ID HSP7F_YEAST Reviewed; 693 AA. AC P32589; D6W3R1; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 27-MAR-2024, entry version 217. DE RecName: Full=Heat shock protein homolog SSE1; DE AltName: Full=Chaperone protein MSI3; GN Name=SSE1; Synonyms=MSI3; OrderedLocusNames=YPL106C; ORFNames=LPG3C; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=ATCC 204626 / S288c / A364A; RX PubMed=8406043; DOI=10.1016/0378-1119(93)90514-4; RA Mukai H., Kuno T., Tanaka H., Hirata D., Miyakawa T., Tanaka C.; RT "Isolation and characterization of SSE1 and SSE2, new members of the yeast RT HSP70 multigene family."; RL Gene 132:57-66(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8413180; DOI=10.1007/bf00280382; RA Shirayama M., Kawakami K., Matsui Y., Tanaka K., Toh-e A.; RT "MSI3, a multicopy suppressor of mutants hyperactivated in the RAS-cAMP RT pathway, encodes a novel HSP70 protein of Saccharomyces cerevisiae."; RL Mol. Gen. Genet. 240:323-332(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169875; RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., RA Vo D.H., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."; RL Nature 387:103-105(1997). RN [4] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [5] RP PROTEIN SEQUENCE OF 100-110. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7895733; DOI=10.1002/elps.11501501210; RA Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., RA Volpe T., Warner J.R., McLaughlin C.S.; RT "Protein identifications for a Saccharomyces cerevisiae protein database."; RL Electrophoresis 15:1466-1486(1994). RN [6] RP PROTEIN SEQUENCE OF 330-339. RC STRAIN=ATCC 38531 / Y41; RX PubMed=8935650; DOI=10.1111/j.1574-6968.1996.tb08073.x; RA Norbeck J., Blomberg A.; RT "Protein expression during exponential growth in 0.7 M NaCl medium of RT Saccharomyces cerevisiae."; RL FEMS Microbiol. Lett. 137:1-8(1996). RN [7] RP ACETYLATION AT SER-2. RX PubMed=9298649; DOI=10.1002/elps.1150180810; RA Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., RA Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R., RA Payne W.E.; RT "Proteome studies of Saccharomyces cerevisiae: identification and RT characterization of abundant proteins."; RL Electrophoresis 18:1347-1360(1997). RN [8] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [9] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-242, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17287358; DOI=10.1073/pnas.0607084104; RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; RT "Analysis of phosphorylation sites on proteins from Saccharomyces RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-660, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [12] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-195, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22106047; DOI=10.1002/pmic.201100166; RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.; RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae."; RL Proteomics 12:236-240(2012). CC -!- FUNCTION: Has a calcium-dependent calmodulin-binding activity. Required CC for normal growth at various temperatures. CC -!- INTERACTION: CC P32589; P02829: HSP82; NbExp=3; IntAct=EBI-8648, EBI-8659; CC P32589; P25294: SIS1; NbExp=2; IntAct=EBI-8648, EBI-17244; CC P32589; P10591: SSA1; NbExp=8; IntAct=EBI-8648, EBI-8591; CC P32589; P11484: SSB1; NbExp=2; IntAct=EBI-8648, EBI-8627; CC P32589; P08107: HSPA1B; Xeno; NbExp=2; IntAct=EBI-8648, EBI-629985; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. CC -!- INDUCTION: Increases a few-fold upon upshift to 37 degrees Celsius. CC -!- MISCELLANEOUS: Present with 71700 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D13319; BAA02576.1; -; mRNA. DR EMBL; D38368; BAA07449.1; -; mRNA. DR EMBL; D38370; BAA07451.1; -; Genomic_DNA. DR EMBL; D13743; BAA02888.1; -; Genomic_DNA. DR EMBL; U43281; AAB68194.1; -; Genomic_DNA. DR EMBL; BK006949; DAA11327.1; -; Genomic_DNA. DR PIR; S46417; S46417. DR RefSeq; NP_015219.1; NM_001183920.1. DR PDB; 2QXL; X-ray; 2.41 A; A/B=2-659. DR PDB; 3C7N; X-ray; 3.12 A; A=1-666. DR PDB; 3D2E; X-ray; 2.35 A; A/C=1-502, A/C=525-693. DR PDB; 3D2F; X-ray; 2.30 A; A/C=1-502, A/C=525-693. DR PDBsum; 2QXL; -. DR PDBsum; 3C7N; -. DR PDBsum; 3D2E; -. DR PDBsum; 3D2F; -. DR AlphaFoldDB; P32589; -. DR SMR; P32589; -. DR BioGRID; 36075; 699. DR DIP; DIP-6645N; -. DR IntAct; P32589; 127. DR MINT; P32589; -. DR STRING; 4932.YPL106C; -. DR CarbonylDB; P32589; -. DR iPTMnet; P32589; -. DR MaxQB; P32589; -. DR PaxDb; 4932-YPL106C; -. DR PeptideAtlas; P32589; -. DR EnsemblFungi; YPL106C_mRNA; YPL106C; YPL106C. DR GeneID; 855998; -. DR KEGG; sce:YPL106C; -. DR AGR; SGD:S000006027; -. DR SGD; S000006027; SSE1. DR VEuPathDB; FungiDB:YPL106C; -. DR eggNOG; KOG0103; Eukaryota. DR GeneTree; ENSGT00940000168707; -. DR HOGENOM; CLU_005965_5_1_1; -. DR InParanoid; P32589; -. DR OMA; WEQSPEI; -. DR OrthoDB; 276440at2759; -. DR BioCyc; YEAST:G3O-34008-MONOMER; -. DR BioGRID-ORCS; 855998; 2 hits in 10 CRISPR screens. DR EvolutionaryTrace; P32589; -. DR PRO; PR:P32589; -. DR Proteomes; UP000002311; Chromosome XVI. DR RNAct; P32589; Protein. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IDA:SGD. DR GO; GO:0005524; F:ATP binding; IDA:SGD. DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro. DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW. DR GO; GO:0042277; F:peptide binding; IDA:SGD. DR GO; GO:0006914; P:autophagy; IMP:SGD. DR GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IGI:SGD. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IGI:SGD. DR GO; GO:0006457; P:protein folding; IMP:SGD. DR GO; GO:0042026; P:protein refolding; IDA:SGD. DR CDD; cd11732; HSP105-110_like_NBD; 1. DR Gene3D; 1.20.1270.10; -; 1. DR Gene3D; 3.30.30.30; -; 1. DR Gene3D; 3.30.420.40; -; 2. DR InterPro; IPR043129; ATPase_NBD. DR InterPro; IPR018181; Heat_shock_70_CS. DR InterPro; IPR029048; HSP70_C_sf. DR InterPro; IPR029047; HSP70_peptide-bd_sf. DR InterPro; IPR013126; Hsp_70_fam. DR PANTHER; PTHR45639:SF4; HSC70CB, ISOFORM G; 1. DR PANTHER; PTHR45639; HSC70CB, ISOFORM G-RELATED; 1. DR Pfam; PF00012; HSP70; 1. DR PRINTS; PR00301; HEATSHOCK70. DR SUPFAM; SSF53067; Actin-like ATPase domain; 2. DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1. DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1. DR PROSITE; PS00329; HSP70_2; 1. DR PROSITE; PS01036; HSP70_3; 1. DR SWISS-2DPAGE; P32589; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP-binding; Calmodulin-binding; Chaperone; KW Cytoplasm; Direct protein sequencing; Isopeptide bond; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Stress response; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:9298649" FT CHAIN 2..693 FT /note="Heat shock protein homolog SSE1" FT /id="PRO_0000078396" FT REGION 653..693 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 671..693 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000269|PubMed:9298649" FT MOD_RES 242 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17287358" FT MOD_RES 660 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT CROSSLNK 195 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT CONFLICT 269..270 FT /note="TA -> NT (in Ref. 1; BAA02576/BAA07449)" FT /evidence="ECO:0000305" FT STRAND 5..8 FT /evidence="ECO:0007829|PDB:3D2F" FT STRAND 11..20 FT /evidence="ECO:0007829|PDB:3D2F" FT STRAND 23..27 FT /evidence="ECO:0007829|PDB:3D2F" FT STRAND 34..37 FT /evidence="ECO:0007829|PDB:3D2F" FT STRAND 40..42 FT /evidence="ECO:0007829|PDB:3D2F" FT STRAND 44..49 FT /evidence="ECO:0007829|PDB:3D2F" FT HELIX 51..57 FT /evidence="ECO:0007829|PDB:3D2F" FT HELIX 61..63 FT /evidence="ECO:0007829|PDB:3D2F" FT HELIX 68..71 FT /evidence="ECO:0007829|PDB:3D2F" FT HELIX 81..85 FT /evidence="ECO:0007829|PDB:3D2F" FT STRAND 90..94 FT /evidence="ECO:0007829|PDB:3D2F" FT STRAND 98..106 FT /evidence="ECO:0007829|PDB:3D2F" FT STRAND 109..114 FT /evidence="ECO:0007829|PDB:3D2F" FT HELIX 115..134 FT /evidence="ECO:0007829|PDB:3D2F" FT STRAND 140..145 FT /evidence="ECO:0007829|PDB:3D2F" FT HELIX 151..163 FT /evidence="ECO:0007829|PDB:3D2F" FT STRAND 167..173 FT /evidence="ECO:0007829|PDB:3D2F" FT HELIX 174..185 FT /evidence="ECO:0007829|PDB:3D2F" FT STRAND 192..194 FT /evidence="ECO:0007829|PDB:3D2F" FT STRAND 197..204 FT /evidence="ECO:0007829|PDB:3D2F" FT STRAND 209..217 FT /evidence="ECO:0007829|PDB:3D2F" FT STRAND 220..229 FT /evidence="ECO:0007829|PDB:3D2F" FT HELIX 234..252 FT /evidence="ECO:0007829|PDB:3D2F" FT HELIX 257..259 FT /evidence="ECO:0007829|PDB:3D2F" FT HELIX 261..280 FT /evidence="ECO:0007829|PDB:3D2F" FT STRAND 282..288 FT /evidence="ECO:0007829|PDB:3D2F" FT STRAND 291..294 FT /evidence="ECO:0007829|PDB:3D2F" FT STRAND 297..302 FT /evidence="ECO:0007829|PDB:3D2F" FT HELIX 303..309 FT /evidence="ECO:0007829|PDB:3D2F" FT HELIX 311..314 FT /evidence="ECO:0007829|PDB:3D2F" FT TURN 315..318 FT /evidence="ECO:0007829|PDB:3D2F" FT HELIX 319..328 FT /evidence="ECO:0007829|PDB:3D2F" FT HELIX 332..334 FT /evidence="ECO:0007829|PDB:3D2F" FT STRAND 337..342 FT /evidence="ECO:0007829|PDB:3D2F" FT HELIX 343..346 FT /evidence="ECO:0007829|PDB:3D2F" FT HELIX 348..358 FT /evidence="ECO:0007829|PDB:3D2F" FT TURN 368..370 FT /evidence="ECO:0007829|PDB:3D2F" FT HELIX 371..382 FT /evidence="ECO:0007829|PDB:3D2F" FT STRAND 385..387 FT /evidence="ECO:0007829|PDB:2QXL" FT STRAND 393..398 FT /evidence="ECO:0007829|PDB:3D2F" FT STRAND 402..406 FT /evidence="ECO:0007829|PDB:3D2F" FT STRAND 414..419 FT /evidence="ECO:0007829|PDB:3D2F" FT STRAND 423..437 FT /evidence="ECO:0007829|PDB:3D2F" FT STRAND 439..446 FT /evidence="ECO:0007829|PDB:3D2F" FT HELIX 448..450 FT /evidence="ECO:0007829|PDB:3D2F" FT STRAND 457..465 FT /evidence="ECO:0007829|PDB:3D2F" FT STRAND 476..484 FT /evidence="ECO:0007829|PDB:3D2F" FT STRAND 490..498 FT /evidence="ECO:0007829|PDB:3D2F" FT STRAND 505..507 FT /evidence="ECO:0007829|PDB:3C7N" FT STRAND 520..522 FT /evidence="ECO:0007829|PDB:3C7N" FT STRAND 529..532 FT /evidence="ECO:0007829|PDB:3D2F" FT STRAND 534..538 FT /evidence="ECO:0007829|PDB:3D2F" FT HELIX 544..585 FT /evidence="ECO:0007829|PDB:3D2F" FT TURN 586..589 FT /evidence="ECO:0007829|PDB:3D2F" FT HELIX 590..592 FT /evidence="ECO:0007829|PDB:3D2F" FT HELIX 595..611 FT /evidence="ECO:0007829|PDB:3D2F" FT TURN 612..614 FT /evidence="ECO:0007829|PDB:3D2F" FT HELIX 615..618 FT /evidence="ECO:0007829|PDB:3D2F" FT HELIX 621..653 FT /evidence="ECO:0007829|PDB:3D2F" SQ SEQUENCE 693 AA; 77366 MW; 6558259111B0BC38 CRC64; MSTPFGLDLG NNNSVLAVAR NRGIDIVVNE VSNRSTPSVV GFGPKNRYLG ETGKNKQTSN IKNTVANLKR IIGLDYHHPD FEQESKHFTS KLVELDDKKT GAEVRFAGEK HVFSATQLAA MFIDKVKDTV KQDTKANITD VCIAVPPWYT EEQRYNIADA ARIAGLNPVR IVNDVTAAGV SYGIFKTDLP EGEEKPRIVA FVDIGHSSYT CSIMAFKKGQ LKVLGTACDK HFGGRDFDLA ITEHFADEFK TKYKIDIREN PKAYNRILTA AEKLKKVLSA NTNAPFSVES VMNDVDVSSQ LSREELEELV KPLLERVTEP VTKALAQAKL SAEEVDFVEI IGGTTRIPTL KQSISEAFGK PLSTTLNQDE AIAKGAAFIC AIHSPTLRVR PFKFEDIHPY SVSYSWDKQV EDEDHMEVFP AGSSFPSTKL ITLNRTGDFS MAASYTDITQ LPPNTPEQIA NWEITGVQLP EGQDSVPVKL KLRCDPSGLH TIEEAYTIED IEVEEPIPLP EDAPEDAEQE FKKVTKTVKK DDLTIVAHTF GLDAKKLNEL IEKENEMLAQ DKLVAETEDR KNTLEEYIYT LRGKLEEEYA PFASDAEKTK LQGMLNKAEE WLYDEGFDSI KAKYIAKYEE LASLGNIIRG RYLAKEEEKK QAIRSKQEAS QMAAMAEKLA AQRKAEAEKK EEKKDTEGDV DMD //