Through binding specific recognition sites in the EBV genome, Epstein-Barr nuclear antigen (EBNA-1) viral protein performs several important functions in latent infection. The 325--376 amino acid region, which is essential for transcriptional activation and viral episome segregation functions of EBNA-1, contains four serines that have been predicted to be phosphorylated and is rich in RGG motifs that are predicted to be methylated. In addition, interactions between EBNA-1 and protein arginine methyltransferases have been identified. Through my research, I investigated a role for post-translational modifications in the regulation of EBNA-1 functions. My data suggests that serine phosphorylation of the 325--376 amino acid region of EBNA-1 may be involved in the regulation of EBNA-1 segregation activity. I also observed an alteration in EBNA-1 cellular localization upon treatment with methyl-transferase inhibitor 5'-deoxy-5'-methyl-thioadenosine (MTA), suggesting a possible role for arginine methylation in the regulation of EBNA-1 activity.