BAIT
RPS6A
ribosomal 40S subunit protein S6A, S6e, rp9, YS4, S6A, S10A, L000004472, YPL090C
Protein component of the small (40S) ribosomal subunit; homologous to mammalian ribosomal protein S6, no bacterial homolog; RPS6A has a paralog, RPS6B, that arose from the whole genome duplication
GO Process (3)
GO Function (1)
GO Component (3)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Saccharomyces cerevisiae (S288c)
PREY
DIS3
MTR17, RRP44, exosome catalytic subunit DIS3, L000003486, YOL021C
Exosome core complex catalytic subunit; has both endonuclease and 3'-5' exonuclease activity; involved in 3'-5' RNA processing and degradation in both the nucleus and the cytoplasm; role in degradation of tRNAs; has similarity to E. coli RNase R and to human DIS3; mutations in Dis3p corresponding to human mutations implicated in multiple myeloma cause phenotypes suggesting impaired exosome function; protein abundance increases in response to DNA replication stress
GO Process (12)
GO Function (3)
GO Component (5)
Gene Ontology Biological Process
- exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [IMP]
- ncRNA 3'-end processing [IMP]
- nonfunctional rRNA decay [IMP]
- nuclear mRNA surveillance [IMP]
- nuclear polyadenylation-dependent CUT catabolic process [IMP]
- nuclear polyadenylation-dependent mRNA catabolic process [IC]
- nuclear polyadenylation-dependent rRNA catabolic process [IMP]
- nuclear polyadenylation-dependent tRNA catabolic process [IDA, IGI, IMP]
- nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay [IC]
- nuclear-transcribed mRNA catabolic process, non-stop decay [IC]
- polyadenylation-dependent snoRNA 3'-end processing [IC]
- rRNA catabolic process [IMP]
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.
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