| Type | Description |
|---|---|
| Definition | Hch1p |
| Date | Results | Publications |
|---|---|---|
| 2018-11-24 11:03:00 | Phosphorylation of human Hsp90alpha at the highly conserved tyrosine (Y) 627 affects it conformation and function. Y627 is not phosphorylated in yeast, but study demonstrated that the non-conserved yeast co-chaperone, Hch1, modifies yeast Hsp90 (Hsp82) through Y606E phosphomimetic mutation raising the possibility that this post-translational modification in higher eukaryotes represents an evolutionary substitution for ... | 28537252 |
| 2014-07-12 11:00:00 | The work here suggests that both Hch1p and Aha1p regulate Hsp90 function through interaction with the catalytic loop but do so in different ways. | 24726918 |
| 2013-05-11 12:40:00 | The co-chaperone Hch1 regulates Hsp90 function differently than its homologue Aha1 and confers sensitivity to yeast to the Hsp90 inhibitor NVP-AUY922. | 23166640 |
| Type | IDs |
|---|---|
| Gene |
UniProtKB-ID:
HCH1_YEAST
UniprotKB:
P53834
UniParc:
UPI000013BA6E
EMBL:
BK006947,
Z71557
EnsemblGenome:
YNL281W
KO:
sce:YNL281W
|
| Nucleutide sequences |
EMBL-CDS:
DAA10279.1,
CAA96193.1
Gene_ORFName:
N0589
EnsemblGenome_TRS:
YNL281W_mRNA
|
| Protein sequencees |
EnsemblGenome_PRO:
YNL281W
RefSeq:
NP_014118.1
|
| Others |
UniRef100:
UniRef100_P53834
UniRef90:
UniRef90_P53834
UniRef50:
UniRef50_P53834
|
| {{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
|---|---|---|---|---|---|---|---|---|
| Refseq |
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| Location | {{protein.contigId}} ( {{protein.positionStart}}..{{protein.positionEnd}} , {{protein.orientation}} ) | |||||||
| 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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