The ubiquitin (Ub) pathway involves three sequential enzymatic steps that facilitate the conjugation of Ub and Ub-like molecules to specific protein substrates. Through the use of a wide range of enzymes that can add or remove ubiquitin, the Ub pathway controls many intracellular processes such as signal transduction, transcriptional activation and cell cycle progression. USP32 (ubiquitin specific peptidase 32), also known as NY-REN-60, is a 1,604 amino acid protein that contains one DUSP domain and three EF-hand calcium binding domains. Localized to membranes in a lipid-anchored fashion and expressed in all normal tissues, USP32 catalyzes the conversion of a ubiquitin C-terminal thioester to a free ubiquitin and a thiol, a reaction that may influence several cellular processes.