3qah

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qah OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qah RCSB], [http://www.ebi.ac.uk/pdbsum/3qah PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qah OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qah RCSB], [http://www.ebi.ac.uk/pdbsum/3qah PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/KAT8_HUMAN KAT8_HUMAN]] Histone acetyltransferase which may be involved in transcriptional activation. May influence the function of ATM. As part of the MSL complex it is involved in acetylation of nucleosomal histone H4 producing specifically H4K16ac. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. That activity is less specific than the one of the MSL complex.<ref>PMID:12397079</ref> <ref>PMID:15923642</ref> <ref>PMID:20018852</ref>
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== References ==
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<references/>
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</StructureSection>
</StructureSection>

Revision as of 09:01, 25 December 2014

Crystal structure of apo-form human MOF catalytic domain

3qah, resolution 2.10Å

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