Update information. Ubiquitin regulatory X (UBX) domain-containing proteins are one of the major subgroups of cofactors of the AAA+ ATPase CDC48/p97 and function in protein quality control involved in diverse cellular processes. However, little is known whether and how the UBX-containing proteins participate in host-microbe interaction. Here, we report a host nucleus-localized effector from Magnaporthe oryzae, MoNLE1, functions as a virulence factor and suppresses rice immunity by specially interferes with a rice UBX-containing (PUX) protein OsPUX8B.2. To reveal the working mechanism of OsPUX8B.2, we performed TurboID-based proximity labeling experiments to probe OsPUX8B.2 interaction proteins. The result showed that OsPUX8B.2 associates with a set of proteins involved in RNA processing and modification, protein folding and heat/light responses. We verified that a SGS domain-containing protein OsBHT, which negatively regulates rice defense against blast pathogen, is targeted by OsPUX8B.2-OsCDC48-6 for subsequent degradation.