Search results for KAT8

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Identifier: R-HSA-9828175
Species: Homo sapiens
Compartment: nucleoplasm
WDR5 is a subunit of an evolutionarily conserved lysine acetyltransferase Non-Specific-Lethal (NSL) complex together with the following proteins: KAT8 (also known as MOF) as the catalytic subunit, KANSL1-3 (also known as NSL1-3), MCRS1, HCFC1 (also known as Host cell factor 1 or HCF1), and one of the paralogous proteins: PHF20 or PHF20-like 1 (PHF20L1) (Smith et al, 2005; Cai et al, 2010; Van et al 2022). The NSL complex is responsible for the acetylation of lysine K5, K8, K12, and K16 of histone H4 (Smith et al, 2005; Cai et al, 2010; Zhao et al, 2013; Radzisheuskaya et al., 2021). The NSL complex binds to the promoters of house-keeping genes and regulates their expression (Radzisheuskaya et al., 2021), therefore in some contexts, it is essential for the viability and proliferation of human cells (Klein et al, 2016; Radzisheuskaya et al., 2021).
Identifier: R-HSA-3321805
Species: Homo sapiens
Compartment: nucleoplasm
KAT8 (MOF, MYST1) is a member of the MYST (Moz-Ybf2/Sas3-Sas2-Tip60) family of histone acetyltransferases (HATs). KAT8 is the catalytic component of the nine-subunit non-specific lethal (NSL) complex (Mendjan et al. 2006, Cai et al. 2010).

NSL acetylates histone H4 on lysines 17 (H4K16), 6 (H4K5) and 9 (H4K8) (Cai et al. 2010).

KAT8 is also the catalytic subunit of the male-specific lethal (MSL) complex, which acetylates almost exclusively H4K16 and is responsible for a large fraction of H4K16 acetylation in human cells (Smith et al. 2005).

N.B. Coordinates of post-translational modifications described here follow UniProt standard practice whereby coordinates refer to the translated protein before any further processing. Histone literature typically refers to coordinates of the protein after the initiating methionine has been removed. Therefore the coordinates of post-translated residues in the Reactome database and described here are frequently +1 when compared with the literature.
Identifier: R-HSA-3321883
Species: Homo sapiens
Compartment: nucleoplasm
The MSL complex has histone acetyltransferase (HAT) activity with a high specificity for histone H4 lysine-17 (H4K16) (Smith et al. 2000, 2005, Conrad et al. 2012). The subunit responsible for this activity is KAT8 (Males Absent on the First, MOF) a member of the MYST (named for yeast and human members MOZ, YBF2, SAS2, and Tip60) HAT family. In Drosophilla, the MSL complex associates at hundreds of sites along the X chromosome in somatic cells, resulting in the hyperacetylation of H4K16 (Lavender et al. 1994, Smith et al. 2000). In humans MSL is responsible for the majority of H4 acetylation at lysine-17 in the cell. KAT8 is a component of other complexes (Smith et al. 2005, Mendjan et al. 2006, Cai et al. 2010).
Identifier: R-HSA-3318413
Species: Homo sapiens
Compartment: nucleoplasm
The Inhibitor of Growth (ING) family are growth regulators, present in all eukaryotes, with five human proteins ING1 to ING5. ING genes are mutated or downregulated in many forms of cancer. They have roles in chromatin modification and remodeling, gene-specific transcription regulation, and DNA repair, recombination, and replication (Saksouk et al. 2008, Awakumovv et al. 2012).

Human INGs can be divided into three groups: ING1/2, ING3, and ING4/5, based on their association with three distinct types of protein complexes (Doyon et al. 2006). All regulate chromatin via histone acetylation and deacetylation. The catalytic histone acetyltransferase (HAT) subunits of ING complexes are members of the MYST family, KAT5 (Tip60), KAT7 (HBO1) KAT6A (MOZ), KAT6B (MORF), and KAT8 (MOF). ING4 exists in vivo as a dimer, binding two lysine-4 trimethylated histone H3 (H3K4me3) modifications (Palacios et al. 2010). Homology modeling suggests that other INGs are likely to be dimers (Culurgioni et al. 2012).

KAT7-ING4/5 complexes interact with lysine-4 trimethylated histone H3 (H3K4me3), acetylating surrounding histone tails to stimulate local transcription (Palacios et al. 2008, Champagne et al. 2008, Hung et al. 2009, Saksouk et al. 2009).
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