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P02829

- HSP82_YEAST

UniProt

P02829 - HSP82_YEAST

Protein

ATP-dependent molecular chaperone HSP82

Gene

HSP82

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 169 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      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. Undergoes a functional cycle that is linked to its ATPase activity. The nucleotide-free form of the dimer is found in an open conformation in which the N-termini are not dimerized and the complex is ready for client protein binding. Binding of ATP induces large conformational changes, resulting in the formation of a ring-like closed structure in which the N-terminal domains associate intramolecularly with the middle domain and also dimerize with each other, stimulating their intrinsic ATPase activity and acting as a clamp on the substrate. Finally, ATP hydrolysis results in the release of the substrate. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for growth at high temperatures.1 Publication

    Enzyme regulationi

    Inhibited by geldanamycin, macbecin I and radicicol, which bind to the ATP-binding pocket. Co-chaperones CDC37, SBA1 and STI1 reduce ATPase activity. Co-chaperones AHA1 and HCH1 increase ATPase activity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei37 – 371ATP1 Publication
    Binding sitei79 – 791ATP1 Publication
    Binding sitei98 – 981ATP1 Publication
    Binding sitei124 – 1241ATP; via amide nitrogen1 Publication
    Binding sitei380 – 3801ATP1 Publication

    GO - Molecular functioni

    1. ATPase activity, coupled Source: SGD
    2. ATP binding Source: UniProtKB-KW
    3. identical protein binding Source: IntAct
    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. positive regulation of telomere maintenance via telomerase Source: SGD
    5. proteasome assembly Source: SGD
    6. protein refolding Source: SGD
    7. protein targeting to mitochondrion Source: SGD
    8. response to osmotic stress Source: SGD

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Stress response

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-34126-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 HSP82
    Alternative name(s):
    82 kDa heat shock protein
    Heat shock protein Hsp90 heat-inducible isoform
    Gene namesi
    Name:HSP82
    Synonyms:HSP90
    Ordered Locus Names:YPL240C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XVI

    Organism-specific databases

    CYGDiYPL240c.
    SGDiS000006161. HSP82.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi22 – 221T → I: Induces a 6-fold increase in ATPase activity and a reduced client protein activation activity, leading to growth defect at high temperatures. 1 Publication
    Mutagenesisi41 – 411A → V: Causes a 98% reduction in ATPase activity and a reduced client protein activation activity, leading to growth defect at high temperatures. 1 Publication
    Mutagenesisi81 – 811G → S: Reduces client protein activation activity, leading to growth defect at high temperatures. 1 Publication
    Mutagenesisi83 – 831G → D: Abolishes ATPase activity. 1 Publication
    Mutagenesisi97 – 971A → I: Abolishes interaction with SBA1. 1 Publication
    Mutagenesisi101 – 1011T → I: Causes a 90% reduction in ATPase activity and a reduced client protein activation activity, leading to growth defect at high temperatures. 1 Publication
    Mutagenesisi107 – 1071A → N: Induces a 6-fold increase in ATPase activity. 1 Publication
    Mutagenesisi170 – 1701G → D: Induces a total loss of function at 34 degrees Celsius. Abolishes interaction with SBA1. 1 Publication
    Mutagenesisi313 – 3131G → N or S: Reduces client protein activation activity, leading to growth defect at high temperatures. 2 Publications
    Mutagenesisi349 – 3491F → A or Q: Induces a loss of ATPase activity. Can be reactivated by AHA1. 1 Publication
    Mutagenesisi380 – 3801R → A: Induces a loss of ATPase activity. 1 Publication
    Mutagenesisi381 – 3811E → K: Reduces client protein activation activity. Resistant to ATPase activation by AHA1. 1 Publication
    Mutagenesisi384 – 3841Q → A: Induces a loss of ATPase activity. 1 Publication
    Mutagenesisi387 – 3871K → A: Decreases AHA1 binding affinity, but has no effect on client protein activation activity. 1 Publication
    Mutagenesisi387 – 3871K → D: Decreases AHA1 binding affinity and substantially reduces client protein activation activity. 1 Publication
    Mutagenesisi431 – 4311E → K: Specifically reduces the activation of the exogenous ligand glucocorticoid receptor. 1 Publication
    Mutagenesisi485 – 4851S → Y: Abolishes interaction with SBA1. 1 Publication
    Mutagenesisi525 – 5251T → I: Abolishes interaction with SBA1. Reduces client protein activation activity, leading to growth defect at high temperatures. 1 Publication
    Mutagenesisi576 – 5761A → T: Reduces client protein activation activity; when associated with K-579. 1 Publication
    Mutagenesisi577 – 5771A → C: Enhances ATPase activity and client protein activation. 1 Publication
    Mutagenesisi577 – 5771A → D: Reduces ATPase activity and client protein activation. 1 Publication
    Mutagenesisi577 – 5771A → I: Enhances homodimerization, ATPase activity and client protein activation. 1 Publication
    Mutagenesisi577 – 5771A → N: Reduces homodimerization, ATPase activity and client protein activation. 1 Publication
    Mutagenesisi579 – 5791R → K: Reduces client protein activation activity; when associated with T-576. 1 Publication
    Mutagenesisi587 – 5871A → T: No effect on ATPase activity. Reduces client protein activation activity, leading to growth defect at high temperatures. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 709708ATP-dependent molecular chaperone HSP82PRO_0000062957Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei657 – 6571PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP02829.
    PeptideAtlasiP02829.
    PRIDEiP02829.

    2D gel databases

    SWISS-2DPAGEP02829.

    Expressioni

    Inductioni

    Expressed constitutively and induced by high temperatures dependent on transcription factor HSF1. According to PubMed:2674684, it is constitutively expressed at low levels, however, due to the specificity of the antibody, this result is unsure.2 Publications

    Gene expression databases

    GenevestigatoriP02829.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with the co-chaperones AHA1, CDC37, CNS1, CPR6, CPR7, HCH1, SBA1, SSE1 and STI1. CNS1, CPR6, CPR7 and STI1. Interacts directly with the substrates GCN2, HAP1 and STE11.18 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself5EBI-8659,EBI-8659
    ACT1P600102EBI-8659,EBI-2169
    ADE1P276162EBI-8659,EBI-14257
    AHA1Q124497EBI-8659,EBI-37072
    BNI4P538582EBI-8659,EBI-3704
    CDC37P061013EBI-8659,EBI-4266
    CNS1P333135EBI-8659,EBI-4806
    CPR6P536912EBI-8659,EBI-5429
    CPR7P471033EBI-8659,EBI-5436
    HAP1P0CS823EBI-8659,EBI-5419From a different organism.
    HXT10P435812EBI-8659,EBI-8750
    MIG1P277053EBI-8659,EBI-10913
    MTH1P351983EBI-8659,EBI-11561
    NPL6P328322EBI-8659,EBI-12202
    PIH1P387682EBI-8659,EBI-24499
    PKH1Q034072EBI-8659,EBI-32467
    PPT1P530438EBI-8659,EBI-13796
    PRO1P322643EBI-8659,EBI-13879
    SBA1P287074EBI-8659,EBI-26838
    SGT1Q084462EBI-8659,EBI-17070
    SLT2Q007724EBI-8659,EBI-17372
    SSA1P105913EBI-8659,EBI-8591
    SSA2P105922EBI-8659,EBI-8603
    SSE1P325893EBI-8659,EBI-8648
    STI1P157059EBI-8659,EBI-18418
    TAH1P256383EBI-8659,EBI-21956
    YDL199CQ124072EBI-8659,EBI-33162

    Protein-protein interaction databases

    BioGridi35923. 1388 interactions.
    DIPiDIP-2262N.
    IntActiP02829. 337 interactions.
    MINTiMINT-560200.
    STRINGi4932.YPL240C.

    Structurei

    Secondary structure

    1
    709
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 74
    Helixi10 – 2112
    Helixi26 – 283
    Helixi29 – 4820
    Turni49 – 513
    Helixi53 – 564
    Beta strandi64 – 696
    Helixi70 – 723
    Beta strandi74 – 796
    Helixi86 – 938
    Turni95 – 973
    Helixi101 – 11010
    Helixi114 – 1207
    Helixi123 – 1297
    Beta strandi131 – 1399
    Beta strandi146 – 1505
    Beta strandi152 – 1609
    Beta strandi162 – 1643
    Beta strandi168 – 17710
    Helixi182 – 1854
    Helixi187 – 19711
    Beta strandi200 – 2034
    Beta strandi205 – 2073
    Helixi276 – 2783
    Helixi281 – 2833
    Helixi286 – 29712
    Beta strandi304 – 3118
    Beta strandi313 – 3153
    Beta strandi317 – 3237
    Turni329 – 3324
    Beta strandi341 – 3455
    Beta strandi348 – 3525
    Beta strandi355 – 3584
    Helixi360 – 3623
    Beta strandi366 – 3738
    Helixi380 – 3834
    Helixi387 – 40822
    Helixi411 – 43121
    Turni433 – 4353
    Helixi436 – 4405
    Beta strandi444 – 4474
    Beta strandi450 – 4567
    Helixi457 – 4626
    Beta strandi470 – 4756
    Helixi479 – 4835
    Helixi488 – 4936
    Beta strandi498 – 5014
    Helixi504 – 51310
    Beta strandi519 – 5235
    Turni524 – 5263
    Beta strandi530 – 5334
    Helixi535 – 55824
    Beta strandi563 – 5675
    Beta strandi573 – 5808
    Beta strandi582 – 5843
    Helixi587 – 59711
    Beta strandi600 – 6023
    Beta strandi611 – 6155
    Helixi620 – 62910
    Turni630 – 6323
    Helixi633 – 6353
    Helixi637 – 65317
    Helixi661 – 67616

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A4HX-ray2.50A1-220[»]
    1AH6X-ray1.80A1-220[»]
    1AH8X-ray2.10A/B1-220[»]
    1AM1X-ray2.00A2-214[»]
    1AMWX-ray1.85A1-214[»]
    1BGQX-ray2.50A1-214[»]
    1HK7X-ray2.50A/B273-560[»]
    1US7X-ray2.30A1-214[»]
    1USUX-ray2.15A273-530[»]
    1USVX-ray2.70A/C/E/G272-530[»]
    1ZW9X-ray1.90A1-220[»]
    1ZWHX-ray1.65A1-220[»]
    2AKPX-ray1.94A/B25-210[»]
    2BRCX-ray1.60A1-214[»]
    2BREX-ray2.00A/B1-219[»]
    2CG9X-ray3.10A/B1-677[»]
    2CGEX-ray3.00A/B/D273-677[»]
    2CGFX-ray2.20A1-214[»]
    2FXSX-ray2.00A1-220[»]
    2IWSX-ray2.70A1-214[»]
    2IWUX-ray2.80A1-214[»]
    2IWXX-ray1.50A1-214[»]
    2LSVNMR-B701-709[»]
    2VW5X-ray1.90A/B/C/D1-214[»]
    2VWCX-ray2.40A1-219[»]
    2WEPX-ray2.00A1-220[»]
    2WEQX-ray2.20A1-220[»]
    2WERX-ray1.60A/B1-220[»]
    2XD6X-ray2.20A1-214[»]
    2XX2X-ray1.85A/B/C/D1-214[»]
    2XX4X-ray2.20A1-214[»]
    2XX5X-ray2.00A1-214[»]
    2YGAX-ray2.37A1-220[»]
    2YGEX-ray1.96A1-220[»]
    2YGFX-ray2.00A1-220[»]
    3C0EX-ray1.90A1-220[»]
    3C11X-ray1.60A1-220[»]
    3FP2X-ray1.98Q698-709[»]
    4AS9X-ray2.71A1-220[»]
    4ASAX-ray2.25A1-220[»]
    4ASBX-ray3.08A1-220[»]
    4ASFX-ray2.60A1-220[»]
    4ASGX-ray2.20A1-220[»]
    4CE1X-ray2.01A1-214[»]
    4CE2X-ray2.38A1-214[»]
    4CE3X-ray2.31A1-214[»]
    ProteinModelPortaliP02829.
    SMRiP02829. Positions 1-677.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02829.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati221 – 225511 Publication
    Repeati226 – 230521 Publication
    Repeati231 – 235531 Publication
    Repeati237 – 241541 Publication
    Repeati250 – 254551 Publication

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni221 – 263435 X 5 AA repeats of [DE]-[DE]-[DE]-K-K; highly charged regionAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi705 – 7095TPR repeat-binding

    Domaini

    The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins like the co-chaperones AHA1, CDC37, CNS1, CPR6, CPR7, HCH1, SBA1, SSE1 and STI1. CNS1, CPR6, CPR7 and STI1.

    Sequence similaritiesi

    Belongs to the heat shock protein 90 family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    GeneTreeiENSGT00550000074382.
    HOGENOMiHOG000031988.
    KOiK04079.
    OMAiASADVHM.
    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.

    P02829-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASETFEFQA EITQLMSLII NTVYSNKEIF LRELISNASD ALDKIRYKSL    50
    SDPKQLETEP DLFIRITPKP EQKVLEIRDS GIGMTKAELI NNLGTIAKSG 100
    TKAFMEALSA GADVSMIGQF GVGFYSLFLV ADRVQVISKS NDDEQYIWES 150
    NAGGSFTVTL DEVNERIGRG TILRLFLKDD QLEYLEEKRI KEVIKRHSEF 200
    VAYPIQLVVT KEVEKEVPIP EEEKKDEEKK DEEKKDEDDK KPKLEEVDEE 250
    EEKKPKTKKV KEEVQEIEEL NKTKPLWTRN PSDITQEEYN AFYKSISNDW 300
    EDPLYVKHFS VEGQLEFRAI LFIPKRAPFD LFESKKKKNN IKLYVRRVFI 350
    TDEAEDLIPE WLSFVKGVVD SEDLPLNLSR EMLQQNKIMK VIRKNIVKKL 400
    IEAFNEIAED SEQFEKFYSA FSKNIKLGVH EDTQNRAALA KLLRYNSTKS 450
    VDELTSLTDY VTRMPEHQKN IYYITGESLK AVEKSPFLDA LKAKNFEVLF 500
    LTDPIDEYAF TQLKEFEGKT LVDITKDFEL EETDEEKAER EKEIKEYEPL 550
    TKALKEILGD QVEKVVVSYK LLDAPAAIRT GQFGWSANME RIMKAQALRD 600
    SSMSSYMSSK KTFEISPKSP IIKELKKRVD EGGAQDKTVK DLTKLLYETA 650
    LLTSGFSLDE PTSFASRINR LISLGLNIDE DEETETAPEA STAAPVEEVP 700
    ADTEMEEVD 709
    Length:709
    Mass (Da):81,406
    Last modified:July 21, 1986 - v1
    Checksum:iD7C35676D668FB63
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti481 – 4811A → S(PubMed:12667448)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K01387 Unassigned RNA. Translation: AAA02743.1.
    Z67751 Genomic DNA. Translation: CAA91604.1.
    Z73596 Genomic DNA. Translation: CAA97961.1.
    BK006949 Genomic DNA. Translation: DAA11197.1.
    PIRiA03313. HHBY90.
    RefSeqiNP_015084.1. NM_001184054.1.

    Genome annotation databases

    EnsemblFungiiYPL240C; YPL240C; YPL240C.
    GeneIDi855836.
    KEGGisce:YPL240C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K01387 Unassigned RNA. Translation: AAA02743.1 .
    Z67751 Genomic DNA. Translation: CAA91604.1 .
    Z73596 Genomic DNA. Translation: CAA97961.1 .
    BK006949 Genomic DNA. Translation: DAA11197.1 .
    PIRi A03313. HHBY90.
    RefSeqi NP_015084.1. NM_001184054.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A4H X-ray 2.50 A 1-220 [» ]
    1AH6 X-ray 1.80 A 1-220 [» ]
    1AH8 X-ray 2.10 A/B 1-220 [» ]
    1AM1 X-ray 2.00 A 2-214 [» ]
    1AMW X-ray 1.85 A 1-214 [» ]
    1BGQ X-ray 2.50 A 1-214 [» ]
    1HK7 X-ray 2.50 A/B 273-560 [» ]
    1US7 X-ray 2.30 A 1-214 [» ]
    1USU X-ray 2.15 A 273-530 [» ]
    1USV X-ray 2.70 A/C/E/G 272-530 [» ]
    1ZW9 X-ray 1.90 A 1-220 [» ]
    1ZWH X-ray 1.65 A 1-220 [» ]
    2AKP X-ray 1.94 A/B 25-210 [» ]
    2BRC X-ray 1.60 A 1-214 [» ]
    2BRE X-ray 2.00 A/B 1-219 [» ]
    2CG9 X-ray 3.10 A/B 1-677 [» ]
    2CGE X-ray 3.00 A/B/D 273-677 [» ]
    2CGF X-ray 2.20 A 1-214 [» ]
    2FXS X-ray 2.00 A 1-220 [» ]
    2IWS X-ray 2.70 A 1-214 [» ]
    2IWU X-ray 2.80 A 1-214 [» ]
    2IWX X-ray 1.50 A 1-214 [» ]
    2LSV NMR - B 701-709 [» ]
    2VW5 X-ray 1.90 A/B/C/D 1-214 [» ]
    2VWC X-ray 2.40 A 1-219 [» ]
    2WEP X-ray 2.00 A 1-220 [» ]
    2WEQ X-ray 2.20 A 1-220 [» ]
    2WER X-ray 1.60 A/B 1-220 [» ]
    2XD6 X-ray 2.20 A 1-214 [» ]
    2XX2 X-ray 1.85 A/B/C/D 1-214 [» ]
    2XX4 X-ray 2.20 A 1-214 [» ]
    2XX5 X-ray 2.00 A 1-214 [» ]
    2YGA X-ray 2.37 A 1-220 [» ]
    2YGE X-ray 1.96 A 1-220 [» ]
    2YGF X-ray 2.00 A 1-220 [» ]
    3C0E X-ray 1.90 A 1-220 [» ]
    3C11 X-ray 1.60 A 1-220 [» ]
    3FP2 X-ray 1.98 Q 698-709 [» ]
    4AS9 X-ray 2.71 A 1-220 [» ]
    4ASA X-ray 2.25 A 1-220 [» ]
    4ASB X-ray 3.08 A 1-220 [» ]
    4ASF X-ray 2.60 A 1-220 [» ]
    4ASG X-ray 2.20 A 1-220 [» ]
    4CE1 X-ray 2.01 A 1-214 [» ]
    4CE2 X-ray 2.38 A 1-214 [» ]
    4CE3 X-ray 2.31 A 1-214 [» ]
    ProteinModelPortali P02829.
    SMRi P02829. Positions 1-677.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35923. 1388 interactions.
    DIPi DIP-2262N.
    IntActi P02829. 337 interactions.
    MINTi MINT-560200.
    STRINGi 4932.YPL240C.

    Chemistry

    BindingDBi P02829.
    ChEMBLi CHEMBL3536.

    2D gel databases

    SWISS-2DPAGE P02829.

    Proteomic databases

    MaxQBi P02829.
    PeptideAtlasi P02829.
    PRIDEi P02829.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YPL240C ; YPL240C ; YPL240C .
    GeneIDi 855836.
    KEGGi sce:YPL240C.

    Organism-specific databases

    CYGDi YPL240c.
    SGDi S000006161. HSP82.

    Phylogenomic databases

    GeneTreei ENSGT00550000074382.
    HOGENOMi HOG000031988.
    KOi K04079.
    OMAi ASADVHM.
    OrthoDBi EOG7BP8B5.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-34126-MONOMER.
    Reactomei REACT_189032. Signaling by constitutively active EGFR.
    REACT_189238. The NLRP3 inflammasome.
    REACT_219346. HSF1-dependent transactivation.

    Miscellaneous databases

    EvolutionaryTracei P02829.
    NextBioi 980407.

    Gene expression databases

    Genevestigatori P02829.

    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. "Complete sequence of the heat shock-inducible HSP90 gene of Saccharomyces cerevisiae."
      Farrelly F.W., Finkelstein D.B.
      J. Biol. Chem. 259:5745-5751(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
    2. "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.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "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: INDUCTION.
    5. "Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl prolyl isomerases."
      Nadeau K., Das A., Walsh C.T.
      J. Biol. Chem. 268:1479-1487(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: ATPASE ACTIVITY.
    6. "Isolation of Hsp90 mutants by screening for decreased steroid receptor function."
      Bohen S.P., Yamamoto K.R.
      Proc. Natl. Acad. Sci. U.S.A. 90:11424-11428(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLY-313; GLU-431; THR-525; ALA-576 AND ARG-579.
    7. "Conservation of Hsp90 macromolecular complexes in Saccharomyces cerevisiae."
      Chang H.-C.J., Lindquist S.
      J. Biol. Chem. 269:24983-24988(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH STI1 AND CPR6.
    8. "Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase."
      Nathan D.F., Lindquist S.
      Mol. Cell. Biol. 15:3917-3925(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF THR-22; ALA-41; GLY-81; THR-101; GLY-170; GLY-313; GLU-381 AND ALA-587.
    9. "A cyclophilin function in Hsp90-dependent signal transduction."
      Duina A.A., Chang H.-C.J., Marsh J.A., Lindquist S., Gaber R.F.
      Science 274:1713-1715(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CPR6 AND CPR7.
    10. "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.
    11. "In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis."
      Obermann W.M., Sondermann H., Russo A.A., Pavletich N.P., Hartl F.U.
      J. Cell Biol. 143:901-910(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SBA1.
    12. "SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins."
      Fang Y., Fliss A.E., Rao J., Caplan A.J.
      Mol. Cell. Biol. 18:3727-3734(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SBA1, MUTAGENESIS OF ALA-97 AND SER-485.
    13. "Molecular mechanism governing heme signaling in yeast: a higher-order complex mediates heme regulation of the transcriptional activator HAP1."
      Zhang L., Hach A., Wang C.
      Mol. Cell. Biol. 18:3819-3828(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HAP1.
    14. "CNS1 encodes an essential p60/Sti1 homolog in Saccharomyces cerevisiae that suppresses cyclophilin 40 mutations and interacts with Hsp90."
      Dolinski K.J., Cardenas M.E., Heitman J.
      Mol. Cell. Biol. 18:7344-7352(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CNS1.
    15. "The yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone."
      Liu X.-D., Morano K.A., Thiele D.J.
      J. Biol. Chem. 274:26654-26660(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SSE1.
    16. "Hsp90 binds and regulates Gcn2, the ligand-inducible kinase of the alpha subunit of eukaryotic translation initiation factor 2."
      Donze O., Picard D.
      Mol. Cell. Biol. 19:8422-8432(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GCN2.
    17. "Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine."
      Scheufler C., Brinker A., Bourenkov G., Pegoraro S., Moroder L., Bartunik H., Hartl F.U., Moarefi I.
      Cell 101:199-210(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: BINDING TO TPR REPEATS.
    18. "The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains."
      Prodromou C., Panaretou B., Chohan S., Siligardi G., O'Brien R., Ladbury J.E., Roe S.M., Piper P.W., Pearl L.H.
      EMBO J. 19:4383-4392(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: ATPASE ACTIVITY, MUTAGENESIS OF ALA-107.
    19. "The molecular chaperone Cdc37 is required for Ste11 function and pheromone-induced cell cycle arrest."
      Abbas-Terki T., Donze O., Picard D.
      FEBS Lett. 467:111-116(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDC37 AND STE11.
    20. Cited for: INTERACTION WITH AHA1 AND HCH1.
    21. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    22. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    23. "The ATPase-dependent chaperoning activity of Hsp90a regulates thick filament formation and integration during skeletal muscle myofibrillogenesis."
      Hawkins T.A., Haramis A.P., Etard C., Prodromou C., Vaughan C.K., Ashworth R., Ray S., Behra M., Holder N., Talbot W.S., Pearl L.H., Strahle U., Wilson S.W.
      Development 135:1147-1156(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLY-83.
    24. "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].
    25. "A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone."
      Prodromou C., Roe S.M., Piper P.W., Pearl L.H.
      Nat. Struct. Biol. 4:477-482(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    26. "Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone."
      Prodromou C., Roe S.M., O'Brien R., Ladbury J.E., Piper P.W., Pearl L.H.
      Cell 90:65-75(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2-214 IN COMPLEX WITH ADP AND GELDANAMYCIN.
    27. "Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions."
      Meyer P., Prodromou C., Hu B., Vaughan C.K., Roe S.M., Panaretou B., Piper P.W., Pearl L.H.
      Mol. Cell 11:647-658(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 273-560, MUTAGENESIS OF PHE-349; ARG-380 AND GLN-384.
    28. "The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37)."
      Roe S.M., Ali M.M., Meyer P., Vaughan C.K., Panaretou B., Piper P.W., Prodromou C., Pearl L.H.
      Cell 116:87-98(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-214 IN COMPLEX WITH HUMAN CDC37.
    29. "Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery."
      Meyer P.
      EMBO J. 23:511-519(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 272-530 IN COMPLEX WITH AHA1, MUTAGENESIS OF LYS-387.
    30. "Hsp90 is regulated by a switch point in the C-terminal domain."
      Retzlaff M., Stahl M., Eberl H.C., Lagleder S., Beck J., Kessler H., Buchner J.
      EMBO Rep. 10:1147-1153(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ALA-577.
    31. "Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin."
      Roe S.M., Prodromou C., O'Brien R., Ladbury J.E., Piper P.W., Pearl L.H.
      J. Med. Chem. 42:260-266(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-214 IN COMPLEX WITH RADICICOL, ATPASE ACTIVITY.
    32. "Inhibition of Hsp90 with synthetic macrolactones: synthesis and structural and biological evaluation of ring and conformational analogs of radicicol."
      Proisy N., Sharp S.Y., Boxall K., Connelly S., Roe S.M., Prodromou C., Slawin A.M., Pearl L.H., Workman P., Moody C.J.
      Chem. Biol. 13:1203-1215(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1-214 IN COMPLEX WITH INHIBITORS, FUNCTION.
    33. Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 25-210, ATPASE ACTIVITY.
    34. "Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex."
      Ali M.M., Roe S.M., Vaughan C.K., Meyer P., Panaretou B., Piper P.W., Prodromou C., Pearl L.H.
      Nature 440:1013-1017(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 1-677 IN COMPLEX WITH SBA1 AND ATP, SUBUNIT.
    35. Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-219 IN COMPLEX WITH INHIBITOR, ATPASE ACTIVITY.
    36. "Structural basis of the radicicol resistance displayed by a fungal hsp90."
      Prodromou C., Nuttall J.M., Millson S.H., Roe S.M., Sim T.S., Tan D., Workman P., Pearl L.H., Piper P.W.
      ACS Chem. Biol. 4:289-297(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-220 IN COMPLEX WITH ADP; GELDANAMYCIN AND RADICICOL.

    Entry informationi

    Entry nameiHSP82_YEAST
    AccessioniPrimary (citable) accession number: P02829
    Secondary accession number(s): D6W3D1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 169 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 444943 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 XVI
      Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

    External Data

    Dasty 3