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From Proteopedia
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/KDM6B_HUMAN KDM6B_HUMAN]] Histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code. Demethylates trimethylated and dimethylated H3 'Lys-27'. Plays a central role in regulation of posterior development, by regulating HOX gene expression. Involved in inflammatory response by participating in macrophage differentiation in case of inflammation by regulating gene expression and macrophage differentiation.<ref>PMID:17825402</ref> <ref>PMID:17851529</ref> | [[http://www.uniprot.org/uniprot/KDM6B_HUMAN KDM6B_HUMAN]] Histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code. Demethylates trimethylated and dimethylated H3 'Lys-27'. Plays a central role in regulation of posterior development, by regulating HOX gene expression. Involved in inflammatory response by participating in macrophage differentiation in case of inflammation by regulating gene expression and macrophage differentiation.<ref>PMID:17825402</ref> <ref>PMID:17851529</ref> | ||
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| - | ==See Also== | ||
| - | *[[Jumonji domain-containing protein|Jumonji domain-containing protein]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 19:09, 24 January 2018
Crystal structure of the human JMJD3 jumonji domain
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Categories: Human | Arrowsmith, C | Bountra, C | Burgess-Brown, N | Che, K H | Daniel, M | Edwards, A | Filippakopoulos, P | Krojer, T | Muniz, J R.C | Ng, S S | Oppermann, U | Savitsky, P | Tumber, A | Ugochukwu, E | Weigelt, J | Yue, W W | Chromatin modification | Histone demethylation | Oxidoreductase | Oxygenase
