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P25294

- SIS1_YEAST

UniProt

P25294 - SIS1_YEAST

Protein

Protein SIS1

Gene

SIS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 1 (01 May 1992)
      Previous versions | rss
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    Functioni

    Required for nuclear migration during mitosis. It is required for the normal initiation of translation. Might mediate the dissociation of a specific protein complex of the translation machinery. Essential for viability.

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. misfolded protein binding Source: SGD
    3. protein binding Source: IntAct

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. misfolded protein transport Source: SGD
    3. nucleus-associated proteasomal ubiquitin-dependent protein catabolic process Source: SGD
    4. protein folding Source: SGD
    5. translational initiation Source: SGD

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Cell cycle

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33049-MONOMER.
    ReactomeiREACT_219346. HSF1-dependent transactivation.
    REACT_221137. Attenuation phase.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein SIS1
    Gene namesi
    Name:SIS1
    Ordered Locus Names:YNL007C
    ORF Names:N2879
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIV

    Organism-specific databases

    CYGDiYNL007c.
    SGDiS000004952. SIS1.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Localized throughout the cell but is more concentrated at the nucleus.

    GO - Cellular componenti

    1. cytosolic small ribosomal subunit Source: SGD
    2. nucleus Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 352352Protein SIS1PRO_0000071090Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei275 – 2751Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP25294.
    PaxDbiP25294.
    PeptideAtlasiP25294.

    Expressioni

    Gene expression databases

    GenevestigatoriP25294.

    Interactioni

    Subunit structurei

    Interacts with polyadenylate-binding protein PAB1.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SSA1P105913EBI-17244,EBI-8591
    SUP35Q7LKB13EBI-17244,EBI-8411471From a different organism.

    Protein-protein interaction databases

    BioGridi35818. 70 interactions.
    DIPiDIP-4385N.
    IntActiP25294. 19 interactions.
    MINTiMINT-472083.
    STRINGi4932.YNL007C.

    Structurei

    Secondary structure

    1
    352
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 116
    Helixi19 – 3315
    Helixi42 – 5514
    Helixi58 – 6710
    Helixi69 – 735
    Beta strandi181 – 1888
    Helixi190 – 1956
    Beta strandi198 – 20710
    Turni208 – 2103
    Beta strandi211 – 22010
    Beta strandi230 – 2356
    Beta strandi237 – 2393
    Beta strandi241 – 2444
    Beta strandi248 – 2558
    Beta strandi259 – 2646
    Beta strandi267 – 2726
    Helixi276 – 2816
    Beta strandi283 – 2886
    Beta strandi290 – 2923
    Beta strandi294 – 3018
    Beta strandi308 – 3103
    Beta strandi319 – 3213
    Beta strandi328 – 3325
    Helixi344 – 3474

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1C3GX-ray2.70A180-349[»]
    2B26X-ray3.20A/B/C181-352[»]
    2O37X-ray1.25A1-89[»]
    ProteinModelPortaliP25294.
    SMRiP25294. Positions 1-81, 180-349.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP25294.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 7067JPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi75 – 16692Gly-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 J domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0484.
    GeneTreeiENSGT00730000110742.
    HOGENOMiHOG000226718.
    OMAiYKVDYPI.
    OrthoDBiEOG7SFJ7D.

    Family and domain databases

    Gene3Di1.10.287.110. 1 hit.
    InterProiIPR002939. DnaJ_C.
    IPR001623. DnaJ_domain.
    IPR018253. DnaJ_domain_CS.
    IPR008971. HSP40/DnaJ_pept-bd.
    [Graphical view]
    PfamiPF01556. CTDII. 1 hit.
    PF00226. DnaJ. 1 hit.
    [Graphical view]
    PRINTSiPR00625. JDOMAIN.
    SMARTiSM00271. DnaJ. 1 hit.
    [Graphical view]
    SUPFAMiSSF46565. SSF46565. 1 hit.
    SSF49493. SSF49493. 2 hits.
    PROSITEiPS00636. DNAJ_1. 1 hit.
    PS50076. DNAJ_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P25294-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVKETKLYDL LGVSPSANEQ ELKKGYRKAA LKYHPDKPTG DTEKFKEISE    50
    AFEILNDPQK REIYDQYGLE AARSGGPSFG PGGPGGAGGA GGFPGGAGGF 100
    SGGHAFSNED AFNIFSQFFG GSSPFGGADD SGFSFSSYPS GGGAGMGGMP 150
    GGMGGMHGGM GGMPGGFRSA SSSPTYPEEE TVQVNLPVSL EDLFVGKKKS 200
    FKIGRKGPHG ASEKTQIDIQ LKPGWKAGTK ITYKNQGDYN PQTGRRKTLQ 250
    FVIQEKSHPN FKRDGDDLIY TLPLSFKESL LGFSKTIQTI DGRTLPLSRV 300
    QPVQPSQTST YPGQGMPTPK NPSQRGNLIV KYKVDYPISL NDAQKRAIDE 350
    NF 352
    Length:352
    Mass (Da):37,590
    Last modified:May 1, 1992 - v1
    Checksum:i642D3709C0FD5682
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58460 Genomic DNA. Translation: CAA41366.1.
    Z71283 Genomic DNA. Translation: CAA95866.1.
    BK006947 Genomic DNA. Translation: DAA10536.1.
    PIRiA39660.
    RefSeqiNP_014391.1. NM_001182846.1.

    Genome annotation databases

    EnsemblFungiiYNL007C; YNL007C; YNL007C.
    GeneIDi855725.
    KEGGisce:YNL007C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58460 Genomic DNA. Translation: CAA41366.1 .
    Z71283 Genomic DNA. Translation: CAA95866.1 .
    BK006947 Genomic DNA. Translation: DAA10536.1 .
    PIRi A39660.
    RefSeqi NP_014391.1. NM_001182846.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1C3G X-ray 2.70 A 180-349 [» ]
    2B26 X-ray 3.20 A/B/C 181-352 [» ]
    2O37 X-ray 1.25 A 1-89 [» ]
    ProteinModelPortali P25294.
    SMRi P25294. Positions 1-81, 180-349.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35818. 70 interactions.
    DIPi DIP-4385N.
    IntActi P25294. 19 interactions.
    MINTi MINT-472083.
    STRINGi 4932.YNL007C.

    Proteomic databases

    MaxQBi P25294.
    PaxDbi P25294.
    PeptideAtlasi P25294.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YNL007C ; YNL007C ; YNL007C .
    GeneIDi 855725.
    KEGGi sce:YNL007C.

    Organism-specific databases

    CYGDi YNL007c.
    SGDi S000004952. SIS1.

    Phylogenomic databases

    eggNOGi COG0484.
    GeneTreei ENSGT00730000110742.
    HOGENOMi HOG000226718.
    OMAi YKVDYPI.
    OrthoDBi EOG7SFJ7D.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-33049-MONOMER.
    Reactomei REACT_219346. HSF1-dependent transactivation.
    REACT_221137. Attenuation phase.

    Miscellaneous databases

    EvolutionaryTracei P25294.
    NextBioi 980096.
    PROi P25294.

    Gene expression databases

    Genevestigatori P25294.

    Family and domain databases

    Gene3Di 1.10.287.110. 1 hit.
    InterProi IPR002939. DnaJ_C.
    IPR001623. DnaJ_domain.
    IPR018253. DnaJ_domain_CS.
    IPR008971. HSP40/DnaJ_pept-bd.
    [Graphical view ]
    Pfami PF01556. CTDII. 1 hit.
    PF00226. DnaJ. 1 hit.
    [Graphical view ]
    PRINTSi PR00625. JDOMAIN.
    SMARTi SM00271. DnaJ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46565. SSF46565. 1 hit.
    SSF49493. SSF49493. 2 hits.
    PROSITEi PS00636. DNAJ_1. 1 hit.
    PS50076. DNAJ_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of SIS1, a Saccharomyces cerevisiae homologue of bacterial dnaJ proteins."
      Luke M.M., Sutton A., Arndt K.T.
      J. Cell Biol. 114:623-638(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
      Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
      , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
      Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "The yeast SIS1 protein, a DnaJ homolog, is required for the initiation of translation."
      Zhong T., Arndt K.T.
      Cell 73:1175-1186(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    5. "The yeast hsp70 homologue Ssa is required for translation and interacts with Sis1 and Pab1 on translating ribosomes."
      Horton L.E., James P., Craig E.A., Hensold J.O.
      J. Biol. Chem. 276:14426-14433(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SSA1.
    6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSIS1_YEAST
    AccessioniPrimary (citable) accession number: P25294
    Secondary accession number(s): D6W1H0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: May 1, 1992
    Last modified: October 1, 2014
    This is version 143 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 20300 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XIV
      Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

    External Data

    Dasty 3