Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q14669 | - |
- |
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 | Comment | Organism |
---|---|---|
TRIP12 | - |
Homo sapiens |
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 |