Search results for KAT8

Showing 8 results out of 8

×

Species

Types

Compartments

Search properties

Species

Types

Compartments

Search properties

Protein (4 results from a total of 4)

Identifier: R-HSA-3321802
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: KAT8: Q9H7Z6
Identifier: R-HSA-3321875
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: KANSL1: Q7Z3B3
Identifier: R-HSA-3321796
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: KANSL2: Q9H9L4
Identifier: R-HSA-3321882
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: KANSL3: Q9P2N6

Reaction (3 results from a total of 3)

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).

Pathway (1 results from a total of 1)

Identifier: R-HSA-6804758
Species: Homo sapiens
Transcriptional activity of TP53 is positively regulated by acetylation of several of its lysine residues. BRD7 binds TP53 and promotes acetylation of TP53 lysine residue K382 by acetyltransferase EP300 (p300). Acetylation of K382 enhances TP53 binding to target promoters, including CDKN1A (p21), MDM2, SERPINE1, TIGAR, TNFRSF10C and NDRG1 (Bensaad et al. 2010, Burrows et al. 2010. Drost et al. 2010). The histone acetyltransferase KAT6A, in the presence of PML, also acetylates TP53 at K382, and, in addition, acetylates K120 of TP53. KAT6A-mediated acetylation increases transcriptional activation of CDKN1A by TP53 (Rokudai et al. 2013). Acetylation of K382 can be reversed by the action of the NuRD complex, containing the TP53-binding MTA2 subunit, resulting in inhibition of TP53 transcriptional activity (Luo et al. 2000). Acetylation of lysine K120 in the DNA binding domain of TP53 by the MYST family acetyltransferases KAT8 (hMOF) and KAT5 (TIP60) can modulate the decision between cell cycle arrest and apoptosis (Sykes et al. 2006, Tang et al. 2006). Studies with acetylation-defective knock-in mutant mice indicate that lysine acetylation in the p53 DNA binding domain acts in part by uncoupling transactivation and transrepression of gene targets, while retaining ability to modulate energy metabolism and production of reactive oxygen species (ROS) and influencing ferroptosis (Li et al. 2012, Jiang et al. 2015).
Cite Us!