Previously, we showed that glycosylation of B7‐H4 alters its protein conformation, which changes the recognition and interaction of the E3 ligase with B7‐H4.[3] In the present study, the mass spectrometry identified the USP10 as a deubiquitinase that upregulates B7‐H4 through counteracts the E3 ligase‐mediated ubiquitylation and degradation, resulting in inhibition of tumor immune response and cellular response to ADC treatment. This evidence concerns the gene VTCN1 and neoplasm.