The potential risk of P2Y12 antagonists for cancer treatment is controversial. Here we show that PSB 0739, a P2Y12 antagonist inhibits human cervical cancer cells (Hela and SiHa) migration without modifying cell proliferation. We identify that the co-acetylation and lactylation of epithelial-mesenchymal transition (EMT)-related protein NCL, MYH9, CTTN, S100A6, and ALDOA revealed by proteomic analysis of posttranslational modifications (PTM), are responsible for the PSB0739-induced migration inhibition in human cervical cancer cells. Our data suggest that as one of P2Y12 antagonists, PSB 0739 has no risk in cervical cancer cell migration. The co-modification of acetylation and lactylation of EMT-associated proteins would be novel promising targets to develop new drug for cancer cell migration beyond contributing the potential mechanism of the use of PSB0379 in human cervical cancer cells.