Function | 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. |
Protein Name | Methionine Aminopeptidase 2Map 2Metap 2Initiation Factor 2-Associated 67 Kda GlycoproteinP67P67eif2Peptidase M |
Database Links | Reactome: R-HSA-2514859 |
Cellular Localisation | CytoplasmAbout 30% Of Expressed Metap2 Associates With Polysomes |
Alternative Protein Names | Methionine Aminopeptidase 2 proteinMap 2 proteinMetap 2 proteinInitiation Factor 2-Associated 67 Kda GlycoproteinP67 proteinP67eif2 proteinPeptidase M proteinMETAP2 proteinMNPEP proteinP67EIF2 protein |
Information sourced from Uniprot.org