The last ten years have witnessed the increasingly notable advances in immobilized metal ion chromatography (IMAC) for phosphoproteomic profiling. Protein phosphorylation is an important post-translational modification (PTM) that participates in multiple cellular processes. Phosphoproteomics provides powerful analysis and unique insights for the study of phosphorylation-related cellular processes and disease mechanisms. IMAC enrichment strategy could capture phosphopeptides with chemical interaction between the phosphoamino acids and the immobilized metal cations. Currently, IMAC materials and workflows have matured and are applied in capturing phosphopeptides at substoichiometric levels. The design of IMAC enrichment materials and matching workflows are particularly vital in phosphoproteomic profiling. This review mainly focuses on overviewing present advances in the materials, workflows, and applications of immobilized metal ion chromatography for phosphoproteomic profiling, including a brief discussion on their advantages, current challenges, and trends in the future development.