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Heat shock protein 104 (Protein aggregation-remodeling factor HSP104)

 HS104_YEAST             Reviewed;         908 AA.
P31539; D6VXX8;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
02-JUN-2021, entry version 194.
RecName: Full=Heat shock protein 104;
AltName: Full=Protein aggregation-remodeling factor HSP104;
Name=HSP104; OrderedLocusNames=YLL026W; ORFNames=L0948;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF LYS-218 AND LYS-620.
STRAIN=ATCC 26109 / X2180 / NCYC 826;
PubMed=1896074; DOI=10.1038/353270a0;
Parsell D.A., Sanchez Y., Stitzel J.D., Lindquist S.L.;
"Hsp104 is a highly conserved protein with two essential nucleotide-binding
sites.";
Nature 353:270-273(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169871;
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
Zollner A., Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
LaBaer J.;
"Approaching a complete repository of sequence-verified protein-encoding
clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 749-908.
STRAIN=ATCC 204508 / S288c;
PubMed=9046100;
DOI=10.1002/(sici)1097-0061(199702)13:2<183::aid-yea65>3.0.co;2-v;
Purnelle B., Goffeau A.;
"The sequence of 32kb on the left arm of yeast chromosome XII reveals six
known genes, a new member of the seripauperins family and a new ABC
transporter homologous to the human multidrug resistance protein.";
Yeast 13:183-188(1997).
[6]
FUNCTION.
PubMed=2188365; DOI=10.1126/science.2188365;
Sanchez Y., Lindquist S.L.;
"HSP104 required for induced thermotolerance.";
Science 248:1112-1115(1990).
[7]
FUNCTION, AND INDUCTION.
PubMed=1600951; DOI=10.1002/j.1460-2075.1992.tb05295.x;
Sanchez Y., Taulien J., Borkovich K.A., Lindquist S.L.;
"Hsp104 is required for tolerance to many forms of stress.";
EMBO J. 11:2357-2364(1992).
[8]
FUNCTION.
PubMed=8407824; DOI=10.1128/jb.175.20.6484-6491.1993;
Sanchez Y., Parsell D.A., Taulien J., Vogel J.L., Craig E.A.,
Lindquist S.L.;
"Genetic evidence for a functional relationship between Hsp104 and Hsp70.";
J. Bacteriol. 175:6484-6491(1993).
[9]
INDUCTION, MUTAGENESIS OF LYS-218 AND LYS-620, SUBUNIT, AND ELECTRON
MICROSCOPY.
PubMed=8308017;
Parsell D.A., Kowal A.S., Lindquist S.L.;
"Saccharomyces cerevisiae Hsp104 protein. Purification and characterization
of ATP-induced structural changes.";
J. Biol. Chem. 269:4480-4487(1994).
[10]
FUNCTION.
PubMed=7984243; DOI=10.1038/372475a0;
Parsell D.A., Kowal A.S., Singer M.A., Lindquist S.L.;
"Protein disaggregation mediated by heat-shock protein Hsp104.";
Nature 372:475-478(1994).
[11]
FUNCTION IN PRION MAINTENANCE.
PubMed=7754373; DOI=10.1126/science.7754373;
Chernoff Y.O., Lindquist S.L., Ono B., Inge-Vechtomov S.G., Liebman S.W.;
"Role of the chaperone protein Hsp104 in propagation of the yeast prion-
like factor [psi+].";
Science 268:880-884(1995).
[12]
FUNCTION, AND INDUCTION.
PubMed=8643570; DOI=10.1073/pnas.93.11.5301;
Lindquist S.L., Kim G.;
"Heat-shock protein 104 expression is sufficient for thermotolerance in
yeast.";
Proc. Natl. Acad. Sci. U.S.A. 93:5301-5306(1996).
[13]
SUBCELLULAR LOCATION.
PubMed=9703962; DOI=10.1006/bbrc.1998.9008;
Fujita K., Kawai R., Iwahashi H., Komatsu Y.;
"Hsp104 responds to heat and oxidative stress with different intracellular
localization in Saccharomyces cerevisiae.";
Biochem. Biophys. Res. Commun. 248:542-547(1998).
[14]
FUNCTION, AND INTERACTION WITH YDJ1.
PubMed=9674429; DOI=10.1016/s0092-8674(00)81223-4;
Glover J.R., Lindquist S.L.;
"Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously
aggregated proteins.";
Cell 94:73-82(1998).
[15]
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF GLY-217; LYS-218; GLY-619
AND LYS-620.
PubMed=9624144; DOI=10.1074/jbc.273.25.15546;
Schirmer E.C., Queitsch C., Kowal A.S., Parsell D.A., Lindquist S.L.;
"The ATPase activity of Hsp104, effects of environmental conditions and
mutations.";
J. Biol. Chem. 273:15546-15552(1998).
[16]
ERRATUM OF PUBMED:9624144.
Schirmer E.C., Queitsch C., Kowal A.S., Parsell D.A., Lindquist S.L.;
J. Biol. Chem. 273:19922-19922(1998).
[17]
FUNCTION, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=9534180; DOI=10.1016/s0076-6879(98)90036-2;
Schirmer E.C., Lindquist S.L.;
"Purification and properties of Hsp104 from yeast.";
Methods Enzymol. 290:430-444(1998).
[18]
SUBCELLULAR LOCATION.
PubMed=10467108; DOI=10.1054/csac.1999.0076;
Kawai R., Fujita K., Iwahashi H., Komatsu Y.;
"Direct evidence for the intracellular localization of Hsp104 in
Saccharomyces cerevisiae by immunoelectron microscopy.";
Cell Stress Chaperones 4:46-53(1999).
[19]
FUNCTION IN PRION PROPAGATION.
PubMed=10678178; DOI=10.1016/s1097-2765(00)80412-8;
Sondheimer N., Lindquist S.L.;
"Rnq1: an epigenetic modifier of protein function in yeast.";
Mol. Cell 5:163-172(2000).
[20]
FUNCTION IN PRION PROPAGATION.
PubMed=11073991; DOI=10.1128/mcb.20.23.8916-8922.2000;
Moriyama H., Edskes H.K., Wickner R.B.;
"[URE3] prion propagation in Saccharomyces cerevisiae: requirement for
chaperone Hsp104 and curing by overexpressed chaperone Ydj1p.";
Mol. Cell. Biol. 20:8916-8922(2000).
[21]
FUNCTION IN PRION PROPAGATION.
PubMed=11375656; DOI=10.1007/s002840010251;
Jung G., Masison D.C.;
"Guanidine hydrochloride inhibits Hsp104 activity in vivo: a possible
explanation for its effect in curing yeast prions.";
Curr. Microbiol. 43:7-10(2001).
[22]
INTERACTION WITH CNS1; CPR7 AND STI1.
PubMed=11604493; DOI=10.1128/mcb.21.22.7569-7575.2001;
Abbas-Terki T., Donze O., Briand P.-A., Picard D.;
"Hsp104 interacts with Hsp90 cochaperones in respiring yeast.";
Mol. Cell. Biol. 21:7569-7575(2001).
[23]
FUNCTION IN PRION PROPAGATION, AND MUTAGENESIS OF LYS-218 AND LYS-620.
PubMed=11442834; DOI=10.1046/j.1365-2958.2001.02478.x;
Ferreira P.C., Ness F., Edwards S.R., Cox B.S., Tuite M.F.;
"The elimination of the yeast [PSI+] prion by guanidine hydrochloride is
the result of Hsp104 inactivation.";
Mol. Microbiol. 40:1357-1369(2001).
[24]
BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF GLY-217;
LYS-218; GLY-619; LYS-620 AND THR-621.
PubMed=11158570; DOI=10.1073/pnas.98.3.914;
Schirmer E.C., Ware D.M., Queitsch C., Kowal A.S., Lindquist S.L.;
"Subunit interactions influence the biochemical and biological properties
of Hsp104.";
Proc. Natl. Acad. Sci. U.S.A. 98:914-919(2001).
[25]
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF THR-317 AND ASN-728.
PubMed=11782421; DOI=10.1093/emboj/21.1.12;
Hattendorf D.A., Lindquist S.L.;
"Cooperative kinetics of both Hsp104 ATPase domains and interdomain
communication revealed by AAA sensor-1 mutants.";
EMBO J. 21:12-21(2002).
[26]
SUBSTRATE-BINDING, AND MUTAGENESIS OF LYS-218; ALA-315; ALA-503 AND
ASN-728.
PubMed=11983167; DOI=10.1016/s1097-2765(02)00499-9;
Cashikar A.G., Schirmer E.C., Hattendorf D.A., Glover J.R.,
Ramakrishnan M.S., Ware D.M., Lindquist S.L.;
"Defining a pathway of communication from the C-terminal peptide binding
domain to the N-terminal ATPase domain in a AAA protein.";
Mol. Cell 9:751-760(2002).
[27]
FUNCTION IN PRION PROPAGATION, AND MUTAGENESIS OF LYS-218 AND LYS-620.
PubMed=12101251; DOI=10.1128/mcb.22.15.5593-5605.2002;
Ness F., Ferreira P.C., Cox B.S., Tuite M.F.;
"Guanidine hydrochloride inhibits the generation of prion 'seeds' but not
prion protein aggregation in yeast.";
Mol. Cell. Biol. 22:5593-5605(2002).
[28]
INDUCTION.
PubMed=11967066; DOI=10.1046/j.1365-2958.2002.02860.x;
Grably M.R., Stanhill A., Tell O., Engelberg D.;
"HSF and Msn2/4p can exclusively or cooperatively activate the yeast HSP104
gene.";
Mol. Microbiol. 44:21-35(2002).
[29]
MUTAGENESIS OF TYR-819 AND ARG-826, AND ATP-BINDING.
PubMed=11867765; DOI=10.1073/pnas.261693199;
Hattendorf D.A., Lindquist S.L.;
"Analysis of the AAA sensor-2 motif in the C-terminal ATPase domain of
Hsp104 with a site-specific fluorescent probe of nucleotide binding.";
Proc. Natl. Acad. Sci. U.S.A. 99:2732-2737(2002).
[30]
MUTAGENESIS OF ASP-184.
PubMed=12105276; DOI=10.1073/pnas.152333299;
Jung G., Jones G., Masison D.C.;
"Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-
curing by guanidine, prion propagation, and thermotolerance.";
Proc. Natl. Acad. Sci. U.S.A. 99:9936-9941(2002).
[31]
FUNCTION IN PRION FRAGMENTATION.
PubMed=14507919; DOI=10.1074/jbc.m307996200;
Kryndushkin D.S., Alexandrov I.M., Ter-Avanesyan M.D., Kushnirov V.V.;
"Yeast [PSI+] prion aggregates are formed by small Sup35 polymers
fragmented by Hsp104.";
J. Biol. Chem. 278:49636-49643(2003).
[32]
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).
[33]
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).
[34]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-620, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=14557538; DOI=10.1073/pnas.2135500100;
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
"A subset of membrane-associated proteins is ubiquitinated in response to
mutations in the endoplasmic reticulum degradation machinery.";
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
[35]
ACTIVITY REGULATION.
PubMed=14668331; DOI=10.1074/jbc.m312403200;
Grimminger V., Richter K., Imhof A., Buchner J., Walter S.;
"The prion curing agent guanidinium chloride specifically inhibits ATP
hydrolysis by Hsp104.";
J. Biol. Chem. 279:7378-7383(2004).
[36]
FUNCTION, MUTAGENESIS OF TYR-257; GLU-645 AND TYR-662, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=15128736; DOI=10.1074/jbc.m403777200;
Lum R., Tkach J.M., Vierling E., Glover J.R.;
"Evidence for an unfolding/threading mechanism for protein disaggregation
by Saccharomyces cerevisiae Hsp104.";
J. Biol. Chem. 279:29139-29146(2004).
[37]
MUTAGENESIS OF GLY-217; THR-499; ALA-503 AND ALA-509.
PubMed=14978213; DOI=10.1091/mbc.e02-08-0502;
Schirmer E.C., Homann O.R., Kowal A.S., Lindquist S.L.;
"Dominant gain-of-function mutations in Hsp104p reveal crucial roles for
the middle region.";
Mol. Biol. Cell 15:2061-2072(2004).
[38]
INDUCTION.
PubMed=15049822; DOI=10.1111/j.1365-2958.2003.03959.x;
Seppae L., Haenninen A.-L., Makarow M.;
"Upregulation of the Hsp104 chaperone at physiological temperature during
recovery from thermal insult.";
Mol. Microbiol. 52:217-225(2004).
[39]
FUNCTION IN PRION PROPAGATION.
PubMed=15155912; DOI=10.1126/science.1098007;
Shorter J., Lindquist S.L.;
"Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion
conformers.";
Science 304:1793-1797(2004).
[40]
FUNCTION.
PubMed=15843375; DOI=10.1074/jbc.m502697200;
Haslbeck M., Miess A., Stromer T., Walter S., Buchner J.;
"Disassembling protein aggregates in the yeast cytosol. The cooperation of
Hsp26 with Ssa1 and Hsp104.";
J. Biol. Chem. 280:23861-23868(2005).
[41]
FUNCTION.
PubMed=15845535; DOI=10.1074/jbc.m502854200;
Cashikar A.G., Duennwald M., Lindquist S.L.;
"A chaperone pathway in protein disaggregation. Hsp26 alters the nature of
protein aggregates to facilitate reactivation by Hsp104.";
J. Biol. Chem. 280:23869-23875(2005).
[42]
ERRATUM OF PUBMED:15845535.
Cashikar A.G., Duennwald M., Lindquist S.L.;
J. Biol. Chem. 281:8996-8996(2006).
[43]
SUBUNIT, AND MUTAGENESIS OF LYS-218; GLU-285; LYS-620 AND GLU-687.
PubMed=16135516; DOI=10.1074/jbc.m506149200;
Boesl B., Grimminger V., Walter S.;
"Substrate binding to the molecular chaperone Hsp104 and its regulation by
nucleotides.";
J. Biol. Chem. 280:38170-38176(2005).
[44]
FUNCTION IN PRION DISASSEMBLY.
PubMed=16570324; DOI=10.1002/cbic.200500382;
Narayanan S., Walter S., Reif B.;
"Yeast prion-protein, sup35, fibril formation proceeds by addition and
substraction of oligomers.";
ChemBioChem 7:757-765(2006).
[45]
FUNCTION IN PRION DISASSEMBLY.
PubMed=16885031; DOI=10.1016/j.molcel.2006.05.042;
Shorter J., Lindquist S.L.;
"Destruction or potentiation of different prions catalyzed by similar
Hsp104 remodeling activities.";
Mol. Cell 23:425-438(2006).
[46]
SUBUNIT, ELECTRON MICROSCOPY, AND MUTAGENESIS OF ARG-334; ARG-419; ARG-444;
ARG-495; ASN-728 AND ARG-765.
PubMed=18160044; DOI=10.1016/j.cell.2007.10.047;
Wendler P., Shorter J., Plisson C., Cashikar A.G., Lindquist S.L.,
Saibil H.R.;
"Atypical AAA+ subunit packing creates an expanded cavity for
disaggregation by the protein-remodeling factor Hsp104.";
Cell 131:1366-1377(2007).
[47]
FUNCTION, AND MUTAGENESIS OF LYS-218; GLU-285; LYS-620 AND GLU-687.
PubMed=17543332; DOI=10.1016/j.jmb.2007.04.070;
Schaupp A., Marcinowski M., Grimminger V., Boesl B., Walter S.;
"Processing of proteins by the molecular chaperone Hsp104.";
J. Mol. Biol. 370:674-686(2007).
[48]
FUNCTION IN PRION PROPAGATION, AND MUTAGENESIS OF LEU-462; PRO-557 AND
ASP-704.
PubMed=17367387; DOI=10.1111/j.1365-2958.2007.05629.x;
Kurahashi H., Nakamura Y.;
"Channel mutations in Hsp104 hexamer distinctively affect thermotolerance
and prion-specific propagation.";
Mol. Microbiol. 63:1669-1683(2007).
[49]
FUNCTION, AND MUTAGENESIS OF LYS-218; THR-317; LYS-620 AND ASN-728.
PubMed=17259993; DOI=10.1038/nsmb1198;
Doyle S.M., Shorter J., Zolkiewski M., Hoskins J.R., Lindquist S.L.,
Wickner S.;
"Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes
protein-remodeling activity.";
Nat. Struct. Mol. Biol. 14:114-122(2007).
[50]
FUNCTION IN PRION PROPAGATION.
PubMed=17253904; DOI=10.1371/journal.pbio.0050024;
Satpute-Krishnan P., Langseth S.X., Serio T.R.;
"Hsp104-dependent remodeling of prion complexes mediates protein-only
inheritance.";
PLoS Biol. 5:251-262(2007).
[51]
INTERACTION WITH CPR7.
PubMed=18197703; DOI=10.1021/bi701714s;
Mackay R.G., Helsen C.W., Tkach J.M., Glover J.R.;
"The C-terminal extension of Saccharomyces cerevisiae Hsp104 plays a role
in oligomer assembly.";
Biochemistry 47:1918-1927(2008).
[52]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-306; THR-499 AND
SER-535, AND 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).
[53]
FUNCTION.
PubMed=18312264; DOI=10.1111/j.1365-2958.2008.06135.x;
Tessarz P., Mogk A., Bukau B.;
"Substrate threading through the central pore of the Hsp104 chaperone as a
common mechanism for protein disaggregation and prion propagation.";
Mol. Microbiol. 68:87-97(2008).
[54]
SUBCELLULAR LOCATION.
PubMed=18756251; DOI=10.1038/nature07195;
Kaganovich D., Kopito R., Frydman J.;
"Misfolded proteins partition between two distinct quality control
compartments.";
Nature 454:1088-1095(2008).
[55]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-778; LYS-782 AND LYS-789.
PubMed=17973656; DOI=10.1111/j.1600-0854.2007.00666.x;
Tkach J.M., Glover J.R.;
"Nucleocytoplasmic trafficking of the molecular chaperone Hsp104 in
unstressed and heat-shocked cells.";
Traffic 9:39-56(2008).
[56]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides insights
into evolution.";
Science 325:1682-1686(2009).
[57]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-terminal
acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[58]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-442, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
-!- FUNCTION: Required, in concert with Hsp40 (YDJ1) and Hsp70 (SSA1) and
small Hsps (HSP26), for the dissociation, resolubilization and
refolding of aggregates of damaged proteins after heat or other
environmental stresses. Extracts proteins from aggregates by unfolding
and threading them in an ATP-dependent process through the axial
channel of the protein hexamer, after which they can be refolded by
components of the Hsp70/Hsp40 chaperone system. Substrate binding is
ATP-dependent, and release of bound polypeptide is triggered by ATP
hydrolysis. Also responsible for the maintenance of prions by
dissociating prion fibrils into smaller oligomers, thereby producing
transmissible seeds that can infect daughter cells during mitosis and
meiosis. Loss of HSP104 can cure yeast cells of the prions [PSI+],
[URE3] and [PIN+]. Excess HSP104 can also specifically cure cells of
[PSI+]. {ECO:0000269|PubMed:10678178, ECO:0000269|PubMed:11073991,
ECO:0000269|PubMed:11375656, ECO:0000269|PubMed:11442834,
ECO:0000269|PubMed:12101251, ECO:0000269|PubMed:14507919,
ECO:0000269|PubMed:15128736, ECO:0000269|PubMed:15155912,
ECO:0000269|PubMed:15843375, ECO:0000269|PubMed:15845535,
ECO:0000269|PubMed:1600951, ECO:0000269|PubMed:16570324,
ECO:0000269|PubMed:16885031, ECO:0000269|PubMed:17253904,
ECO:0000269|PubMed:17259993, ECO:0000269|PubMed:17367387,
ECO:0000269|PubMed:17543332, ECO:0000269|PubMed:18312264,
ECO:0000269|PubMed:2188365, ECO:0000269|PubMed:7754373,
ECO:0000269|PubMed:7984243, ECO:0000269|PubMed:8407824,
ECO:0000269|PubMed:8643570, ECO:0000269|PubMed:9534180,
ECO:0000269|PubMed:9674429}.
-!- ACTIVITY REGULATION: Inhibited by micromolar concentrations of
guanidinium chloride. Inhibits the ATPase activity, but does not
dissociate the hexameric protein. {ECO:0000269|PubMed:14668331}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=170 uM for ATP (at NBD1) {ECO:0000269|PubMed:11158570,
ECO:0000269|PubMed:11782421, ECO:0000269|PubMed:15128736,
ECO:0000269|PubMed:9534180, ECO:0000269|PubMed:9624144};
KM=4.7 uM for ATP (at NBD2) {ECO:0000269|PubMed:11158570,
ECO:0000269|PubMed:11782421, ECO:0000269|PubMed:15128736,
ECO:0000269|PubMed:9534180, ECO:0000269|PubMed:9624144};
Vmax=1.25 nmol/min/ug enzyme for ATP {ECO:0000269|PubMed:11158570,
ECO:0000269|PubMed:11782421, ECO:0000269|PubMed:15128736,
ECO:0000269|PubMed:9534180, ECO:0000269|PubMed:9624144};
-!- SUBUNIT: Homohexamer, forming a ring with a central pore. The hexamer
is stabilized by high protein concentrations and by ADP or ATP.
Oligomerization influences ATP hydrolysis activity at NBD2. Interacts
with YDJ1. Interacts (via C-terminal DDLD tetrapeptide) with CNS1, CPR7
and STI1 (via TPR repeats); under respiratory growth conditions.
{ECO:0000269|PubMed:11158570, ECO:0000269|PubMed:11604493,
ECO:0000269|PubMed:16135516, ECO:0000269|PubMed:18160044,
ECO:0000269|PubMed:18197703, ECO:0000269|PubMed:8308017,
ECO:0000269|PubMed:9534180, ECO:0000269|PubMed:9674429}.
-!- INTERACTION:
P31539; P31539: HSP104; NbExp=3; IntAct=EBI-8050, EBI-8050;
P31539; Q12285: MDY2; NbExp=2; IntAct=EBI-8050, EBI-34904;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between the
cytoplasm and the nucleus in an importin KAP95- and KAP121-dependent
and an exportin XPO1-dependent manner. Accumulation in the nucleus is
enhanced by severe heat shock. In the cytoplasm, concentrates on a
perivacuolar compartment, the 'insoluble protein deposit' (IPOD), in
which terminally aggregated proteins are sequestered. It is also found,
to a lesser extent, at a 'juxtanuclear quality control' (JUNQ)
compartment, where soluble ubiquitinated misfolded proteins accumulate.
-!- INDUCTION: By heat stress dependent on the heat shock transcription
factor HSF1 and the general stress transcription factors MSN2 and MSN4.
Expressed at a higher level in respiring cells than in fermenting
cells. Expressed in stationary phase cells and spores (at protein
level). {ECO:0000269|PubMed:11967066, ECO:0000269|PubMed:15049822,
ECO:0000269|PubMed:1600951, ECO:0000269|PubMed:8308017,
ECO:0000269|PubMed:8643570}.
-!- DOMAIN: Has 2 AAA ATPase type nucleotide-binding domains (NBDs) per
monomer, a low-affinity, high-turnover site (NBD1) and a high-affinity
site (NBD2) with a 300-fold slower rate of hydrolysis. There is
allosteric regulation between the 2 sites. ATP binding to NBD1 triggers
binding of polypeptides and stimulates ATP hydrolysis at NBD2.
Nucleotide binding to NBD2 is crucial for oligomerization.
-!- DOMAIN: The C-terminal extension is involved in oligomerization.
-!- MISCELLANEOUS: Present with 32800 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
---------------------------------------------------------------------------
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EMBL; M67479; AAA50477.1; -; Genomic_DNA.
EMBL; Z73131; CAA97475.1; -; Genomic_DNA.
EMBL; Z73130; CAA97474.1; -; Genomic_DNA.
EMBL; AY693002; AAT93021.1; -; Genomic_DNA.
EMBL; X97560; CAA66164.1; -; Genomic_DNA.
EMBL; BK006945; DAA09294.1; -; Genomic_DNA.
PIR; S61476; S61476.
RefSeq; NP_013074.1; NM_001181846.1.
PDB; 5KNE; EM; 5.64 A; A/B/C/D/E/F=6-857.
PDB; 5U2U; X-ray; 2.54 A; A/B/C=1-166.
PDB; 5VJH; EM; 4.00 A; A/B/C/D/E/F=1-908.
PDB; 5VY8; EM; 4.00 A; A/B/C/D/E/F=1-908.
PDB; 5VY9; EM; 4.00 A; A/B/C/D/E/F=1-908.
PDB; 5VYA; EM; 4.00 A; A/B/C/D/E/F=1-908.
PDB; 5WBW; X-ray; 2.60 A; A/B/D=4-356.
PDB; 6AHF; EM; 6.78 A; A/B/C/D/E/F=1-908.
PDB; 6AMN; X-ray; 2.82 A; A=4-352.
PDB; 6N8T; EM; 7.70 A; A/B/C/D/E/F=6-884.
PDB; 6N8V; EM; 5.64 A; A/B/C/D/E/F=6-884.
PDB; 6N8Z; EM; 9.30 A; A/B/C/D/E/F=6-884.
PDBsum; 5KNE; -.
PDBsum; 5U2U; -.
PDBsum; 5VJH; -.
PDBsum; 5VY8; -.
PDBsum; 5VY9; -.
PDBsum; 5VYA; -.
PDBsum; 5WBW; -.
PDBsum; 6AHF; -.
PDBsum; 6AMN; -.
PDBsum; 6N8T; -.
PDBsum; 6N8V; -.
PDBsum; 6N8Z; -.
SMR; P31539; -.
BioGRID; 31226; 472.
ComplexPortal; CPX-1861; GET4-GET5 transmembrane domain recognition complex.
DIP; DIP-2252N; -.
IntAct; P31539; 28.
MINT; P31539; -.
STRING; 4932.YLL026W; -.
CarbonylDB; P31539; -.
iPTMnet; P31539; -.
SWISS-2DPAGE; P31539; -.
MaxQB; P31539; -.
PaxDb; P31539; -.
PRIDE; P31539; -.
EnsemblFungi; YLL026W_mRNA; YLL026W; YLL026W.
GeneID; 850633; -.
KEGG; sce:YLL026W; -.
SGD; S000003949; HSP104.
VEuPathDB; FungiDB:YLL026W; -.
eggNOG; KOG1051; Eukaryota.
GeneTree; ENSGT00960000189194; -.
HOGENOM; CLU_005070_4_0_1; -.
InParanoid; P31539; -.
OMA; ERMKAVM; -.
SABIO-RK; P31539; -.
PRO; PR:P31539; -.
Proteomes; UP000002311; Chromosome XII.
RNAct; P31539; protein.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0034399; C:nuclear periphery; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0072380; C:TRC complex; IDA:SGD.
GO; GO:0043531; F:ADP binding; IMP:SGD.
GO; GO:0005524; F:ATP binding; IMP:SGD.
GO; GO:0016887; F:ATPase activity; IDA:SGD.
GO; GO:0051087; F:chaperone binding; IDA:SGD.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
GO; GO:0070370; P:cellular heat acclimation; IMP:SGD.
GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IDA:SGD.
GO; GO:0034975; P:protein folding in endoplasmic reticulum; IMP:SGD.
GO; GO:0042026; P:protein refolding; IBA:GO_Central.
GO; GO:0043335; P:protein unfolding; IMP:SGD.
GO; GO:0035617; P:stress granule disassembly; IDA:SGD.
GO; GO:0070414; P:trehalose metabolism in response to heat stress; IMP:SGD.
Gene3D; 1.10.1780.10; -; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR019489; Clp_ATPase_C.
InterPro; IPR036628; Clp_N_dom_sf.
InterPro; IPR004176; Clp_R_dom.
InterPro; IPR001270; ClpA/B.
InterPro; IPR018368; ClpA/B_CS1.
InterPro; IPR028299; ClpA/B_CS2.
InterPro; IPR041546; ClpA/ClpB_AAA_lid.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00004; AAA; 1.
Pfam; PF07724; AAA_2; 1.
Pfam; PF17871; AAA_lid_9; 1.
Pfam; PF02861; Clp_N; 2.
Pfam; PF10431; ClpB_D2-small; 1.
PRINTS; PR00300; CLPPROTEASEA.
SMART; SM00382; AAA; 2.
SMART; SM01086; ClpB_D2-small; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF81923; SSF81923; 1.
PROSITE; PS51903; CLP_R; 1.
PROSITE; PS00870; CLPAB_1; 1.
PROSITE; PS00871; CLPAB_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Chaperone; Coiled coil; Cytoplasm;
Isopeptide bond; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Stress response; Ubl conjugation.
CHAIN 1..908
/note="Heat shock protein 104"
/id="PRO_0000191212"
DOMAIN 4..150
/note="Clp R"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
NP_BIND 212..219
/note="ATP 1"
/evidence="ECO:0000255"
NP_BIND 614..621
/note="ATP 2"
/evidence="ECO:0000255"
REGION 7..76
/note="Repeat 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
REGION 88..150
/note="Repeat 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
REGION 167..411
/note="NBD1"
REGION 541..731
/note="NBD2"
REGION 883..908
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 905..908
/note="Interaction surface for TPR repeats"
COILED 412..536
/evidence="ECO:0000255"
MOTIF 773..789
/note="Nuclear localization signal"
COMPBIAS 891..908
/note="Acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOD_RES 1
/note="N-acetylmethionine"
/evidence="ECO:0007744|PubMed:22814378"
MOD_RES 206
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18407956,
ECO:0007744|PubMed:19779198"
MOD_RES 306
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18407956"
MOD_RES 499
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:18407956"
MOD_RES 535
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18407956"
CROSSLNK 442
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0007744|PubMed:22106047"
CROSSLNK 620
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000269|PubMed:14557538"
MUTAGEN 184
/note="D->A,D,F,N,L,Q,S: Confers resistance to prion-curing
by guanidine."
/evidence="ECO:0000269|PubMed:12105276"
MUTAGEN 184
/note="D->K,W,Y: Impairs prion propagation."
/evidence="ECO:0000269|PubMed:12105276"
MUTAGEN 217
/note="G->S: Largely reduces ATP hydrolysis. Alters bud
morphology and causes septin mislocalization; when
associated with I-499."
/evidence="ECO:0000269|PubMed:11158570,
ECO:0000269|PubMed:14978213, ECO:0000269|PubMed:9624144"
MUTAGEN 217
/note="G->V: Completely abolishes ATP hydrolysis."
/evidence="ECO:0000269|PubMed:11158570,
ECO:0000269|PubMed:14978213, ECO:0000269|PubMed:9624144"
MUTAGEN 218
/note="K->T: Abolishes substrate binding. Unable to confer
thermotolerance. Reduces ATP hydrolysis by 98%; when
associated with T-315. Comletely abolishes ATPase activity;
when associated with T-620."
/evidence="ECO:0000269|PubMed:11158570,
ECO:0000269|PubMed:11442834, ECO:0000269|PubMed:11983167,
ECO:0000269|PubMed:12101251, ECO:0000269|PubMed:16135516,
ECO:0000269|PubMed:17259993, ECO:0000269|PubMed:17543332,
ECO:0000269|PubMed:1896074, ECO:0000269|PubMed:8308017,
ECO:0000269|PubMed:9624144"
MUTAGEN 257
/note="Y->A: Reduces thermotolerance 10-fold."
/evidence="ECO:0000269|PubMed:15128736"
MUTAGEN 285
/note="E->Q: In HSP104(TRAP); completely abolishes ATP
hydrolysis, but does not affect nucleotide binding, thus
keeping HSP104 in an ATP-bound state; when associated with
Q-687."
/evidence="ECO:0000269|PubMed:16135516,
ECO:0000269|PubMed:17543332"
MUTAGEN 315
/note="A->T: Reduces ATP hydrolysis by 98%; when associated
with T-218."
/evidence="ECO:0000269|PubMed:11983167"
MUTAGEN 317
/note="T->A: Reduces rate of ATP hydrolysis at NBD1 nearly
10-fold. No effect on oligomerization."
/evidence="ECO:0000269|PubMed:11782421,
ECO:0000269|PubMed:17259993"
MUTAGEN 334
/note="R->M: Reduces ATPase activity by 80%. Impairs
oligomerization."
/evidence="ECO:0000269|PubMed:18160044"
MUTAGEN 419
/note="R->M: Reduces ATPase activity by 80%."
/evidence="ECO:0000269|PubMed:18160044"
MUTAGEN 444
/note="R->M: Reduces ATPase activity by 80%."
/evidence="ECO:0000269|PubMed:18160044"
MUTAGEN 462
/note="L->R: Impairs prion propagation, but does not affect
thermotolerance."
/evidence="ECO:0000269|PubMed:17367387"
MUTAGEN 495
/note="R->M: Increases ATPase activity 3-fold."
/evidence="ECO:0000269|PubMed:18160044"
MUTAGEN 499
/note="T->I: Reduces ATP hydrolysis by 50%. Alters bud
morphology and causes septin mislocalization; when
associated with S-217."
/evidence="ECO:0000269|PubMed:14978213"
MUTAGEN 503
/note="A->V: Increases basal level of ATPase activity and
abolishes stimulation of ATP hydrolysis upon substrate
binding. Inhibits growth at 37 degrees Celsius."
/evidence="ECO:0000269|PubMed:11983167,
ECO:0000269|PubMed:14978213"
MUTAGEN 509
/note="A->D: Reduces thermotolerance."
/evidence="ECO:0000269|PubMed:14978213"
MUTAGEN 557
/note="P->L: Impairs prion propagation, but does not affect
thermotolerance."
/evidence="ECO:0000269|PubMed:17367387"
MUTAGEN 619
/note="G->V: Impairs oligomerization at low protein
concentrations."
/evidence="ECO:0000269|PubMed:11158570,
ECO:0000269|PubMed:9624144"
MUTAGEN 620
/note="K->T: Impairs oligomerization at low protein
concentrations. Reduces ATP hydrolysis rate. Unable to
confer thermotolerance. Comletely abolishes ATPase
activity; when associated with T-218."
/evidence="ECO:0000269|PubMed:11158570,
ECO:0000269|PubMed:11442834, ECO:0000269|PubMed:12101251,
ECO:0000269|PubMed:16135516, ECO:0000269|PubMed:17259993,
ECO:0000269|PubMed:17543332, ECO:0000269|PubMed:1896074,
ECO:0000269|PubMed:8308017, ECO:0000269|PubMed:9624144"
MUTAGEN 621
/note="T->A: Reduces ATP hydrolysis, but does not affect
oligomerization."
/evidence="ECO:0000269|PubMed:11158570"
MUTAGEN 645
/note="E->K: Abolishes the ability to refold aggregated
protein in vitro and to provide thermotolerance in vivo."
/evidence="ECO:0000269|PubMed:15128736"
MUTAGEN 662
/note="Y->A,K: Abolishes the ability to refold aggregated
protein in vitro and to provide thermotolerance in vivo."
/evidence="ECO:0000269|PubMed:15128736"
MUTAGEN 662
/note="Y->F,W: No effect."
/evidence="ECO:0000269|PubMed:15128736"
MUTAGEN 687
/note="E->Q: In HSP104(TRAP); completely abolishes ATP
hydrolysis, but does not affect nucleotide binding, thus
keeping HSP104 in an ATP-bound state; when associated with
Q-285."
/evidence="ECO:0000269|PubMed:16135516,
ECO:0000269|PubMed:17543332"
MUTAGEN 704
/note="D->N: Impairs prion propagation, but does not affect
thermotolerance."
/evidence="ECO:0000269|PubMed:17367387"
MUTAGEN 728
/note="N->A: Almost completely abolishes ATP hydrolysis at
NBD2, but does not affect nucleotide binding, thus keeping
NBD2 in an ATP-bound state. Reduces stimulation of ATP
hydrolysis upon substrate binding."
/evidence="ECO:0000269|PubMed:11782421,
ECO:0000269|PubMed:11983167, ECO:0000269|PubMed:17259993,
ECO:0000269|PubMed:18160044"
MUTAGEN 765
/note="R->M: Can oligomerize in the absence of
nucleotides."
/evidence="ECO:0000269|PubMed:18160044"
MUTAGEN 778
/note="K->A: In NLS17KA; fails to concentrate in the
nucleus; when associated with A-782 and A-789."
/evidence="ECO:0000269|PubMed:17973656"
MUTAGEN 782
/note="K->A: In NLS17KA; fails to concentrate in the
nucleus; when associated with A-778 and A-789."
/evidence="ECO:0000269|PubMed:17973656"
MUTAGEN 789
/note="K->A: In NLS17KA; fails to concentrate in the
nucleus; when associated with A-778 and A-782."
/evidence="ECO:0000269|PubMed:17973656"
MUTAGEN 819
/note="Y->W: Site-specific fluorescent probe in an
otherwise Trp-less HSP104. Fluorescence of this Trp changes
in response to ATP and ADP binding at NBD2. Has no effect
on ATP hydrolysis or protein stability."
/evidence="ECO:0000269|PubMed:11867765"
MUTAGEN 826
/note="R->M: Reduces ATP and ADP binding at NBD2 6-fold,
but does not affect ATP hydrolysis at NBD2. Reduces
catalytic rate at NBD1."
/evidence="ECO:0000269|PubMed:11867765"
HELIX 9..24
/evidence="ECO:0007829|PDB:5U2U"
STRAND 28..30
/evidence="ECO:0007829|PDB:5U2U"
HELIX 32..39
/evidence="ECO:0007829|PDB:5U2U"
HELIX 50..57
/evidence="ECO:0007829|PDB:5U2U"
HELIX 62..73
/evidence="ECO:0007829|PDB:5U2U"
HELIX 90..105
/evidence="ECO:0007829|PDB:5U2U"
STRAND 109..111
/evidence="ECO:0007829|PDB:5U2U"
HELIX 113..120
/evidence="ECO:0007829|PDB:5U2U"
HELIX 124..132
/evidence="ECO:0007829|PDB:5U2U"
HELIX 137..148
/evidence="ECO:0007829|PDB:5U2U"
HELIX 165..170
/evidence="ECO:0007829|PDB:5WBW"
STRAND 171..173
/evidence="ECO:0007829|PDB:5WBW"
HELIX 174..179
/evidence="ECO:0007829|PDB:5WBW"
HELIX 190..200
/evidence="ECO:0007829|PDB:5WBW"
STRAND 203..205
/evidence="ECO:0007829|PDB:5WBW"
STRAND 207..212
/evidence="ECO:0007829|PDB:5WBW"
HELIX 218..230
/evidence="ECO:0007829|PDB:5WBW"
HELIX 236..238
/evidence="ECO:0007829|PDB:5WBW"
STRAND 242..246
/evidence="ECO:0007829|PDB:5WBW"
HELIX 248..252
/evidence="ECO:0007829|PDB:5WBW"
HELIX 260..273
/evidence="ECO:0007829|PDB:5WBW"
STRAND 279..283
/evidence="ECO:0007829|PDB:5WBW"
TURN 284..286
/evidence="ECO:0007829|PDB:5WBW"
HELIX 287..290
/evidence="ECO:0007829|PDB:5WBW"
HELIX 298..306
/evidence="ECO:0007829|PDB:5WBW"
STRAND 311..316
/evidence="ECO:0007829|PDB:5WBW"
HELIX 318..327
/evidence="ECO:0007829|PDB:5WBW"
HELIX 330..334
/evidence="ECO:0007829|PDB:5WBW"
STRAND 335..339
/evidence="ECO:0007829|PDB:5WBW"
TURN 344..346
/evidence="ECO:0007829|PDB:5WBW"
HELIX 347..350
/evidence="ECO:0007829|PDB:5WBW"
TURN 351..355
/evidence="ECO:0007829|PDB:5WBW"
SEQUENCE 908 AA; 102035 MW; 4AD0E7E3AF98E318 CRC64;
MNDQTQFTER ALTILTLAQK LASDHQHPQL QPIHILAAFI ETPEDGSVPY LQNLIEKGRY
DYDLFKKVVN RNLVRIPQQQ PAPAEITPSY ALGKVLQDAA KIQKQQKDSF IAQDHILFAL
FNDSSIQQIF KEAQVDIEAI KQQALELRGN TRIDSRGADT NTPLEYLSKY AIDMTEQARQ
GKLDPVIGRE EEIRSTIRVL ARRIKSNPCL IGEPGIGKTA IIEGVAQRII DDDVPTILQG
AKLFSLDLAA LTAGAKYKGD FEERFKGVLK EIEESKTLIV LFIDEIHMLM GNGKDDAANI
LKPALSRGQL KVIGATTNNE YRSIVEKDGA FERRFQKIEV AEPSVRQTVA ILRGLQPKYE
IHHGVRILDS ALVTAAQLAK RYLPYRRLPD SALDLVDISC AGVAVARDSK PEELDSKERQ
LQLIQVEIKA LERDEDADST TKDRLKLARQ KEASLQEELE PLRQRYNEEK HGHEELTQAK
KKLDELENKA LDAERRYDTA TAADLRYFAI PDIKKQIEKL EDQVAEEERR AGANSMIQNV
VDSDTISETA ARLTGIPVKK LSESENEKLI HMERDLSSEV VGQMDAIKAV SNAVRLSRSG
LANPRQPASF LFLGLSGSGK TELAKKVAGF LFNDEDMMIR VDCSELSEKY AVSKLLGTTA
GYVGYDEGGF LTNQLQYKPY SVLLFDEVEK AHPDVLTVML QMLDDGRITS GQGKTIDCSN
CIVIMTSNLG AEFINSQQGS KIQESTKNLV MGAVRQHFRP EFLNRISSIV IFNKLSRKAI
HKIVDIRLKE IEERFEQNDK HYKLNLTQEA KDFLAKYGYS DDMGARPLNR LIQNEILNKL
ALRILKNEIK DKETVNVVLK KGKSRDENVP EEAEECLEVL PNHEATIGAD TLGDDDNEDS
MEIDDDLD


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hsp-104 Recombinant Saccharomyces cerevisiae Heat Shock Protein 104 HSP104 1mg
SA6030X Heat shock protein 104 _ HSP104 (1-908) antigen Purified 0.5 mg
SA6030 Heat shock protein 104 _ HSP104 (1-908) antigen Purified 0.1 mg
10-663-45494 Heat Shock Protein 27kD (HSP27) Human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.05 mg
10-663-45494 Heat Shock Protein 27kD (HSP27) Human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.01 mg
10-663-45494 Heat Shock Protein 27kD (HSP27) Human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 1 mg
228-10785-1 Recombinant Saccharomyces cerevisiae Heat Shock Protein 104 (HSP104) 10
228-10785-3 Recombinant Saccharomyces cerevisiae Heat Shock Protein 104 (HSP104) 1 mg
SP5395A Heat shock protein 104 _ HSP104 Rabbit antibody Ab Serum 0.1 ml
'SP5395A Heat shock protein 104 HSP104 antibody Ab host: Rabbit 0.1 ml
Pathways :
WP1692: Protein export
WP1644: DNA replication
WP2032: TSH signaling pathway
WP1657: Glycerolipid metabolism
WP1165: G Protein Signaling Pathways
WP1700: Selenoamino acid metabolism
WP731: Sterol regulatory element binding protein related
WP1371: G Protein Signaling Pathways
WP1663: Homologous recombination
WP2218: sGC
WP1673: Naphthalene and anthracene degradation
WP232: G Protein Signaling Pathways
WP1502: Mitochondrial biogenesis
WP1892: Protein folding
WP1613: 1,4-Dichlorobenzene degradation
WP1909: Signal regulatory protein (SIRP) family interactions
WP1678: Nucleotide excision repair
WP1690: Propanoate metabolism
WP35: G Protein Signaling Pathways
WP1625: Base excision repair
WP211: BMP signaling pathway
WP1694: Pyrimidine metabolism
WP73: G Protein Signaling Pathways
WP1654: gamma-Hexachlorocyclohexane degradation
WP1714: Tyrosine metabolism

Related Genes :
[HSP104 YLL026W L0948] Heat shock protein 104 (Protein aggregation-remodeling factor HSP104)
[hsp104 SPBC16D10.08c] Heat shock protein 104 (Protein aggregation-remodeling factor hsp104)
[SWI1 ADR6 GAM3 YPL016W LPA1] SWI/SNF chromatin-remodeling complex subunit SWI1 (Regulatory protein GAM3) (SWI/SNF complex subunit SWI1) (Transcription regulatory protein ADR6) (Transcription regulatory protein SWI1)
[hsp98 NCU00104] Heat shock protein hsp98 (Protein aggregation-remodeling factor hsp98)
[Hsp90ab1 Hsp84 Hsp84-1 Hspcb] Heat shock protein HSP 90-beta (Heat shock 84 kDa) (HSP 84) (HSP84) (Tumor-specific transplantation 84 kDa antigen) (TSTA)
[HSPB1 HSP27 HSP28] Heat shock protein beta-1 (HspB1) (28 kDa heat shock protein) (Estrogen-regulated 24 kDa protein) (Heat shock 27 kDa protein) (HSP 27) (Stress-responsive protein 27) (SRP27)
[CRYAA CRYA1 HSPB4] Alpha-crystallin A chain (Heat shock protein beta-4) (HspB4) [Cleaved into: Alpha-crystallin A(1-172); Alpha-crystallin A(1-168); Alpha-crystallin A(1-162)]
[HSF1 HSTF1] Heat shock factor protein 1 (HSF 1) (Heat shock transcription factor 1) (HSTF 1)
[Hsf1] Heat shock factor protein 1 (HSF 1) (Heat shock transcription factor 1) (HSTF 1)
[HSF1] Heat shock factor protein 1 (HSF 1) (Heat shock transcription factor 1) (HSTF 1)
[HSF4] Heat shock factor protein 4 (HSF 4) (hHSF4) (Heat shock transcription factor 4) (HSTF 4)
[Hspb1 Hsp25 Hsp27] Heat shock protein beta-1 (HspB1) (Growth-related 25 kDa protein) (Heat shock 25 kDa protein) (HSP 25) (Heat shock 27 kDa protein) (HSP 27) (p25)
[HSF2 HSTF2] Heat shock factor protein 2 (HSF 2) (Heat shock transcription factor 2) (HSTF 2)
[HSPA1A HSP72 HSPA1 HSX70] Heat shock 70 kDa protein 1A (Heat shock 70 kDa protein 1) (HSP70-1) (HSP70.1)
[DNAJB2 HSJ1 HSPF3] DnaJ homolog subfamily B member 2 (Heat shock 40 kDa protein 3) (Heat shock protein J1) (HSJ-1)
[Hsf2] Heat shock factor protein 2 (HSF 2) (Heat shock transcription factor 2) (HSTF 2)
[HSPA1B HSP72] Heat shock 70 kDa protein 1B (Heat shock 70 kDa protein 2) (HSP70-2) (HSP70.2)
[HSP90AB1 HSP90B HSPC2 HSPCB] Heat shock protein HSP 90-beta (HSP 90) (Heat shock 84 kDa) (HSP 84) (HSP84)
[Hsp90ab1 Hsp84 Hspcb] Heat shock protein HSP 90-beta (Heat shock 84 kDa) (HSP 84) (HSP84)
[Hspa5 Grp78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[Hspb1 Hsp27] Heat shock protein beta-1 (HspB1) (Heat shock 27 kDa protein) (HSP 27)
[rpoH fam hin htpR b3461 JW3426] RNA polymerase sigma factor RpoH (Heat shock regulatory protein F33.4) (RNA polymerase sigma-32 factor)
[CLPB1 HSP101 Os05g0519700 LOC_Os05g44340 OsJ_19232 P0483D07.3 P0599F04.13] Chaperone protein ClpB1 (ATP-dependent Clp protease ATP-binding subunit ClpB homolog 1) (Casein lytic proteinase B1) (Heat shock protein 101)
[HSP90AB1 QccE-21185] Heat shock protein HSP 90-beta
[SSB1 YG101 YDL229W] Ribosome-associated molecular chaperone SSB1 (EC 3.6.4.10) (Cold-inducible protein YG101) (Heat shock protein SSB1) (Hsp70 chaperone Ssb)
[HSP90AB1 HSPCB] Heat shock protein HSP 90-beta
[HSP90AB1 HSPCB] Heat shock protein HSP 90-beta
[dnaJ groP b0015 JW0014] Chaperone protein DnaJ (HSP40) (Heat shock protein J)
[HSP90AB1 HSPCB] Heat shock protein HSP 90-beta
[Hsp90aa1 Hsp86 Hsp86-1 Hspca] Heat shock protein HSP 90-alpha (EC 3.6.4.10) (Heat shock 86 kDa) (HSP 86) (HSP86) (Tumor-specific transplantation 86 kDa antigen) (TSTA)

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