BAIT

POG1

YIL122W
Nuclear chromatin-associated protein of unknown function; may have a role in cell cycle regulation; overexpression promotes recovery from pheromone induced arrest and suppresses the stress sensitivity caused by a mutation in the E3 ubiquitin ligase Rsp5p; binds upstream of BAR1 and cell cycle-related genes; phsosphoylated form may be ubiquitinated by Dma2p; potential Cdc28p substrate; SBF regulated
GO Process (2)
GO Function (1)
GO Component (2)
Saccharomyces cerevisiae (S288c)
PREY

POG1

YIL122W
Nuclear chromatin-associated protein of unknown function; may have a role in cell cycle regulation; overexpression promotes recovery from pheromone induced arrest and suppresses the stress sensitivity caused by a mutation in the E3 ubiquitin ligase Rsp5p; binds upstream of BAR1 and cell cycle-related genes; phsosphoylated form may be ubiquitinated by Dma2p; potential Cdc28p substrate; SBF regulated
GO Process (2)
GO Function (1)
GO Component (2)
Saccharomyces cerevisiae (S288c)

Protein-peptide

An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments.

Publication

Isolation and mapping of self-assembling protein domains encoded by the Saccharomyces cerevisiae genome using lambda repressor fusions.

Marino-Ramirez L, Hu JC

Understanding how proteins are able to form stable complexes is of fundamental interest from the perspective of protein structure and function. Here we show that lambda repressor fusions can be used to identify and characterize homotypic interaction domains encoded by the genome of Saccharomyces cerevisiae, using a selection for polypeptides that can drive the assembly of the DNA binding domain ... [more]

Yeast May. 01, 2002; 19(7);641-50 [Pubmed: 11967834]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
POG1 POG1
Two-hybrid
Two-hybrid

Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.

High-BioGRID
-

Curated By

  • BioGRID