SIS1_YEAST
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 03-AUG-2022, entry version 206.
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 PDBsum; 1C3G; -.
DR PDBsum; 2B26; -.
DR PDBsum; 4RWU; -.
DR PDBsum; 6D6X; -.
DR AlphaFoldDB; P25294; -.
DR SMR; P25294; -.
DR BioGRID; 35818; 289.
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; P25294; -.
DR PRIDE; P25294; -.
DR EnsemblFungi; YNL007C_mRNA; YNL007C; YNL007C.
DR GeneID; 855725; -.
DR KEGG; sce:YNL007C; -.
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; IVHPGMK; -.
DR BioCyc; YEAST:G3O-33049-MON; -.
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 Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
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:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051787; F:misfolded protein binding; IDA:SGD.
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 Gene3D; 1.10.287.110; -; 1.
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 Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF49493; SSF49493; 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
