Objective To screen key phosphorylated proteins involved in vascular remodeling of aortic coarctation (CoA) using phosphoproteomics and to investigate the role of the Golgi protein GORASP1 in its pathogenesis. Methods Paired tissue samples from CoA stenotic segments and control aortic tissues (n=5 pairs) were collected. Differentially phosphorylated proteins were identified through phosphoproteomic profiling. Bioinformatics analyses were performed to elucidate the functions of these proteins and delineate the mechanism by which GORASP1 contributes to CoA. Results Functional analysis of the differential proteins between the CoA and control groups revealed significant enrichment in pathways such as oxidative stress and energy metabolism, suggesting these biological processes play important roles in CoA pathology. Notably, GORASP1 was identified as the most significantly differentially phosphorylated protein. Its functions were primarily associated with Golgi organization and the autophagy pathway, suggesting that GORASP1 may act as a key nodal molecule linking these common pathological processes to organelle dysfunction. Conclusion The specific phosphorylation signature in CoA is closely related to oxidative stress. GORASP1 likely participates in vascular remodeling by regulating organelle function and autophagy processes, providing new directions for mechanistic research and therapeutic target development in CoA.