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P32589

- HSP7F_YEAST

UniProt

P32589 - HSP7F_YEAST

Protein

Heat shock protein homolog SSE1

Gene

SSE1

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 145 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Has a calcium-dependent calmodulin-binding activity. Required for normal growth at various temperatures.

    GO - Molecular functioni

    1. adenyl-nucleotide exchange factor activity Source: SGD
    2. ATP binding Source: SGD
    3. peptide binding Source: SGD
    4. protein binding Source: IntAct

    GO - Biological processi

    1. protein folding Source: SGD
    2. protein refolding Source: SGD
    3. regulation of catalytic activity Source: GOC
    4. response to stress Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Stress response

    Keywords - Ligandi

    ATP-binding, Calmodulin-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-34008-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heat shock protein homolog SSE1
    Alternative name(s):
    Chaperone protein MSI3
    Gene namesi
    Name:SSE1
    Synonyms:MSI3
    Ordered Locus Names:YPL106C
    ORF Names:LPG3C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XVI

    Organism-specific databases

    SGDiS000006027. SSE1.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. polysome Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 693692Heat shock protein homolog SSE1PRO_0000078396Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei242 – 2421Phosphothreonine1 Publication
    Modified residuei660 – 6601Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP32589.
    PaxDbiP32589.
    PeptideAtlasiP32589.
    PRIDEiP32589.

    2D gel databases

    SWISS-2DPAGEP32589.

    Expressioni

    Inductioni

    Increases a few-fold upon upshift to 37 degrees Celsius.

    Gene expression databases

    GenevestigatoriP32589.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HSP82P028293EBI-8648,EBI-8659
    HSPA1BP081072EBI-8648,EBI-629985From a different organism.
    SSA1P105918EBI-8648,EBI-8591
    SSB1P114842EBI-8648,EBI-8627

    Protein-protein interaction databases

    BioGridi36075. 256 interactions.
    DIPiDIP-6645N.
    IntActiP32589. 126 interactions.
    MINTiMINT-8285491.
    STRINGi4932.YPL106C.

    Structurei

    Secondary structure

    1
    693
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 84
    Beta strandi11 – 2010
    Beta strandi23 – 275
    Beta strandi34 – 374
    Beta strandi40 – 423
    Beta strandi44 – 496
    Helixi51 – 577
    Helixi61 – 633
    Helixi68 – 714
    Helixi81 – 855
    Beta strandi90 – 945
    Beta strandi98 – 1069
    Beta strandi109 – 1146
    Helixi115 – 13420
    Beta strandi140 – 1456
    Helixi151 – 16313
    Beta strandi167 – 1737
    Helixi174 – 18512
    Beta strandi192 – 1943
    Beta strandi197 – 2048
    Beta strandi209 – 2179
    Beta strandi220 – 22910
    Helixi234 – 25219
    Helixi257 – 2593
    Helixi261 – 28020
    Beta strandi282 – 2887
    Beta strandi291 – 2944
    Beta strandi297 – 3026
    Helixi303 – 3097
    Helixi311 – 3144
    Turni315 – 3184
    Helixi319 – 32810
    Helixi332 – 3343
    Beta strandi337 – 3426
    Helixi343 – 3464
    Helixi348 – 35811
    Turni368 – 3703
    Helixi371 – 38212
    Beta strandi387 – 3893
    Beta strandi393 – 3986
    Beta strandi402 – 4065
    Beta strandi414 – 4196
    Beta strandi423 – 43715
    Beta strandi439 – 4468
    Helixi448 – 4503
    Beta strandi457 – 4659
    Beta strandi476 – 4849
    Beta strandi490 – 4989
    Beta strandi505 – 5073
    Beta strandi520 – 5223
    Beta strandi529 – 5324
    Beta strandi534 – 5385
    Helixi544 – 58542
    Turni586 – 5894
    Helixi590 – 5923
    Helixi595 – 61117
    Turni612 – 6143
    Helixi615 – 6184
    Helixi621 – 65333

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2QXLX-ray2.41A/B2-659[»]
    3C7NX-ray3.12A1-666[»]
    3D2EX-ray2.35A/C1-502[»]
    A/C525-693[»]
    3D2FX-ray2.30A/C1-502[»]
    A/C525-693[»]
    ProteinModelPortaliP32589.
    SMRiP32589. Positions 1-649.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32589.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the heat shock protein 70 family.Curated

    Phylogenomic databases

    eggNOGiCOG0443.
    GeneTreeiENSGT00390000016919.
    HOGENOMiHOG000228138.
    KOiK09485.
    OMAiEARYKEW.
    OrthoDBiEOG7B8SC7.

    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. 2 hits.
    SSF100934. SSF100934. 1 hit.
    PROSITEiPS00329. 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.

    P32589-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTPFGLDLG NNNSVLAVAR NRGIDIVVNE VSNRSTPSVV GFGPKNRYLG    50
    ETGKNKQTSN IKNTVANLKR IIGLDYHHPD FEQESKHFTS KLVELDDKKT 100
    GAEVRFAGEK HVFSATQLAA MFIDKVKDTV KQDTKANITD VCIAVPPWYT 150
    EEQRYNIADA ARIAGLNPVR IVNDVTAAGV SYGIFKTDLP EGEEKPRIVA 200
    FVDIGHSSYT CSIMAFKKGQ LKVLGTACDK HFGGRDFDLA ITEHFADEFK 250
    TKYKIDIREN PKAYNRILTA AEKLKKVLSA NTNAPFSVES VMNDVDVSSQ 300
    LSREELEELV KPLLERVTEP VTKALAQAKL SAEEVDFVEI IGGTTRIPTL 350
    KQSISEAFGK PLSTTLNQDE AIAKGAAFIC AIHSPTLRVR PFKFEDIHPY 400
    SVSYSWDKQV EDEDHMEVFP AGSSFPSTKL ITLNRTGDFS MAASYTDITQ 450
    LPPNTPEQIA NWEITGVQLP EGQDSVPVKL KLRCDPSGLH TIEEAYTIED 500
    IEVEEPIPLP EDAPEDAEQE FKKVTKTVKK DDLTIVAHTF GLDAKKLNEL 550
    IEKENEMLAQ DKLVAETEDR KNTLEEYIYT LRGKLEEEYA PFASDAEKTK 600
    LQGMLNKAEE WLYDEGFDSI KAKYIAKYEE LASLGNIIRG RYLAKEEEKK 650
    QAIRSKQEAS QMAAMAEKLA AQRKAEAEKK EEKKDTEGDV DMD 693
    Length:693
    Mass (Da):77,366
    Last modified:January 23, 2007 - v4
    Checksum:i6558259111B0BC38
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti269 – 2702TA → NT in BAA02576. (PubMed:8406043)Curated
    Sequence conflicti269 – 2702TA → NT in BAA07449. (PubMed:8406043)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D13319 mRNA. Translation: BAA02576.1.
    D38368 mRNA. Translation: BAA07449.1.
    D38370 Genomic DNA. Translation: BAA07451.1.
    D13743 Genomic DNA. Translation: BAA02888.1.
    U43281 Genomic DNA. Translation: AAB68194.1.
    BK006949 Genomic DNA. Translation: DAA11327.1.
    PIRiS46417.
    RefSeqiNP_015219.1. NM_001183920.1.

    Genome annotation databases

    EnsemblFungiiYPL106C; YPL106C; YPL106C.
    GeneIDi855998.
    KEGGisce:YPL106C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D13319 mRNA. Translation: BAA02576.1 .
    D38368 mRNA. Translation: BAA07449.1 .
    D38370 Genomic DNA. Translation: BAA07451.1 .
    D13743 Genomic DNA. Translation: BAA02888.1 .
    U43281 Genomic DNA. Translation: AAB68194.1 .
    BK006949 Genomic DNA. Translation: DAA11327.1 .
    PIRi S46417.
    RefSeqi NP_015219.1. NM_001183920.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2QXL X-ray 2.41 A/B 2-659 [» ]
    3C7N X-ray 3.12 A 1-666 [» ]
    3D2E X-ray 2.35 A/C 1-502 [» ]
    A/C 525-693 [» ]
    3D2F X-ray 2.30 A/C 1-502 [» ]
    A/C 525-693 [» ]
    ProteinModelPortali P32589.
    SMRi P32589. Positions 1-649.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36075. 256 interactions.
    DIPi DIP-6645N.
    IntActi P32589. 126 interactions.
    MINTi MINT-8285491.
    STRINGi 4932.YPL106C.

    2D gel databases

    SWISS-2DPAGE P32589.

    Proteomic databases

    MaxQBi P32589.
    PaxDbi P32589.
    PeptideAtlasi P32589.
    PRIDEi P32589.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YPL106C ; YPL106C ; YPL106C .
    GeneIDi 855998.
    KEGGi sce:YPL106C.

    Organism-specific databases

    SGDi S000006027. SSE1.

    Phylogenomic databases

    eggNOGi COG0443.
    GeneTreei ENSGT00390000016919.
    HOGENOMi HOG000228138.
    KOi K09485.
    OMAi EARYKEW.
    OrthoDBi EOG7B8SC7.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-34008-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P32589.
    NextBioi 980863.
    PROi P32589.

    Gene expression databases

    Genevestigatori P32589.

    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. 2 hits.
    SSF100934. SSF100934. 1 hit.
    PROSITEi PS00329. HSP70_2. 1 hit.
    PS01036. HSP70_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of SSE1 and SSE2, new members of the yeast HSP70 multigene family."
      Mukai H., Kuno T., Tanaka H., Hirata D., Miyakawa T., Tanaka C.
      Gene 132:57-66(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: ATCC 204626 / S288c / A364A.
    2. "MSI3, a multicopy suppressor of mutants hyperactivated in the RAS-cAMP pathway, encodes a novel HSP70 protein of Saccharomyces cerevisiae."
      Shirayama M., Kawakami K., Matsui Y., Tanaka K., Toh-e A.
      Mol. Gen. Genet. 240:323-332(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
      Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
      , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
      Nature 387:103-105(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. Cited for: PROTEIN SEQUENCE OF 100-110.
      Strain: ATCC 204508 / S288c.
    6. "Protein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae."
      Norbeck J., Blomberg A.
      FEMS Microbiol. Lett. 137:1-8(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 330-339.
      Strain: ATCC 38531 / Y41.
    7. "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 SER-2.
    8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    10. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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 SER-660, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiHSP7F_YEAST
    AccessioniPrimary (citable) accession number: P32589
    Secondary accession number(s): D6W3R1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 145 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 71700 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 XVI
      Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

    External Data

    Dasty 3