BAIT

SSB1

YG101, Hsp70 family ATPase SSB1, L000002073, L000002508, YDL229W
Cytoplasmic ATPase that is a ribosome-associated molecular chaperone; functions with J-protein partner Zuo1p; may be involved in folding of newly-made polypeptide chains; member of the HSP70 family; interacts with phosphatase subunit Reg1p; SSB1 has a paralog, SSB2, that arose from the whole genome duplication
Saccharomyces cerevisiae (S288c)
PREY

SIP1

L000001890, YDR422C
Alternate beta-subunit of the Snf1p kinase complex; may confer substrate specificity; vacuolar protein containing KIS (Kinase-Interacting Sequence) and ASC (Association with Snf1 kinase Complex) domains involved in protein interactions
Kinome Project (Sc)
GO Process (3)
GO Function (1)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)

Affinity Capture-MS

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.

Publication

The Hsp70 homolog Ssb and the 14-3-3 protein Bmh1 jointly regulate transcription of glucose repressed genes in Saccharomyces cerevisiae.

Huebscher V, Mudholkar K, Chiabudini M, Fitzke E, Woelfle T, Pfeifer D, Drepper F, Warscheid B, Rospert S

Chaperones of the Hsp70 family interact with a multitude of newly synthesized polypeptides and prevent their aggregation. Saccharomyces cerevisiae cells lacking the Hsp70 homolog Ssb suffer from pleiotropic defects, among others a defect in glucose-repression. The highly conserved heterotrimeric kinase SNF1/AMPK (AMP-activated protein kinase) is required for the release from glucose-repression in yeast and is a key regulator of energy ... [more]

Nucleic Acids Res. Jul. 08, 2016; 44(12);5629-45 [Pubmed: 27001512]

Throughput

  • High Throughput

Additional Notes

  • Table 1

Curated By

  • BioGRID