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YEAST:HSP82
Contents |
| Species (Taxon ID) | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). ([1]) | |
| Gene Name(s) | HSP82 (synonyms: HSP90) | |
| Protein Name(s) | ATP-dependent molecular chaperone HSP82
82 kDa heat shock protein Heat shock protein Hsp90 heat-inducible isoform | |
| External Links | ||
| EMBL | K01387 Z67751 Z73596 BK006949 | |
| PIR | A03313 | |
| RefSeq | NP_015084.1 | |
| PDB | 1A4H 1AH6 1AH8 1AM1 1AMW 1BGQ 1HK7 1US7 1USU 1USV 1ZW9 1ZWH 2AKP 2BRC 2BRE 2CG9 2CGE 2CGF 2FXS 2IWS 2IWU 2IWX 2VW5 2VWC 2WEP 2WEQ 2WER 2XD6 3C0E 3C11 3FP2 | |
| PDBsum | 1A4H 1AH6 1AH8 1AM1 1AMW 1BGQ 1HK7 1US7 1USU 1USV 1ZW9 1ZWH 2AKP 2BRC 2BRE 2CG9 2CGE 2CGF 2FXS 2IWS 2IWU 2IWX 2VW5 2VWC 2WEP 2WEQ 2WER 2XD6 3C0E 3C11 3FP2 | |
| ProteinModelPortal | P02829 | |
| SMR | P02829 | |
| DIP | DIP-2262N | |
| IntAct | P02829 | |
| MINT | MINT-560200 | |
| STRING | P02829 | |
| SWISS-2DPAGE | P02829 | |
| PeptideAtlas | P02829 | |
| PRIDE | P02829 | |
| EnsemblFungi | YPL240C | |
| GeneID | 855836 | |
| KEGG | sce:YPL240C | |
| NMPDR | fig|4932.3.peg.6211 | |
| CYGD | YPL240c | |
| SGD | S000006161 | |
| eggNOG | fuNOG05217 | |
| GeneTree | EFGT00050000005875 | |
| HOGENOM | HBG631012 | |
| OMA | GFSKNIK | |
| OrthoDB | EOG4643M4 | |
| PhylomeDB | P02829 | |
| NextBio | 980407 | |
| ArrayExpress | P02829 | |
| Genevestigator | P02829 | |
| GermOnline | YPL240C | |
| GO | GO:0005737 GO:0005524 GO:0042623 GO:0051082 GO:0006458 GO:0032212 GO:0043248 GO:0042026 GO:0006626 GO:0006970 | |
| InterPro | IPR003594 IPR019805 IPR001404 IPR020575 IPR020568 | |
| Gene3D | G3DSA:3.30.565.10 | |
| PANTHER | PTHR11528 | |
| Pfam | PF02518 PF00183 | |
| PIRSF | PIRSF002583 | |
| PRINTS | PR00775 | |
| SMART | SM00387 | |
| SUPFAM | SSF55874 SSF54211 | |
| PROSITE | PS00298 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | Evidence Code | with/from | Aspect | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0000166 |
nucleotide binding |
IEA: Inferred from Electronic Annotation |
F |
Seeded From UniProt |
||||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded From UniProt |
||||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded From UniProt |
||||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded From UniProt |
||||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded From UniProt |
||||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded From UniProt |
||||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded From UniProt |
||||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded From UniProt |
||||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded From UniProt |
||||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded From UniProt |
||||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded From UniProt |
||||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded From UniProt |
||||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded From UniProt |
||||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded From UniProt |
||||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded From UniProt |
||||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded From UniProt |
||||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded From UniProt |
||||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded From UniProt |
||||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded From UniProt |
||||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded From UniProt |
||||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded From UniProt |
||||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded From UniProt |
||||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded From UniProt |
||||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded From UniProt |
||||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded From UniProt |
||||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded From UniProt |
||||
| GO:0005524 |
ATP binding |
IEA: Inferred from Electronic Annotation |
F |
Seeded From UniProt |
||||
| GO:0005524 |
ATP binding |
IEA: Inferred from Electronic Annotation |
F |
Seeded From UniProt |
||||
| GO:0005524 |
ATP binding |
IEA: Inferred from Electronic Annotation |
F |
Seeded From UniProt |
||||
| GO:0005524 |
ATP binding |
IEA: Inferred from Electronic Annotation |
F |
Seeded From UniProt |
||||
| GO:0005737 |
cytoplasm |
IEA: Inferred from Electronic Annotation |
C |
Seeded From UniProt |
||||
| GO:0005737 |
cytoplasm |
IEA: Inferred from Electronic Annotation |
SP_SL:SL-0086 |
C |
Seeded From UniProt |
|||
| GO:0005737 |
cytoplasm |
IDA: Inferred from Direct Assay |
|
C |
Seeded From UniProt |
|||
| GO:0005737 |
cytoplasm |
IDA: Inferred from Direct Assay |
|
C |
Seeded From UniProt |
|||
| GO:0006457 |
protein folding |
IEA: Inferred from Electronic Annotation |
P |
Seeded From UniProt |
||||
| GO:0006457 |
protein folding |
IEA: Inferred from Electronic Annotation |
P |
Seeded From UniProt |
||||
| GO:0006458 |
'de novo' protein folding |
IDA: Inferred from Direct Assay |
|
P |
Seeded From UniProt |
|||
| GO:0006458 |
'de novo' protein folding |
IMP: Inferred from Mutant Phenotype |
|
P |
Seeded From UniProt |
|||
| GO:0006626 |
protein targeting to mitochondrion |
IPI: Inferred from Physical Interaction |
SGD:S000005065 |
P |
Seeded From UniProt |
|||
| GO:0006950 |
response to stress |
IEA: Inferred from Electronic Annotation |
P |
Seeded From UniProt |
||||
| GO:0006950 |
response to stress |
IEA: Inferred from Electronic Annotation |
P |
Seeded From UniProt |
||||
| GO:0006950 |
response to stress |
IEA: Inferred from Electronic Annotation |
P |
Seeded From UniProt |
||||
| GO:0006950 |
response to stress |
IMP: Inferred from Mutant Phenotype |
|
P |
Seeded From UniProt |
|||
| GO:0006970 |
response to osmotic stress |
IMP: Inferred from Mutant Phenotype |
|
P |
Seeded From UniProt |
|||
| GO:0032212 |
positive regulation of telomere maintenance via telomerase |
IDA: Inferred from Direct Assay |
|
P |
Seeded From UniProt |
|||
| GO:0042026 |
protein refolding |
IMP: Inferred from Mutant Phenotype |
|
P |
Seeded From UniProt |
|||
| GO:0042623 |
ATPase activity, coupled |
IDA: Inferred from Direct Assay |
|
F |
Seeded From UniProt |
|||
| GO:0043248 |
proteasome assembly |
IGI: Inferred from Genetic Interaction |
|
P |
Seeded From UniProt |
|||
| GO:0051082 |
unfolded protein binding |
IEA: Inferred from Electronic Annotation |
F |
Seeded From UniProt |
||||
| GO:0051082 |
unfolded protein binding |
IEA: Inferred from Electronic Annotation |
F |
Seeded From UniProt |
||||
| GO:0051082 |
unfolded protein binding |
IDA: Inferred from Direct Assay |
|
F |
Seeded From UniProt |
|||
| GO:0032204 |
regulation of telomere maintenance |
IMP: Inferred from Mutant Phenotype |
P |
Figure 1B. |
complete | |||
| edit table |
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Baetz KK et al. (2004) The ctf13-30/CTF13 genomic haploinsufficiency modifier screen identifies the yeast chromatin remodeling complex RSC, which is required for the establishment of sister chromatid cohesion. Mol Cell Biol 24: 1232-44 PubMed GONUTS page
- ↑ Lan C et al. (2004) A novel mode of chaperone action: heme activation of Hap1 by enhanced association of Hsp90 with the repressed Hsp70-Hap1 complex. J Biol Chem 279: 27607-12 PubMed GONUTS page
- ↑ 3.00 3.01 3.02 3.03 3.04 3.05 3.06 3.07 3.08 3.09 3.10 3.11 3.12 3.13 Zhao R et al. (2005) Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone. Cell 120: 715-27 PubMed GONUTS page
- ↑ 4.0 4.1 Millson SH et al. (2005) A two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p). Eukaryot Cell 4: 849-60 PubMed GONUTS page
- ↑ Gavin AC et al. (2006) Proteome survey reveals modularity of the yeast cell machinery. Nature 440: 631-6 PubMed GONUTS page
- ↑ 6.0 6.1 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
- ↑ Obermann WM et al. (1998) In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis. J Cell Biol 143: 901-10 PubMed GONUTS page
- ↑ 8.0 8.1 8.2 Marsh JA et al. (1998) Cns1 is an essential protein associated with the hsp90 chaperone complex in Saccharomyces cerevisiae that can restore cyclophilin 40-dependent functions in cpr7Delta cells. Mol Cell Biol 18: 7353-9 PubMed GONUTS page
- ↑ Kumar A et al. (2002) Subcellular localization of the yeast proteome. Genes Dev 16: 707-19 PubMed GONUTS page
- ↑ Huh WK et al. (2003) Global analysis of protein localization in budding yeast. Nature 425: 686-91 PubMed GONUTS page
- ↑ 11.0 11.1 Scheibel T et al. (1999) Contribution of N- and C-terminal domains to the function of Hsp90 in Saccharomyces cerevisiae. Mol Microbiol 34: 701-13 PubMed GONUTS page
- ↑ 12.0 12.1 Nathan DF et al. (1997) In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone. Proc Natl Acad Sci U S A 94: 12949-56 PubMed GONUTS page
- ↑ Young JC et al. (2003) Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70. Cell 112: 41-50 PubMed GONUTS page
- ↑ 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
- ↑ Yang XX et al. (2006) The molecular chaperone Hsp90 is required for high osmotic stress response in Saccharomyces cerevisiae. FEMS Yeast Res 6: 195-204 PubMed GONUTS page
- ↑ Toogun OA et al. (2008) The hsp90 molecular chaperone modulates multiple telomerase activities. Mol Cell Biol 28: 457-67 PubMed GONUTS page
- ↑ Richter K et al. (2002) N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle. J Biol Chem 277: 44905-10 PubMed GONUTS page
- ↑ 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
- ↑ Laskar S et al. (2011) HSP90 controls SIR2 mediated gene silencing. PLoS One 6: e23406 PubMed GONUTS page
