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)
Saccharomyces cerevisiae (S288c)
PREY

RIM21

PAL2, YNL294C
pH sensor molecule, component of the RIM101 pathway; has a role in cell wall construction and alkaline pH response; is glycosylated and phosphorylated; interacts with Dfg16p and Rim9p to form a pH-sensing complex; localization to the plasma membrane is dependent on Dfg16p and Rim9p; has similarity to A. nidulans PalH
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