| Type | Description |
|---|---|
| Definition | Hsp90 cochaperone SBA1 |
| Date | Results | Publications |
|---|---|---|
| 2013-02-09 10:30:00 | Data support a model in which p23 molecular chaperone and GCN5 regulate diverse multistep pathways by controlling the longevity of protein-DNA complexes. | 23022381 |
| 2010-01-21 00:00:00 | Structure-function analysis suggests that Sba1p undergoes structural rearrangements upon binding Hsp90, and the large size of the p23/Sba1p-Hsp90 interaction surface facilitates maintenance of high affinity despite sequence divergence during evolution. | 18362168 |
| 2010-01-21 00:00:00 | SBA1 is required for teleomere length maintenance. It can moderate telomerase DNA binding and extension activities in vitro. | 17389357 |
| 2010-01-21 00:00:00 | crystal structure of full-length yeast Hsp90 in complex with an ATP analogue and the co-chaperone p23/Sba1 | 16625188 |
| Type | IDs |
|---|---|
| Synonymous | CST18 |
| Gene |
UniProtKB-ID:
SBA1_YEAST
UniprotKB:
P28707
UniParc:
UPI000004F939
EMBL:
BK006944,
S93804,
Z28117
EnsemblGenome:
YKL117W
KO:
sce:YKL117W
|
| Nucleutide sequences |
EMBL-CDS:
AAB22000.1,
CAA81957.1,
DAA09042.1
Gene_ORFName:
YKL518
EnsemblGenome_TRS:
YKL117W_mRNA
|
| Protein sequencees |
EnsemblGenome_PRO:
YKL117W
RefSeq:
NP_012805.1
|
| Others |
UniRef100:
UniRef100_P28707
UniRef90:
UniRef90_P28707
UniRef50:
UniRef50_P28707
|
| {{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
|---|---|---|---|---|---|---|---|---|
| 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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