Extensive literature links the aberrant crosstalk between N-glycosylation and itself, as well as site-specific phosphorylation to oncogenic signaling: tumor-associated hyper-branching, terminal sialylation or core fucosylation of N-linked glycans can mask phosphodegrons, disrupt kinase- or β-TrCP recognition, and simultaneously engage lectin/siglec pathways, collectively fueling malignant transformation, metastasis and inflammation28,29,30. This evidence concerns the gene BTRC and neoplasm.