4qyl

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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=4qyl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qyl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qyl RCSB], [http://www.ebi.ac.uk/pdbsum/4qyl 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=4qyl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qyl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qyl RCSB], [http://www.ebi.ac.uk/pdbsum/4qyl PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/BRPF1_HUMAN BRPF1_HUMAN]] Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. Positively regulates the transcription of RUNX1 and RUNX2.<ref>PMID:16387653</ref> <ref>PMID:18794358</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 14:14, 25 December 2014

Crystal Structure of the human BRPF1 bromodomain in complex with a histone H2AK5ac peptide

4qyl, resolution 1.80Å

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