ID   HS104_YEAST             Reviewed;         908 AA.
AC   P31539;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   25-NOV-2008, entry version 81.
DE   RecName: Full=Heat shock protein 104;
GN   Name=HSP104; OrderedLocusNames=YLL026W; ORFNames=L0948;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 26109 / X2180;
RX   MEDLINE=91375541; PubMed=1896074; DOI=10.1038/353270a0;
RA   Parsell D.A., Sanchez Y., Stitzel J.D., Lindquist S.;
RT   "Hsp104 is a highly conserved protein with two essential nucleotide-
RT   binding sites.";
RL   Nature 353:270-273(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   MEDLINE=97313267; PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
RA   Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
RA   Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
RA   Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
RA   Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
RA   Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
RA   Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
RA   Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
RA   Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
RA   Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
RA   Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
RA   Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 749-908.
RC   STRAIN=ATCC 204508 / S288c;
RX   MEDLINE=97197984; PubMed=9046100;
RX   DOI=10.1002/(SICI)1097-0061(199702)13:2<183::AID-YEA65>3.3.CO;2-M;
RA   Purnelle B., Goffeau A.;
RT   "The sequence of 32kb on the left arm of yeast chromosome XII reveals
RT   six known genes, a new member of the seripauperins family and a new
RT   ABC transporter homologous to the human multidrug resistance
RT   protein.";
RL   Yeast 13:183-188(1997).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-620, AND MASS
RP   SPECTROMETRY.
RX   PubMed=14557538; DOI=10.1073/pnas.2135500100;
RA   Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
RT   "A subset of membrane-associated proteins is ubiquitinated in response
RT   to mutations in the endoplasmic reticulum degradation machinery.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, AND MASS
RP   SPECTROMETRY.
RX   PubMed=17563356; DOI=10.1073/pnas.0701622104;
RA   Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
RT   "Proteome-wide identification of in vivo targets of DNA damage
RT   checkpoint kinases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-87; SER-155; THR-162;
RP   SER-206; SER-306; THR-499; SER-535; SER-577; SER-578 AND SER-768, AND
RP   MASS SPECTROMETRY.
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: Vital for tolerance to heat, ethanol and other stresses.
CC   -!- INTERACTION:
CC       P39940:RSP5; NbExp=1; IntAct=EBI-8050, EBI-16219;
CC       P40318:SSM4; NbExp=1; IntAct=EBI-8050, EBI-18208;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- MISCELLANEOUS: Present with 32800 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the clpA/clpB family.
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DR   EMBL; M67479; AAA50477.1; -; Genomic_DNA.
DR   EMBL; Z73131; CAA97475.1; -; Genomic_DNA.
DR   EMBL; Z73130; CAA97474.1; -; Genomic_DNA.
DR   EMBL; AY693002; AAT93021.1; -; Genomic_DNA.
DR   EMBL; X97560; CAA66164.1; -; Genomic_DNA.
DR   PIR; S61476; S61476.
DR   RefSeq; NP_013074.1; -.
DR   HSSP; P03815; 1JBK.
DR   DIP; DIP:2252N; -.
DR   IntAct; P31539; -.
DR   SWISS-2DPAGE; P31539; -.
DR   PeptideAtlas; P31539; -.
DR   Ensembl; YLL026W; Saccharomyces cerevisiae.
DR   GeneID; 850633; -.
DR   GenomeReviews; Y13138_GR; YLL026W.
DR   KEGG; sce:YLL026W; -.
DR   NMPDR; fig|4932.3.peg.4065; -.
DR   CYGD; YLL026w; -.
DR   SGD; S000003949; HSP104.
DR   HOGENOM; P31539; -.
DR   LinkHub; P31539; -.
DR   NextBio; 966553; -.
DR   ArrayExpress; P31539; -.
DR   GermOnline; YLL026W; Saccharomyces cerevisiae.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0042623; F:ATPase activity, coupled; IDA:SGD.
DR   GO; GO:0051087; F:chaperone binding; IDA:SGD.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein folding; IDA:SGD.
DR   GO; GO:0042026; P:protein refolding; IDA:SGD.
DR   GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR   InterPro; IPR003593; AAA+_ATPase_core.
DR   InterPro; IPR003959; AAA_ATPase_core.
DR   InterPro; IPR013093; ATPase_AAA-2.
DR   InterPro; IPR001270; Chaprnin_clpA/B.
DR   InterPro; IPR004176; Clp_N.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF02861; Clp_N; 2.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Repeat; Stress response;
KW   Ubl conjugation.
FT   CHAIN         1    908       Heat shock protein 104.
FT                                /FTId=PRO_0000191212.
FT   NP_BIND     212    219       ATP (Potential).
FT   NP_BIND     614    621       ATP (Potential).
FT   REGION      167    411       I.
FT   REGION      541    731       II.
FT   MOD_RES      87     87       Phosphothreonine.
FT   MOD_RES     155    155       Phosphoserine.
FT   MOD_RES     162    162       Phosphothreonine.
FT   MOD_RES     206    206       Phosphoserine.
FT   MOD_RES     306    306       Phosphoserine.
FT   MOD_RES     499    499       Phosphothreonine.
FT   MOD_RES     535    535       Phosphoserine.
FT   MOD_RES     577    577       Phosphoserine.
FT   MOD_RES     578    578       Phosphoserine.
FT   MOD_RES     768    768       Phosphoserine.
FT   CROSSLNK    620    620       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
SQ   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
//