ID   SIS1_YEAST              Reviewed;         352 AA.
AC   P25294; D6W1H0;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   27-MAR-2024, entry version 215.
DE   RecName: Full=Protein SIS1;
GN   Name=SIS1; OrderedLocusNames=YNL007C; ORFNames=N2879;
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 [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=1714460; DOI=10.1083/jcb.114.4.623;
RA   Luke M.M., Sutton A., Arndt K.T.;
RT   "Characterization of SIS1, a Saccharomyces cerevisiae homologue of
RT   bacterial dnaJ proteins.";
RL   J. Cell Biol. 114:623-638(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [3]
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   [4]
RP   CHARACTERIZATION.
RX   PubMed=8513501; DOI=10.1016/0092-8674(93)90646-8;
RA   Zhong T., Arndt K.T.;
RT   "The yeast SIS1 protein, a DnaJ homolog, is required for the initiation of
RT   translation.";
RL   Cell 73:1175-1186(1993).
RN   [5]
RP   INTERACTION WITH SSA1.
RX   PubMed=11279042; DOI=10.1074/jbc.m100266200;
RA   Horton L.E., James P., Craig E.A., Hensold J.O.;
RT   "The yeast hsp70 homologue Ssa is required for translation and interacts
RT   with Sis1 and Pab1 on translating ribosomes.";
RL   J. Biol. Chem. 276:14426-14433(2001).
RN   [6]
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   [7]
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   [8]
RP   IDENTIFICATION BY 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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Required for nuclear migration during mitosis. It is required
CC       for the normal initiation of translation. Might mediate the
CC       dissociation of a specific protein complex of the translation
CC       machinery. Essential for viability.
CC   -!- SUBUNIT: Interacts with polyadenylate-binding protein PAB1.
CC       {ECO:0000269|PubMed:11279042}.
CC   -!- INTERACTION:
CC       P25294; P25367: RNQ1; NbExp=2; IntAct=EBI-17244, EBI-21708;
CC       P25294; P10591: SSA1; NbExp=4; IntAct=EBI-17244, EBI-8591;
CC       P25294; P10592: SSA2; NbExp=2; IntAct=EBI-17244, EBI-8603;
CC       P25294; P32589: SSE1; NbExp=2; IntAct=EBI-17244, EBI-8648;
CC       P25294; Q7LKB1: SUP35; Xeno; NbExp=3; IntAct=EBI-17244, EBI-8411471;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000269|PubMed:14562095}. Note=Localized throughout the cell but
CC       is more concentrated at the nucleus.
CC   -!- MISCELLANEOUS: Present with 20300 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
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DR   EMBL; X58460; CAA41366.1; -; Genomic_DNA.
DR   EMBL; Z71283; CAA95866.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10536.1; -; Genomic_DNA.
DR   PIR; A39660; A39660.
DR   RefSeq; NP_014391.1; NM_001182846.1.
DR   PDB; 1C3G; X-ray; 2.70 A; A=180-349.
DR   PDB; 2B26; X-ray; 3.20 A; A/B/C=181-352.
DR   PDB; 4RWU; X-ray; 1.25 A; A=1-89.
DR   PDB; 6D6X; NMR; -; A=2-81.
DR   PDB; 8EOD; NMR; -; A=2-81.
DR   PDBsum; 1C3G; -.
DR   PDBsum; 2B26; -.
DR   PDBsum; 4RWU; -.
DR   PDBsum; 6D6X; -.
DR   PDBsum; 8EOD; -.
DR   AlphaFoldDB; P25294; -.
DR   SMR; P25294; -.
DR   BioGRID; 35818; 317.
DR   DIP; DIP-4385N; -.
DR   IntAct; P25294; 29.
DR   MINT; P25294; -.
DR   STRING; 4932.YNL007C; -.
DR   TCDB; 3.A.16.1.6; the endoplasmic reticular retrotranslocon (er-rt) family.
DR   iPTMnet; P25294; -.
DR   MaxQB; P25294; -.
DR   PaxDb; 4932-YNL007C; -.
DR   PeptideAtlas; P25294; -.
DR   EnsemblFungi; YNL007C_mRNA; YNL007C; YNL007C.
DR   GeneID; 855725; -.
DR   KEGG; sce:YNL007C; -.
DR   AGR; SGD:S000004952; -.
DR   SGD; S000004952; SIS1.
DR   VEuPathDB; FungiDB:YNL007C; -.
DR   eggNOG; KOG0714; Eukaryota.
DR   GeneTree; ENSGT00940000176484; -.
DR   HOGENOM; CLU_017633_0_0_1; -.
DR   InParanoid; P25294; -.
DR   OMA; KQDPPIT; -.
DR   OrthoDB; 2785358at2759; -.
DR   BioCyc; YEAST:G3O-33049-MONOMER; -.
DR   Reactome; R-SCE-3371453; Regulation of HSF1-mediated heat shock response.
DR   Reactome; R-SCE-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR   Reactome; R-SCE-3371568; Attenuation phase.
DR   Reactome; R-SCE-3371571; HSF1-dependent transactivation.
DR   BioGRID-ORCS; 855725; 2 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P25294; -.
DR   PRO; PR:P25294; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P25294; Protein.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0051787; F:misfolded protein binding; IDA:SGD.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR   GO; GO:0070843; P:misfolded protein transport; IMP:SGD.
DR   GO; GO:0072671; P:mitochondria-associated ubiquitin-dependent protein catabolic process; IMP:SGD.
DR   GO; GO:0071630; P:nuclear protein quality control by the ubiquitin-proteasome system; IMP:SGD.
DR   GO; GO:0006457; P:protein folding; IDA:SGD.
DR   GO; GO:0006413; P:translational initiation; IMP:SGD.
DR   GO; GO:0035719; P:tRNA import into nucleus; IMP:SGD.
DR   CDD; cd06257; DnaJ; 1.
DR   CDD; cd10747; DnaJ_C; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2.
DR   InterPro; IPR002939; DnaJ_C.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR   InterPro; IPR036869; J_dom_sf.
DR   PANTHER; PTHR24078; DNAJ HOMOLOG SUBFAMILY C MEMBER; 1.
DR   PANTHER; PTHR24078:SF538; PROTEIN SIS1; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF01556; DnaJ_C; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Chaperone; Cytoplasm; DNA-binding; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..352
FT                   /note="Protein SIS1"
FT                   /id="PRO_0000071090"
FT   DOMAIN          4..70
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   REGION          300..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         275
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   HELIX           6..11
FT                   /evidence="ECO:0007829|PDB:4RWU"
FT   HELIX           19..33
FT                   /evidence="ECO:0007829|PDB:4RWU"
FT   HELIX           42..55
FT                   /evidence="ECO:0007829|PDB:4RWU"
FT   HELIX           58..67
FT                   /evidence="ECO:0007829|PDB:4RWU"
FT   HELIX           69..73
FT                   /evidence="ECO:0007829|PDB:4RWU"
FT   STRAND          181..188
FT                   /evidence="ECO:0007829|PDB:1C3G"
FT   HELIX           190..195
FT                   /evidence="ECO:0007829|PDB:1C3G"
FT   STRAND          198..207
FT                   /evidence="ECO:0007829|PDB:1C3G"
FT   TURN            208..210
FT                   /evidence="ECO:0007829|PDB:1C3G"
FT   STRAND          211..220
FT                   /evidence="ECO:0007829|PDB:1C3G"
FT   STRAND          230..235
FT                   /evidence="ECO:0007829|PDB:1C3G"
FT   STRAND          237..239
FT                   /evidence="ECO:0007829|PDB:1C3G"
FT   STRAND          241..244
FT                   /evidence="ECO:0007829|PDB:1C3G"
FT   STRAND          248..255
FT                   /evidence="ECO:0007829|PDB:1C3G"
FT   STRAND          259..264
FT                   /evidence="ECO:0007829|PDB:1C3G"
FT   STRAND          267..272
FT                   /evidence="ECO:0007829|PDB:1C3G"
FT   HELIX           276..281
FT                   /evidence="ECO:0007829|PDB:1C3G"
FT   STRAND          283..288
FT                   /evidence="ECO:0007829|PDB:1C3G"
FT   STRAND          290..292
FT                   /evidence="ECO:0007829|PDB:1C3G"
FT   STRAND          294..301
FT                   /evidence="ECO:0007829|PDB:1C3G"
FT   STRAND          308..310
FT                   /evidence="ECO:0007829|PDB:1C3G"
FT   STRAND          319..321
FT                   /evidence="ECO:0007829|PDB:2B26"
FT   STRAND          328..332
FT                   /evidence="ECO:0007829|PDB:1C3G"
FT   HELIX           344..347
FT                   /evidence="ECO:0007829|PDB:1C3G"
SQ   SEQUENCE   352 AA;  37590 MW;  642D3709C0FD5682 CRC64;
     MVKETKLYDL LGVSPSANEQ ELKKGYRKAA LKYHPDKPTG DTEKFKEISE AFEILNDPQK
     REIYDQYGLE AARSGGPSFG PGGPGGAGGA GGFPGGAGGF SGGHAFSNED AFNIFSQFFG
     GSSPFGGADD SGFSFSSYPS GGGAGMGGMP GGMGGMHGGM GGMPGGFRSA SSSPTYPEEE
     TVQVNLPVSL EDLFVGKKKS FKIGRKGPHG ASEKTQIDIQ LKPGWKAGTK ITYKNQGDYN
     PQTGRRKTLQ FVIQEKSHPN FKRDGDDLIY TLPLSFKESL LGFSKTIQTI DGRTLPLSRV
     QPVQPSQTST YPGQGMPTPK NPSQRGNLIV KYKVDYPISL NDAQKRAIDE NF
//