BAIT

UBE2G1

2700059C12Rik, AI256795, AU014992, AW552068, D130023C12Rik, RP23-32B6.1
ubiquitin-conjugating enzyme E2G 1
Mus musculus
PREY

UBC

2700054O04Rik, AI194771, Rps27a, TI-225, Uba52, Ubb
ubiquitin C
GO Process (1)
GO Function (3)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Mus musculus

Biochemical Activity (Ubiquitination)

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.

Publication

Differential ubiquitin binding by the acidic loops of Ube2g1 and Ube2r1 enzymes distinguishes their Lys-48-ubiquitylation activities.

Choi YS, Lee YJ, Lee SY, Shi L, Ha JH, Cheong HK, Cheong C, Cohen RE, Ryu KS

The ubiquitin E2 enzymes, Ube2g1 and Ube2r1, are able to synthesize Lys-48-linked polyubiquitins without an E3 ligase but how that is accomplished has been unclear. Although both E2s contain essential acidic loops, only Ube2r1 requires an additional C-terminal extension (184-196) for efficient Lys-48-ubiquitylation activity. The presence of Tyr-102 and Tyr-104 in the Ube2g1 acidic loop enhanced both ubiquitin binding and ... [more]

J. Biol. Chem. Jan. 23, 2015; 290(4);2251-63 [Pubmed: 25471371]

Throughput

  • Low Throughput

Additional Notes

  • Both Ube2g1 and Ube2r1 can synthesize Lys-48-linked polyubiquitin adducts in the absence of E3 ligase

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
UBE2G1 UBC
Co-crystal Structure
Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Low-BioGRID
1513573

Curated By

  • BioGRID