BAIT
TOM1
E3 ubiquitin-protein ligase TOM1, L000002983, YDR457W
E3 ubiquitin ligase of the hect-domain class; has a role in mRNA export from the nucleus and may regulate transcriptional coactivators; involved in degradation of excess histones; interacts with Dia2p and is required for Dia2p degradation; required to target Cdc6p for ubiquitin-mediated destruction during G1 phase
GO Process (10)
GO Function (1)
GO Component (3)
Gene Ontology Biological Process
- cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [IMP]
- endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [IMP]
- endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [IMP]
- endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [IMP]
- mitotic nuclear division [IMP]
- nucleocytoplasmic transport [IMP]
- nucleus organization [IMP]
- protein ubiquitination [IDA]
- protein ubiquitination involved in ubiquitin-dependent protein catabolic process [IBA, IMP]
- regulation of cell size [IMP]
Gene Ontology Molecular Function
Saccharomyces cerevisiae (S288c)
PREY
FCF2
YLR051C
Nucleolar protein involved in the early steps of 35S rRNA processing; interacts with Faf1p; member of a transcriptionally co-regulated set of genes called the RRB regulon; essential gene
GO Process (3)
GO Function (0)
GO Component (2)
Gene Ontology Biological Process
- endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [IMP]
- endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [IMP]
- endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [IMP]
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
The social and structural architecture of the yeast protein interactome.
Cellular functions are mediated by protein-protein interactions, and mapping the interactome provides fundamental insights into biological systems. Affinity purification coupled to mass spectrometry is an ideal tool for such mapping, but it has been difficult to identify low copy number complexes, membrane complexes and complexes that are disrupted by protein tagging. As a result, our current knowledge of the interactome ... [more]
Nature Nov. 15, 2023; (); [Pubmed: 37968396]
Quantitative Score
- 2.0 [Score_FDR+correlation]
Throughput
- High Throughput
Additional Notes
- Protein interactions were identified using statistically significant enrichment of the proteins in the forward and reverse pull-downs, as well as making use of the profile similarities of interacting proteins in a correlation analysis. High confidence interactions have a total score >=2. This score is a sum of the FDR score of the forward pull-down + FDR score of the reverse pull-down + correlation score.
Curated By
- BioGRID