PRMT2 is a histone arginine methyltransferase that catalyzes H3R8 asymmetric dimethylation (H3R8me2a) and methylates multiple protein substrates including STAT3, FBL, and histone H4 1. As a transcriptional coactivator, PRMT2 enhances nuclear receptor-mediated transactivation of androgen receptor, estrogen receptor, progesterone receptor, and peroxisome proliferator-activated receptor 23. PRMT2 also suppresses NF-κB signaling and inflammatory responses 45. Clinically, PRMT2 is significantly upregulated in multiple cancers. In renal cell carcinoma, PRMT2 overexpression promotes H3R8me2a enrichment at the WNT5A promoter, enhancing WNT5A transcription and Wnt signaling activation; high PRMT2 correlates with poor survival 6. Similarly, in colorectal cancer, PRMT2 drives WNT5A-mediated malignant progression while promoting M2-like macrophage polarization and T cell dysfunction 7. In glioblastoma, HIF1α-induced PRMT2 activation drives hypoxia-responsive transcriptional programs and tumor progression 8. Conversely, in acute myeloid leukemia, low PRMT2 expression associates with elevated inflammatory signatures and inferior survival, revealing a context-dependent role in controlling NF-κB and STAT3 signaling 4. Additionally, PRMT2 promotes HIV-1 latency by methylating Tat and preventing its incorporation into the Super Elongation Complex 9.