| Function | 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. |
| Protein Name | Ubiquitin Carboxyl-Terminal Hydrolase Isozyme L3Uch-L3Ubiquitin Thioesterase L3 |
| Database Links | Reactome: R-HSA-5689603Reactome: R-HSA-8866652Reactome: R-HSA-8951664 |
| Cellular Localisation | Cytoplasm |
| Alternative Protein Names | Ubiquitin Carboxyl-Terminal Hydrolase Isozyme L3 proteinUch-L3 proteinUbiquitin Thioesterase L3 proteinUCHL3 protein |
Information sourced from Uniprot.org
