Histone methyltransferase

euchromatic histone-lysine N-methyltransferase 1

Identifiers
Symbol	EHMT1
Entrez	79813
HUGO	24650
OMIM	607001
RefSeq	NM_024757
UniProt	Q9H9B1
Other data
EC number	2.1.1.43
Locus	Chr. 9 [1]

Histone methyltransferases (HMT) are enzymes, histone-lysine N-methyltransferase and histone-arginine N-methyltransferase, that catalyze the transfer of one to three methyl groups from the cofactor S-Adenosyl methionine to lysine and arginine residues of histone proteins. These proteins often contain a SET (Su(var)3-9, Enhancer of Zeste, Trithorax) domain, however the recently discovered HMT Dot1 lacks the characteristic SET domain.^{[citation needed]}

Role in gene regulation

Histone methylation serves in epigenetic gene regulation. Methylated histones bind DNA more tightly, which inhibits transcription.^{[citation needed]}

Methylated histones can either repress or activate transcription as different experimental findings suggest. See Histone#Chromatin regulation.

See also

• Histone-Modifying Enzymes
• Histone acetyltransferase
• Histone deacetylase
• RNA polymerase control by chromatin structure
• Histone methylation

External links

• GeneReviews/NCBI/NIH/UW entry on Kleefstra Syndrome
• MeSH Histone-Lysine+N-Methyltransferase
• MeSH Protein-Arginine+N-Methyltransferase
• Structure and Function of Histone Methyltransferases. Trievel. 2004
• The Dot1 Histone Methyltransferase and the Rad9 Checkpoint Adaptor Contribute to Cohesin-Dependent Double-Strand Break Repair by Sister Chromatid Recombination in Saccharomyces cerevisiae.