This study investigates how engineered N-glycan remodeling affects phosphorylation signaling networks in human cells. We generated a glycoengineered HEK293 cell line (AI) with eliminated core fucosylation, enhanced sialylation, and reduced GlcNAc branching through sequential CRISPR/Cas9 knockouts (FUT8, MGAT4A/B, MGAT5, GMDS) and knock-in of sialuria-associated GNE mutations (R263L/R266Q), combined with stable overexpression of ST6Gal1, B4GalT1, MGAT1, and MGAT2. Both wildtype (WT) and AI cells were subjected to three treatment conditions in biological triplicate: normal growth in complete medium, 12-hour serum starvation, and 12-hour starvation followed by 30-minute serum re-stimulation (10% FBS). We performed integrated multi-omics profiling using TMT18-based quantitative proteomics to simultaneously characterize the global proteome (24 fractions), phosphoproteome (12 Fe-IMAC enriched fractions), and glycoproteome (12 MAX-enriched fractions) across all conditions. This dataset enables systematic interrogation of glycan-phosphorylation crosstalk and identifies glycan-dependent signaling rewiring in response to growth factor stimulation.