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Histone H3 acetylated at Lysine 56 are assembled into chromatin in human cells, forming foci that colocalise with sites of DNA repair. Acetylation of H3K56 is increased in multiple types of cancer, correlating with increased levels of the histone chaperone ASF1A, in these tumours. ASF1A is required for the acetylation and CAF-1 is required for the incorporation of acetylated H3 into the nucleosome (PMID: 19270680). H3K56ac levels in human cells are differentially regulated at telomeres and globally in response to cell cycle arrest (PMID: 19625767). During DNA damage, H3K56 acetylation levels increased, and this acetylated H3K56 is also localised at the DNA repair sites. It also colocalised with other proteins involved in DNA damage signalling pathways such as phospho-ATM, Chk2, and p53 demonstrating its involvement in DNA damage repair (PMID: 20587414 ).

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H3K56ac infosheet
Modified variants Histone H3.1, Histone H3.2, Histone H3.3
Writer/s CREB-binding protein, Histone acetyltransferase p300
Eraser/s Histone deacetylase 1, NAD-dependent deacetylase sirtuin-2, NAD-dependent deacetylase sirtuin-3, mitochondrial, NAD-dependent deacetylase sirtuin-6
Disease associationsNo disease associations known for H3K56ac

Sites of lysine acetylation H1K25ac, H2AK5ac, H2AK9ac, H2BK120ac, H2BK12ac, H2BK15ac, H2BK16ac, H2BK20ac, H2BK46ac, H2BK5ac, H3K14ac, H3K18ac, H3K23ac, H3K27ac, H3K36ac, H3K4ac, H3K56ac, H3K9ac, H4K12ac, H4K16ac, H4K5ac, H4K8ac, H4K91ac