METAP2
Function
The protein expressed by the MAP2 gene cotranslationally removes the N-terminal methionine from nascent proteins, particularly when the second residue is small and uncharged. In comparison to METAP1, the catalytic activity of human METAP2 towards Met-Val peptides is consistently much higher, indicating its role in processing proteins with N-terminal Met-Val and Met-Thr sequences in vivo. Additionally, it protects the eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases, such as EIF2AK2/PKR and EIF2AK1/HCR, playing a critical role in the regulation of protein synthesis. This supplementary information is collated from multiple sources and compiled automatically.
Post-translational modifications
Contains approximately 12 O-linked N-acetylglucosamine (GlcNAc) residues. O-glycosylation is required for EIF2S1 binding.
Sequence Similarities
Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily.
Cellular localization
- Cytoplasm
- About 30% of expressed METAP2 associates with polysomes.
Alternative names
MNPEP, P67EIF2, METAP2, Methionine aminopeptidase 2, MAP 2, MetAP 2, Initiation factor 2-associated 67 kDa glycoprotein, Peptidase M, p67, p67eIF2