BAIT
HEL2
E3 ubiquitin-protein ligase HEL2, YDR266C
RING finger ubiquitin ligase (E3); involved in ubiquitylation and degradation of excess histones; interacts with Ubc4p and Rad53p; null mutant sensitive to hydroxyurea (HU); green fluorescent protein (GFP)-fusion protein localizes to the cytoplasm; computational analysis suggests a role as a transcription factor
GO Process (2)
GO Function (1)
GO Component (2)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Saccharomyces cerevisiae (S288c)
PREY
HEL2
E3 ubiquitin-protein ligase HEL2, YDR266C
RING finger ubiquitin ligase (E3); involved in ubiquitylation and degradation of excess histones; interacts with Ubc4p and Rad53p; null mutant sensitive to hydroxyurea (HU); green fluorescent protein (GFP)-fusion protein localizes to the cytoplasm; computational analysis suggests a role as a transcription factor
GO Process (2)
GO Function (1)
GO Component (2)
Gene Ontology Biological Process
Gene Ontology Molecular Function
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.
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
Curated By
- BioGRID