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Literature summary for extracted from

  • Park, Y.; Yoon, S.K.; Yoon, J.B.
    The HECT domain of TRIP12 ubiquitinates substrates of the ubiquitin fusion degradation pathway (2009), J. Biol. Chem., 284, 1540-1549.
    View publication on PubMed


Organism UniProt Comment Textmining
Homo sapiens P51668

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-ubiquitinyl-[Uba1]-L-cysteine + [Ubc5a]-L-cysteine
Homo sapiens [Uba1]-L-cysteine + S-ubiquitinyl-[Ubc5a]-L-cysteine the E1 enzyme Uba1, the E2 enzyme UbcH5a, and the E3 enzyme TRIP12 are responsible for ubiquitylation of ubiquitin mutant G76V ?


Synonyms Comment Organism
Homo sapiens

General Information

General Information Comment Organism
physiological function isoform TRIP12 catalyzes in vitro ubiquitination of ubiquitin fusion degradation substrates in conjunction with E1, E2, and E4 enzymes. Knockdown of TRIP12 stabilizes artificial ubiquitin fusion degradation substrates and physiological substrate, mutant ubiquitin UBB+1. TRIP12 knockdown reduces UBB+1-induced cell death in human neuroblastoma cells. Complementation of TRIP12 knockdown cells with the TRIP12 HECT domain mostly restores efficient degradation of ubiquitin fusion degradation substrates. The TRIP12 HECT domain directs ubiquitination of ubiquitin fusion degradation substrates in vitro and can be specifically cross-linked to the ubiquitin moiety of the substrates in vivo. A mutant ubiquitin that cannot be conjugated to other proteins is a substrate of the TRIP12 HECT domain both in vivo and in vitro Homo sapiens