NMT2

N-myristoyltransferase (NMT) catalyzes the reaction of N-terminal myristoylation of many signaling proteins. It transfers myristic acid from myristoyl coenzyme A to the amino group of a protein's N-terminal glycine residue. Biochemical evidence indicates the presence of several distinct NMTs, varying in apparent molecular weight and /or subcellular distribution. The predicted 498-amino acid of human NMT2 protein shares 77% and 96% sequence identity with human NMT1 and mouse Nmt2 comprise two distinct families of N-myristoyltransferases. [provided by RefSeq]

N-myristoyltransferase 2

Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins (PubMed:25255805, PubMed:9506952).
Also able to mediate N-terminal lysine myristoylation of proteins: catalyzes myristoylation of ARF6 on both 'Gly-2' and 'Lys-3' (PubMed:32103017).
Lysine myristoylation is required to maintain ARF6 on membranes during the GTPase cycle (PubMed:32103017).

Intracellular transport of virusTAS:Reactome
N-terminal peptidyl-glycine N-myristoylationManual Assertion Based On ExperimentIDA:UniProtKB
Regulation of rhodopsin mediated signaling pathwayTAS:Reactome

Cytoplasm
Membrane