InterPro : IPR025788

Name  Histone-lysine N-methyltransferase, SET2, fungi Short Name  Hist-Lys_N-MeTrfase_SET2_fun
Type  Family Description  This enzyme methylates histone H3 to form H3K36me. It is involved in transcription elongation as well as in transcription repression [, ]. The methyltransferase activity requires the recruitment to the RNA polymerase II, which is CTK1 dependent [, , , , , , ]. It has been shown that this enzyme interacts with the RNA polymerase II hyperphosphorylated CTD and also with CYC8 in Saccharomyces cerevisiae [, , , , , , ].Methyltransferases (EC 2.1.1.-) constitute an important class of enzymes present in every life form. They transfer a methyl group most frequently from S-adenosyl L-methionine (SAM or AdoMet) to a nucleophilic acceptor such as oxygen leading to S-adenosyl-L-homocysteine (AdoHcy) and a methylated molecule [, , ]. All these enzymes have in common a conserved region of about 130 amino acid residues that allow them to bind SAM []. The substrates that are methylated by these enzymes cover virtually every kind of biomolecules ranging from small molecules, to lipids, proteins and nucleic acids [, , ]. Methyltransferase are therefore involved in many essential cellular processes including biosynthesis, signal transduction, protein repair, chromatin regulation and gene silencing [, , ]. More than 230 families of methyltransferases have been described so far, of which more than 220 use SAM as the methyl donor.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

0 Contains

0 Found In

0 Parent Features

15 Publications

First Author Title Year Journal Volume Pages
Schluckebier G Universal catalytic domain structure of AdoMet-dependent methyltransferases. 1995 J Mol Biol 247 16-20
Schubert HL Many paths to methyltransfer: a chronicle of convergence. 2003 Trends Biochem Sci 28 329-35
Kozbial PZ Natural history of S-adenosylmethionine-binding proteins. 2005 BMC Struct Biol 5 19
Wlodarski T Comprehensive structural and substrate specificity classification of the Saccharomyces cerevisiae methyltransferome. 2011 PLoS One 6 e23168
Kizer KO A novel domain in Set2 mediates RNA polymerase II interaction and couples histone H3 K36 methylation with transcript elongation. 2005 Mol Cell Biol 25 3305-16
Strahl BD Set2 is a nucleosomal histone H3-selective methyltransferase that mediates transcriptional repression. 2002 Mol Cell Biol 22 1298-306
Xiao T Phosphorylation of RNA polymerase II CTD regulates H3 methylation in yeast. 2003 Genes Dev 17 654-63
Krogan NJ Methylation of histone H3 by Set2 in Saccharomyces cerevisiae is linked to transcriptional elongation by RNA polymerase II. 2003 Mol Cell Biol 23 4207-18
Landry J Set2-catalyzed methylation of histone H3 represses basal expression of GAL4 in Saccharomyces cerevisiae. 2003 Mol Cell Biol 23 5972-8
Schaft D The histone 3 lysine 36 methyltransferase, SET2, is involved in transcriptional elongation. 2003 Nucleic Acids Res 31 2475-82
Rao B Dimethylation of histone H3 at lysine 36 demarcates regulatory and nonregulatory chromatin genome-wide. 2005 Mol Cell Biol 25 9447-59
Li J Association of the histone methyltransferase Set2 with RNA polymerase II plays a role in transcription elongation. 2002 J Biol Chem 277 49383-8
Li B The Set2 histone methyltransferase functions through the phosphorylated carboxyl-terminal domain of RNA polymerase II. 2003 J Biol Chem 278 8897-903
Tripic T The Set2 methyltransferase associates with Ssn6 yet Tup1-Ssn6 repression is independent of histone methylation. 2006 Biochem Biophys Res Commun 339 905-14
Morris SA Histone H3 K36 methylation is associated with transcription elongation in Schizosaccharomyces pombe. 2005 Eukaryot Cell 4 1446-54

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)