Histone Acetyltransferases

Histone Acetyltransferases (HATs; also known as Lysine Aceyltransferases or KATs) are domains found in a diverse range of enzymes, which catalyze the acetylation of lysine residues. This post-translational modification involves the transfer of an acetyl group from acetyl CoA to form ε-N-acetyl lysine. The reverse reaction is carried out by histone deacetylases (HDACs).

Literature (1)
Gene Data

Histone Acetyltransferase Inhibitors

Cat. No. Product Name / Activity
6387 A 485
Potent and selective p300/CBP inhibitor; orally bioavailable
3084 Anacardic acid
Noncompetitive PCAF/p300 inhibitor
4200 C 646
p300/CBP inhibitor
5646 EML 425
Reversible and non-competitive CBP/p300 inhibitor
7270 iP300w
Potent p300/CBP inhibitor
4903 NU 9056
Inhibitor of KAT5 (Tip60)
5964 SI-2 hydrochloride
Steroid receptor coactivator 3 (SRC-3) inhibitor
6692 WM 1119
High affinity KAT6A (MOZ) competitive inhibitor
7366 WM 3835
Lysine acetyltransferase HBO1 (KAT7) inhibitor
6693 WM 8014
Potent and selective KAT6A and KAT6B inhibitor


Cat. No. Product Name / Activity
7682 JQAD1
Potent and selective EP300 Degrader


Cat. No. Product Name / Activity
7584 iP300v
Negative control for iP300w (Cat. No. 7270)


Cat. No. Product Name / Activity
4889 SGC-CBP30
Potent CBP/p300 BRD inhibitor

Histone Acetyltransferases (HATs; also known as Lysine Aceyltransferases or KATs) are catalytic domains found in a diverse range of proteins; there are 37 endogenous mammalian proteins that are thought to have HAT activity. HAT domains can be found in proteins alongside other epigenetic domains, such as bromodomains, which recognize acetylated lysine residues. Proteins with HAT activity are found in multiprotein complexes, the components of which regulate HAT specificity and integration with other proteins, as well as enabling the detection of post-translational modifications.

HATs are grouped into families based on their amino acid sequence homology:

  • MYST family, including MOZ (also known as KAT6A or MYST3), Tip60 (KAT5), HBO1 (KAT7) and MOF (KAT8)
  • p300/CBP family, including CBP (CREB-binding protein; KAT3A) and p300 (KAT3B)
  • GNAT family, including GCN5 (KAT2A) and PCAF (KAT2B)

Function of HATs

The function of HATs is to catalyze the acetylation of lysine residues in proteins, by the transfer of an acetyl group from acetyl CoA to form ε-N-acetyl lysine. The reverse process, removal of acetylation marks, is catalyzed by histone deacetylases (HDACs; also known as lysine deacetylases or KDACs). Over 2000 actylation targets have been identified including proteins from most subcellular compartments and organelles. Acetylation of lysine residues can affect the cellular localization and catalytic activity of a protein, as well as its ability to interact with other proteins. This post-translation modification governs the ability of proteins to respond to intracellular and extracellular processes.

HATs act on gene regulatory elements of transcriptionally-active genes, such as promoter and enhancer regions, to modulate transcriptional output. For example, MOF and GNC5 localize to promoter regions of their targets, and their identification correlates with increased transcriptional activity. Similarly, p300 and CBP activate transcription via their recruitment by transcription factors, to enhancer and promoter regions. p53 recruits p300 and CBP to its target loci in response to DNA damage, where they mediate the acetylation of histone 3 lysine 18 (H3K18) and H3K27, stimulating RNA polymerase II to leave the promotor and activate transcriptional elongation.

Acetylation of Histones

A key function of HATs is the acetylation of lysine residues on histone protein tails, which is an important epigenetic regulator of chromatin architecture and gene transcription. Acetylation of histone lysine residues, such as H4K16ac, can disrupt interactions between neighbouring nucleosomes, and between histones and DNA. These changes create an environment that is more conducive to transcription. Some histone acetylation marks are also associated with increased release of RNA polymerase, while other acetylation marks affect the recruitment of bromodomain containing proteins.

External sources of pharmacological information for Histone Acetyltransferases :

    Literature for Histone Acetyltransferases

    Tocris offers the following scientific literature for Histone Acetyltransferases to showcase our products. We invite you to request* your copy today!

    *Please note that Tocris will only send literature to established scientific business / institute addresses.

    Epigenetics Scientific Review

    Epigenetics Scientific Review

    Written by Susanne Müller-Knapp and Peter J. Brown, this review gives an overview of the development of chemical probes for epigenetic targets, as well as the impact of these tool compounds being made available to the scientific community. In addition, their biological effects are also discussed. Epigenetic compounds available from Tocris are listed.

    Histone Acetyltransferase Gene Data

    Gene Species Gene Symbol Gene Accession No. Protein Accession No.
    Histone acetyltransferase 1 Human HAT1 NM_003642 O14929
    Mouse Hat1 NM_026115 Q8BY71
    Rat Hat1 NM_001009657 Q5M939
    K(lysine) acetyltransferase 2A Human KAT2A NM_021078 Q92830
    Mouse Kat2a NM_020004 Q9JHD2
    Rat Kat2a NM_001107050 D4ACX5
    K(lysine) acetyltransferase 2B Human KAT2B NM_003884 Q92831
    Mouse Kat2b NM_020005 Q9JHD1
    Rat - - -
    K(lysine) acetyltransferase 5 Human KAT5 NM_006388 Q92993
    Mouse Kat5 NM_178637 Q8CHK4
    Rat Kat5 NM_001005872 Q99MK2
    K(lysine) acetyltransferase 6A Human KAT6A NM_006766 Q92794
    Mouse Myst3 NM_001081149 G3X940
    Rat Kat6a NM_001100570 Q5TKR9
    K(lysine) acetyltransferase 6B Human KAT6B NM_012330 Q8WYB5
    Mouse Myst4 NM_017479 Q8BRB7
    Rat - - -
    K(lysine) acetyltransferase 7 Human KAT7 NM_007067 Q95251
    Mouse Myst2 NM_001195003 Q5SVQ0
    Rat Kat7 NM_181081 Q810T5
    K(lysine) acetyltransferase 8 Human KAT8 NM_032188 Q9H7Z6
    Mouse Kat8 NM_026370 Q9D1P2
    Rat Kat8 NM_001017378 Q5XI06
    Clock homolog (mouse) Human CLOCK NM_004898 O15516
    Mouse Clock NM_007715 O08785
    Rat Clock NM_021856 Q9WVS9
    CREB binding protein Human CREBBP NM_004380 Q92793
    Mouse Crebbp NM_001025432 P45481
    Rat Crebbp NM_133381 Q6JHU9
    E1A binding protein p300 Human EP300 NM_001429 Q09472
    Mouse Ep300 NM_001429 Q09472
    Rat Ep300 XM_576312 Q91XT0
    General transcription factor IIIC, polypeptide 4, 90kDa Human GTF3C4 NM_012204 Q9UKN8
    Mouse Gtf3c4 NM_001166033 Q8BMQ2
    Rat Gtf3c4 NM_001109473 D3ZD80
    Nuclear receptor coactivator 1 Human NCOA1 NM_147223 Q15788
    Mouse Ncoa1 NM_010881 P70365
    Rat Ncoa1 NM_001108012 D4ADD6
    Nuclear receptor coactivator 2 Human NCOA2 NM_006540 Q15596
    Mouse Ncoa2 NM_008678 Q61026
    Rat Ncoa2 NM_031822 Q9WUI9
    Nuclear receptor coactivator 3 Human NCOA3 NM_006534 Q9Y6Q9
    Mouse Ncoa3 NM_008679 Q05BA5
    Rat Ncoa3 XM_215947 Q5I0G5
    Retinoblastoma binding protein 7 Human RBBP7 NM_002893 Q16576
    Mouse Rbbp7 NM_009031 Q60973
    Rat Rbbp7 NM_031816 Q71UF4
    TAF1 RNA polymerase II, TAT box binding protein (TBP)-associated factor, 250kDa Human TAF1 NM_004606 P21675
    Mouse Taf1 NM_001081008 Q80UV9
    Rat Taf1 NM_001191723 D3ZM43