USP47 is a deubiquitinating enzyme that plays crucial roles in cancer progression, immune regulation, and neurological function through substrate-specific protein stabilization. The enzyme functions by removing ubiquitin modifications from target proteins, thereby preventing their proteasomal degradation 1. In cancer contexts, USP47 promotes tumor progression through multiple mechanisms: it stabilizes c-Myc to enhance cell proliferation 2, deubiquitinates PD-L1 to facilitate immune evasion 3, stabilizes NRP1 to promote angiogenesis 4, and deubiquitinates Snai1 to activate epithelial-mesenchymal transition 5. USP47 expression is frequently upregulated in various cancers and correlates with poor prognosis 34. In immune regulation, USP47 maintains regulatory T cell homeostasis by preventing YTHDF1 ubiquitination, which reduces m6A-dependent c-Myc translation 6. Neurologically, USP47 regulates synaptic plasticity by preventing degradation of ubiquitinated AMPA receptor subunit GluR1, with elevated levels observed in epileptic models 7. The crystal structure reveals that USP47's catalytic activity increases upon ubiquitin binding through realignment of catalytic triads 1. These diverse functions make USP47 an attractive therapeutic target for cancer, autoimmune diseases, and neurological disorders.