Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins. Specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). Has also methyltransferase activity toward non-histone proteins such as p53/TP53 and RB1. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates 'Lys-860' of RB1/RB. Interacts with RNA polymerase II and HELZ. Interacts with SIN3A and HDAC1. Interacts (via MYND-type zinc finger) with EPB41L3. Interacts (via SET domain) with p53/TP53. Interacts with RB1 and HSP90AA1. Expression is repressed by CEBPA. Note: This description may include information from UniProtKB.
Protein type: Methyltransferase, protein lysine; EC 2.1.1.; Methyltransferase; EC 2.1.1.-; EC 188.8.131.52
Cellular Component: cytoplasm; cytosol; nucleus
Molecular Function: protein binding; p53 binding; metal ion binding; protein-lysine N-methyltransferase activity; histone lysine N-methyltransferase activity (H3-K36 specific)
Biological Process: negative regulation of cell proliferation; transcription, DNA-dependent; peptidyl-lysine di-methylation; peptidyl-lysine mono-methylation; histone H3-K36 methylation; negative regulation of transcription from RNA polymerase II promoter; regulation of DNA damage response, signal transduction by p53 class mediator
Alt. Names/Synonyms: HSKM-B; KMT3C; Lysine N-methyltransferase 3C; MGC119305; SET and MYND domain containing 2; SET and MYND domain-containing protein 2; SMYD2; zinc finger, MYND domain containing 14; ZMYND14
SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.