Ubiquitination is a type of post-translational modification (PTM) that involves the attachment of Ubiquitin to a protein's lysine residue. Ubiquitin is a highly conserved protein of approximately 8.5 kDa which has a normal role in the targeting of proteins for proteolytic degradation. In order to perform this function, Ubiquitin is appended to the target protein to be degraded via the C-terminal glycine of Ubiquitin. The ubiquitinated complex is then recognized by a complex of degradative enzymes. Proteins may be monoubiquitinated or polyubiquitinated; the latter are recognized by the 26S proteasome, which catalyzes the degradation of the target protein. The 26S proteasome is also responsible for recycling Ubiquitin after the target protein's degradation.
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