Human Methionine Aminopeptidase 2 (METAP2, MAP2) is a member of the M24 family of metalloproteases. METAPs catalyze the removal of the initiator methionine residue from nascent peptides and are essential for cell growth. MAP2 binds 2 cobalt or manganese ions and contains approximately 12 O-linked N-acetylglucosamine (GlcNAc) residues. It is found in all organisms and is especially important because of its critical role in tissue repair and protein degradation. METAP2 plays an important role in the development of different types of cancer and has been a novel target for developing anti-cancer drugs. This protein functions both by protecting the alpha subunit of eukaryotic initiation factor 2 from inhibitory phosphorylation and by removing the amno-terminal methionine residue from nascent protein. MAP2 protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. It also plays a critical role in the regulation of protein synthesis.
