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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: 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)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

  • 'de novo' protein folding Source: SGD
  • box C/D snoRNP assembly Source: SGD
  • positive regulation of telomere maintenance via telomerase Source: SGD
  • proteasome assembly Source: SGD
  • protein maturation Source: SGD
  • protein refolding Source: SGD
  • protein targeting to mitochondrion Source: SGD
  • regulation of telomere maintenance Source: CACAO
  • 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.

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

EuPathDBiFungiDB:YPL240C.
SGDiS000006161. HSP82.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
Complete GO annotation...

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
Initiator methionineiRemovedBy similarity
ChainiPRO_00000629572 – 709ATP-dependent molecular chaperone HSP82Add BLAST708

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei657PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP02829.
PRIDEiP02829.

2D gel databases

SWISS-2DPAGEP02829.

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

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

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • unfolded protein binding Source: SGD

Protein-protein interaction databases

BioGridi35923. 1484 interactors.
DIPiDIP-2262N.
IntActiP02829. 338 interactors.
MINTiMINT-560200.

Chemistry databases

BindingDBiP02829.

Structurei

Secondary structure

1709
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 7Combined sources4
Helixi10 – 21Combined sources12
Helixi26 – 28Combined sources3
Helixi29 – 48Combined sources20
Turni49 – 51Combined sources3
Helixi53 – 56Combined sources4
Beta strandi64 – 69Combined sources6
Helixi70 – 72Combined sources3
Beta strandi74 – 79Combined sources6
Helixi86 – 93Combined sources8
Turni95 – 97Combined sources3
Helixi101 – 110Combined sources10
Helixi114 – 120Combined sources7
Helixi123 – 129Combined sources7
Beta strandi131 – 139Combined sources9
Beta strandi146 – 150Combined sources5
Beta strandi152 – 160Combined sources9
Beta strandi162 – 164Combined sources3
Beta strandi168 – 177Combined sources10
Helixi182 – 185Combined sources4
Helixi187 – 197Combined sources11
Beta strandi200 – 203Combined sources4
Beta strandi205 – 207Combined sources3
Helixi276 – 278Combined sources3
Helixi281 – 283Combined sources3
Helixi286 – 297Combined sources12
Beta strandi304 – 311Combined sources8
Beta strandi313 – 315Combined sources3
Beta strandi317 – 323Combined sources7
Turni329 – 332Combined sources4
Beta strandi335 – 337Combined sources3
Beta strandi341 – 345Combined sources5
Beta strandi348 – 352Combined sources5
Beta strandi355 – 358Combined sources4
Helixi360 – 362Combined sources3
Beta strandi366 – 373Combined sources8
Helixi380 – 383Combined sources4
Helixi387 – 408Combined sources22
Helixi411 – 431Combined sources21
Turni433 – 435Combined sources3
Helixi436 – 440Combined sources5
Beta strandi444 – 447Combined sources4
Beta strandi450 – 456Combined sources7
Helixi457 – 462Combined sources6
Beta strandi470 – 475Combined sources6
Helixi479 – 483Combined sources5
Helixi488 – 493Combined sources6
Beta strandi498 – 501Combined sources4
Helixi504 – 513Combined sources10
Beta strandi519 – 523Combined sources5
Turni524 – 526Combined sources3
Beta strandi530 – 533Combined sources4
Helixi535 – 558Combined sources24
Beta strandi563 – 567Combined sources5
Beta strandi573 – 580Combined sources8
Beta strandi582 – 584Combined sources3
Helixi587 – 597Combined sources11
Beta strandi600 – 602Combined sources3
Beta strandi611 – 615Combined sources5
Helixi620 – 629Combined sources10
Turni630 – 632Combined sources3
Helixi633 – 635Combined sources3
Helixi637 – 653Combined sources17
Helixi661 – 676Combined sources16

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[»]
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

GeneTreeiENSGT00850000132363.
HOGENOMiHOG000031988.
InParanoidiP02829.
KOiK04079.
OMAiFISYSIY.
OrthoDBiEOG092C1GW3.

Family and domain databases

Gene3Di3.30.565.10. 1 hit.
HAMAPiMF_00505. HSP90. 1 hit.
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)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.

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[»]
ProteinModelPortaliP02829.
SMRiP02829.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35923. 1484 interactors.
DIPiDIP-2262N.
IntActiP02829. 338 interactors.
MINTiMINT-560200.

Chemistry databases

BindingDBiP02829.
ChEMBLiCHEMBL3536.

PTM databases

iPTMnetiP02829.

2D gel databases

SWISS-2DPAGEP02829.

Proteomic databases

MaxQBiP02829.
PRIDEiP02829.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YPL240C.
SGDiS000006161. HSP82.

Phylogenomic databases

GeneTreeiENSGT00850000132363.
HOGENOMiHOG000031988.
InParanoidiP02829.
KOiK04079.
OMAiFISYSIY.
OrthoDBiEOG092C1GW3.

Enzyme and pathway databases

BioCyciYEAST:G3O-34126-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP02829.
PROiP02829.

Family and domain databases

Gene3Di3.30.565.10. 1 hit.
HAMAPiMF_00505. HSP90. 1 hit.
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]
ProtoNetiSearch...

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 30, 2016
This is version 194 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.