Many protein subunit vaccines and biologics contain glycosylated antigens and antibodies, yet quantitative frameworks for comparing glycosylation across lots, manufacturers, and production platforms remain limited. We performed site specific glycosylation LC-MS/MS analysis for intact N-linked glycopeptides on licensed protein subunit vaccines, including influenza from egg-, MDCK-, and Sf9-derived products, plus Sf9 SARS-CoV-2 spike and CHO varicella-zoster virus glycoprotein E. Glycopeptide abundance distribution spectra were compared using the NIST MS Search dot-product score to quantify similarity of site-specific glycan distributions. Across all sites, distributions clustered into six recurrent classes (two high-mannose, three core-fucosylated complex, and one multi-sialylated complex profile). Replicate analyses, year-to-year formulations, and different manufacturers within the same platform were highly similar (scores 978, 961, and 960 out of 999), whereas intra-protein sites, influenza inter-strain sites, and different production sources were less similar (scores 554, 540, and 209). Interestingly, glycosylation differences between production sources tracked phylogenetic relatedness of host species.