However, STUB1 (CHIP) has been considered a double‐edged sword in tumor development, depending on the cell types and substrates.[22] We found that the K63‐linked ubiquitin chains of Rab22a‐NeoF1 fusion protein mediated by STUB1 are recognized by NDP52, an autophagy receptor, to be degraded by lysosome, and that IFNα, β, and γ increased NDP52 to reduce endogenous and exogenous Rab22a‐NeoF1 protein levels. Here, IFNA1 is linked to neoplasm.