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(Difference between revisions)
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/DOT1L_HUMAN DOT1L_HUMAN]] Histone methyltransferase. Methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones. Binds to DNA. | [[http://www.uniprot.org/uniprot/DOT1L_HUMAN DOT1L_HUMAN]] Histone methyltransferase. Methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones. Binds to DNA. | ||
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| - | ==See Also== | ||
| - | *[[Histone methyltransferase|Histone methyltransferase]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
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[[Category: Histone]] | [[Category: Histone]] | ||
[[Category: Methyltransferase]] | [[Category: Methyltransferase]] | ||
| + | [[Category: Sgc]] | ||
[[Category: Transferase-transferase inhibitor complex]] | [[Category: Transferase-transferase inhibitor complex]] | ||
Revision as of 08:07, 15 November 2017
Crystal structure of human DOT1L in complex with inhibitor FED2
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Categories: Histone-lysine N-methyltransferase | Human | Arrowsmith, C H | Bountra, C | Bradner, J E | Brown, P J | Edwards, A M | Federation, A | Li, Y | Marineau, J | Nguyen, K T | Qi, J | Structural genomic | Schapira, M | Tempel, W | Vedadi, M | Wernimont, A K | Yu, W | Epigenetic | Histone | Methyltransferase | Sgc | Transferase-transferase inhibitor complex
