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EC Number Posttranslational Modification Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.19.12lipoprotein C-terminal farnesylation promotes the association of UCH-L1 with membranes. Inhibition of UCH-L1 farnesylation by farnesyltransferase inhibitor FTI-277 710422
Display the word mapDisplay the reaction diagram Show all sequences 3.4.19.12more cysteine residues of UCH-L1 are readily carbonylated by 4-hydroxy-2-nonenal or other unsaturated aldehydes, and the carbonylated UCH-L1 exhibits altered properties in hydrolase activity and protein-protein interactions -, 710082
Display the word mapDisplay the reaction diagram Show all sequences 3.4.19.12ubiquitination monoubiquitination is a posttranslational modification of UCH-L1 that controls the function of UCH-L1. It may occur reversibly to a lysine residue near the active site, probably K157, of UCH-L1. This modification restricts enzyme activity by preventing binding to the ubiquitinated targets, and permanent mono-ubiquitination, as mimicked by a ubiquitin-UCH-L1 fusion, inhibits UCH-L1 in its capacity to increase free ubiquitin levels. However, the lifetime of this modification on UCH-L1 is regulated by auto-deubiquitination 707579
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