Based on literature data reporting that PRMTs are associated with their substrates [12] and in silico
sequence analysis of KAP1 protein revealing the presence of potential sites for PRMT5 methylation
(motifs RG) [13] on the arginine residues at positions 308 and 523 (Figure 1b), we hypothesized that
PRMT5 can methylate KAP1. To verify this hypothesis, we performed an in vitro methylation assay
by using the recombinant protein Myc-PRMT5, immunoprecipitated from HEK293 cells, and the