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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/KDM3B_HUMAN KDM3B_HUMAN]] Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate. May have tumor suppressor activity.<ref>PMID:16603237</ref> | [[http://www.uniprot.org/uniprot/KDM3B_HUMAN KDM3B_HUMAN]] Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate. May have tumor suppressor activity.<ref>PMID:16603237</ref> | ||
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| - | ==See Also== | ||
| - | *[[Jumonji domain-containing protein|Jumonji domain-containing protein]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 19:47, 24 January 2018
Crystal structure of JmjC domain of human histone 3 Lysine-specific demethylase 3B (KDM3B)
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Categories: Human | Arrowsmith, C H | Bountra, C | Crawley, L | Delft, F von | Edwards, A | Gileadi, C | Goubin, S | Johansson, C | Krojer, T | Oppermann, U | Szykowska, A | Vollmar, M | Oxidoreductase
