USP5 (ubiquitin specific peptidase 5) is a zinc-binding, multidomain, deubiquitinating protein belonging to the ubiquitin-specific protease (USP) family. It comprises of a zinc finger (ZnF) domain responsible for catalytic activity. USP5 has been reported as a putative p53 target gene in cancer treatment. The suppressed expression of USP5 increases the level and transcriptional activity of p53.
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The Journal of biological chemistry, 284(8), 5030-5041 (2008-12-23)
Both p53 and its repressor Mdm2 are subject to ubiquitination and proteasomal degradation. We show that knockdown of the deubiquitinating enzyme USP5 (isopeptidase T) results in an increase in the level and transcriptional activity of p53. Suppression of USP5 stabilizes
Human ubiquitin-specific cysteine protease 5 (USP5, also known as ISOT and isopeptidase T), an 835-residue multidomain enzyme, recycles ubiquitin by hydrolyzing isopeptide bonds in a variety of unanchored polyubiquitin substrates. Activation of the enzyme's hydrolytic activity toward ubiquitin-AMC (7-amino-4-methylcoumarin), a
The human isopeptidase T (isoT) is a zinc-binding deubiquitinating enzyme involved in the disassembly of free K48-linked polyubiquitin chains into ubiquitin monomers. The catalytic site of this enzyme is thought to be composed of Cys335, Asp435, His786 and His795. These
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