We previously identified an orphan protein METTL13 (methyltransferase-like protein13) as the physiologic enzyme that specifically catalyzes dimethylation of eEF1A at lysine 55 (eEF1AK55me2). Targeting of METTL13 may have potent anti-cancer activity while causing minimal toxicity in normal tissues. The mechanism whereby the METTL13-eEF1AK55me2 alters mRNA translation to drive tumorigenesis is obscure. We have previously shown that eEF1AK55me2 bolsters bulk protein synthesis by promoting global elongation rates. Nonetheless, the effects of eEF1AK55me2 on selective reprogramming of protein synthesis are still unknown. Importantly selective reprograming of the translatome is required to establish malignant proteomes that fuel neoplastic growth.To directly investigate the role of eEF1AK55me2 in the establishment of malignant proteomes, a quantitative noncanonical amino acid tagging (QuaNCAT) strategy was used for global profiling of protein synthesis in cultured cell lines, focusing our analyses on T3M4 cells, a KRASQ61H-harboring pancreatic cancer cell line in which translation rates are known to be regulated by METTL13.