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.
Isoform USB25a is found in most adult and fetal tissues; expression is moderately high in testis, pancreas, kidney, skeletal muscle, liver, lung, placenta, brain, heart, but very low in peripheral blood, colon, small intestine, ovary, prostate, thymus and spleen. Isoform USB25b is found in all tissues except heart and skeletal muscle. Isoform USB25m is heart and skeletal muscle specific.
Belongs to the peptidase C19 family. Contains 1 UBA-like domain. Contains 2 UIM (ubiquitin-interacting motif) repeats.
Acetylated. Sumoylation impairs binding to and hydrolysis of ubiquitin chains. Sumoylated preferentially by 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.
Cytoplasm and Cytoplasm. Nucleus. Some transient punctuate nuclear location in myotubes during myocyte development.