Aim. Study on a possible role of methylation of lysine residues of еЕF1А2 in its interactions with the elongation translation complex eEF1B. Methods. Mutagenesis, cloning, 293 human cell culture, BRET (bioluminescence resonance energy transfer), cell transfection, HaloTag pull down of protein complexes, Western blot, densitometry. Results. Five mutants of eEF1A2 with a single substitution of methylable lysine residue for arginine and the mutant with all five lysine residues mutated were generated. BRET analysis and HaloTag pull down experiments of isolated protein complexes have shown no differences in interactions of eEF1B subunits with eEF1A2 and its unmethylable mutants. Conclusion. Methylation of eEF1A2 apparently does not influence the interactions of eEF1A2 with eEF1B subunits.