Search results for KAT2A

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Protein (1 results from a total of 1)

Identifier: R-HSA-3006516
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: KAT2A: Q92830

Reaction (4 results from a total of 4)

Identifier: R-NUL-4549228
Species: Homo sapiens, Xenopus laevis
Compartment: nucleoplasm
KAT2A (GCN5) and KAT2B (PCAF) are histone acetyltransferases (HATs) that act as part of large multimember complexes to facilitate transcription by acetylating histones H3 and H4. In eukaryotes the SPT-ADA-GCN5 acetyltransferase (SAGA) complex has 19 subunits including TRRAP, ENY2, USP22 and subunits belonging to the ADA, SPT, TAF, and SGF group of proteins (Nagy et al. 2009). The ADA2A-containing (ATAC) complex shares with SAGA a core composed of KAT2A-TADA3 (ADA3)-CCDC101 (STAF36, SGF29) and either TADA2A (ADA2a) in ATAC, or TADA2B (ADA2b) in SAGA. ATAC complexes contain a second putative HAT, called CSRP2BP (ATAC2), and five other subunits; YEATS2, ZZZ3, MBIP, WDR5, and DR1 (NC2-Beta) (Guelman et al. 2009). CSRP2BP has weak HAT activity in vitro but it's main function is to maintain the structural integrity of ATAC (Guelman et al. 2009). At present, the biological function of the ATAC complex is not well understood. In vitro GCN5 acetylates mainly histone H3K14 (lysine-15 in the UniProt peptide which retains the initiating methionine), but when incorporated into the SAGA complex GCN5 becomes more efficient as an H3K14 acetylase and can also acetylate H3K9 and H3K18 (Brand et al. 1999, Grant et al. 1999), H3K23, and H3K27 (Kuo et al. 1996, Kuo & Andrews 2013). Drosophila ATAC mainly acetylates histone H4 (Ciurciu et al. 2006, Suganuma et al. 2008), suggested to be due to the presence of CSRP2BP in the complex (Suganuma et al. 2008) but different human ATAC preparations have exhibited a range of specificities with no clear difference between SAGA and ATAC (Guelman et al. 2009, Wang et al. 2008, Nagy et al. 2010). SAGA and ATAC complexes from mouse and human contain either GCN5 or PCAF in a mutually exclusive manner (Nagy et al. 2010, Krebs et al. 2010, Spedale et al. 2012).

The SAGA complex consists of KAT2A (hGCN5), TADA1 (STAF42), TADA2B (ADA2b), TADA3 (STAF54, ADA3), SUPT3H (SPT3), SUPT7L (STAF65G), TAF5L (PAF65B), TAF6L (PAF65A), TAF9 (TAFII31), TAF12 (TAFII20), TAF10 (TAFII31), TRRAP, SAP130 (Martinez et al. 2001), CCDC101, ATXN7, a factor termed STAF55 that cannot be identified, two further factors described as probable members that cannot be identified STAF46 and STAF60 (Nagy & Tora 2007) plus ATXN7L3, USP22, ENY2 (Zhao et al. 2008) and SUPT20H (Nagy et al. 2009).
Identifier: R-HSA-5250938
Species: Homo sapiens
Compartment: nucleoplasm
Histone acetyltransferases recruited by the B‑WICH complex acetylate histone H3 at lysine‑9. Knockdown of the BAZ1B (WSTF) and MYOIC components of B‑WICH cause a loss of histone acetyltransferases KAT2B (PCAF), KAT2A (GCN5), and EP300 (p300) and a reduction of acetylated histone H3. Knockdown of KAT2B (PCAF) causes a reduction in acetylation of histone H3 at lysine‑9, leading to reduced rRNA synthesis levels (Sarshad et al. 2013, Shen et al. 2013).
Identifier: R-HSA-5250930
Species: Homo sapiens
Compartment: nucleoplasm
Direct interactions between BAZ1B (WSTF) and histone acetyltransferases KAT2B, KAT2A, and EP300 are weak (Vintermist et al. 2011) so the acetyltransferases may interact with other subunits of B‑WICH or with proteins not in the B‑WICH complex. The ERCC6 (CSB) component of B‑WICH and MYOIC interact with KAT2B (PCAF) (Sarshad et al. 2013, Shen et al. 2013). The histone acetyltransferases are believed to acetylate histone H3 at lysine‑9 in rDNA since this modification is reduced in WSTF and MYOIC knockdown cells (Vintermist et al. 2011, Sarshad et al. 2013). Knockdown of KAT2B causes loss of acetylation on histone H4 and on histone H3 at lysine‑9 (Shen et al. 2013).
Identifier: R-HSA-3301237
Species: Homo sapiens
Compartment: nucleoplasm
KAT2A (GCN5) and KAT2B (PCAF) are histone acetyltransferases (HATs) that act as part of large multimember complexes to facilitate transcription by acetylating histones H3 and H4. In eukaryotes the SPT-ADA-GCN5 acetyltransferase (SAGA) complex has 19 subunits including TRRAP, ENY2, USP22 and subunits belonging to the ADA, SPT, TAF, and SGF group of proteins (Nagy et al. 2009). The ADA2A-containing (ATAC) complex shares with SAGA a core composed of KAT2A-TADA3 (ADA3)-CCDC101 (STAF36, SGF29) and either TADA2A (ADA2a) in ATAC, or TADA2B (ADA2b) in SAGA. ATAC complexes contain a second putative HAT, called CSRP2BP (ATAC2), and five other subunits; YEATS2, ZZZ3, MBIP, WDR5, and DR1 (NC2-Beta) (Guelman et al. 2009). CSRP2BP has weak HAT activity in vitro but it's main function is to maintain the structural integrity of ATAC (Guelman et al. 2009). At present, the biological function of the ATAC complex is not well understood. In vitro GCN5 acetylates mainly histone H3K14 (lysine-15 in the UniProt peptide which retains the initiating methionine), but when incorporated into the SAGA complex GCN5 becomes more efficient as an H3K14 acetylase and can also acetylate H3K9 and H3K18 (Brand et al. 1999, Grant et al. 1999), H3K23, and H3K27 (Kuo et al. 1996, Kuo & Andrews 2013). Drosophila ATAC mainly acetylates histone H4 (Ciurciu et al. 2006, Suganuma et al. 2008), suggested to be due to the presence of CSRP2BP in the complex (Suganuma et al. 2008) but different human ATAC preparations have exhibited a range of specificities with no clear difference between SAGA and ATAC (Guelman et al. 2009, Wang et al. 2008, Nagy et al. 2010). SAGA and ATAC complexes from mouse and human contain either GCN5 or PCAF in a mutually exclusive manner (Nagy et al. 2010, Krebs et al. 2010, Spedale et al. 2012).

The SAGA complex consists of KAT2A (hGCN5), TADA1 (STAF42), TADA2B (ADA2b), TADA3 (STAF54, ADA3), SUPT3H (SPT3), SUPT7L (STAF65G), TAF5L (PAF65B), TAF6L (PAF65A), TAF9 (TAFII31), TAF12 (TAFII20), TAF10 (TAFII31), TRRAP, SAP130 (Martinez et al. 2001), CCDC101, ATXN7, a factor termed STAF55 that cannot be identified, two further factors described as probable members that cannot be identified STAF46 and STAF60 (Nagy & Tora 2007) plus ATXN7L3, USP22, ENY2 (Zhao et al. 2008) and SUPT20H (Nagy et al. 2009).

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.

Set (2 results from a total of 2)

Identifier: R-HSA-3662319
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-3322934
Species: Homo sapiens
Compartment: nucleoplasm

Icon (1 results from a total of 1)

Species: Homo sapiens
Curator: Bruce May
Designer: Cristoffer Sevilla
KAT2A,B icon
Set of Histone acetyltransferase KAT2A and KAT2B
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