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
COX23
YHR116W
Protein that functions in mitochondrial copper homeostasis; mitochondrial intermembrane space protein; essential for functional cytochrome oxidase expression; homologous to Cox17p; contains twin cysteine-x9-cysteine motifs
GO Process (1)
GO Function (0)
GO Component (2)
Gene Ontology Biological Process
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