BAIT
SBA1
CST18, L000004284, L000002999, S000029122, YKL117W
Co-chaperone that binds and regulates Hsp90 family chaperones; plays a role in determining prion variants; important for pp60v-src activity in yeast; homologous to the mammalian p23 proteins, and like p23 can regulate telomerase activity; protein abundance increases in response to DNA replication stress
GO Process (4)
GO Function (1)
GO Component (2)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Saccharomyces cerevisiae (S288c)
PREY
CCH1
L000003440, YGR217W
Voltage-gated high-affinity calcium channel; involved in calcium influx in response to some environmental stresses as well as exposure to mating pheromones; interacts and partially co-localizes with Mid1p; however, evidence suggests CCH1 is not required for Mid1p function
GO Process (1)
GO Function (2)
GO Component (2)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Saccharomyces cerevisiae (S288c)
Synthetic Lethality
A genetic interaction is inferred when mutations or deletions in separate genes, each of which alone causes a minimal phenotype, result in lethality when combined in the same cell under a given condition.
Publication
Global Functional Map of the p23 Molecular Chaperone Reveals an Extensive Cellular Network.
In parallel with evolutionary developments, the Hsp90 molecular chaperone system shifted from a simple prokaryotic factor into an expansive network that includes a variety of cochaperones. We have taken high-throughput genomic and proteomic approaches to better understand the abundant yeast p23 cochaperone Sba1. Our work revealed an unexpected p23 network that displayed considerable independence from known Hsp90 clients. Additionally, our ... [more]
Mol. Cell Jul. 22, 2011; 43(2);229-41 [Pubmed: 21777812]
Throughput
- High Throughput
Ontology Terms
- phenotype: inviable (APO:0000112)
Additional Notes
- SGA
Curated By
- BioGRID