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
Saccharomyces cerevisiae (S288c)
PREY

YPR158W-B

gag-pol fusion protein
Retrotransposon TYA Gag and TYB Pol genes; transcribed/translated as one unit; polyprotein is processed to make a nucleocapsid-like protein (Gag), reverse transcriptase (RT), protease (PR), and integrase (IN); similar to retroviral genes
GO Process (1)
GO Function (5)
GO Component (2)
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

A conserved quality-control pathway that mediates degradation of unassembled ribosomal proteins.

Sung MK, Porras-Yakushi TR, Reitsma JM, Huber FM, Sweredoski MJ, Hoelz A, Hess S, Deshaies RJ

Overproduced yeast ribosomal protein (RP) Rpl26 fails to assemble into ribosomes and is degraded in the nucleus/nucleolus by a ubiquitin-proteasome system quality control pathway comprising the E2 enzymes Ubc4/Ubc5 and the ubiquitin ligase Tom1. tom1 cells show reduced ubiquitination of multiple RPs, exceptional accumulation of detergent-insoluble proteins including multiple RPs, and hypersensitivity to imbalances in production of RPs and rRNA, ... [more]

Elife Aug. 23, 2016; 5(0); [Pubmed: 27552055]

Throughput

  • High Throughput

Curated By

  • BioGRID