ASH1 like histone lysine methyltransferase
Last updated 18 Aug 2020
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The ASH1L gene, also known as KMT2H, provides instructions for making an enzyme, called lysine-specific methyltransferase 2H, that is found in many organs and tissues of the body. Lysine-specific methyltransferase 2H functions as a histone methyltransferase. Histone methyltransferases are enzymes that modify proteins called histones. Histones are structural proteins that attach (bind) to DNA and give chromosomes their shape. By adding a molecule called a methyl group to histones (a process called methylation), histone methyltransferases control (regulate) the activity of certain genes. Lysine-specific methyltransferase 2H appears to turn on (activate) certain genes that are especially important for development of the brain.
Normal function
The ASH1L gene, also known as KMT2H, provides instructions for making an enzyme, called lysine-specific methyltransferase 2H, that is found in many organs and tissues of the body. Lysine-specific methyltransferase 2H functions as a histone methyltransferase. Histone methyltransferases are enzymes that modify proteins called histones. Histones are structural proteins that attach (bind) to DNA and give chromosomes their shape. By adding a molecule called a methyl group to histones (a process called methylation), histone methyltransferases control (regulate) the activity of certain genes. Lysine-specific methyltransferase 2H appears to turn on (activate) certain genes that are especially important for development of the brain.
Conditions referring to this gene or chromosome
Other names
absent small and homeotic disks protein 1 homolog
ASH1
ash1 (absent, small, or homeotic)-like
ASH1-like protein
ASH1L1
histone-lysine N-methyltransferase ASH1L
huASH1
KMT2H
lysine N-methyltransferase 2H
probable histone-lysine N-methyltransferase ASH1L
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Further reading and references
- ASH1 like histone lysine methyltransferase; MedlinePlus, National Library of Medicine.
- Eram MS, Kuznetsova E, Li F, Lima-Fernandes E, Kennedy S, Chau I, Arrowsmith CH, Schapira M, Vedadi M. Kinetic characterization of human histone H3 lysine 36 methyltransferases, ASH1L and SETD2. Biochim Biophys Acta. 2015 Sep;1850(9):1842-8. doi: 10.1016/j.bbagen.2015.05.013. Epub 2015 May 19.
- Rogawski DS, Ndoj J, Cho HJ, Maillard I, Grembecka J, Cierpicki T. Two Loops Undergoing Concerted Dynamics Regulate the Activity of the ASH1L Histone Methyltransferase. Biochemistry. 2015 Sep 8;54(35):5401-13. doi: 10.1021/acs.biochem.5b00697. Epub 2015 Aug 25.
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