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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: -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

Miscellaneous

Present with 444943 molecules/cell in log phase SD medium.1 Publication

Activity 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)DescriptionActionsGraphical viewLength
Binding sitei33ATPCombined sources1 Publication1
Binding sitei37ATPCombined sources1 Publication1
Binding sitei79ATPCombined sources1 Publication1
Binding sitei84ATPCombined sources1 Publication1
Binding sitei92ATPCombined sources1 Publication1
Binding sitei98ATPCombined sources1 Publication1
Binding sitei171ATPCombined sources1 Publication1
Binding sitei380ATPCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi99 – 100ATPCombined sources1 Publication2
Nucleotide bindingi119 – 124ATPCombined sources1 Publication6

GO - Molecular functioni

  • ATPase activity, coupled Source: SGD
  • ATP binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • unfolded protein binding Source: SGD

GO - Biological processi

Keywordsi

Molecular functionChaperone
Biological processStress response
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-34126-MONOMER
ReactomeiR-SCE-1474151 Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation
R-SCE-203615 eNOS activation
R-SCE-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-SCE-3371511 HSF1 activation
R-SCE-3371568 Attenuation phase
R-SCE-3371571 HSF1-dependent transactivation
R-SCE-5218920 VEGFR2 mediated vascular permeability
R-SCE-6785807 Interleukin-4 and Interleukin-13 signaling
R-SCE-6798695 Neutrophil degranulation
R-SCE-844456 The NLRP3 inflammasome
R-SCE-8939211 ESR-mediated signaling

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
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

SGDiS000006161 HSP82

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi22T → I: Induces a 6-fold increase in ATPase activity and a reduced client protein activation activity, leading to growth defect at high temperatures. 1 Publication1
Mutagenesisi41A → V: Causes a 98% reduction in ATPase activity and a reduced client protein activation activity, leading to growth defect at high temperatures. 1 Publication1
Mutagenesisi81G → S: Reduces client protein activation activity, leading to growth defect at high temperatures. 1 Publication1
Mutagenesisi83G → D: Abolishes ATPase activity. 1 Publication1
Mutagenesisi97A → I: Abolishes interaction with SBA1. 1 Publication1
Mutagenesisi101T → I: Causes a 90% reduction in ATPase activity and a reduced client protein activation activity, leading to growth defect at high temperatures. 1 Publication1
Mutagenesisi107A → N: Induces a 6-fold increase in ATPase activity. 1 Publication1
Mutagenesisi170G → D: Induces a total loss of function at 34 degrees Celsius. Abolishes interaction with SBA1. 1 Publication1
Mutagenesisi313G → N or S: Reduces client protein activation activity, leading to growth defect at high temperatures. 2 Publications1
Mutagenesisi349F → A or Q: Induces a loss of ATPase activity. Can be reactivated by AHA1. 1 Publication1
Mutagenesisi380R → A: Induces a loss of ATPase activity. 1 Publication1
Mutagenesisi381E → K: Reduces client protein activation activity. Resistant to ATPase activation by AHA1. 1 Publication1
Mutagenesisi384Q → A: Induces a loss of ATPase activity. 1 Publication1
Mutagenesisi387K → A: Decreases AHA1 binding affinity, but has no effect on client protein activation activity. 1 Publication1
Mutagenesisi387K → D: Decreases AHA1 binding affinity and substantially reduces client protein activation activity. 1 Publication1
Mutagenesisi431E → K: Specifically reduces the activation of the exogenous ligand glucocorticoid receptor. 1 Publication1
Mutagenesisi485S → Y: Abolishes interaction with SBA1. 1 Publication1
Mutagenesisi525T → I: Abolishes interaction with SBA1. Reduces client protein activation activity, leading to growth defect at high temperatures. 1 Publication1
Mutagenesisi576A → T: Reduces client protein activation activity; when associated with K-579. 1 Publication1
Mutagenesisi577A → C: Enhances ATPase activity and client protein activation. 1 Publication1
Mutagenesisi577A → D: Reduces ATPase activity and client protein activation. 1 Publication1
Mutagenesisi577A → I: Enhances homodimerization, ATPase activity and client protein activation. 1 Publication1
Mutagenesisi577A → N: Reduces homodimerization, ATPase activity and client protein activation. 1 Publication1
Mutagenesisi579R → K: Reduces client protein activation activity; when associated with T-576. 1 Publication1
Mutagenesisi587A → T: No effect on ATPase activity. Reduces client protein activation activity, leading to growth defect at high temperatures. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3536

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000629571 – 709ATP-dependent molecular chaperone HSP82Add BLAST709

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei657PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP02829
PaxDbiP02829
PRIDEiP02829

2D gel databases

SWISS-2DPAGEiP02829

PTM databases

iPTMnetiP02829

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

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi35923, 1612 interactors
ComplexPortaliCPX-1276 HMC complex
DIPiDIP-2262N
IntActiP02829, 381 interactors
MINTiP02829
STRINGi4932.YPL240C

Chemistry databases

BindingDBiP02829

Structurei

Secondary structure

1709
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP02829
SMRiP02829
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02829

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati221 – 22511 Publication5
Repeati226 – 23021 Publication5
Repeati231 – 23531 Publication5
Repeati237 – 24141 Publication5
Repeati250 – 25451 Publication5

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni221 – 2635 X 5 AA repeats of [DE]-[DE]-[DE]-K-K; highly charged regionAdd BLAST43

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi705 – 709TPR repeat-binding5

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

GeneTreeiENSGT00920000149061
HOGENOMiHOG000031988
InParanoidiP02829
KOiK04079
OMAiVKRHSEF
OrthoDBiEOG092C1GW3

Family and domain databases

CDDicd00075 HATPase_c, 1 hit
Gene3Di1.20.120.790, 1 hit
3.30.565.10, 1 hit
HAMAPiMF_00505 HSP90, 1 hit
InterProiView protein in InterPro
IPR003594 HATPase_C
IPR036890 HATPase_C_sf
IPR019805 Heat_shock_protein_90_CS
IPR037196 HSP90_C
IPR001404 Hsp90_fam
IPR020575 Hsp90_N
IPR020568 Ribosomal_S5_D2-typ_fold
PANTHERiPTHR11528 PTHR11528, 1 hit
PfamiView protein in Pfam
PF02518 HATPase_c, 1 hit
PF00183 HSP90, 1 hit
PIRSFiPIRSF002583 Hsp90, 1 hit
PRINTSiPR00775 HEATSHOCK90
SMARTiView protein in SMART
SM00387 HATPase_c, 1 hit
SUPFAMiSSF110942 SSF110942, 1 hit
SSF54211 SSF54211, 1 hit
SSF55874 SSF55874, 1 hit
PROSITEiView protein in PROSITE
PS00298 HSP90, 1 hit

Sequencei

Sequence statusi: Complete.

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)DescriptionActionsGraphical viewLength
Sequence conflicti481A → S (PubMed:12667448).Curated1

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

Similar proteinsi

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
PIRiA03313 HHBY90
RefSeqiNP_015084.1, NM_001184054.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5MGXX-ray2.18A/B/C/D702-709[»]
ProteinModelPortaliP02829
SMRiP02829
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35923, 1612 interactors
ComplexPortaliCPX-1276 HMC complex
DIPiDIP-2262N
IntActiP02829, 381 interactors
MINTiP02829
STRINGi4932.YPL240C

Chemistry databases

BindingDBiP02829
ChEMBLiCHEMBL3536

PTM databases

iPTMnetiP02829

2D gel databases

SWISS-2DPAGEiP02829

Proteomic databases

MaxQBiP02829
PaxDbiP02829
PRIDEiP02829

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL240C; YPL240C; YPL240C
GeneIDi855836
KEGGisce:YPL240C

Organism-specific databases

SGDiS000006161 HSP82

Phylogenomic databases

GeneTreeiENSGT00920000149061
HOGENOMiHOG000031988
InParanoidiP02829
KOiK04079
OMAiVKRHSEF
OrthoDBiEOG092C1GW3

Enzyme and pathway databases

BioCyciYEAST:G3O-34126-MONOMER
ReactomeiR-SCE-1474151 Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation
R-SCE-203615 eNOS activation
R-SCE-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-SCE-3371511 HSF1 activation
R-SCE-3371568 Attenuation phase
R-SCE-3371571 HSF1-dependent transactivation
R-SCE-5218920 VEGFR2 mediated vascular permeability
R-SCE-6785807 Interleukin-4 and Interleukin-13 signaling
R-SCE-6798695 Neutrophil degranulation
R-SCE-844456 The NLRP3 inflammasome
R-SCE-8939211 ESR-mediated signaling

Miscellaneous databases

EvolutionaryTraceiP02829
PROiPR:P02829

Family and domain databases

CDDicd00075 HATPase_c, 1 hit
Gene3Di1.20.120.790, 1 hit
3.30.565.10, 1 hit
HAMAPiMF_00505 HSP90, 1 hit
InterProiView protein in InterPro
IPR003594 HATPase_C
IPR036890 HATPase_C_sf
IPR019805 Heat_shock_protein_90_CS
IPR037196 HSP90_C
IPR001404 Hsp90_fam
IPR020575 Hsp90_N
IPR020568 Ribosomal_S5_D2-typ_fold
PANTHERiPTHR11528 PTHR11528, 1 hit
PfamiView protein in Pfam
PF02518 HATPase_c, 1 hit
PF00183 HSP90, 1 hit
PIRSFiPIRSF002583 Hsp90, 1 hit
PRINTSiPR00775 HEATSHOCK90
SMARTiView protein in SMART
SM00387 HATPase_c, 1 hit
SUPFAMiSSF110942 SSF110942, 1 hit
SSF54211 SSF54211, 1 hit
SSF55874 SSF55874, 1 hit
PROSITEiView protein in PROSITE
PS00298 HSP90, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiHSP82_YEAST
AccessioniPrimary (citable) accession number: P02829
Secondary accession number(s): D6W3D1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 7, 2018
This is version 213 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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