Structural highlights
Function
UBP14_MOUSE Proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. Ensures the regeneration of ubiquitin at the proteasome. Maintains the cellular levels of monomeric ubiquitin in cells. Indispensable for synaptic development and function at neuromuscular junctions (NMJs). Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell. Required for the degradation of the chemokine receptor cxcr4 which is critical for CXCL12-induced cell chemotaxis. Serves also as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum proteins via interaction with ERN1.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ Anderson C, Crimmins S, Wilson JA, Korbel GA, Ploegh HL, Wilson SM. Loss of Usp14 results in reduced levels of ubiquitin in ataxia mice. J Neurochem. 2005 Nov;95(3):724-31. Epub 2005 Sep 29. PMID:16190881 doi:http://dx.doi.org/10.1111/j.1471-4159.2005.03409.x
- ↑ Chen PC, Qin LN, Li XM, Walters BJ, Wilson JA, Mei L, Wilson SM. The proteasome-associated deubiquitinating enzyme Usp14 is essential for the maintenance of synaptic ubiquitin levels and the development of neuromuscular junctions. J Neurosci. 2009 Sep 2;29(35):10909-19. doi: 10.1523/JNEUROSCI.2635-09.2009. PMID:19726649 doi:http://dx.doi.org/10.1523/JNEUROSCI.2635-09.2009
