Glycosylation of proteins greatly affects their structure and function, but traditional genomics and transcriptomics are not able to precisely capture tissue- or species-specific glycosylation patterns. We describe here a novel approach to link different ‘omics’ data based on exhaustive quantitative glycomics of murine dermis and epidermis. We first examined the dermal and epidermal N-glycome of mouse by recently established glycoblotting technique. We found that the Gala1-3Gal epitope was solely expressed in epidermis tissue and was preferentially attached to adhesion molecules in a glycosylation site–specific manner. Clarified glycomic and protemic information combined with publicly available microarray datasets allowed us to identify galectin-3 as a receptor of Gala1-3Gal epitope. These findings provide mechanistic insight into the causal connection between the genotype and the phenotype seen in a3GalT-1–deficient mice and transgenic mice expressing endo-ß-galactosidase C. Because humans do not possess the Gala1-3Gal structure on their tissues, we further examined the human dermal and epidermal N-glycome. Comparative glycomics revealed that the GalNAcß1-4GlcNAc (LacdiNAc) epitope, instead of the Gala1-3Gal epitope, was highly expressed in human epidermis.