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

CUL5-ARIH2 E3-E3 ubiquitin ligase structure reveals cullin-specific NEDD8 activation.

Kostrhon S, Prabu JR, Baek K, Horn-Ghetko D, von Gronau S, Kluegel M, Basquin J, Alpi AF, Schulman BA

An emerging mechanism of ubiquitylation involves partnering of two distinct E3 ligases. In the best-characterized E3-E3 pathways, ARIH-family RING-between-RING (RBR) E3s ligate ubiquitin to substrates of neddylated cullin-RING E3s. The E3 ARIH2 has been implicated in ubiquitylation of substrates of neddylated CUL5-RBX2-based E3s, including APOBEC3-family substrates of the host E3 hijacked by HIV-1 virion infectivity factor (Vif). However, the structural ... [more]

Nat Chem Biol Dec. 01, 2020; 17(10);1075-1083 [Pubmed: 34518685]

Throughput

  • Low Throughput

Additional Notes

  • The reaction contained E1, RNF7 and UBE2L3 [E2], and CUL5 and ARIH2 [E3]

Curated By

  • BioGRID