Histone-lysine N-methyltransferase SETMAR is a ~78 kDa protein. Protein derived from the fusion of a methylase with the transposase of an Hsmar1 transposon that plays a role in DNA double-strand break repair, stalled replication fork restart and DNA integration. DNA-binding protein, it is indirectly recruited to sites of DNA damage through protein-protein interactions. Also has kept a sequence-specific DNA-binding activity recognizing the 19-mer core of the 5'-terminal inverted repeats (TIRs) of the Hsmar1 element and displays a DNA nicking and end joining activity. In parallel, has a histone methyltransferase activity and methylates 'Lys-4' and 'Lys-36' of histone H3. Specifically mediates dimethylation of H3 'Lys-36' at sites of DNA double-strand break and may recruit proteins required for efficient DSB repair through non-homologous end-joining. 1. Lee, SH. et al. (2005) Proceedings of the National Academy of Sciences of the United States of America 102, 18075-80. PMID: 163329632. Cordaux, R. et al. (2006) Proceedings of the National Academy of Sciences of the United States of America 103, 8101-6. PMID: 166723663. Miskey, C. et al. (2007) Molecular and cellular biology 27, 4589-600. PMID: 174038975. Beck, BD. et al. (2008) The Journal of biological chemistry 283, 9023-30. PMID: 182638766. Goodwin, KD. et al. (2010) Biochemistry 49, 5705-13. PMID: 205218428. Kim, HS. et al. (2014) The Journal of biological chemistry 289, 10930-10938. PMID: 245736779. Fnu, S. et al. (2011) Proceedings of the National Academy of Sciences of the United States of America 108, 540-5. PMID: 2118742810. Williamson, EA. et al. (2008) Nucleic acids research 36, 5822-31. PMID: 18790802 | 
