BAIT

RPS12

ribosomal 40S subunit protein S12, S12e, S12, L000002785, YOR369C
Protein component of the small (40S) ribosomal subunit; homologous to mammalian ribosomal protein S12, no bacterial homolog
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

YER010C

Bifunctional HMG aldolase/oxaloacetate decarboxylase; requires divalent metal ions for activity; competitively inhibited by oxalate; forms a ring-shaped homotrimer; similar to members of the prokaryotic RraA family of class II (divalent metal ion dependent) pyruvate aldolases from the meta cleavage pathways of protocatechuate and gallate
GO Process (1)
GO Function (2)
GO Component (0)

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.

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