Ubiquitin-protein hydrolase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. Also binds to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer may have ATP-independent ubiquitin ligase activity. Monomer. Homodimer. Interacts with SNCA. Interacts with COPS5. Found in neuronal cell bodies and processes throughout the neocortex. Expressed in neurons and cells of the diffuse neuroendocrine system and their tumors. Weakly expressed in ovary. Down-regulated in brains from Parkinson disease and Alzheimer disease patients. Belongs to the peptidase C12 family. Note: This description may include information from UniProtKB.
Protein type: EC 184.108.40.206; Cell development/differentiation; Protease; Ligase; Ubiquitin conjugating system
LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.