TY - JOUR AU - Mazur, Pawel K. AU - Gozani, Or AU - Sage, Julien AU - Reynoird, Nicolas PY - 2016 TI - Novel insights into the oncogenic function of the SMYD3 lysine methyltransferase JF - Translational Cancer Research; Vol 5, No 3 (June 29, 2016): Translational Cancer Research Y2 - 2016 KW - N2 - SMYD3 is a member of the SMYD family of lysine methyltransferases (KMTs). In humans, there are five SMYD members (SMYD1–5) that are characterized by the presence of a split catalytic SET domain interrupted by a MYND zinc finger domain. The MYND domain is thought to potentially mediate DNA or protein binding but a clear function is yet to be established. SMYD homologs have been described in a wide range of organisms, such as zebrafish, drosophila and budding yeast (1,2). While methylation activity has been clearly established for SMYD2 and SMYD3 (3-6), the activities of SMYD1, 4 and 5 are not well understood. UR - https://tcr.amegroups.org/article/view/8176