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P15108

- HSC82_YEAST

UniProt

P15108 - HSC82_YEAST

Protein

ATP-dependent molecular chaperone HSC82

Gene

HSC82

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 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction such as CNA2. Undergoes a functional cycle that is linked to its ATPase activity By similarity. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for growth at high temperatures.By similarity1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei37 – 371ATPBy similarity
    Binding sitei79 – 791ATPBy similarity
    Binding sitei98 – 981ATPBy similarity
    Binding sitei124 – 1241ATP; via amide nitrogenBy similarity
    Binding sitei376 – 3761ATPBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. 'de novo' protein folding Source: SGD
    2. ATP catabolic process Source: GOC
    3. box C/D snoRNP assembly Source: SGD
    4. cellular response to heat Source: SGD
    5. proteasome assembly Source: SGD
    6. protein folding Source: SGD
    7. protein refolding Source: SGD
    8. telomere maintenance Source: SGD

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Stress response

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32874-MONOMER.
    ReactomeiREACT_189032. Signaling by constitutively active EGFR.
    REACT_189238. The NLRP3 inflammasome.
    REACT_219346. HSF1-dependent transactivation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent molecular chaperone HSC82
    Alternative name(s):
    82 kDa heat shock cognate protein
    Heat shock protein Hsp90 constitutive isoform
    Gene namesi
    Name:HSC82
    Ordered Locus Names:YMR186W
    ORF Names:YM8010.16
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIII

    Organism-specific databases

    SGDiS000004798. HSC82.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi453 – 4531L → A: Leads to growth defect at 37 degrees Celsius, probably by disrupting the intramolecular interaction of the N-termini with the middle domains; when associated with A-493. 1 Publication
    Mutagenesisi493 – 4931E → A: Leads to growth defect at 37 degrees Celsius, probably by disrupting the intramolecular interaction of the N-termini with the middle domains; when associated with A-453. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 705704ATP-dependent molecular chaperone HSC82PRO_0000062958Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei653 – 6531Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP15108.
    PaxDbiP15108.
    PeptideAtlasiP15108.
    PRIDEiP15108.

    2D gel databases

    SWISS-2DPAGEP15108.

    Expressioni

    Inductioni

    Expressed constitutively at a high level and is moderately induced by high temperatures dependent on transcription factor HSF1.2 Publications

    Gene expression databases

    GenevestigatoriP15108.

    Interactioni

    Subunit structurei

    Interacts with the co-chaperone SGT1. Interacts directly with the substrate CNA2. Interacts with NAP1.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AHA1Q124493EBI-8666,EBI-37072
    ARO1P085663EBI-8666,EBI-2883
    CNS1P333132EBI-8666,EBI-4806
    CPR7P471032EBI-8666,EBI-5436
    PPT1P530433EBI-8666,EBI-13796
    SSA1P105912EBI-8666,EBI-8591
    STI1P157053EBI-8666,EBI-18418

    Protein-protein interaction databases

    BioGridi35364. 1042 interactions.
    DIPiDIP-1524N.
    IntActiP15108. 142 interactions.
    MINTiMINT-393096.
    STRINGi4932.YMR186W.

    Structurei

    3D structure databases

    ProteinModelPortaliP15108.
    SMRiP15108. Positions 2-673.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati221 – 22551
    Repeati226 – 23052
    Repeati232 – 23653
    Repeati246 – 25054

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni221 – 259394 X 5 AA repeats of [DE]-[DE]-[DE]-K-K; highly charged regionAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi701 – 7055TPR repeat-binding

    Domaini

    The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins.By similarity

    Sequence similaritiesi

    Belongs to the heat shock protein 90 family.Curated

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiCOG0326.
    GeneTreeiENSGT00750000117672.
    HOGENOMiHOG000031988.
    KOiK04079.
    OMAiSINSENM.
    OrthoDBiEOG7BP8B5.

    Family and domain databases

    Gene3Di3.30.565.10. 1 hit.
    HAMAPiMF_00505. HSP90.
    InterProiIPR003594. HATPase_ATP-bd.
    IPR019805. Heat_shock_protein_90_CS.
    IPR001404. Hsp90_fam.
    IPR020575. Hsp90_N.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    [Graphical view]
    PANTHERiPTHR11528. PTHR11528. 1 hit.
    PfamiPF02518. HATPase_c. 1 hit.
    PF00183. HSP90. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002583. Hsp90. 1 hit.
    PRINTSiPR00775. HEATSHOCK90.
    SMARTiSM00387. HATPase_c. 1 hit.
    [Graphical view]
    SUPFAMiSSF54211. SSF54211. 1 hit.
    SSF55874. SSF55874. 1 hit.
    PROSITEiPS00298. HSP90. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P15108-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGETFEFQA EITQLMSLII NTVYSNKEIF LRELISNASD ALDKIRYQAL    50
    SDPKQLETEP DLFIRITPKP EEKVLEIRDS GIGMTKAELI NNLGTIAKSG 100
    TKAFMEALSA GADVSMIGQF GVGFYSLFLV ADRVQVISKN NEDEQYIWES 150
    NAGGSFTVTL DEVNERIGRG TVLRLFLKDD QLEYLEEKRI KEVIKRHSEF 200
    VAYPIQLLVT KEVEKEVPIP EEEKKDEEKK DEDDKKPKLE EVDEEEEEKK 250
    PKTKKVKEEV QELEELNKTK PLWTRNPSDI TQEEYNAFYK SISNDWEDPL 300
    YVKHFSVEGQ LEFRAILFIP KRAPFDLFES KKKKNNIKLY VRRVFITDEA 350
    EDLIPEWLSF VKGVVDSEDL PLNLSREMLQ QNKIMKVIRK NIVKKLIEAF 400
    NEIAEDSEQF DKFYSAFAKN IKLGVHEDTQ NRAALAKLLR YNSTKSVDEL 450
    TSLTDYVTRM PEHQKNIYYI TGESLKAVEK SPFLDALKAK NFEVLFLTDP 500
    IDEYAFTQLK EFEGKTLVDI TKDFELEETD EEKAEREKEI KEYEPLTKAL 550
    KDILGDQVEK VVVSYKLLDA PAAIRTGQFG WSANMERIMK AQALRDSSMS 600
    SYMSSKKTFE ISPKSPIIKE LKKRVDEGGA QDKTVKDLTN LLFETALLTS 650
    GFSLEEPTSF ASRINRLISL GLNIDEDEET ETAPEASTEA PVEEVPADTE 700
    MEEVD 705
    Length:705
    Mass (Da):80,900
    Last modified:January 23, 2007 - v4
    Checksum:iDBD41524091B1F9B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti619 – 6191K → I(PubMed:2674684)Curated
    Sequence conflicti621 – 6211L → T(PubMed:2674684)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26044 Unassigned DNA. Translation: AAA02813.1.
    Z49808 Genomic DNA. Translation: CAA89919.1.
    BK006946 Genomic DNA. Translation: DAA10084.1.
    PIRiS55133.
    RefSeqiNP_013911.1. NM_001182692.1.

    Genome annotation databases

    EnsemblFungiiYMR186W; YMR186W; YMR186W.
    GeneIDi855224.
    KEGGisce:YMR186W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26044 Unassigned DNA. Translation: AAA02813.1 .
    Z49808 Genomic DNA. Translation: CAA89919.1 .
    BK006946 Genomic DNA. Translation: DAA10084.1 .
    PIRi S55133.
    RefSeqi NP_013911.1. NM_001182692.1.

    3D structure databases

    ProteinModelPortali P15108.
    SMRi P15108. Positions 2-673.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35364. 1042 interactions.
    DIPi DIP-1524N.
    IntActi P15108. 142 interactions.
    MINTi MINT-393096.
    STRINGi 4932.YMR186W.

    Chemistry

    ChEMBLi CHEMBL4199.

    2D gel databases

    SWISS-2DPAGE P15108.

    Proteomic databases

    MaxQBi P15108.
    PaxDbi P15108.
    PeptideAtlasi P15108.
    PRIDEi P15108.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YMR186W ; YMR186W ; YMR186W .
    GeneIDi 855224.
    KEGGi sce:YMR186W.

    Organism-specific databases

    SGDi S000004798. HSC82.

    Phylogenomic databases

    eggNOGi COG0326.
    GeneTreei ENSGT00750000117672.
    HOGENOMi HOG000031988.
    KOi K04079.
    OMAi SINSENM.
    OrthoDBi EOG7BP8B5.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32874-MONOMER.
    Reactomei REACT_189032. Signaling by constitutively active EGFR.
    REACT_189238. The NLRP3 inflammasome.
    REACT_219346. HSF1-dependent transactivation.

    Miscellaneous databases

    NextBioi 978750.

    Gene expression databases

    Genevestigatori P15108.

    Family and domain databases

    Gene3Di 3.30.565.10. 1 hit.
    HAMAPi MF_00505. HSP90.
    InterProi IPR003594. HATPase_ATP-bd.
    IPR019805. Heat_shock_protein_90_CS.
    IPR001404. Hsp90_fam.
    IPR020575. Hsp90_N.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    [Graphical view ]
    PANTHERi PTHR11528. PTHR11528. 1 hit.
    Pfami PF02518. HATPase_c. 1 hit.
    PF00183. HSP90. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002583. Hsp90. 1 hit.
    PRINTSi PR00775. HEATSHOCK90.
    SMARTi SM00387. HATPase_c. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54211. SSF54211. 1 hit.
    SSF55874. SSF55874. 1 hit.
    PROSITEi PS00298. HSP90. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures."
      Borkovich K.A., Farrelly F.W., Finkelstein D.B., Taulien J., Lindquist S.
      Mol. Cell. Biol. 9:3919-3930(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE, INDUCTION.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Two-dimensional protein map of Saccharomyces cerevisiae: construction of a gene-protein index."
      Boucherie H., Dujardin G., Kermorgant M., Monribot C., Slonimski P.P., Perrot M.
      Yeast 11:601-613(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-8.
      Strain: ATCC 204508 / S288c.
    5. "A yeast heat shock transcription factor (Hsf1) mutant is defective in both Hsc82/Hsp82 synthesis and spindle pole body duplication."
      Zarzov P., Boucherie H., Mann C.
      J. Cell Sci. 110:1879-1891(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    6. "Role of HSP90 in salt stress tolerance via stabilization and regulation of calcineurin."
      Imai J., Yahara I.
      Mol. Cell. Biol. 20:9262-9270(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CNA2.
    7. "Interaction between the N-terminal and middle regions is essential for the in vivo function of HSP90 molecular chaperone."
      Matsumoto S., Tanaka E., Nemoto T.K., Ono T., Takagi T., Imai J., Kimura Y., Yahara I., Kobayakawa T., Ayuse T., Oi K., Mizuno A.
      J. Biol. Chem. 277:34959-34966(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LEU-453 AND GLU-493.
    8. "Sgt1 associates with Hsp90: an initial step of assembly of the core kinetochore complex."
      Bansal P.K., Abdulle R., Kitagawa K.
      Mol. Cell. Biol. 24:8069-8079(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SGT1.
    9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Strain: ATCC 76625 / YPH499.
    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 SER-653, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiHSC82_YEAST
    AccessioniPrimary (citable) accession number: P15108
    Secondary accession number(s): D6W010
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 147 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 132053 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3