BAIT

TUL1

ubiquitin-protein ligase TUL1, YKL034W
Subunit of the DSC ubiquitin ligase complex; golgi-localized RING-finger ubiquitin ligase (E3) involved in sorting polar transmembrane domain containing membrane proteins to multivesicular bodies for delivery to the vacuole; proposed involvement in the quality control of misfolded TMD containing proteins; ortholog of fission yeast dsc1
Saccharomyces cerevisiae (S288c)
PREY

DID2

CHM1, FTI1, VPL30, VPS46, L000004496, YKR035W-A
Class E protein of the vacuolar protein-sorting (Vps) pathway; binds Vps4p and directs it to dissociate ESCRT-III complexes; forms a functional and physical complex with Ist1p; human ortholog may be altered in breast tumors
GO Process (3)
GO Function (0)
GO Component (2)
Saccharomyces cerevisiae (S288c)

Synthetic Lethality

A genetic interaction is inferred when mutations or deletions in separate genes, each of which alone causes a minimal phenotype, result in lethality when combined in the same cell under a given condition.

Publication

Identification of Candidate Substrates for the Golgi Tul1 E3 Ligase Using Quantitative diGly Proteomics in Yeast.

Tong Z, Kim MS, Pandey A, Espenshade PJ

Maintenance of protein homeostasis is essential for cellular survival. Central to this regulation are mechanisms of protein quality control in which misfolded proteins are recognized and degraded by the ubiquitin-proteasome system. One well-studied protein quality control pathway requires ER resident, multi-subunit E3 ubiquitin ligases that function in ER-associated degradation (ERAD). Using fission yeast, our lab identified the Golgi Dsc E3 ... [more]

Mol. Cell Proteomics Jul. 30, 2014; 0(0); [Pubmed: 25078903]

Throughput

  • Low Throughput

Ontology Terms

  • phenotype: inviable (APO:0000112)

Additional Notes

  • 37 deg C

Curated By

  • BioGRID