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. USP14 (ubiquitin specific peptidase 14), also known as TGT (tRNA-guanine transglycosylase), is a cytoplasmic protein that belongs to the ubiquitin-specific processing family of deubiquitinating enzymes. Existing as a homodimer within the cell, USP14 functions to cleave ubiquitin residues from both ubiquitinylated proteins and ubiquitin-fused precursors, thereby saving these proteins from proteasomal degradation. In mice, defects or mutations in the gene encoding USP14 cause retarded growth or fetal death, indicating that USP14 plays a key role in early developmental processes. Multiple isoforms of USP14 are expressed due to alternative splicing events.