Histone Acetyltransferases

Histone Acetyltransferases (HATs) are a family of enzymes that catalyze the acetylation of lysine residues on histone protein tails. This post-translational modification involves the transfer of an acetyl group from acetyl CoA to form ε-N-acetyl lysine.

Gene Data


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
Selective p300/CBP inhibitor
5646 EML 425
Reversible and non-competitive CBP/p300 inhibitor
4827 Garcinol
PCAF/p300 inhibitor; anticancer
Dual CBP/p300 and BRD4 bromodomain inhibitor
5045 L002
p300 inhibitor
5103 Lys-CoA
Selective p300 inhibitor
4903 NU 9056
Inhibitor of KAT5 (Tip60)
5964 SI-2 hydrochloride
Steroid receptor coactivator 3 (SRC-3) inhibitor


Cat No Product Name / Activity
4891 I-CBP 112
Selective CBP/p300 BRD inhibitor
4889 SGC-CBP30
Potent CBP/p300 BRD inhibitor

Histone Acetyltransferases (HATs) are a family of enzymes that catalyze the acetylation of lysine residues on histone protein tails. 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).

Acetylation of key lysine residues on histone proteins is an important epigenetic regulator of chromatin architecture, and therefore gene transcription. Histone acetylation levels have been associated with an open chromatin structure, yet specific marks - including acetylated histone H4 lysine 16 (H4K19) - have been linked to chromatin condensation. Since chromatin architecture directly regulates transcriptional activation, both histone acetylation and histone deacetylation have major influences on the control of cell fate. As a result, dysregulation of chromatin acetylation has been linked to the development of cancer and inflammation.

In addition to altering DNA accessibility, histone acetylation also facilitates the recruitment of bromodomain-containing proteins. Bromodomains are highly conserved protein interaction modules, found in many chromatin remodeling proteins, which recognize and bind to ε-N-acetyl lysine motifs. If histone acetyltransferases are the "writers" of acetylated lysine motifs, and histone deacetylases are the "erasers", bromodomains can be considered to be the "readers" of these epigenetic marks.

Literature for Histone Acetyltransferases

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

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


Cancer Research Product Guide

A collection of over 750 products for cancer research, the guide includes research tools for the study of:

  • Cancer Metabolism
  • Epigenetics in Cancer
  • Receptor Signaling
  • Cell Cycle and DNA Damage Repair
  • Angiogenesis
  • Invasion and Metastasis

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.


Epigenetics Research Bulletin

Produced by Tocris and updated in 2014, the epigenetics research bulletin gives an introduction into mechanisms of epigenetic regulation, and highlights key Tocris products for epigenetics targets including:

  • Bromodomains
  • DNA Methyltransferases
  • Histone Deacetylases
  • Histone Demethylases
  • Histone Methyltransferases

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