BAIT

RPS3

SUF14, ribosomal 40S subunit protein S3, rp13, YS3, S3, L000002161, L000001749, YNL178W
Protein component of the small (40S) ribosomal subunit; has apurinic/apyrimidinic (AP) endonuclease activity; essential for viability; homologous to mammalian ribosomal protein S3 and bacterial S3
Saccharomyces cerevisiae (S288c)
PREY

PCM1

AGM1, phosphoacetylglucosamine mutase PCM1, L000001351, YEL058W
Essential N-acetylglucosamine-phosphate mutase; converts GlcNAc-6-P to GlcNAc-1-P, which is a precursor for the biosynthesis of chitin and for the formation of N-glycosylated mannoproteins and glycosylphosphatidylinositol anchors
GO Process (3)
GO Function (2)
GO Component (3)

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