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From the following article:

ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression

Xiaobing Shi, Tao Hong, Kay L. Walter, Mark Ewalt, Eriko Michishita, Tiffany Hung, Dylan Carney, Pedro Peña, Fei Lan, Mohan R. Kaadige, Nicolas Lacoste, Christelle Cayrou, Foteini Davrazou, Anjanabha Saha, Bradley R. Cairns, Donald E. Ayer, Tatiana G. Kutateladze, Yang Shi, Jacques Côté, Katrin F. Chua & Or Gozani

Nature 442, 96-99(6 July 2006)

doi:10.1038/nature04835

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Figure 1 - Unfortunately we are unable to provide accessible alternative text for this. If you require assistance to access this image, or to obtain a text description, please contact npg@nature.com

Figure 1

The ING2 PHD domain specifically binds to H3K4me3 in vitro.

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Figure 2

Methylated H3K4 recognition by the ING2 PHD domain enhances ING2-associated HDAC1 histone deacetylase activity in vitro.

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Figure 3

The ING2 interaction with trimethylated H3K4 occurs in vivo and requires an intact PHD domain.

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Figure 4

Recognition of H3K4me3 by ING2 PHD domain in vivo is critical for ING2 function.

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