Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). 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. Protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. Plays a critical role in the regulation of protein synthesis.
Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily.
Contains approximately 12 O-linked N-acetylglucosamine (GlcNAc) residues. O-glycosylation is required for EIF2S1 binding.
Cytoplasm. About 30% of expressed METAP2 associates with polysomes.
Detection of Methionine Aminopeptidase 2 by Western Blot of Immunprecipitate.
Lane 1: ab123523 at 1µg/ml staining Methionine Aminopeptidase 2 in HeLa whole cell lysate immunoprecipitated using ab123523 at 6µg/mg lysate (1 mg/IP; 20% of IP loaded/lane). Lane 2: Control IgG
Detection: Chemiluminescence with exposure time of 10 seconds.
Western blot - Anti-Methionine Aminopeptidase 2 antibody (ab123523)
All lanes : Anti-Methionine Aminopeptidase 2 antibody (ab123523) at 0.1 µg/ml
Lane 1 : HeLa whole cell lysate at 50 µg Lane 2 : HeLa whole cell lysate at 15 µg Lane 3 : 293T whole cell lysate at 50 µg Lane 4 : Jurkat whole cell lysate at 50 µg Lane 5 : NIH3T3 whole cell lysate at 50 µg