Ubiquitination is an important mechanism through which three classes of enzymes act in concert to target short-lived or abnormal proteins for destruction. The three classes of enzymes involved in ubiquitination are the ubiquitin-activating enzymes (E1s), the ubiquitin-conjugating enzymes (E2s) and the ubiquitin-protein ligases (E3s). Ubr7 (ubiquitin protein ligase E3 component n-recognin 7), also known as C14orf130 or N-recognin-7, is a 425 amino acid protein that contains one UBR-type zinc finger and one PHD zinc finger. Participating in protein modification events within the N-end rule pathway, Ubr7 functions as an E3 ubiquitin-protein ligase that recognizes and binds proteins that contain destabilizing N-terminal residues, thereby leading to their ubiquitination and subsequent degradation.