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P02829

- HSP82_YEAST

UniProt

P02829 - HSP82_YEAST

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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

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. 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
Complete GO annotation...

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_209789. HSF1 activation.
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-KW
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

GeneTreeiENSGT00770000120625.
HOGENOMiHOG000031988.
InParanoidiP02829.
KOiK04079.
OMAiASADVHM.
OrthoDBiEOG7BP8B5.

Family and domain databases

Gene3Di3.30.565.10. 1 hit.
HAMAPiMF_00505. HSP90.
InterProiIPR003594. HATPase_C.
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

        10         20         30         40         50
MASETFEFQA EITQLMSLII NTVYSNKEIF LRELISNASD ALDKIRYKSL
60 70 80 90 100
SDPKQLETEP DLFIRITPKP EQKVLEIRDS GIGMTKAELI NNLGTIAKSG
110 120 130 140 150
TKAFMEALSA GADVSMIGQF GVGFYSLFLV ADRVQVISKS NDDEQYIWES
160 170 180 190 200
NAGGSFTVTL DEVNERIGRG TILRLFLKDD QLEYLEEKRI KEVIKRHSEF
210 220 230 240 250
VAYPIQLVVT KEVEKEVPIP EEEKKDEEKK DEEKKDEDDK KPKLEEVDEE
260 270 280 290 300
EEKKPKTKKV KEEVQEIEEL NKTKPLWTRN PSDITQEEYN AFYKSISNDW
310 320 330 340 350
EDPLYVKHFS VEGQLEFRAI LFIPKRAPFD LFESKKKKNN IKLYVRRVFI
360 370 380 390 400
TDEAEDLIPE WLSFVKGVVD SEDLPLNLSR EMLQQNKIMK VIRKNIVKKL
410 420 430 440 450
IEAFNEIAED SEQFEKFYSA FSKNIKLGVH EDTQNRAALA KLLRYNSTKS
460 470 480 490 500
VDELTSLTDY VTRMPEHQKN IYYITGESLK AVEKSPFLDA LKAKNFEVLF
510 520 530 540 550
LTDPIDEYAF TQLKEFEGKT LVDITKDFEL EETDEEKAER EKEIKEYEPL
560 570 580 590 600
TKALKEILGD QVEKVVVSYK LLDAPAAIRT GQFGWSANME RIMKAQALRD
610 620 630 640 650
SSMSSYMSSK KTFEISPKSP IIKELKKRVD EGGAQDKTVK DLTKLLYETA
660 670 680 690 700
LLTSGFSLDE PTSFASRINR LISLGLNIDE DEETETAPEA STAAPVEEVP

ADTEMEEVD
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 ENSGT00770000120625.
HOGENOMi HOG000031988.
InParanoidi P02829.
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_209789. HSF1 activation.
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_C.
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.
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Publicationsi

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  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: November 26, 2014
This is version 171 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