BAIT

UBC

HMG20
ubiquitin C
GO Process (75)
GO Function (3)
GO Component (6)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Homo sapiens
PREY

RNF38

RP11-84P7.4
ring finger protein 38
GO Process (1)
GO Function (1)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Homo sapiens

Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Publication

Activation of a primed RING E3-E2-ubiquitin complex by non-covalent ubiquitin.

Buetow L, Gabrielsen M, Anthony NG, Dou H, Patel A, Aitkenhead H, Sibbet GJ, Smith BO, Huang DT

RING ubiquitin ligases (E3) recruit ubiquitin-conjugate enzymes (E2) charged with ubiquitin (Ub) to catalyze ubiquitination. Non-covalent Ub binding to the backside of certain E2s promotes processive polyUb formation, but the mechanism remains elusive. Here, we show that backside bound Ub (Ub(B)) enhances both RING-independent and RING-dependent UbcH5B-catalyzed donor Ub (Ub(D)) transfer, but with a more prominent effect in RING-dependent transfer. ... [more]

Mol. Cell Apr. 16, 2015; 58(2);297-310 [Pubmed: 25801170]

Throughput

  • Low Throughput

Additional Notes

  • #LPPI
  • Likely protein-protein interaction

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
RNF38 UBC
Biochemical Activity
Biochemical Activity

An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.

Low-BioGRID
1505315

Curated By

  • BioGRID