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- The ubiquitin carboxyl-terminal hydrolase 27 (EC 3.4.19.12), also known as deubiquitinating enzyme 27, ubiquitin thioesterase 27 and USP27X, is a deubiquitinating enzyme which is mainly characterized for cleaving ubiquitin (Ub) from proteins and other molecules. Ubiquitin binds to proteins so as to regulate the degradation of them via the proteasome and lysosome among many other functions. USP27X is encoded by the ubiquitin specific peptidase 27 X-linked gene, found in chromosome X in region Xp11.23. It is mainly found in the cytosol and nucleus of cells, as well as the nucleoplasm and in vesicles. It is an intracellular protein found in many human tissues with low blood cell specificity. DUBs belong to the superfamily of proteases enzymes. Proteases can be classified into five different classes depending on the mechanism of catalysis: aspartic, metallo, serine, threonine and cystein proteases. Cysteine proteases comprise ubiquitin C-terminal hydrolases (UCHs), Machada Josepchin domain proteases (MJDs), ovarian tumour proteases (OTU) and ubiquitin-specific proteases (USPs). USP27X is included in the ubiquitin-specific proteases enzymes. (en)
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