Ubiquitin-Conjugating Enzyme E2 Z (ZUBE2Z) is a member of the E2 ubiquitin-conjugating enzyme family. ZUBE2Z is widely expressed in many tissues, with high expression found in the placenta, pancreas, spleen, and testis. It is ubiquitinates proteins that catalyze the covalent attachment of ubiquitin to other proteins. It has shown that ZUBE2Z participate in signaling pathways, and may be involved in apoptosis regulation.
Polyubiquitin-B(UBB) is one of Ubiquitins. Ubiquitin is one of the most conserved proteins known in eukaryotic organisms. Ubiquitin is required for ATP-dependent, non-lysosomal intracellular protein degradation of abnormal proteins and normal proteins with a rapid turnover. Ubiquitin is covalently bound to proteins to be degraded, and presumably labels these proteins for degradation.
Ubiquitin Carboxyl-Terminal Hydrolase Isozyme L1 (UCHL1) belongs to the Peptidase C12 family. UCHL1 is specifically expressed in the neurons and in cells of the diffuse neuroendocrine system. UCHL1 is a component of the ubiquitin system, which has a fundamental role in regulating various biological activities. UCHL1 is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. UCHL1 also binds to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer of UCHL1 may have ATP-independent ubiquitin ligase activity.
Ubiquitin carboxyl-terminal hydrolase isozyme L1, also known as UCH-L1, Ubiquitin thioesterase L1, PGP9.5 and UCHL1, is a deubiqutinating enzyme with important functions in recycling of ubiquitin. Regulated proteolysis by the ubiquitin pathway has been implicated in control of the cell cycle, transcriptional activation, cell fate and growth, and synaptogenesis. The ubiquitin-proteasome system is involved in synaptic plasticity and is proposed to be part of a molecular switch that converts short-term synaptic potentiation to long-term changes in synaptic strength. UCHL1 is found in neuronal cell bodies and processes throughout the neocortex (at protein level). It is expressed in neurons and cells of the diffuse neuroendocrine system and their tumors. UCHL1 is weakly expressed in ovary. UCHL1 is a ubiquitin-protein hydrolase. It is 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. UCHL1 also binds to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer of UCHL1 may have ATP-independent ubiquitin ligase activity. UCHL1 dysfunction has been associated with neurodegeneration in Parkinson's, Alzheimer's, and Huntington's disease patients. Reduced UCHL1 function may jeopardize the survival of CNS neurons.
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