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

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

AFG1

L000000055, YEL052W
Protein that may act as a chaperone for cytochrome c oxidase subunits; conserved protein; may act as a chaperone in the degradation of misfolded or unassembled cytochrome c oxidase subunits; localized to matrix face of the mitochondrial inner membrane; member of the AAA family but lacks a protease domain
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.

Echtenkamp FJ, Zelin E, Oxelmark E, Woo JI, Andrews BJ, Garabedian M, Freeman BC

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