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SGD:HSC82

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Contents

Species (Taxon ID) Saccharomyces cerevisiae (baker's yeast) (taxon:4932)
Gene Name(s) HSC82 ( synonyms: YMR186W, HSP90 )
Protein Name(s) Cytoplasmic chaperone of the Hsp90 family,
External Links
SGD S000004798

Annotations

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0000166

nucleotide binding

SGD_REF:S000148669

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0547

F

From SGD

GO:0000492

box C/D snoRNP assembly

SGD_REF:S000136091
PMID:18268103[1]

IMP: Inferred from Mutant Phenotype

P

From SGD

GO:0000723

telomere maintenance

SGD_REF:S000124509
PMID:17954556[2]

IMP: Inferred from Mutant Phenotype

P

From SGD

GO:0001950

plasma membrane enriched fraction

SGD_REF:S000115094
PMID:16622836[3]

IDA: Inferred from Direct Assay

C

From SGD

GO:0005524

ATP binding

SGD_REF:S000124036

IEA: Inferred from Electronic Annotation

InterPro:IPR019805
InterPro:IPR001404
InterPro:IPR003594

F

From SGD

GO:0005524

ATP binding

SGD_REF:S000148669

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0067

F

From SGD

GO:0005737

cytoplasm

SGD_REF:S000074185
PMID:14562095[4]

IDA: Inferred from Direct Assay

C

From SGD

GO:0005737

cytoplasm

SGD_REF:S000148669

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0963

C

From SGD

GO:0005737

cytoplasm

SGD_REF:S000148671

IEA: Inferred from Electronic Annotation

UniProtKB-SubCell:SL-0086

C

From SGD

GO:0005739

mitochondrion

SGD_REF:S000075100
PMID:14576278[5]

IDA: Inferred from Direct Assay

C

From SGD

GO:0005739

mitochondrion

SGD_REF:S000117178
PMID:16823961[6]

IDA: Inferred from Direct Assay

C

From SGD

GO:0005739

mitochondrion

SGD_REF:S000148669

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0496

C

From SGD

GO:0005739

mitochondrion

SGD_REF:S000148671

IEA: Inferred from Electronic Annotation

UniProtKB-SubCell:SL-0173

C

From SGD

GO:0006457

protein folding

SGD_REF:S000040744
PMID:7791797[7]

IMP: Inferred from Mutant Phenotype

P

From SGD

GO:0006457

protein folding

SGD_REF:S000124036

IEA: Inferred from Electronic Annotation

InterPro:IPR019805
InterPro:IPR001404

P

From SGD

GO:0006458

'de novo' protein folding

SGD_REF:S000043994
PMID:2674684[8]

ISS: Inferred from Sequence or Structural Similarity

SGD:S000006161

P

From SGD

GO:0006950

response to stress

SGD_REF:S000043994
PMID:2674684[8]

IMP: Inferred from Mutant Phenotype

P

From SGD

GO:0006950

response to stress

SGD_REF:S000124036

IEA: Inferred from Electronic Annotation

InterPro:IPR001404
InterPro:IPR019805

P

From SGD

GO:0006950

response to stress

SGD_REF:S000148669

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0346

P

From SGD

GO:0016887

ATPase activity

SGD_REF:S000135902
PMID:18492664[9]

IDA: Inferred from Direct Assay

F

From SGD

GO:0042026

protein refolding

SGD_REF:S000043994
PMID:2674684[8]

ISS: Inferred from Sequence or Structural Similarity

SGD:S000006161

P

From SGD

GO:0042623

ATPase activity, coupled

SGD_REF:S000043994
PMID:2674684[8]

ISS: Inferred from Sequence or Structural Similarity

SGD:S000006161

F

From SGD

GO:0043248

proteasome assembly

SGD_REF:S000074028
PMID:12853471[10]

IMP: Inferred from Mutant Phenotype

P

From SGD

GO:0043248

proteasome assembly

SGD_REF:S000074028
PMID:12853471[10]

IPI: Inferred from Physical Interaction

P

From SGD

GO:0051082

unfolded protein binding

SGD_REF:S000050722
PMID:9465043[11]

IDA: Inferred from Direct Assay

F

From SGD

GO:0051082

unfolded protein binding

SGD_REF:S000124036

IEA: Inferred from Electronic Annotation

InterPro:IPR019805
InterPro:IPR001404

F

From SGD


Notes

References

See Help:References for how to manage references in GONUTS.
  1. 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
  2. Toogun OA et al. (2008) The hsp90 molecular chaperone modulates multiple telomerase activities. Mol Cell Biol 28: 457-67 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. Huh WK et al. (2003) Global analysis of protein localization in budding yeast. Nature 425: 686-91 PubMed GONUTS page
  5. Sickmann A et al. (2003) The proteome of Saccharomyces cerevisiae mitochondria. Proc Natl Acad Sci U S A 100: 13207-12 PubMed GONUTS page
  6. 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
  7. 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
  8. 8.0 8.1 8.2 8.3 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
  9. 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
  10. 10.0 10.1 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
  11. 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
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