BAIT

RPL20A

RPL18A2, ribosomal 60S subunit protein L20A, L20e, L20A, L18A, L000004458, L000003149, YMR242C
Ribosomal 60S subunit protein L20A; homologous to mammalian ribosomal protein L18A, no bacterial homolog; RPL20A has a paralog, RPL20B, 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)
PREY

RPL18A

RP28A, ribosomal 60S subunit protein L18A, L18e, L18A, L000001668, YOL120C
Ribosomal 60S subunit protein L18A; intron of RPL18A pre-mRNA forms stem-loop structures that are a target for Rnt1p cleavage leading to degradation; homologous to mammalian ribosomal protein L18, no bacterial homolog; RPL18A has a paralog, RPL18B, 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

  • 4.0 [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.

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
RPL18A RPL20A
Affinity Capture-MS
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.

High-BioGRID
-

Curated By

  • BioGRID