USP10 and neoplasm: 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.