BAIT

RPL7A

ribosomal 60S subunit protein L7A, YL8, L7A, L6A, L30, rp11, L000002704, L000003255, YGL076C
Ribosomal 60S subunit protein L7A; required for processing of 27SA3 pre-rRNA to 27SB pre-rRNA during assembly of large ribosomal subunit; depletion leads to a turnover of pre-rRNA; contains a conserved C-terminal Nucleic acid Binding Domain (NDB2); binds to Domain II of 25S and 5.8S rRNAs; homologous to mammalian ribosomal protein L7 and bacterial L30; RPL7A has a paralog, RPL7B, that arose from the whole genome duplication
GO Process (3)
GO Function (1)
GO Component (3)
Saccharomyces cerevisiae (S288c)
PREY

RPL37A

ribosomal 60S subunit protein L37A, L37e, YL35, L43, L37A, L000002884, YLR185W
Ribosomal 60S subunit protein L37A; homologous to mammalian ribosomal protein L37, no bacterial homolog; RPL37A has a paralog, RPL37B, 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

  • 8.0 [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