Literature summary for 2.3.2.26 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.

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q14669	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
S-ubiquitinyl-[UbcH5a]-L-cysteine + [ubiquitin mutant G76V]-L-lysine	-	Homo sapiens	[UbcH5a]-L-cysteine + N6-ubiquitinyl-[mutant G76V]-L-lysine	-	?
S-ubiquitinyl-[UbcH5a]-L-cysteine + [ubiquitin-DELTAGG]-L-lysine	ubiquitin-DELTAGG i.e. mutant ubiquitin lacking the two C-terminal glycine residues, cannot be conjugated to other proteins	Homo sapiens	[UbcH5a]-L-cysteine + N6-ubiquitinyl-[ubiquitin-DELTAGG]-L-lysine	-	?

Synonyms

Synonyms	Comment	Organism
TRIP12	-	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

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Release 2023.1 (January 2023)