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P11484

- HSP75_YEAST

UniProt

P11484 - HSP75_YEAST

Protein

Heat shock protein SSB1

Gene

SSB1

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 147 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    May aid in the passage of the nascent polypeptide chain through the ribosome channel into the cytosol. Such an interaction could be crucial for continuous transport of the polypeptide; could serve to prevent the nascent polypeptide from interfering with translation by clogging the ribosome channel.1 Publication

    GO - Molecular functioni

    1. ATPase activity Source: SGD
    2. ATP binding Source: UniProtKB-KW
    3. calmodulin binding Source: SGD
    4. protein binding Source: IntAct
    5. unfolded protein binding Source: SGD

    GO - Biological processi

    1. 'de novo' cotranslational protein folding Source: SGD
    2. ATP catabolic process Source: GOC
    3. cellular response to glucose starvation Source: SGD
    4. cytoplasmic translation Source: SGD
    5. regulation of translational fidelity Source: SGD
    6. ribosomal subunit export from nucleus Source: SGD
    7. rRNA processing Source: SGD
    8. translational frameshifting Source: SGD
    9. translational termination Source: SGD

    Keywords - Biological processi

    Protein biosynthesis, Stress response

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29608-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heat shock protein SSB1
    Alternative name(s):
    Cold-inducible protein YG101
    Gene namesi
    Name:SSB1
    Synonyms:YG101
    Ordered Locus Names:YDL229W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    SGDiS000002388. SSB1.

    Subcellular locationi

    Cytoplasm
    Note: Associated with translating ribosomes, may bind directly to the nascent polypeptide.

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. polysome Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 613612Heat shock protein SSB1PRO_0000078389Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei47 – 471Phosphothreonine1 Publication
    Modified residuei431 – 4311Phosphothreonine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP11484.
    PeptideAtlasiP11484.
    PRIDEiP11484.

    2D gel databases

    COMPLUYEAST-2DPAGEP11484.
    SWISS-2DPAGEP11484.
    UCD-2DPAGEP11484.

    Expressioni

    Gene expression databases

    GenevestigatoriP11484.

    Interactioni

    Subunit structurei

    Interacts with NAP1.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BUD27P435733EBI-8627,EBI-22787
    PFK26P404332EBI-8627,EBI-1956
    SSE1P325892EBI-8627,EBI-8648

    Protein-protein interaction databases

    BioGridi31882. 623 interactions.
    DIPiDIP-2254N.
    IntActiP11484. 741 interactions.
    MINTiMINT-1325604.

    Structurei

    Secondary structure

    1
    613
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 134
    Beta strandi16 – 3015
    Beta strandi38 – 414
    Beta strandi44 – 463
    Beta strandi51 – 544
    Helixi55 – 595
    Helixi61 – 633
    Helixi65 – 673
    Helixi72 – 743
    Turni75 – 773
    Helixi83 – 897
    Beta strandi93 – 997
    Beta strandi102 – 1098
    Beta strandi112 – 1165
    Helixi118 – 13720
    Beta strandi143 – 1486
    Helixi154 – 16613
    Beta strandi170 – 1767
    Helixi177 – 1848
    Turni185 – 1906
    Beta strandi196 – 2038
    Beta strandi208 – 2169
    Beta strandi219 – 22810
    Helixi233 – 25220
    Helixi260 – 27617
    Turni277 – 2793
    Beta strandi280 – 29112
    Beta strandi294 – 3018
    Helixi302 – 3087
    Helixi310 – 3156
    Helixi317 – 32711
    Helixi331 – 3333
    Beta strandi336 – 3416
    Helixi342 – 3454
    Helixi347 – 35610
    Turni357 – 3593
    Turni368 – 3703
    Helixi371 – 38313

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3GL1X-ray1.92A/B1-384[»]
    ProteinModelPortaliP11484.
    SMRiP11484. Positions 2-601.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11484.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the heat shock protein 70 family.Curated

    Phylogenomic databases

    GeneTreeiENSGT00740000115745.
    HOGENOMiHOG000228135.
    OMAiFEEINST.
    OrthoDBiEOG728916.

    Family and domain databases

    Gene3Di1.20.1270.10. 1 hit.
    2.60.34.10. 1 hit.
    InterProiIPR018181. Heat_shock_70_CS.
    IPR029048. HSP70_C.
    IPR029047. HSP70_peptide-bd.
    IPR013126. Hsp_70_fam.
    [Graphical view]
    PfamiPF00012. HSP70. 1 hit.
    [Graphical view]
    PRINTSiPR00301. HEATSHOCK70.
    SUPFAMiSSF100920. SSF100920. 1 hit.
    SSF100934. SSF100934. 1 hit.
    PROSITEiPS00297. HSP70_1. 1 hit.
    PS00329. HSP70_2. 1 hit.
    PS01036. HSP70_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P11484-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEGVFQGAI GIDLGTTYSC VATYESSVEI IANEQGNRVT PSFVAFTPEE    50
    RLIGDAAKNQ AALNPRNTVF DAKRLIGRRF DDESVQKDMK TWPFKVIDVD 100
    GNPVIEVQYL EETKTFSPQE ISAMVLTKMK EIAEAKIGKK VEKAVITVPA 150
    YFNDAQRQAT KDAGAISGLN VLRIINEPTA AAIAYGLGAG KSEKERHVLI 200
    FDLGGGTFDV SLLHIAGGVY TVKSTSGNTH LGGQDFDTNL LEHFKAEFKK 250
    KTGLDISDDA RALRRLRTAA ERAKRTLSSV TQTTVEVDSL FDGEDFESSL 300
    TRARFEDLNA ALFKSTLEPV EQVLKDAKIS KSQIDEVVLV GGSTRIPKVQ 350
    KLLSDFFDGK QLEKSINPDE AVAYGAAVQG AILTGQSTSD ETKDLLLLDV 400
    APLSLGVGMQ GDMFGIVVPR NTTVPTIKRR TFTTCADNQT TVQFPVYQGE 450
    RVNCKENTLL GEFDLKNIPM MPAGEPVLEA IFEVDANGIL KVTAVEKSTG 500
    KSSNITISNA VGRLSSEEIE KMVNQAEEFK AADEAFAKKH EARQRLESYV 550
    ASIEQTVTDP VLSSKLKRGS KSKIEAALSD ALAALQIEDP SADELRKAEV 600
    GLKRVVTKAM SSR 613
    Length:613
    Mass (Da):66,602
    Last modified:January 23, 2007 - v3
    Checksum:iF16FA7C25A40321A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti180 – 1845AAAIA → VVVIV in AAA34692. (PubMed:6761581)Curated
    Sequence conflicti189 – 1891A → V in AAA34692. (PubMed:6761581)Curated
    Sequence conflicti192 – 1921S → F in AAA34692. (PubMed:6761581)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13713 Genomic DNA. Translation: CAA31995.1.
    M25395 mRNA. Translation: AAA35099.1.
    Z74277 Genomic DNA. Translation: CAA98807.1.
    M17585 Genomic DNA. Translation: AAA34692.1.
    BK006938 Genomic DNA. Translation: DAA11637.1.
    PIRiS20149.
    RefSeqiNP_010052.1. NM_001180289.1.

    Genome annotation databases

    EnsemblFungiiYDL229W; YDL229W; YDL229W.
    GeneIDi851369.
    KEGGisce:YDL229W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13713 Genomic DNA. Translation: CAA31995.1 .
    M25395 mRNA. Translation: AAA35099.1 .
    Z74277 Genomic DNA. Translation: CAA98807.1 .
    M17585 Genomic DNA. Translation: AAA34692.1 .
    BK006938 Genomic DNA. Translation: DAA11637.1 .
    PIRi S20149.
    RefSeqi NP_010052.1. NM_001180289.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3GL1 X-ray 1.92 A/B 1-384 [» ]
    ProteinModelPortali P11484.
    SMRi P11484. Positions 2-601.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31882. 623 interactions.
    DIPi DIP-2254N.
    IntActi P11484. 741 interactions.
    MINTi MINT-1325604.

    2D gel databases

    COMPLUYEAST-2DPAGE P11484.
    SWISS-2DPAGE P11484.
    UCD-2DPAGE P11484.

    Proteomic databases

    MaxQBi P11484.
    PeptideAtlasi P11484.
    PRIDEi P11484.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDL229W ; YDL229W ; YDL229W .
    GeneIDi 851369.
    KEGGi sce:YDL229W.

    Organism-specific databases

    SGDi S000002388. SSB1.

    Phylogenomic databases

    GeneTreei ENSGT00740000115745.
    HOGENOMi HOG000228135.
    OMAi FEEINST.
    OrthoDBi EOG728916.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29608-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P11484.
    NextBioi 968489.

    Gene expression databases

    Genevestigatori P11484.

    Family and domain databases

    Gene3Di 1.20.1270.10. 1 hit.
    2.60.34.10. 1 hit.
    InterProi IPR018181. Heat_shock_70_CS.
    IPR029048. HSP70_C.
    IPR029047. HSP70_peptide-bd.
    IPR013126. Hsp_70_fam.
    [Graphical view ]
    Pfami PF00012. HSP70. 1 hit.
    [Graphical view ]
    PRINTSi PR00301. HEATSHOCK70.
    SUPFAMi SSF100920. SSF100920. 1 hit.
    SSF100934. SSF100934. 1 hit.
    PROSITEi PS00297. HSP70_1. 1 hit.
    PS00329. HSP70_2. 1 hit.
    PS01036. HSP70_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The SSB1 heat shock cognate gene of the yeast Saccharomyces cerevisiae."
      Slater M.R., Craig E.A.
      Nucleic Acids Res. 17:4891-4891(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. "S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP."
      Normington K., Kohno K., Kozutsumi Y., Gething M.J., Sambrook J.
      Cell 57:1223-1236(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Gene linkage of two-dimensional polyacrylamide gel electrophoresis resolved proteins from isogene families in Saccharomyces cerevisiae by microsequencing of in-gel trypsin generated peptides."
      Norbeck J., Blomberg A.
      Electrophoresis 16:149-156(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 39-49 AND 431-439.
      Strain: ATCC 38531 / Y41.
    6. Cited for: PROTEIN SEQUENCE OF 145-159.
      Strain: ATCC 204508 / S288c.
    7. "Saccharomyces cerevisiae contains a complex multigene family related to the major heat shock-inducible gene of Drosophila."
      Ingolia T.D., Slater M.R., Craig E.A.
      Mol. Cell. Biol. 2:1388-1398(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 180-403.
    8. "The translation machinery and 70 kd heat shock protein cooperate in protein synthesis."
      Nelson R.J., Ziegelhoffer T., Nicolet C., Werner-Washburne M., Craig E.A.
      Cell 71:97-105(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins."
      Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R., Payne W.E.
      Electrophoresis 18:1347-1360(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT ALA-2.
    10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    11. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    12. "Phosphorylation by casein kinase 2 regulates Nap1 localization and function."
      Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F., Pemberton L.F.
      Mol. Cell. Biol. 28:1313-1325(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NAP1, IDENTIFICATION BY MASS SPECTROMETRY.
    13. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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 THR-431, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiHSP75_YEAST
    AccessioniPrimary (citable) accession number: P11484
    Secondary accession number(s): D6VRC7, Q05834
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 147 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 170000 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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 IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3