N-lysine methyltransferase SMYD2

Definition:

Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The activity requires interaction with HSP90alpha. Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'.

References:

[1]. Jing Huang, et al. p53 is regulated by the lysine demethylase LSD1. Nature. 2007 Sep 6;449(7158):105-8. [Content Brief]

[2]. Jing Huang, et al. Repression of p53 activity by Smyd2-mediated methylation. Nature. 2006 Nov 30;444(7119):629-32. [Content Brief]

[3]. Louis A Saddic, et al. Methylation of the retinoblastoma tumor suppressor by SMYD2. J Biol Chem. 2010 Nov 26;285(48):37733-40. [Content Brief]

[4]. Andrew D Ferguson, et al. Structural basis of substrate methylation and inhibition of SMYD2. Structure. 2011 Sep 7;19(9):1262-73. [Content Brief]

[5]. Li Wang, et al. Structure of human SMYD2 protein reveals the basis of p53 tumor suppressor methylation. J Biol Chem. 2011 Nov 4;286(44):38725-38737. [Content Brief]

[6]. Mohamed Abu-Farha, et al. The tale of two domains: proteomics and genomics analysis of SMYD2, a new histone methyltransferase. Mol Cell Proteomics. 2008 Mar;7(3):560-72. [Content Brief]

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