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

UBC1

E2 ubiquitin-conjugating protein UBC1, L000002406, YDR177W
Ubiquitin-conjugating enzyme; key E2 partner with Ubc4p for the anaphase-promoting complex (APC); mediates selective degradation of short-lived and abnormal proteins; plays a role in vesicle biogenesis and ER-associated protein degradation (ERAD); component of the cellular stress response; protein abundance increases in response to DNA replication stress key E2 partner with Ubc4p for the anaphase-promoting complex (APC)
GO Process (3)
GO Function (1)
GO Component (1)
Saccharomyces cerevisiae (S288c)

Two-hybrid

Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.

Publication

Ubc13-Mms2 cooperates with a family of RING E3 proteins in budding yeast membrane protein sorting.

Renz C, Albanese V, Troester V, Albert TK, Santt O, Jacobs SC, Khmelinskii A, Leon S, Ulrich HD

Polyubiquitin chains linked via lysine (K) 63 play an important role in endocytosis and membrane trafficking. Their primary source is the ubiquitin protein ligase (E3) Rsp5/NEDD4, which acts as a key regulator of membrane protein sorting. The heterodimeric ubiquitin-conjugating enzyme (E2), Ubc13-Mms2, catalyses K63-specific polyubiquitylation in genome maintenance and inflammatory signalling. In budding yeast, the only E3 proteins known to ... [more]

J Cell Sci Dec. 27, 2019; 133(10); [Pubmed: 32265276]

Throughput

  • Low Throughput

Curated By

  • BioGRID