EEF1AKMT2 (also known as METTL10) is a protein-lysine methyltransferase that catalyzes the selective trimethylation of elongation factor 1A (eEF1A) at lysine-318 1. The enzyme employs a unique beta-hairpin recognition motif extending from its core methyltransferase fold to achieve high substrate selectivity, with a critical phenylalanine residue (F220) essential for catalytic activity 1. EEF1AKMT2-mediated methylation of eEF1A is negatively regulated by phosphorylation at nearby serine-314 and competitively inhibited by the eEF1A guanine nucleotide exchange factor eEF1Bα 1. EEF1A methylation by EEF1AKMT2 may have neurological significance, as genome-wide association studies identified EEF1AKMT2 as a shared causal gene between primary open-angle glaucoma and optic chiasm volume 2, and as a pleiotropic risk locus modulating cortical structure and delirium risk in elderly individuals 3. These findings suggest EEF1AKMT2 represents a potential neuroprotective drug target, though further investigation is needed to elucidate its specific mechanisms in glaucoma pathology and neurodegeneration.