 INGInhibitor of growth proteins N-terminal histone-binding | |
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| SMART ACC: | SM001408 |
| Description: | 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. |
| InterPro ACC: | IPR024610 |
| InterPro abstract: | 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 … expand |
| Family alignment: | View the Family alignment or the Alignment consensus sequence |
| There are 0 ING domains in 0 proteins in SMART's NRDB database. | |
Predicted cellular role
| Cellular role: | Signalling |
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Relevant references for this domain
Primary literature for the ING domain is listed below.
KEGG pathways involving proteins which contain this domain
This information is based on the mapping of SMART genomic protein database to KEGG orthologous groups. Percentages are related to the number of proteins containing a ING domain which could be assigned to a KEGG orthologous group, and not all proteins containing ING domains. Please note that proteins can be included in multiple pathways, ie. the numbers below will not add to 100%.