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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei33 – 331ATPCombined sources1 Publication
Binding sitei37 – 371ATPCombined sources1 Publication
Binding sitei79 – 791ATPCombined sources1 Publication
Binding sitei84 – 841ATPCombined sources1 Publication
Binding sitei92 – 921ATPCombined sources1 Publication
Binding sitei98 – 981ATPCombined sources1 Publication
Binding sitei171 – 1711ATPCombined sources1 Publication
Binding sitei380 – 3801ATPCombined sources1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi99 – 1002ATPCombined sources1 Publication
Nucleotide bindingi119 – 1246ATPCombined sources1 Publication

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.
ReactomeiR-SCE-1474151. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
R-SCE-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-SCE-203615. eNOS activation.
R-SCE-3371511. HSF1 activation.
R-SCE-3371568. Attenuation phase.
R-SCE-3371571. HSF1-dependent transactivation.
R-SCE-399954. Sema3A PAK dependent Axon repulsion.
R-SCE-5218920. VEGFR2 mediated vascular permeability.
R-SCE-844456. The NLRP3 inflammasome.

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

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

Chemistry

ChEMBLiCHEMBL3536.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy 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.
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 interactions.
DIPiDIP-2262N.
IntActiP02829. 338 interactions.
MINTiMINT-560200.

Chemistry

BindingDBiP02829.

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 strandi335 – 3373Combined 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

GeneTreeiENSGT00840000130044.
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)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.
PIRiA03313. HHBY90.
RefSeqiNP_015084.1. NM_001184054.1.

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...

Protein-protein interaction databases

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

Chemistry

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

GeneTreeiENSGT00840000130044.
HOGENOMiHOG000031988.
InParanoidiP02829.
KOiK04079.
OMAiFISYSIY.
OrthoDBiEOG092C1GW3.

Enzyme and pathway databases

BioCyciYEAST:G3O-34126-MONOMER.
ReactomeiR-SCE-1474151. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
R-SCE-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-SCE-203615. eNOS activation.
R-SCE-3371511. HSF1 activation.
R-SCE-3371568. Attenuation phase.
R-SCE-3371571. HSF1-dependent transactivation.
R-SCE-399954. Sema3A PAK dependent Axon repulsion.
R-SCE-5218920. VEGFR2 mediated vascular permeability.
R-SCE-844456. The NLRP3 inflammasome.

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: September 7, 2016
This is version 191 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.