Source:http://linkedlifedata.com/resource/umls/id/C0077678
MSH: A diverse class of enzymes that interact with UBIQUITIN-CONJUGATING ENZYMES and ubiquitination-specific protein substrates. Each member of this enzyme group has its own distinct specificity for a substrate and ubiquitin-conjugating enzyme. Ubiquitin-protein ligases exist as both monomeric proteins multiprotein complexes.,NCI: E3 Ubiquitin Ligases are ATP-dependent enzymes that catalyze the formation of a covalent bond between ubiquitous intracellular Ubiquitin proteins and other proteins, often to mark them for nonlysosomal proteasomal degradation or targeted transport. Ubiquitination requires sequential action of an activating enzyme (E1), a conjugating enzyme (E2), and a ligase (E3). Ubiquitin is coupled to protein by a peptide bond between the ubiquitin C-terminal glycine and protein lysine alpha-amino groups. Ubiquitination regulates protein degradation, chromatin remodeling, cell cycle progression, differentiation, gene expression, stress response, ribosome biogenesis, antigen presentation, apoptosi