BAIT

BZZ1

LSB7, YHR114W
SH3 domain protein implicated in regulating actin polymerization; able to recruit actin polymerization machinery through its SH3 domains; colocalizes with cortical actin patches and Las17p; interacts with type I myosins
GO Process (4)
GO Function (1)
GO Component (4)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

ATG17

APG17, protein kinase regulatory subunit ATG17, YLR423C
Scaffold protein responsible for phagophore assembly site organization; regulatory subunit of an autophagy-specific complex that includes Atg1p and Atg13p; stimulates Atg1p kinase activity; human ortholog RB1CC1/FIP200 interacts with p53, which inhibits autophagy in human cells
Saccharomyces cerevisiae (S288c)

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.

Publication

High-quality binary protein interaction map of the yeast interactome network.

Yu H, Braun P, Yildirim MA, Lemmens I, Venkatesan K, Sahalie J, Hirozane-Kishikawa T, Gebreab F, Li N, Simonis N, Hao T, Rual JF, Dricot A, Vazquez A, Murray RR, Simon C, Tardivo L, Tam S, Svrzikapa N, Fan C, de Smet AS, Motyl A, Hudson ME, Park J, Xin X, Cusick ME, Moore T, Boone C, Snyder M, Roth FP, Barabasi AL, Tavernier J, Hill DE, Vidal M

Current yeast interactome network maps contain several hundred molecular complexes with limited and somewhat controversial representation of direct binary interactions. We carried out a comparative quality assessment of current yeast interactome data sets, demonstrating that high-throughput yeast two-hybrid (Y2H) screening provides high-quality binary interaction information. Because a large fraction of the yeast binary interactome remains to be mapped, we developed ... [more]

Science Oct. 03, 2008; 322(5898);104-10 [Pubmed: 18719252]

Throughput

  • High Throughput

Curated By

  • BioGRID