Deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins. Thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. Has a 10-fold preference for Arg and Lys at position P3", and exhibits a preference towards 'Lys-48'-linked Ubiquitin chains. Deubiquitinates ENAC in apical compartments, thereby regulating apical membrane recycling. Indirectly increases the phosphorylation of IGFIR, AKT and FOXO1 and promotes insulin-signaling and insulin-induced adipogenesis. Required for stress-response retinal, skeletal muscle and germ cell maintenance. May be involved in working memory. Can hydrolyze UBB(+1), a mutated form of ubiquitin which is not effectively degraded by the proteasome and is associated with neurogenerative disorders.
|Gene Name:||ubiquitin carboxyl-terminal esterase L3 (ubiquitin thiolesterase)|
|Family/Subfamily:||Protease , Cysteine C12|
|Synonyms:||UCHL3, Ubiquitin thiolesterase, Ubiquitin thioesterase L3, UCH-L3|
|Target Sequences:||NM_006002 NP_005993.1 P15374|
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