Type | Description |
---|---|
Definition | Hsp90 family chaperone HSC82 |
Date | Results | Publications |
---|---|---|
2013-11-30 11:58:00 | Mutation or inhibition of Hsp90 resulted in decreased accumulation of Ura2, indicating it is an Hsp90 client. Cpr6 interacted with Ura2 in the absence of stable Cpr6-Hsp90 interaction, suggesting a direct interaction. | 23926110 |
2011-09-24 12:07:00 | Hsc82 is more critical than Hsp82 for growth at 37 degrees C in the absence of mitochondrial DNA. | 21439406 |
2010-01-21 00:00:00 | Hsp90 prevented the death of calcineurin- and Cmk2-deficient cells. | 18806210 |
2010-01-21 00:00:00 | These data support a conserved three-state chaperone cycle where the conformational equilibrium varies between species, implicating evolutionary tuning to meet the particular client protein and metabolic environment of an organism. | 19061638 |
2010-01-21 00:00:00 | Structural-thermodynamic relationships of interactions in the N-terminal ATP-binding domain of Hsp90. | 19631219 |
Type | IDs |
---|---|
Synonymous | HSP90 |
Gene |
UniProtKB-ID:
HSC82_YEAST
UniprotKB:
P15108
UniParc:
UPI0000052EE0
EMBL:
M26044,
BK006946,
Z49808
EnsemblGenome:
YMR186W
KO:
sce:YMR186W
|
Nucleutide sequences |
EMBL-CDS:
AAA02813.1,
CAA89919.1,
DAA10084.1
Gene_ORFName:
YM8010.16
EnsemblGenome_TRS:
YMR186W_mRNA
|
Protein sequencees |
EnsemblGenome_PRO:
YMR186W
RefSeq:
NP_013911.1
|
Others |
UniRef100:
UniRef100_P15108
UniRef90:
UniRef90_P15108
UniRef50:
UniRef50_P15108
|
{{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
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Refseq |
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Conserved domain | Region: {{conservedDomain.region == '' || conservedDomain.region == null ? "-": conservedDomain.region}} GFID: {{conservedDomain.gfid == '' || conservedDomain.gfid == null ? "-": conservedDomain.gfid}} Family: {{conservedDomain.family == '' || conservedDomain.family == null ? "-": conservedDomain.family}} CDD: {{conservedDomain.cdd}} - |
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