USP25

Ubiquitin (MIM 191339) is a highly conserved 76-amino acid protein involved in regulation of intracellular protein breakdown, cell cycle regulation, and stress response. Ubiquitin is released from degraded proteins by disassembly of the polyubiquitin chains, which is mediated by ubiquitin-specific proteases (USPs), such as USP25.

ubiquitin specific peptidase 25

Deubiquitinating enzyme that hydrolyzes ubiquitin moieties conjugated to substrates and thus, functions to process newly synthesized Ubiquitin, to recycle ubiquitin molecules or to edit polyubiquitin chains and prevents proteasomal degradation of substrates. Hydrolyzes both 'Lys-48'- and 'Lys-63'-linked tetraubiquitin chains.
The muscle-specific isoform (USP25m) may have a role in the regulation of muscular differentiation and function.

Biological Process negative regulation of ERAD pathway Source:ParkinsonsUK-UCL1 Publication
Biological Process protein deubiquitination Source:ParkinsonsUK-UCL1 Publication
Biological Process protein K48-linked deubiquitination Source:UniProtKB1 Publication
Biological Process protein K63-linked deubiquitination Source:UniProtKB1 Publication
Biological Process protein modification process Source:ProtInc1 Publication
Biological Process proteolysis Source:ProtInc1 Publication
Biological Process ubiquitin-dependent protein catabolic process Source:InterPro

Cytoplasm
Isoform USP25m
Cytoplasm
Nucleus
Some transient punctuate nuclear location in myotubes during myocyte development.

Acetylated.
Sumoylation impairs binding to and hydrolysis of ubiquitin chains. Sumoylated preferentially with SUMO2 or SUMO3. Desumoylated by SENP1. Regulated by ubiquitination on the same residue.
Preferentially monoubiquitinated but can also be polyubiquitinated. Autodeubiquitinated. Ubiquitination activates the enzymatic activity either by preventing sumoylation or by allowing novel interactions.
Phosphorylation in the C-terminal by SYK regulates USP25 cellular levels.