The domain within your query sequence starts at position 5 and ends at position 107; the E-value for the ING domain shown below is 5.5e-35.



PFAM accession number:PF12998
Interpro abstract (IPR024610):

Histones undergo numerous post-translational modifications, including acetylation and methylation, at residues which are then probable docking sites for various chromatin remodelling complexes. Inhibitor of growth proteins (INGs) specifically bind to residues that have been thus modified. INGs carry a well-characterised C-terminal PHD-type zinc-finger domain, binding with lysine 4-tri-methylated histone H3 (H3K4me3), as well as this N-terminal domain that binds unmodified H3 tails. Although these two regions can bind histones independently, together they increase the apparent association of the ING for the H3 tail.

This entry represents the N-terminal histone binding domain found in inhibitor proteins.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry ING