Meat quality development is highly influenced by the pH decline caused by the postmortem (PM) glycolysis. Protein phosphorylation is an important mechanism in regulating the activity of glycometabolic enzymes. Here, a gel‐based phosphoproteomic study was performed to analyze the protein phosphorylation in sarcoplasmic proteins from three groups of pigs with different pH decline rates from PM 1 to 24 h. Globally, the fast pH decline group had the highest phosphorylation level at PM 1 h, but lowest at 24 h, whereas the slow pH decline group showed the reverse case. The same pattern was also observed in most individual bands in 1‐DE. The protein phosphorylation levels of 12 bands were significantly affected by the synergy effects of pH and time (p <0.05). Protein identification revealed that most of the phosphoproteins were glycometabolism‐related enzymes, and the others were involved in stress response, phosphocreatine metabolism, and other functions. The phosphorylation of pyruvate kinase and triosephosphate isomerase‐1 showed to be related to PM muscle pH decline rate. Our work sheds light on the potential role of protein phosphorylation on regulating meat quality development.