BAIT

RPS28A

RPS33A, ribosomal 40S subunit protein S28A, S28e, YS27, S33A, S28A, L000001767, YOR167C
Protein component of the small (40S) ribosomal subunit; homologous to mammalian ribosomal protein S28, no bacterial homolog; has an extraribosomal function in regulation of RPS28B, in which Rps28Ap binds to a decapping complex via Edc3p, which then binds to RPS28B mRNA leading to its decapping and degradation; RPS28A has a paralog, RPS28B, that arose from the whole genome duplication
GO Process (3)
GO Function (1)
GO Component (1)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

RPS29B

ribosomal 40S subunit protein S29B, S14, YS29, S36B, S29B, YS29B, L000002550, YDL061C
Protein component of the small (40S) ribosomal subunit; homologous to mammalian ribosomal protein S29 and bacterial S14; RPS29B has a paralog, RPS29A, that arose from the whole genome duplication
GO Process (1)
GO Function (1)
GO Component (1)

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 social and structural architecture of the yeast protein interactome.

Michaelis AC, Brunner AD, Zwiebel M, Meier F, Strauss MT, Bludau I, Mann M

Cellular functions are mediated by protein-protein interactions, and mapping the interactome provides fundamental insights into biological systems. Affinity purification coupled to mass spectrometry is an ideal tool for such mapping, but it has been difficult to identify low copy number complexes, membrane complexes and complexes that are disrupted by protein tagging. As a result, our current knowledge of the interactome ... [more]

Nature Nov. 15, 2023; (); [Pubmed: 37968396]

Quantitative Score

  • 3.0 [Score_FDR+correlation]

Throughput

  • High Throughput

Additional Notes

  • Protein interactions were identified using statistically significant enrichment of the proteins in the forward and reverse pull-downs, as well as making use of the profile similarities of interacting proteins in a correlation analysis. High confidence interactions have a total score >=2. This score is a sum of the FDR score of the forward pull-down + FDR score of the reverse pull-down + correlation score.

Curated By

  • BioGRID