BAIT

UBC-1

CELE_C35B1.1, C35B1.1
ubc-1 encodes an E2 ubiquitin-conjugating enzyme that contains a novel 40 amino acid C-terminal tail, and is homologous to Saccharomyces cerevisiae RAD6/UBC2 which is involved in DNA repair; although loss of UBC-1 activity via RNA-mediated interference (RNAi) does not result in any abnormalities, UBC-1 is able to complement the DNA repair defects of a Saccharomyces cerevisiae rad6 null mutant, suggesting that UBC-1 can function in the DNA repair pathway; ubc-1 mRNA is detectable in embryos.
GO Process (4)
GO Function (4)
GO Component (1)
Caenorhabditis elegans
PREY

UBR-1

CELE_C32E8.11, C32E8.11
UBR E3 ubiquitin ligase homolog
GO Process (0)
GO Function (1)
GO Component (0)

Gene Ontology Molecular Function

Caenorhabditis elegans

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

Characterization of C. elegans RING finger protein 1, a binding partner of ubiquitin-conjugating enzyme 1.

Crowe E, Candido EP

In a yeast two-hybrid screen, RING finger protein 1 (RFP-1) and UBR1 were identified as potential binding partners of C. elegans UBC-1, a ubiquitin-conjugating enzyme with a high degree of identity to S. cerevisiae UBC2/RAD6. The interaction of RFP-1 and UBC-1 was confirmed by co-immunoprecipitation experiments. Yeast interaction trap experiments mapped the region of interaction to the basic N-terminal 313 ... [more]

Dev. Biol. Jan. 15, 2004; 265(2);446-59 [Pubmed: 14732404]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
UBC-1 UBR-1
Co-fractionation
Co-fractionation

Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex.

High0.827BioGRID
2580300

Curated By

  • BioGRID