BAIT
RPS13
RPS13B, RPS13C, ribosomal 40S subunit protein S13, YS15, S27a, S15, S13, L000002900, L000002655, YDR064W
Protein component of the small (40S) ribosomal subunit; homologous to mammalian ribosomal protein S13 and bacterial S15
GO Process (2)
GO Function (2)
GO Component (2)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Saccharomyces cerevisiae (S288c)
PREY
EDC3
DCP3, LSM16, YEL015W
Non-essential conserved protein with a role in mRNA decapping; specifically affects the function of the decapping enzyme Dcp1p; mediates decay of the RPS28B mRNA via binding to both Rps28Bp (or Rps28Ap) and the RPS28B mRNA; mediates decay of the YRA1 mRNA by a different, translation-independent mechanism; localizes to cytoplasmic mRNA processing bodies; forms cytoplasmic foci upon DNA replication stress
GO Process (3)
GO Function (1)
GO Component (3)
Gene Ontology Biological Process
Gene Ontology Molecular Function
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
Tsr4 and Nap1, two novel members of the ribosomal protein chaperOME.
Dedicated chaperones protect newly synthesized ribosomal proteins (r-proteins) from aggregation and accompany them on their way to assembly into nascent ribosomes. Currently, only nine of the ?80 eukaryotic r-proteins are known to be guarded by such chaperones. In search of new dedicated r-protein chaperones, we performed a tandem-affinity purification based screen and looked for factors co-enriched with individual small subunit ... [more]
Nucleic Acids Res. Dec. 26, 2018; 47(13);6984-7002 [Pubmed: 31062022]
Throughput
- High Throughput
Curated By
- BioGRID