GONUTS is under stress! The website is currently experiencing long-wait times and frequent time-outs due to the record number of students, groups, and annotations related to CACAO this semester. We are currently working on increasing performance -- please accept our apologies for the technical difficulties.
You can help reduce stress on the server by:
- not reloading pages frequently - this just adds
- opening links in new windows (so you can read the old page)
SGD:HSP82
Contents |
| Species (Taxon ID) | Saccharomyces cerevisiae (baker's yeast) (taxon:4932) | |
| Gene Name(s) | HSP82 ( synonyms: YPL240C, HSP90 ) | |
| Protein Name(s) | Hsp90 chaperone involved in pheromone signaling and regulating Hsf1p, | |
| External Links | ||
| SGD | S000006161 | |
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 |
IMP: Inferred from Mutant Phenotype |
P |
From SGD |
|||
| GO:0005524 |
ATP binding |
SGD_REF:S000124036 |
IEA: Inferred from Electronic Annotation |
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:S000069459 |
IDA: Inferred from Direct Assay |
C |
From SGD |
|||
| GO:0005737 |
cytoplasm |
SGD_REF:S000074185 |
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:0006457 |
protein folding |
SGD_REF:S000124036 |
IEA: Inferred from Electronic Annotation |
P |
From SGD |
|||
| GO:0006458 |
'de novo' protein folding |
SGD_REF:S000043873 |
IDA: Inferred from Direct Assay |
P |
From SGD |
|||
| GO:0006458 |
'de novo' protein folding |
SGD_REF:S000045779 |
IMP: Inferred from Mutant Phenotype |
P |
From SGD |
|||
| GO:0006626 |
protein targeting to mitochondrion |
SGD_REF:S000072572 |
IPI: Inferred from Physical Interaction |
SGD:S000005065 |
P |
From SGD |
||
| GO:0006950 |
response to stress |
SGD_REF:S000043994 |
IMP: Inferred from Mutant Phenotype |
P |
From SGD |
|||
| GO:0006950 |
response to stress |
SGD_REF:S000124036 |
IEA: Inferred from Electronic Annotation |
P |
From SGD |
|||
| GO:0006950 |
response to stress |
SGD_REF:S000148669 |
IEA: Inferred from Electronic Annotation |
UniProtKB-KW:KW-0346 |
P |
From SGD |
||
| GO:0006970 |
response to osmotic stress |
SGD_REF:S000114463 |
IMP: Inferred from Mutant Phenotype |
P |
From SGD |
|||
| GO:0032212 |
positive regulation of telomere maintenance via telomerase |
SGD_REF:S000124509 |
IDA: Inferred from Direct Assay |
P |
From SGD |
|||
| GO:0032212 |
positive regulation of telomere maintenance via telomerase |
SGD_REF:S000124509 |
IMP: Inferred from Mutant Phenotype |
P |
From SGD |
|||
| GO:0032212 |
positive regulation of telomere maintenance via telomerase |
SGD_REF:S000124509 |
IPI: Inferred from Physical Interaction |
P |
From SGD |
|||
| GO:0042026 |
protein refolding |
SGD_REF:S000045779 |
IMP: Inferred from Mutant Phenotype |
P |
From SGD |
|||
| GO:0042623 |
ATPase activity, coupled |
SGD_REF:S000072038 |
IDA: Inferred from Direct Assay |
F |
From SGD |
|||
| GO:0043248 |
proteasome assembly |
SGD_REF:S000074028 |
IDA: Inferred from Direct Assay |
P |
From SGD |
|||
| GO:0043248 |
proteasome assembly |
SGD_REF:S000074028 |
IGI: Inferred from Genetic Interaction |
P |
From SGD |
|||
| GO:0043248 |
proteasome assembly |
SGD_REF:S000074028 |
IMP: Inferred from Mutant Phenotype |
P |
From SGD |
|||
| GO:0051082 |
unfolded protein binding |
SGD_REF:S000043873 |
IDA: Inferred from Direct Assay |
F |
From SGD |
|||
| GO:0051082 |
unfolded protein binding |
SGD_REF:S000124036 |
IEA: Inferred from Electronic Annotation |
F |
From SGD |
| ||
| edit table |
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 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
- ↑ 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
- ↑ 4.0 4.1 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
- ↑ 5.0 5.1 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
- ↑ 9.0 9.1 9.2 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
- ↑ 11.0 11.1 11.2 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
'abc |
np |
p cont.ru |
