Removes the N-terminal methionine from nascent proteins. The catalytic activity of human METAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N-terminal Met-Val and Met-Thr sequences in vivo. Interacts strongly with the eIF-2 gamma-subunit EIF2S3. Binds EIF2S1 at low magnesium concentrations. Belongs to the peptidase M24A family. Note: This description may include information from UniProtKB.
Protein type: Protease; EC 188.8.131.52
Cellular Component: cytoplasm; cytosol
Molecular Function: metalloexopeptidase activity; metal ion binding; aminopeptidase activity
Biological Process: rhodopsin mediated signaling; phototransduction, visible light; regulation of rhodopsin mediated signaling; peptidyl-methionine modification; protein processing; N-terminal protein amino acid modification
SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.