METAP2 (P50579) - Overview - Molecular Target Synopsis
METAP2, Methionine aminopeptidase 2
Enzyme Classification 184.108.40.206
Also Known as MAP2_HUMAN, METAP2, MNPEP, P67EIF2
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. Interacts strongly with the eIF-2 gamma-subunit EIF2S3 (By similarity). Binds EIF2S1 at low magnesium concentrations.
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UniProt: METAP2 is active in the following subcellular-locations: cytoplasm.
GO terms: METAP2 is active in the following subcellular-locations: cytoplasm, cytosol, plasma membrane.