Parkinson disease (PD) is the second most common age-related neurodegenerative disorder, which is related to neurotransmitter secretion impartment and the dysfunction of vesicle transport. Secretory granules (SGs) are a class of intracellular vesicles different from synaptic vesicles (SVs) in neurons and the neuroendocrine cells. They represent the primary subcellular site for the biosynthesis, storage and releasing of the neuropeptides, neurotransmitters and hormones. In the current study, we characterized the proteome of secretory granules in dopaminergic neurons in PD. Liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis was used to identify proteins in SGs. A total of 4249 proteins were identified in the SGs in normal and MPP+-treated SH-Sy5Y dopaminergic neurons in total. This study regarded the biological alternations of SGs in PD as an entry point. By studying the significantly differentially expressed proteins, it is helpful to better understand the molecular mechanisms of SGs disorders in the pathology of PD, and provide a basis for vesicle transport theory in pathogenesis of PD.