147-1153(2009).
[32]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-214 IN COMPLEX WITH
RADICICOL, AND ATPASE ACTIVITY.
PubMed=9925731; DOI=10.1021/jm980403y;
Roe S.M., Prodromou C., O'Brien R., Ladbury J.E., Piper P.W.,
Pearl L.H.;
"Structural basis for inhibition of the Hsp90 molecular chaperone by
the antitumor antibiotics radicicol and geldanamycin.";
J. Med. Chem. 42:260-266(1999).
[33]
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1-214 IN COMPLEX WITH
INHIBITORS, AND FUNCTION.
PubMed=17114002; DOI=10.1016/j.chembiol.2006.09.015;
Proisy N., Sharp S.Y., Boxall K., Connelly S., Roe S.M., Prodromou C.,
Slawin A.M., Pearl L.H., Workman P., Moody C.J.;
"Inhibition of Hsp90 with synthetic macrolactones: synthesis and
structural and biological evaluation of ring and conformational
analogs of radicicol.";
Chem. Biol. 13:1203-1215(2006).
[34]
X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 25-210, AND ATPASE ACTIVITY.
PubMed=16461354; DOI=10.1074/jbc.M510142200;
Richter K., Moser S., Hagn F., Friedrich R., Hainzl O., Heller M.,
Schlee S., Kessler H., Reinstein J., Buchner J.;
"Intrinsic inhibition of the Hsp90 ATPase activity.";
J. Biol. Chem. 281:11301-11311(2006).
[35]
X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 1-677 IN COMPLEX WITH SBA1
AND ATP, AND SUBUNIT.
PubMed=16625188; DOI=10.1038/nature04716;
Ali M.M., Roe S.M., Vaughan C.K., Meyer P., Panaretou B., Piper P.W.,
Prodromou C., Pearl L.H.;
"Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone
complex.";
Nature 440:1013-1017(2006).
[36]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-219 IN COMPLEX WITH
INHIBITOR, AND ATPASE ACTIVITY.
PubMed=18357975; DOI=10.1021/jm701558c;
Martin C.J., Gaisser S., Challis I.R., Carletti I., Wilkinson B.,
Gregory M., Prodromou C., Roe S.M., Pearl L.H., Boyd S.M., Zhang M.Q.;
"Molecular characterization of macbecin as an Hsp90 inhibitor.";
J. Med. Chem. 51:2853-2857(2008).
[37]
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-220 IN COMPLEX WITH ADP;
GELDANAMYCIN AND RADICICOL.
PubMed=19236053; DOI=10.1021/cb9000316;
Prodromou C., Nuttall J.M., Millson S.H., Roe S.M., Sim T.S., Tan D.,
Workman P., Pearl L.H., Piper P.W.;
"Structural basis of the radicicol resistance displayed by a fungal
hsp90.";
ACS Chem. Biol. 4:289-297(2009).
-!- FUNCTION: Molecular chaperone that promotes the maturation,
structural maintenance and proper regulation of specific target
proteins involved in cell cycle control and signal transduction.
Undergoes a functional cycle that is linked to its ATPase
activity. The nucleotide-free form of the dimer is found in an
open conformation in which the N-termini are not dimerized and the
complex is ready for client protein binding. Binding of ATP
induces large conformational changes, resulting in the formation
of a ring-like closed structure in which the N-terminal domains
associate intramolecularly with the middle domain and also
dimerize with each other, stimulating their intrinsic ATPase
activity and acting as a clamp on the substrate. Finally, ATP
hydrolysis results in the release of the substrate. This cycle
probably induces conformational changes in the client proteins,
thereby causing their activation. Interacts dynamically with
various co-chaperones that modulate its substrate recognition,
ATPase cycle and chaperone function. Required for growth at high
temperatures. {ECO:0000269|PubMed:17114002}.
-!- ENZYME REGULATION: Inhibited by geldanamycin, macbecin I and
radicicol, which bind to the ATP-binding pocket. Co-chaperones
CDC37, SBA1 and STI1 reduce ATPase activity. Co-chaperones AHA1
and HCH1 increase ATPase activity.
-!- SUBUNIT: Homodimer. Interacts with the co-chaperones AHA1, CDC37,
CNS1, CPR6, CPR7, HCH1, SBA1, SSE1 and STI1. CNS1, CPR6, CPR7 and
STI1. Interacts directly with the substrates GCN2, HAP1 and STE11.
{ECO:0000269|PubMed:10480867, ECO:0000269|PubMed:10567567,
ECO:0000269|PubMed:10664467, ECO:0000269|PubMed:12504007,
ECO:0000269|PubMed:14718169, ECO:0000269|PubMed:14739935,
ECO:0000269|PubMed:16625188, ECO:0000269|PubMed:17114002,
ECO:0000269|PubMed:18357975, ECO:0000269|PubMed:19236053,
ECO:0000269|PubMed:7929182, ECO:0000269|PubMed:8939862,
ECO:0000269|PubMed:9230303, ECO:0000269|PubMed:9632755,
ECO:0000269|PubMed:9632766, ECO:0000269|PubMed:9817749,
ECO:0000269|PubMed:9819421, ECO:0000269|PubMed:9925731}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-8659, EBI-8659;
P60010:ACT1; NbExp=2; IntAct=EBI-8659, EBI-2169;
P27616:ADE1; NbExp=2; IntAct=EBI-8659, EBI-14257;
Q12449:AHA1; NbExp=8; IntAct=EBI-8659, EBI-37072;
P46672:ARC1; NbExp=2; IntAct=EBI-8659, EBI-7224;
P00830:ATP2; NbExp=2; IntAct=EBI-8659, EBI-3242;
P53858:BNI4; NbExp=2; IntAct=EBI-8659, EBI-3704;
P33322:CBF5; NbExp=4; IntAct=EBI-8659, EBI-4105;
P06101:CDC37; NbExp=6; IntAct=EBI-8659, EBI-4266;
Q12102:CFT2; NbExp=2; IntAct=EBI-8659, EBI-31412;
P33313:CNS1; NbExp=6; IntAct=EBI-8659, EBI-4806;
P53691:CPR6; NbExp=16; IntAct=EBI-8659, EBI-5429;
P47103:CPR7; NbExp=3; IntAct=EBI-8659, EBI-5436;
Q01454:CTF4; NbExp=2; IntAct=EBI-8659, EBI-5209;
P38241:ECM2; NbExp=4; IntAct=EBI-8659, EBI-780;
P53743:ESF2; NbExp=2; IntAct=EBI-8659, EBI-28537;
P38866:FMO1; NbExp=3; IntAct=EBI-8659, EBI-24830;
Q07825:FRA1; NbExp=2; IntAct=EBI-8659, EBI-32387;
P15442:GCN2; NbExp=3; IntAct=EBI-8659, EBI-330;
P0CS82:HAP1 (xeno); NbExp=4; IntAct=EBI-8659, EBI-5419;
P53834:HCH1; NbExp=2; IntAct=EBI-8659, EBI-28288;
Q12276:HER1; NbExp=2; IntAct=EBI-8659, EBI-35056;
Q08109:HRD1; NbExp=3; IntAct=EBI-8659, EBI-37613;
P15108:HSC82; NbExp=44; IntAct=EBI-8659, EBI-8666;
P43581:HXT10; NbExp=2; IntAct=EBI-8659, EBI-8750;
P38828:LSM12; NbExp=3; IntAct=EBI-8659, EBI-24700;
P39534:MBB1; NbExp=2; IntAct=EBI-8659, EBI-26211;
P27705:MIG1; NbExp=3; IntAct=EBI-8659, EBI-10913;
P33759:MRPS5; NbExp=12; IntAct=EBI-8659, EBI-413;
P35198:MTH1; NbExp=3; IntAct=EBI-8659, EBI-11561;
P32832:NPL6; NbExp=2; IntAct=EBI-8659, EBI-12202;
P38264:PHO88; NbExp=2; IntAct=EBI-8659, EBI-13350;
P38768:PIH1; NbExp=3; IntAct=EBI-8659, EBI-24499;
Q03407:PKH1; NbExp=2; IntAct=EBI-8659, EBI-32467;
P53043:PPT1; NbExp=13; IntAct=EBI-8659, EBI-13796;
P32264:PRO1; NbExp=3; IntAct=EBI-8659, EBI-13879;
P25635:PWP2; NbExp=2; IntAct=EBI-8659, EBI-14332;
P38764:RPN1; NbExp=2; IntAct=EBI-8659, EBI-15913;
P28707:SBA1; NbExp=4; IntAct=EBI-8659, EBI-26838;
Q08446:SGT1; NbExp=2; IntAct=EBI-8659, EBI-17070;
P17883:SKI3; NbExp=2; IntAct=EBI-8659, EBI-1861;
Q00772:SLT2; NbExp=4; IntAct=EBI-8659, EBI-17372;
P10591:SSA1; NbExp=5; IntAct=EBI-8659, EBI-8591;
P10592:SSA2; NbExp=3; IntAct=EBI-8659, EBI-8603;
P11484:SSB1; NbExp=3; IntAct=EBI-8659, EBI-8627;
P32589:SSE1; NbExp=5; IntAct=EBI-8659, EBI-8648;
P53599:SSK2; NbExp=2; IntAct=EBI-8659, EBI-18191;
P38788:SSZ1; NbExp=3; IntAct=EBI-8659, EBI-24570;
P15705:STI1; NbExp=34; IntAct=EBI-8659, EBI-18418;
P38129:TAF5; NbExp=3; IntAct=EBI-8659, EBI-18868;
P25638:TAH1; NbExp=4; IntAct=EBI-8659, EBI-21956;
P00359:TDH3; NbExp=2; IntAct=EBI-8659, EBI-7218;
P53874:UBP10; NbExp=2; IntAct=EBI-8659, EBI-19873;
P25491:YDJ1; NbExp=3; IntAct=EBI-8659, EBI-10420;
Q12407:YDL199C; NbExp=3; IntAct=EBI-8659, EBI-33162;
P38887:YHR202W; NbExp=2; IntAct=EBI-8659, EBI-24252;
P38746:YLF2; NbExp=2; IntAct=EBI-8659, EBI-27201;
Q06224:YSH1; NbExp=2; IntAct=EBI-8659, EBI-38345;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
-!- INDUCTION: Expressed constitutively and induced by high
temperatures dependent on transcription factor HSF1. According to
PubMed:2674684, it is constitutively expressed at low levels,
however, due to the specificity of the antibody, this result is
unsure. {ECO:0000269|PubMed:2674684, ECO:0000269|PubMed:9296388}.
-!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
repeat-containing proteins like the co-chaperones AHA1, CDC37,
CNS1, CPR6, CPR7, HCH1, SBA1, SSE1 and STI1. CNS1, CPR6, CPR7 and
STI1.
-!- MISCELLANEOUS: Present with 444943 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the heat shock protein 90 family.
{ECO:0000305}.
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EMBL; K01387; AAA02743.1; -; Unassigned_RNA.
EMBL; Z67751; CAA91604.1; -; Genomic_DNA.
EMBL; Z73596; CAA97961.1; -; Genomic_DNA.
EMBL; BK006949; DAA11197.1; -; Genomic_DNA.
PIR; A03313; HHBY90.
RefSeq; NP_015084.1; NM_001184054.1.
PDB; 1A4H; X-ray; 2.50 A; A=1-220.
PDB; 1AH6; X-ray; 1.80 A; A=1-220.
PDB; 1AH8; X-ray; 2.10 A; A/B=1-220.
PDB; 1AM1; X-ray; 2.00 A; A=2-214.
PDB; 1AMW; X-ray; 1.85 A; A=1-214.
PDB; 1BGQ; X-ray; 2.50 A; A=1-214.
PDB; 1HK7; X-ray; 2.50 A; A/B=273-560.
PDB; 1US7; X-ray; 2.30 A; A=1-214.
PDB; 1USU; X-ray; 2.15 A; A=273-530.
PDB; 1USV; X-ray; 2.70 A; A/C/E/G=272-530.
PDB; 1ZW9; X-ray; 1.90 A; A=1-220.
PDB; 1ZWH; X-ray; 1.65 A; A=1-220.
PDB; 2AKP; X-ray; 1.94 A; A/B=25-210.
PDB; 2BRC; X-ray; 1.60 A; A=1-214.
PDB; 2BRE; X-ray; 2.00 A; A/B=1-219.
PDB; 2CG9; X-ray; 3.10 A; A/B=1-677.
PDB; 2CGE; X-ray; 3.00 A; A/B/D=273-677.
PDB; 2CGF; X-ray; 2.20 A; A=1-214.
PDB; 2FXS; X-ray; 2.00 A; A=1-220.
PDB; 2IWS; X-ray; 2.70 A; A=1-214.
PDB; 2IWU; X-ray; 2.80 A; A=1-214.
PDB; 2IWX; X-ray; 1.50 A; A=1-214.
PDB; 2LSV; NMR; -; B=701-709.
PDB; 2VW5; X-ray; 1.90 A; A/B/C/D=1-214.
PDB; 2VWC; X-ray; 2.40 A; A=1-219.
PDB; 2WEP; X-ray; 2.00 A; A=1-220.
PDB; 2WEQ; X-ray; 2.20 A; A=1-220.
PDB; 2WER; X-ray; 1.60 A; A/B=1-220.
PDB; 2XD6; X-ray; 2.20 A; A=1-214.
PDB; 2XX2; X-ray; 1.85 A; A/B/C/D=1-214.
PDB; 2XX4; X-ray; 2.20 A; A=1-214.
PDB; 2XX5; X-ray; 2.00 A; A=1-214.
PDB; 2YGA; X-ray; 2.37 A; A=1-220.
PDB; 2YGE; X-ray; 1.96 A; A=1-220.
PDB; 2YGF; X-ray; 2.00 A; A=1-220.
PDB; 3C0E; X-ray; 1.90 A; A=1-220.
PDB; 3C11; X-ray; 1.60 A; A=1-220.
PDB; 3FP2; X-ray; 1.98 A; Q=698-709.
PDB; 4AS9; X-ray; 2.71 A; A=1-220.
PDB; 4ASA; X-ray; 2.25 A; A=1-220.
PDB; 4ASB; X-ray; 3.08 A; A=1-220.
PDB; 4ASF; X-ray; 2.60 A; A=1-220.
PDB; 4ASG; X-ray; 2.20 A; A=1-220.
PDB; 4CE1; X-ray; 2.01 A; A=1-214.
PDB; 4CE2; X-ray; 2.38 A; A=1-214.
PDB; 4CE3; X-ray; 2.31 A; A=1-214.
PDB; 5MGX; X-ray; 2.18 A; A/B/C/D=702-709.
PDBsum; 1A4H; -.
PDBsum; 1AH6; -.
PDBsum; 1AH8; -.
PDBsum; 1AM1; -.
PDBsum; 1AMW; -.
PDBsum; 1BGQ; -.
PDBsum; 1HK7; -.
PDBsum; 1US7; -.
PDBsum; 1USU; -.
PDBsum; 1USV; -.
PDBsum; 1ZW9; -.
PDBsum; 1ZWH; -.
PDBsum; 2AKP; -.
PDBsum; 2BRC; -.
PDBsum; 2BRE; -.
PDBsum; 2CG9; -.
PDBsum; 2CGE; -.
PDBsum; 2CGF; -.
PDBsum; 2FXS; -.
PDBsum; 2IWS; -.
PDBsum; 2IWU; -.
PDBsum; 2IWX; -.
PDBsum; 2LSV; -.
PDBsum; 2VW5; -.
PDBsum; 2VWC; -.
PDBsum; 2WEP; -.
PDBsum; 2WEQ; -.
PDBsum; 2WER; -.
PDBsum; 2XD6; -.
PDBsum; 2XX2; -.
PDBsum; 2XX4; -.
PDBsum; 2XX5; -.
PDBsum; 2YGA; -.
PDBsum; 2YGE; -.
PDBsum; 2YGF; -.
PDBsum; 3C0E; -.
PDBsum; 3C11; -.
PDBsum; 3FP2; -.
PDBsum; 4AS9; -.
PDBsum; 4ASA; -.
PDBsum; 4ASB; -.
PDBsum; 4ASF; -.
PDBsum; 4ASG; -.
PDBsum; 4CE1; -.
PDBsum; 4CE2; -.
PDBsum; 4CE3; -.
PDBsum; 5MGX; -.
ProteinModelPortal; P02829; -.
SMR; P02829; -.
BioGrid; 35923; 1598.
DIP; DIP-2262N; -.
IntAct; P02829; 1150.
MINT; MINT-560200; -.
STRING; 4932.YPL240C; -.
BindingDB; P02829; -.
ChEMBL; CHEMBL3536; -.
iPTMnet; P02829; -.
SWISS-2DPAGE; P02829; -.
MaxQB; P02829; -.
PRIDE; P02829; -.
EnsemblFungi; YPL240C; YPL240C; YPL240C.
GeneID; 855836; -.
KEGG; sce:YPL240C; -.
EuPathDB; FungiDB:YPL240C; -.
SGD; S000006161; HSP82.
GeneTree; ENSGT00840000129758; -.
HOGENOM; HOG000031988; -.
InParanoid; P02829; -.
KO; K04079; -.
OMA; LRYHSSQ; -.
OrthoDB; EOG092C1GW3; -.
BioCyc; YEAST:G3O-34126-MONOMER; -.
Reactome; R-SCE-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
Reactome; R-SCE-203615; eNOS activation.
Reactome; R-SCE-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-SCE-3371511; HSF1 activation.
Reactome; R-SCE-3371568; Attenuation phase.
Reactome; R-SCE-3371571; HSF1-dependent transactivation.
Reactome; R-SCE-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-SCE-6798695; Neutrophil degranulation.
Reactome; R-SCE-844456; The NLRP3 inflammasome.
EvolutionaryTrace; P02829; -.
PRO; PR:P02829; -.
Proteomes; UP000002311; Chromosome XVI.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042623; F:ATPase activity, coupled; IDA:SGD.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
GO; GO:0006458; P:'de novo' protein folding; IDA:SGD.
GO; GO:0000492; P:box C/D snoRNP assembly; IMP:SGD.
GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IDA:SGD.
GO; GO:0043248; P:proteasome assembly; IDA:SGD.
GO; GO:0051604; P:protein maturation; IMP:SGD.
GO; GO:0042026; P:protein refolding; IMP:SGD.
GO; GO:0006626; P:protein targeting to mitochondrion; IPI:SGD.
GO; GO:0032204; P:regulation of telomere maintenance; IMP:CACAO.
GO; GO:0006970; P:response to osmotic stress; IMP:SGD.
Gene3D; 3.30.565.10; -; 1.
HAMAP; MF_00505; HSP90; 1.
InterPro; IPR003594; HATPase_C.
InterPro; IPR019805; Heat_shock_protein_90_CS.
InterPro; IPR001404; Hsp90_fam.
InterPro; IPR020575; Hsp90_N.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
PANTHER; PTHR11528; PTHR11528; 1.
Pfam; PF02518; HATPase_c; 1.
Pfam; PF00183; HSP90; 1.
PIRSF; PIRSF002583; Hsp90; 1.
PRINTS; PR00775; HEATSHOCK90.
SMART; SM00387; HATPase_c; 1.
SUPFAM; SSF54211; SSF54211; 1.
SUPFAM; SSF55874; SSF55874; 1.
PROSITE; PS00298; HSP90; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Chaperone; Complete proteome; Cytoplasm;
Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
Stress response.
CHAIN 1 709 ATP-dependent molecular chaperone HSP82.
/FTId=PRO_0000062957.
REPEAT 221 225 1. {ECO:0000269|PubMed:10786835}.
REPEAT 226 230 2. {ECO:0000269|PubMed:10786835}.
REPEAT 231 235 3. {ECO:0000269|PubMed:10786835}.
REPEAT 237 241 4. {ECO:0000269|PubMed:10786835}.
REPEAT 250 254 5. {ECO:0000269|PubMed:10786835}.
NP_BIND 99 100 ATP. {ECO:0000244|PDB:2CG9,
ECO:0000269|PubMed:16625188}.
NP_BIND 119 124 ATP. {ECO:0000244|PDB:2CG9,
ECO:0000269|PubMed:16625188}.
REGION 221 263 5 X 5 AA repeats of [DE]-[DE]-[DE]-K-K;
highly charged region.
MOTIF 705 709 TPR repeat-binding.
BINDING 33 33 ATP. {ECO:0000244|PDB:2CG9,
ECO:0000269|PubMed:16625188}.
BINDING 37 37 ATP. {ECO:0000244|PDB:2CG9,
ECO:0000269|PubMed:16625188}.
BINDING 79 79 ATP. {ECO:0000244|PDB:2CG9,
ECO:0000269|PubMed:16625188}.
BINDING 84 84 ATP. {ECO:0000244|PDB:2CG9,
ECO:0000269|PubMed:16625188}.
BINDING 92 92 ATP. {ECO:0000244|PDB:2CG9,
ECO:0000269|PubMed:16625188}.
BINDING 98 98 ATP. {ECO:0000244|PDB:2CG9,
ECO:0000269|PubMed:16625188}.
BINDING 171 171 ATP. {ECO:0000244|PDB:2CG9,
ECO:0000269|PubMed:16625188}.
BINDING 380 380 ATP. {ECO:0000244|PDB:2CG9,
ECO:0000269|PubMed:16625188}.
MOD_RES 657 657 Phosphoserine.
{ECO:0000250|UniProtKB:P15108}.
MUTAGEN 22 22 T->I: Induces a 6-fold increase in ATPase
activity and a reduced client protein
activation activity, leading to growth
defect at high temperatures.
{ECO:0000269|PubMed:7791797}.
MUTAGEN 41 41 A->V: Causes a 98% reduction in ATPase
activity and a reduced client protein
activation activity, leading to growth
defect at high temperatures.
{ECO:0000269|PubMed:7791797}.
MUTAGEN 81 81 G->S: Reduces client protein activation
activity, leading to growth defect at
high temperatures.
{ECO:0000269|PubMed:7791797}.
MUTAGEN 83 83 G->D: Abolishes ATPase activity.
{ECO:0000269|PubMed:18256191}.
MUTAGEN 97 97 A->I: Abolishes interaction with SBA1.
{ECO:0000269|PubMed:9632755}.
MUTAGEN 101 101 T->I: Causes a 90% reduction in ATPase
activity and a reduced client protein
activation activity, leading to growth
defect at high temperatures.
{ECO:0000269|PubMed:7791797}.
MUTAGEN 107 107 A->N: Induces a 6-fold increase in ATPase
activity. {ECO:0000269|PubMed:10944121}.
MUTAGEN 170 170 G->D: Induces a total loss of function at
34 degrees Celsius. Abolishes interaction
with SBA1. {ECO:0000269|PubMed:7791797}.
MUTAGEN 313 313 G->N,S: Reduces client protein activation
activity, leading to growth defect at
high temperatures.
{ECO:0000269|PubMed:7791797,
ECO:0000269|PubMed:8248264}.
MUTAGEN 349 349 F->A,Q: Induces a loss of ATPase
activity. Can be reactivated by AHA1.
{ECO:0000269|PubMed:12667448}.
MUTAGEN 380 380 R->A: Induces a loss of ATPase activity.
{ECO:0000269|PubMed:12667448}.
MUTAGEN 381 381 E->K: Reduces client protein activation
activity. Resistant to ATPase activation
by AHA1. {ECO:0000269|PubMed:7791797}.
MUTAGEN 384 384 Q->A: Induces a loss of ATPase activity.
{ECO:0000269|PubMed:12667448}.
MUTAGEN 387 387 K->A: Decreases AHA1 binding affinity,
but has no effect on client protein
activation activity.
{ECO:0000269|PubMed:14739935}.
MUTAGEN 387 387 K->D: Decreases AHA1 binding affinity and
substantially reduces client protein
activation activity.
{ECO:0000269|PubMed:14739935}.
MUTAGEN 431 431 E->K: Specifically reduces the activation
of the exogenous ligand glucocorticoid
receptor. {ECO:0000269|PubMed:8248264}.
MUTAGEN 485 485 S->Y: Abolishes interaction with SBA1.
{ECO:0000269|PubMed:9632755}.
MUTAGEN 525 525 T->I: Abolishes interaction with SBA1.
Reduces client protein activation
activity, leading to growth defect at
high temperatures.
{ECO:0000269|PubMed:8248264}.
MUTAGEN 576 576 A->T: Reduces client protein activation
activity; when associated with K-579.
{ECO:0000269|PubMed:8248264}.
MUTAGEN 577 577 A->C: Enhances ATPase activity and client
protein activation.
{ECO:0000269|PubMed:19696785}.
MUTAGEN 577 577 A->D: Reduces ATPase activity and client
protein activation.
{ECO:0000269|PubMed:19696785}.
MUTAGEN 577 577 A->I: Enhances homodimerization, ATPase
activity and client protein activation.
{ECO:0000269|PubMed:19696785}.
MUTAGEN 577 577 A->N: Reduces homodimerization, ATPase
activity and client protein activation.
{ECO:0000269|PubMed:19696785}.
MUTAGEN 579 579 R->K: Reduces client protein activation
activity; when associated with T-576.
{ECO:0000269|PubMed:8248264}.
MUTAGEN 587 587 A->T: No effect on ATPase activity.
Reduces client protein activation
activity, leading to growth defect at
high temperatures.
{ECO:0000269|PubMed:7791797}.
CONFLICT 481 481 A -> S (in Ref. 27). {ECO:0000305}.
STRAND 4 7 {ECO:0000244|PDB:2IWX}.
HELIX 10 21 {ECO:0000244|PDB:2IWX}.
HELIX 26 28 {ECO:0000244|PDB:4ASB}.
HELIX 29 48 {ECO:0000244|PDB:2IWX}.
TURN 49 51 {ECO:0000244|PDB:2IWX}.
HELIX 53 56 {ECO:0000244|PDB:2IWX}.
STRAND 64 69 {ECO:0000244|PDB:2IWX}.
HELIX 70 72 {ECO:0000244|PDB:2IWX}.
STRAND 74 79 {ECO:0000244|PDB:2IWX}.
HELIX 86 93 {ECO:0000244|PDB:2IWX}.
TURN 95 97 {ECO:0000244|PDB:2BRC}.
HELIX 101 110 {ECO:0000244|PDB:2IWX}.
HELIX 114 120 {ECO:0000244|PDB:2IWX}.
HELIX 123 129 {ECO:0000244|PDB:2IWX}.
STRAND 131 139 {ECO:0000244|PDB:2IWX}.
STRAND 146 150 {ECO:0000244|PDB:2IWX}.
STRAND 152 160 {ECO:0000244|PDB:2IWX}.
STRAND 162 164 {ECO:0000244|PDB:2IWX}.
STRAND 168 177 {ECO:0000244|PDB:2IWX}.
HELIX 182 185 {ECO:0000244|PDB:2IWX}.
HELIX 187 197 {ECO:0000244|PDB:2IWX}.
STRAND 200 203 {ECO:0000244|PDB:2AKP}.
STRAND 205 207 {ECO:0000244|PDB:2IWX}.
HELIX 276 278 {ECO:0000244|PDB:1USU}.
HELIX 281 283 {ECO:0000244|PDB:1USU}.
HELIX 286 297 {ECO:0000244|PDB:1USU}.
STRAND 304 311 {ECO:0000244|PDB:1USU}.
STRAND 313 315 {ECO:0000244|PDB:1USU}.
STRAND 317 323 {ECO:0000244|PDB:1USU}.
TURN 329 332 {ECO:0000244|PDB:1USU}.
STRAND 335 337 {ECO:0000244|PDB:2CG9}.
STRAND 341 345 {ECO:0000244|PDB:1USU}.
STRAND 348 352 {ECO:0000244|PDB:1USU}.
STRAND 355 358 {ECO:0000244|PDB:1HK7}.
HELIX 360 362 {ECO:0000244|PDB:1USU}.
STRAND 366 373 {ECO:0000244|PDB:1USU}.
HELIX 380 383 {ECO:0000244|PDB:1HK7}.
HELIX 387 408 {ECO:0000244|PDB:1USU}.
HELIX 411 431 {ECO:0000244|PDB:1USU}.
TURN 433 435 {ECO:0000244|PDB:1USU}.
HELIX 436 440 {ECO:0000244|PDB:1USU}.
STRAND 444 447 {ECO:0000244|PDB:1USU}.
STRAND 450 456 {ECO:0000244|PDB:1USU}.
HELIX 457 462 {ECO:0000244|PDB:1USU}.
STRAND 470 475 {ECO:0000244|PDB:1USU}.
HELIX 479 483 {ECO:0000244|PDB:1USU}.
HELIX 488 493 {ECO:0000244|PDB:1USU}.
STRAND 498 501 {ECO:0000244|PDB:1USU}.
HELIX 504 513 {ECO:0000244|PDB:1USU}.
STRAND 519 523 {ECO:0000244|PDB:1USU}.
TURN 524 526 {ECO:0000244|PDB:1HK7}.
STRAND 530 533 {ECO:0000244|PDB:2CGE}.
HELIX 535 558 {ECO:0000244|PDB:2CGE}.
STRAND 563 567 {ECO:0000244|PDB:2CGE}.
STRAND 573 580 {ECO:0000244|PDB:2CGE}.
STRAND 582 584 {ECO:0000244|PDB:2CGE}.
HELIX 587 597 {ECO:0000244|PDB:2CGE}.
STRAND 600 602 {ECO:0000244|PDB:2CGE}.
STRAND 611 615 {ECO:0000244|PDB:2CGE}.
HELIX 620 629 {ECO:0000244|PDB:2CGE}.
TURN 630 632 {ECO:0000244|PDB:2CGE}.
HELIX 633 635 {ECO:0000244|PDB:2CGE}.
HELIX 637 653 {ECO:0000244|PDB:2CGE}.
HELIX 661 676 {ECO:0000244|PDB:2CGE}.
SEQUENCE 709 AA; 81406 MW; D7C35676D668FB63 CRC64;
MASETFEFQA EITQLMSLII NTVYSNKEIF LRELISNASD ALDKIRYKSL SDPKQLETEP
DLFIRITPKP EQKVLEIRDS GIGMTKAELI NNLGTIAKSG TKAFMEALSA GADVSMIGQF
GVGFYSLFLV ADRVQVISKS NDDEQYIWES NAGGSFTVTL DEVNERIGRG TILRLFLKDD
QLEYLEEKRI KEVIKRHSEF VAYPIQLVVT KEVEKEVPIP EEEKKDEEKK DEEKKDEDDK
KPKLEEVDEE EEKKPKTKKV KEEVQEIEEL NKTKPLWTRN PSDITQEEYN AFYKSISNDW
EDPLYVKHFS VEGQLEFRAI LFIPKRAPFD LFESKKKKNN IKLYVRRVFI TDEAEDLIPE
WLSFVKGVVD SEDLPLNLSR EMLQQNKIMK VIRKNIVKKL IEAFNEIAED SEQFEKFYSA
FSKNIKLGVH EDTQNRAALA KLLRYNSTKS VDELTSLTDY VTRMPEHQKN IYYITGESLK
AVEKSPFLDA LKAKNFEVLF LTDPIDEYAF TQLKEFEGKT LVDITKDFEL EETDEEKAER
EKEIKEYEPL TKALKEILGD QVEKVVVSYK LLDAPAAIRT GQFGWSANME RIMKAQALRD
SSMSSYMSSK KTFEISPKSP IIKELKKRVD EGGAQDKTVK DLTKLLYETA LLTSGFSLDE
PTSFASRINR LISLGLNIDE DEETETAPEA STAAPVEEVP ADTEMEEVD


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YSGSPA822D Heat Shock Protein 70 (Hsp70), Heat Shock Cognate 70 (Hsc70), Inducible & Constitutive, ~72&73kD, Clone BB70, Mab anti_Chicken, Human, Mouse, Rat, Beluga, Bovine, Dog, Drosophila, Euglena gracilis, F 50 µg.
25-272 The heat-shock response is elicited by exposure of cells to thermal and chemical stress and through the activation of HSFs (heat shock factors) results in the elevated expression of heat-shock induced 0.05 mg
YSGSPA820 Heat Shock Protein 70 (Hsp70), Heat Shock Cognate 70 (Hsc70), Inducible & Constitutive, Rabbit anti_Human, Mouse, Rat, Beluga, Bovine, Dog, Chicken, Fish, Guinea pig, Hamster, Lobster, Monkey, Mussel, 200 µg.
YSGSPA820AP Heat Shock Protein 70 (Hsp70), Heat Shock Cognate 70 (Hsc70), Inducible & Constitutive, Rabbit anti_Human, Mouse, Rat, Beluga, Bovine, Dog, Chicken, Fish, Guinea pig, Hamster, Lobster, Monkey, Mussel, 200 µl.
YSGSPA757E Heat Shock Protein 70 (Hsp70), Heat Shock Cognate 70 (Hsc70), Inducible & Constitutive, ~72&73kD, Rabbit anti_Rat, Human, Mouse, Bovine, Chicken, Dog, Drosophila, Fish, Guinea pig, Hamster, Monkey, Sw 100 µl.
YSGSPA757C Heat Shock Protein 70 (Hsp70), Heat Shock Cognate 70 (Hsc70), Inducible & Constitutive, ~72&73kD, Rabbit anti_Rat, Human, Mouse, Bovine, Chicken, Dog, Drosophila, Fish, Guinea pig, Hamster, Monkey, Sw 25 µl.
YSGSPA820APD Heat Shock Protein 70 (Hsp70), Heat Shock Cognate 70 (Hsc70), Inducible & Constitutive, Rabbit anti_Human, Mouse, Rat, Beluga, Bovine, Dog, Chicken, Fish, Guinea pig, Hamster, Lobster, Monkey, Mussel, 50 µl.
U0693c CLIA 25 kDa IAP,Actin polymerization inhibitor,Chicken,Gallus gallus,Heat shock 25 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,HSP 25,HSP 27,HspB1,HSPB1 96T


 

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