The changes in antigenic epitopes and allergenicity of silver carp parvalbumin (PV) after glycation and phosphorylation were investigated by spectroscopy, mass spectrometry and KU812 cell assay. The results showed that glycation combined with phosphorylation increased the molecular mass, reduced the free amino acid content, and changed the secondary structure and conformation of PV. The modified PV had eight glycation sites (K33, K46, K55, K65, K84, K88, K97 and K108) and one phosphorylation site (S56). The modification significantly reduced the ability of PV to bind IgG and IgE, and decreased histamine and interleukin-6 release from KU812 cells. Thus, glycation combined with phosphorylation reduced PV allergencity by masking the linear epitopes and damaging the conformational epitopes at the glyclation and phosphorylation sites. The results of this study may provide an important theoretical basis for the development of hypoallergenic fish products.