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
Saccharomyces cerevisiae (S288c)
PREY

GCD10

TRM6, L000000676, YNL062C
Subunit of tRNA (1-methyladenosine) methyltransferase with Gcd14p; required for the modification of the adenine at position 58 in tRNAs, especially tRNAi-Met; first identified as a negative regulator of GCN4 expression
GO Process (1)
GO Function (1)
GO Component (2)

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

Tsr4 and Nap1, two novel members of the ribosomal protein chaperOME.

Roessler I, Embacher J, Pillet B, Murat G, Liesinger L, Hafner J, Unterluggauer JJ, Birner-Gruenberger R, Kressler D, Pertschy B

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