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
TCA17
YEL048C
Component of transport protein particle (TRAPP) complex II; TRAPPII is a multimeric guanine nucleotide-exchange factor for the GTPase Ypt1p, regulating intra-Golgi and endosome-Golgi traffic; promotes association of TRAPPII-specific subunits with the TRAPP core complex; sedlin related; human Sedlin mutations cause SEDT, a skeletal disorder
GO Process (2)
GO Function (0)
GO Component (3)
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