| Primary Identifier | IPR017155 | Type | Family |
| Short Name | Hist-Lys_N-MeTrfase_SET |
| description | This entry represents histone-lysine N-methyltransferase (SETD7 or SET7/9) (), which contains a SET domain []. This enzyme specifically monomethylate Lys-4 of histone H3, thereby creating a specific tag for epigenetic transcriptional activation. Methylation of lysine residues in the N-terminal tails of histones is thought to represent an important component of the mechanism that regulates chromatin structure. As such SETD7 plays a central role in the transcriptional activation of genes such as collagenase and insulin. It is recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. SETD7 also has methyltransferase activity toward non-histone proteins, including TAF10 and p53/TP53. SETD7 monomethylates Lys-189 of TAF10, which increases the affinity of TAF10 for RNA polymerase II. SETD7 monomethylates Lys-372 of p53/TP53, which stabilises p53/TP53 and increases p53/TP53-mediated transcriptional activation []. These enzymes contain a SET domain, which is necessary but not sufficient for histone methyltransferase activity []. Human SETD7 contains an N-terminal β-sheet domain in addition to the conserved SET domain []. Mutagenesis studies []identified two residues in the C terminus of the protein that appear essential for catalytic activity toward lysine-4 of histone H3; cofactor AdoMet binds to this domain. |
