| Tissue Specificity | |
| Post Translational Modifications | Contains approximately 12 O-linked N-acetylglucosamine (GlcNAc) residues. O-glycosylation is required for EIF2S1 binding. |
| 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 ELISA Names | Methionine Aminopeptidase 2 ELISA kitMap 2 ELISA kitMetap 2 ELISA kitInitiation Factor 2-Associated 67 Kda Glycoprotein ELISA kitP67 ELISA kitP67eif2 ELISA kitPeptidase M ELISA kitMETAP2 ELISA kitMNPEP ELISA kitP67EIF2 ELISA kit |
| output | |
Information sourced from Uniprot.org
