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YEAST:HSC82

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Species (Taxon ID) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s) HSC82
Protein Name(s) ATP-dependent molecular chaperone HSC82

82 kDa heat shock cognate protein Heat shock protein Hsp90 constitutive isoform

External Links
UniProt P15108
EMBL M26044
Z49808
BK006946
PIR S55133
RefSeq NP_013911.1
ProteinModelPortal P15108
SMR P15108
BioGrid 35364
DIP DIP-1524N
IntAct P15108
MINT MINT-393096
STRING 4932.YMR186W
ChEMBL CHEMBL4199
SWISS-2DPAGE P15108
MaxQB P15108
PaxDb P15108
PeptideAtlas P15108
PRIDE P15108
EnsemblFungi [example_ID YMR186W]
GeneID 855224
KEGG sce:YMR186W
SGD S000004798
eggNOG COG0326
GeneTree ENSGT00760000119253
HOGENOM HOG000031988
InParanoid P15108
KO K04079
OrthoDB EOG7BP8B5
BioCyc YEAST:G3O-32874-MONOMER
Reactome REACT_189032
REACT_189238
REACT_209789
REACT_219346
NextBio 978750
Proteomes UP000002311
Genevestigator P15108
GO GO:0005739
GO:0005524
GO:0016887
GO:0042623
GO:0051082
GO:0006458
GO:0006200
GO:0000492
GO:0034605
GO:0043248
GO:0006457
GO:0042026
GO:0000723
Gene3D 3.30.565.10
HAMAP MF_00505
InterPro IPR003594
IPR019805
IPR001404
IPR020575
IPR020568
PANTHER PTHR11528
Pfam PF02518
PF00183
PIRSF PIRSF002583
PRINTS PR00775
SMART SM00387
SUPFAM SSF54211
SSF55874
PROSITE PS00298

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

part_of

GO:0005739

mitochondrion

PMID:16823961[1]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:14562095[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

PMID:16622836[3]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:14576278[4]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

PMID:9465043[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0043248

proteasome assembly

PMID:12853471[6]

ECO:0000353

physical interaction evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0043248

proteasome assembly

PMID:12853471[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0042623

ATPase activity, coupled

PMID:2674684[7]

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P02829

F

Seeded From UniProt

complete

involved_in

GO:0042026

protein refolding

PMID:2674684[7]

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P02829

P

Seeded From UniProt

complete

involved_in

GO:0034605

cellular response to heat

PMID:2674684[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0016887

ATPase activity

PMID:18492664[8]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006458

'de novo' protein folding

PMID:2674684[7]

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P02829

P

Seeded From UniProt

complete

involved_in

GO:0006457

protein folding

PMID:7791797[9]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0000723

telomere maintenance

PMID:17954556[10]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0000492

box C/D snoRNP assembly

PMID:18268103[11]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

PMID:21873635[12]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0001233
PANTHER:PTN000163629
PomBase:SPAC926.04c
SGD:S000004798
SGD:S000006161

F

Seeded From UniProt

complete

involved_in

GO:0050821

protein stabilization

PMID:21873635[12]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000163629
UniProtKB:P07900
UniProtKB:P11501

P

Seeded From UniProt

complete

part_of

GO:0048471

perinuclear region of cytoplasm

PMID:21873635[12]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0001233
MGI:MGI:96250
PANTHER:PTN000163629
RGD:631409
WB:WBGene00000915

C

Seeded From UniProt

complete

enables

GO:0042623

ATPase activity, coupled

PMID:21873635[12]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000201062
PANTHER:PTN000898156
SGD:S000006161

F

Seeded From UniProt

complete

involved_in

GO:0034605

cellular response to heat

PMID:21873635[12]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000201062
PANTHER:PTN000163629
SGD:S000004798

P

Seeded From UniProt

complete

part_of

GO:0032991

protein-containing complex

PMID:21873635[12]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000163629
RGD:631409
UniProtKB:P07900
UniProtKB:P11501
WB:WBGene00000915

C

Seeded From UniProt

complete

part_of

GO:0009986

cell surface

PMID:21873635[12]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000201062
PANTHER:PTN000163629
RGD:631409
UniProtKB:P11501

C

Seeded From UniProt

complete

involved_in

GO:0009408

response to heat

PMID:21873635[12]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000201062
FB:FBgn0001233
PANTHER:PTN000163629
RGD:631409
SGD:S000004798
UniProtKB:P11501

P

Seeded From UniProt

complete

part_of

GO:0009277

fungal-type cell wall

PMID:21873635[12]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000201062
PANTHER:PTN000898156
UniProtKB:P40292

C

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

PMID:21873635[12]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000201062
MGI:MGI:96250
PANTHER:PTN000163629
RGD:631409
TAIR:locus:2161775
TAIR:locus:2161790
UniProtKB:P11501

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[12]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:96250
PANTHER:PTN000163629
RGD:631409
TAIR:locus:2161775
UniProtKB:P11501
UniProtKB:P40292
dictyBase:DDB_G0267400

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:21873635[12]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000201062
FB:FBgn0001233
MGI:MGI:96250
PANTHER:PTN000163629
RGD:631409
SGD:S000006161
TAIR:locus:2161775
TAIR:locus:2161790
UniProtKB:P07900
UniProtKB:P11501
UniProtKB:P40292
UniProtKB:Q76LV2
UniProtKB:Q8I0V4
WB:WBGene00000915
ZFIN:ZDB-GENE-990415-94
dictyBase:DDB_G0267400

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

PMID:21873635[12]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000898156
PomBase:SPAC926.04c

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001404
InterPro:IPR019805

F

Seeded From UniProt

complete

involved_in

GO:0006457

protein folding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001404
InterPro:IPR019805

P

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001404
InterPro:IPR019805

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0496
UniProtKB-SubCell:SL-0173

C

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

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Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ Reinders, J et al. (2006) Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J. Proteome Res. 5 1543-54 PubMed GONUTS page
  2. ↑ Huh, WK et al. (2003) Global analysis of protein localization in budding yeast. Nature 425 686-91 PubMed GONUTS page
  3. ↑ Delom, F et al. (2006) The plasma membrane proteome of Saccharomyces cerevisiae and its response to the antifungal calcofluor. Proteomics 6 3029-39 PubMed GONUTS page
  4. ↑ Sickmann, A et al. (2003) The proteome of Saccharomyces cerevisiae mitochondria. Proc. Natl. Acad. Sci. U.S.A. 100 13207-12 PubMed GONUTS page
  5. ↑ Scheibel, T et al. (1998) Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence. Proc. Natl. Acad. Sci. U.S.A. 95 1495-9 PubMed GONUTS page
  6. ↑ 6.0 6.1 Imai, J et al. (2003) The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome. EMBO J. 22 3557-67 PubMed GONUTS page
  7. ↑ 7.0 7.1 7.2 7.3 Borkovich, KA et al. (1989) hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures. Mol. Cell. Biol. 9 3919-30 PubMed GONUTS page
  8. ↑ Cunningham, CN et al. (2008) Intra- and intermonomer interactions are required to synergistically facilitate ATP hydrolysis in Hsp90. J. Biol. Chem. 283 21170-8 PubMed GONUTS page
  9. ↑ Nathan, DF & Lindquist, S (1995) Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase. Mol. Cell. Biol. 15 3917-25 PubMed GONUTS page
  10. ↑ Toogun, OA et al. (2008) The hsp90 molecular chaperone modulates multiple telomerase activities. Mol. Cell. Biol. 28 457-67 PubMed GONUTS page
  11. ↑ Zhao, R et al. (2008) Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation. J. Cell Biol. 180 563-78 PubMed GONUTS page
  12. ↑ 12.00 12.01 12.02 12.03 12.04 12.05 12.06 12.07 12.08 12.09 12.10 12.11 12.12 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
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