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Literature summary for 2.3.1.48 extracted from
- Lysine acetyltransferase inhibitors structure-activity relationships and potential therapeutic implications (2018), Future Med. Chem., 10, 1067-1091 .
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| Asf1 | - |
Saccharomyces cerevisiae | |
| LoCAM | i.e. SPV106, 137% activation at 0.05 mM | Homo sapiens |  |
| additional information | Rtt109 has a low catalytic efficiency in isolation, but it is much more active when associated with the histone chaperones Asf1 and Vps75. The two chaperones also determine substrate specificity, with the preferred substrate being H3K56 when Rtt109 is associated with Asf1, whereas H3K9 and H3K23 are acetylated when in complex with Vps75 | Saccharomyces cerevisiae | |
| VPS75 | - |
Saccharomyces cerevisiae |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| (2E)-2-(ethoxycarbonyl)heptadec-2-enoic acid | - |
Homo sapiens | |
| (2E)-2-(ethoxycarbonyl)hexadec-2-enoic acid | - |
Homo sapiens | |
| 2-[2-(4-heptylphenyl)ethyl]-6-hydroxybenzoic acid | - |
Homo sapiens | |
| 4-amino-1-naphthol | 4A1N | Homo sapiens | |
| A-485 | - |
Homo sapiens | |
| anacardic acid | - |
Drosophila melanogaster | |
| anacardic acid | - |
Homo sapiens | |
| BF1 | - |
Homo sapiens | |
| C646 | - |
Homo sapiens | |
| CPTH2 | - |
Homo sapiens | |
| CPTH6 | 27% inhibition at 0.1 mM; 40% inhibition at 0.8 mM; 40% inhibition at 0.8 mM | Homo sapiens | |
| CtpB | - |
Homo sapiens | |
| curcumin | - |
Homo sapiens | |
| diethyl pentadecylidenepropanedioate | i.e. SPV106, a long-chain alkylidenemalonate (LoCAM), 74% inhibition at 0.05 mM | Homo sapiens | |
| embelin | - |
Homo sapiens | |
| EML425 | - |
Homo sapiens | |
| epigallocatechin-3-gallate | EGCG; EGCG; EGCG | Homo sapiens | |
| ethyl (2E)-2-acetylheptadec-2-enoate | - |
Homo sapiens | |
| ethyl (2E)-2-acetylhexadec-2-enoate | - |
Homo sapiens | |
| ethyl 2-methyl-6-([5-[(prop-2-yn-1-yl)amino]pentyl]oxy)quinoline-3-carboxylate | - |
Homo sapiens | |
| garcinol | - |
Homo sapiens | |
| isogarcinol | - |
Homo sapiens | |
| L002 | i.e. NSC764414 | Homo sapiens | |
| LTK-14 | - |
Homo sapiens | |
| Lys-CoA | - |
Homo sapiens | |
| MB-3 | an alpha-methylene-gamma-butyrolactone, shows reversible, noncovalent mode of inhibition; an alpha-methylene-gamma-butyrolactone, shows reversible, noncovalent mode of inhibition | Homo sapiens | |
| MC1626 | - |
Homo sapiens | |
| MC1752 | - |
Homo sapiens | |
| MC1823 | - |
Homo sapiens | |
| additional information | analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview | Drosophila melanogaster | |
| additional information | analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141 | Homo sapiens | |
| additional information | analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview | Saccharomyces cerevisiae | |
| N-[5-[(5-[[5-([4-[(5-[[5-([5-[(5-[[3-(dimethylamino)propyl]carbamoyl]-1-methyl-1H-pyrrol-3-yl)carbamoyl]-1-methyl-1H-pyrrol-3-yl]carbamoyl)-1-methyl-1H-pyrrol-3-yl]carbamoyl]-1-methyl-1H-pyrrol-3-yl)amino]-4-oxobutyl]carbamoyl)-1-methyl-1H-pyrrol-3-yl]carbamoyl]-1-methyl-1H-pyrrol-3-yl)carbamoyl]-1-methyl-1H-pyrrol-3-yl]-4-[(N-[[2-(2-[4-[(4Z)-4-[[5-(2,3-dimethyl-6-nitrophenyl)furan-2-yl]methylidene]-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl]benzamido]ethoxy)ethoxy]acetyl]-beta-alanyl)amino]-1-methyl-1H-pyrrole-2-carboxamide | - |
Homo sapiens | |
| NK13650A | - |
Homo sapiens | |
| NK13650B | - |
Homo sapiens | |
| NU9056 | - |
Homo sapiens | |
| peptide conjugate Boc-C5-CoA | peptide Boc-C5-CoA, the molecule exploits an additional electron-rich pocket (P2) about 10 A away from the lysine binding pocket (P1). Boc-C5-CoA that shows high affinity for, comprises a CoA moiety which binds to the P1 pocket, a 1,5-pentanediamine linker and a tert-butoxycarbonyl cap, which is accommodated by the P2 pocket. CoA is connected to the N1 of the linker through a carboxymethylene bridge, while the tert-butoxycarbonyl cap protects the N5 | Homo sapiens | |
| peptide conjugate H3-CoA-20 | peptide H3-CoA-20 resembles the K14-containing sequence of histone H3, the main substrate of PCAF, R1 is A-P-R-K-Q-L-OH and R2 is G-G-T-S-L-R-A-T-Q-K-T-R-A-NHCH3 | Homo sapiens | |
| peptide conjugate H4-K16-CoA | peptide H4-K16-CoA, R1 is K-A-G-G-K-G-L-G-K-G-G-K-G-R-G-S-OCH3 and R2 is R-H-R-K-NH2; peptide H4-K16-CoA, R1 is K-A-G-G-K-G-L-G-K-G-G-K-G-R-G-S-OCH3 and R2 is R-H-R-K-NH2 | Homo sapiens | |
| phenylpyrazolocurcumin CTK7A | - |
Homo sapiens | |
| Plumbagin | - |
Homo sapiens | |
| PU139 | - |
Homo sapiens | |
| Spd(N1)-CoA | obtained by linking the polyamine spermidine to CoA using a carboxymethylene bridge | Homo sapiens | |
| TH1834 | 60% inhibition at 0.5 mM | Homo sapiens | |
| TTK21 | - |
Homo sapiens | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| nucleus | - |
Homo sapiens | 5634 | - |
| nucleus | - |
Saccharomyces cerevisiae | 5634 | - |
| nucleus | - |
Drosophila melanogaster | 5634 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetyl-CoA + [ATM]-L-lysine | Homo sapiens | - |
CoA + [ATM]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [ATM]-L-lysine | Drosophila melanogaster | - |
CoA + [ATM]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [beta-catenin]-L-lysine | Homo sapiens | - |
CoA + [beta-catenin]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [c-myc]-L-lysine | Homo sapiens | - |
CoA + [c-myc]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [c-myc]-L-lysine | Drosophila melanogaster | - |
CoA + [c-myc]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [CDC6]-L-lysine | Homo sapiens | - |
CoA + [CDC6]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [connexin 43]-L-lysine | Homo sapiens | - |
CoA + [connexin 43]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [DNMT1]-L-lysine | Homo sapiens | - |
CoA + [DNMT1]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [DNMT1]-L-lysine | Drosophila melanogaster | - |
CoA + [DNMT1]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [E2F1]-L-lysine | Homo sapiens | - |
CoA + [E2F1]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [E2F1]-L-lysine | Drosophila melanogaster | - |
CoA + [E2F1]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [Foxo1]-L-lysine | Homo sapiens | - |
CoA + [Foxo1]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [histone H2A]-L-lysine5 | Homo sapiens | - |
CoA + [histone H2A]-N6-acetyl-L-lysine5 | - |
? | |
| acetyl-CoA + [histone H2B]-L-lysine | Homo sapiens | - |
CoA + [histone H2B]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [histone H2B]-L-lysine12 | Homo sapiens | - |
CoA + [histone H2B]-N6-acetyl-L-lysine12 | - |
? | |
| acetyl-CoA + [histone H2B]-L-lysine15 | Homo sapiens | - |
CoA + [histone H2B]-N6-acetyl-L-lysine15 | - |
? | |
| acetyl-CoA + [histone H3]-L-lysine | Homo sapiens | - |
CoA + [histone H3]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [histone H3]-L-lysine | Saccharomyces cerevisiae | - |
CoA + [histone H3]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [histone H3]-L-lysine | Drosophila melanogaster | - |
CoA + [histone H3]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [histone H3]-L-lysine | Saccharomyces cerevisiae ATCC 204508 | - |
CoA + [histone H3]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [histone H3]-L-lysine14 | Homo sapiens | - |
CoA + [histone H3]-N6-acetyl-L-lysine14 | - |
? | |
| acetyl-CoA + [histone H3]-L-lysine14 | Saccharomyces cerevisiae | - |
CoA + [histone H3]-N6-acetyl-L-lysine14 | - |
? | |
| acetyl-CoA + [histone H3]-L-lysine14 | Saccharomyces cerevisiae ATCC 204508 | - |
CoA + [histone H3]-N6-acetyl-L-lysine14 | - |
? | |
| acetyl-CoA + [histone H3]-L-lysine18 | Homo sapiens | - |
CoA + [histone H3]-N6-acetyl-L-lysine18 | - |
? | |
| acetyl-CoA + [histone H3]-L-lysine23 | Saccharomyces cerevisiae | - |
CoA + [histone H3]-N6-acetyl-L-lysine23 | - |
? | |
| acetyl-CoA + [histone H3]-L-lysine23 | Saccharomyces cerevisiae ATCC 204508 | - |
CoA + [histone H3]-N6-acetyl-L-lysine23 | - |
? | |
| acetyl-CoA + [histone H3]-L-lysine56 | Saccharomyces cerevisiae | - |
CoA + [histone H3]-N6-acetyl-L-lysine56 | - |
? | |
| acetyl-CoA + [histone H3]-L-lysine56 | Saccharomyces cerevisiae ATCC 204508 | - |
CoA + [histone H3]-N6-acetyl-L-lysine56 | - |
? | |
| acetyl-CoA + [histone H3]-L-lysine9 | Homo sapiens | - |
CoA + [histone H3]-N6-acetyl-L-lysine9 | - |
? | |
| acetyl-CoA + [histone H3]-L-lysine9 | Saccharomyces cerevisiae | - |
CoA + [histone H3]-N6-acetyl-L-lysine9 | - |
? | |
| acetyl-CoA + [histone H3]-L-lysine9 | Saccharomyces cerevisiae ATCC 204508 | - |
CoA + [histone H3]-N6-acetyl-L-lysine9 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine | Saccharomyces cerevisiae | - |
CoA + [histone H4]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine | Homo sapiens | - |
CoA + [histone H4]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine | Drosophila melanogaster | - |
CoA + [histone H4]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine | Saccharomyces cerevisiae ATCC 204508 | - |
CoA + [histone H4]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine12 | Homo sapiens | - |
CoA + [histone H4]-N6-acetyl-L-lysine12 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine12 | Saccharomyces cerevisiae | - |
CoA + [histone H4]-N6-acetyl-L-lysine12 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine12 | Drosophila melanogaster | - |
CoA + [histone H4]-N6-acetyl-L-lysine12 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine12 | Saccharomyces cerevisiae ATCC 204508 | - |
CoA + [histone H4]-N6-acetyl-L-lysine12 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine16 | Homo sapiens | - |
CoA + [histone H4]-N6-acetyl-L-lysine16 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine16 | Drosophila melanogaster | - |
CoA + [histone H4]-N6-acetyl-L-lysine16 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine16 | Homo sapiens | main substrate | CoA + [histone H4]-N6-acetyl-L-lysine16 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine16 | Drosophila melanogaster | main substrate | CoA + [histone H4]-N6-acetyl-L-lysine16 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine5 | Homo sapiens | - |
CoA + [histone H4]-N6-acetyl-L-lysine5 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine5 | Saccharomyces cerevisiae | - |
CoA + [histone H4]-N6-acetyl-L-lysine5 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine5 | Drosophila melanogaster | - |
CoA + [histone H4]-N6-acetyl-L-lysine5 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine5 | Saccharomyces cerevisiae ATCC 204508 | - |
CoA + [histone H4]-N6-acetyl-L-lysine5 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine8 | Homo sapiens | - |
CoA + [histone H4]-N6-acetyl-L-lysine8 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine8 | Saccharomyces cerevisiae | - |
CoA + [histone H4]-N6-acetyl-L-lysine8 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine8 | Drosophila melanogaster | - |
CoA + [histone H4]-N6-acetyl-L-lysine8 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine8 | Saccharomyces cerevisiae ATCC 204508 | - |
CoA + [histone H4]-N6-acetyl-L-lysine8 | - |
? | |
| acetyl-CoA + [NFkappaB]-L-lysine | Homo sapiens | - |
CoA + [NFkappaB]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [p27]-L-lysine | Homo sapiens | - |
CoA + [p27]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [p53]-L-lysine | Homo sapiens | - |
CoA + [p53]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [p53]-L-lysine | Drosophila melanogaster | - |
CoA + [p53]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [p53]-L-lysine120 | Homo sapiens | - |
CoA + [p53]-N6-acetyl-L-lysine120 | - |
? | |
| acetyl-CoA + [p53]-L-lysine120 | Drosophila melanogaster | - |
CoA + [p53]-N6-acetyl-L-lysine120 | - |
? | |
| acetyl-CoA + [PGC-1alpha]-L-lysine | Homo sapiens | - |
CoA + [PGC-1alpha]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [PGC-1]-L-lysine | Homo sapiens | - |
CoA + [PGC-1]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [PTEN]-L-lysine | Homo sapiens | acetylation of the oncosuppressor protein PTEN on two lysine residues (Lys125 and Lys128) | CoA + [PTEN]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [STAT3]-L-lysine | Homo sapiens | - |
CoA + [STAT3]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [TIP5]-L-lysine | Homo sapiens | - |
CoA + [TIP5]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [TIP5]-L-lysine | Drosophila melanogaster | - |
CoA + [TIP5]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [TRRAP]-L-lysine | Homo sapiens | - |
CoA + [TRRAP]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [TRRAP]-L-lysine | Drosophila melanogaster | - |
CoA + [TRRAP]-N6-acetyl-L-lysine | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Drosophila melanogaster | O02193 | - |
- |
| Drosophila melanogaster | P51123 | - |
- |
| Drosophila melanogaster | Q960X4 | - |
- |
| Homo sapiens | O15516 | - |
- |
| Homo sapiens | O95251 | - |
- |
| Homo sapiens | P21675 | - |
- |
| Homo sapiens | Q15788 | - |
- |
| Homo sapiens | Q8WYB5 | - |
- |
| Homo sapiens | Q92793 | - |
- |
| Homo sapiens | Q92794 | - |
- |
| Homo sapiens | Q92830 | - |
- |
| Homo sapiens | Q92831 | - |
- |
| Homo sapiens | Q92993 | - |
- |
| Homo sapiens | Q9BQG0 | - |
- |
| Homo sapiens | Q9H7Z6 | - |
- |
| Homo sapiens | Q9H9T3 | - |
- |
| Homo sapiens | Q9UKN8 | - |
- |
| Homo sapiens | Q9Y6Q9 | - |
- |
| Saccharomyces cerevisiae | P39979 | - |
- |
| Saccharomyces cerevisiae | P46677 | - |
- |
| Saccharomyces cerevisiae | P53114 | - |
- |
| Saccharomyces cerevisiae | Q06592 | - |
- |
| Saccharomyces cerevisiae | Q07794 | - |
- |
| Saccharomyces cerevisiae ATCC 204508 | P39979 | - |
- |
| Saccharomyces cerevisiae ATCC 204508 | P46677 | - |
- |
| Saccharomyces cerevisiae ATCC 204508 | P53114 | - |
- |
| Saccharomyces cerevisiae ATCC 204508 | Q06592 | - |
- |
| Saccharomyces cerevisiae ATCC 204508 | Q07794 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| acetylation | MYST enzymes have their acetylase activity regulated by autoacetylation. Autoacetylation is an important process in modulating the activity of MYST family members | Homo sapiens |
| acetylation | MYST enzymes have their acetylase activity regulated by autoacetylation. Autoacetylation is an important process in modulating the activity of MYST family members | Drosophila melanogaster |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| breast cancer cell | - |
Homo sapiens | - |
| colonic cancer cell | - |
Homo sapiens | - |
| colorectal cancer cell | - |
Homo sapiens | - |
| esophageal squamous cell carcinoma cell | - |
Homo sapiens | - |
| gastric cancer cell | - |
Homo sapiens | - |
| glioma cell | - |
Homo sapiens | - |
| hepatoma cell | - |
Homo sapiens | - |
| lung cancer cell | - |
Homo sapiens | - |
| medulloblastoma cell | - |
Homo sapiens | - |
| additional information | enzyme MOF/MYST1 is downregulated in ovarian, medulloblastoma, breast, colorectal and gastric carcinomas. Upregulated in NSCLC and oral tongue squamous cell carcinoma where it is associated with tumor growth | Homo sapiens | - |
| additional information | GCN5 is upregulated in non-small cell lung carcinoma cells, colon cancer, and glioma | Homo sapiens | - |
| additional information | KAT2B is underexpressed in hepatocellular carcinoma, esophageal squamous cell carcinoma, and ovarian and gastric cancer | Homo sapiens | - |
| additional information | MYST2/HBO1 is overexpressed in different types of cancer | Homo sapiens | - |
| additional information | Tip60 is downregulated in breast cancer | Homo sapiens | - |
| non-small cell lung cancer cell | - |
Homo sapiens | - |
| oral tongue squamous cell carcinoma cell | - |
Homo sapiens | - |
| ovary cancer cell | - |
Homo sapiens | - |
| U-937 cell | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetyl-CoA + [ATM]-L-lysine | - |
Homo sapiens | CoA + [ATM]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [ATM]-L-lysine | - |
Drosophila melanogaster | CoA + [ATM]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [beta-catenin]-L-lysine | - |
Homo sapiens | CoA + [beta-catenin]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [c-myc]-L-lysine | - |
Homo sapiens | CoA + [c-myc]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [c-myc]-L-lysine | - |
Drosophila melanogaster | CoA + [c-myc]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [CDC6]-L-lysine | - |
Homo sapiens | CoA + [CDC6]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [connexin 43]-L-lysine | - |
Homo sapiens | CoA + [connexin 43]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [DNMT1]-L-lysine | - |
Homo sapiens | CoA + [DNMT1]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [DNMT1]-L-lysine | - |
Drosophila melanogaster | CoA + [DNMT1]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [E2F1]-L-lysine | - |
Homo sapiens | CoA + [E2F1]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [E2F1]-L-lysine | - |
Drosophila melanogaster | CoA + [E2F1]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [Foxo1]-L-lysine | - |
Homo sapiens | CoA + [Foxo1]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [histone H2A]-L-lysine5 | - |
Homo sapiens | CoA + [histone H2A]-N6-acetyl-L-lysine5 | - |
? | |
| acetyl-CoA + [histone H2B]-L-lysine | - |
Homo sapiens | CoA + [histone H2B]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [histone H2B]-L-lysine12 | - |
Homo sapiens | CoA + [histone H2B]-N6-acetyl-L-lysine12 | - |
? | |
| acetyl-CoA + [histone H2B]-L-lysine15 | - |
Homo sapiens | CoA + [histone H2B]-N6-acetyl-L-lysine15 | - |
? | |
| acetyl-CoA + [histone H3]-L-lysine | - |
Homo sapiens | CoA + [histone H3]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [histone H3]-L-lysine | - |
Saccharomyces cerevisiae | CoA + [histone H3]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [histone H3]-L-lysine | - |
Drosophila melanogaster | CoA + [histone H3]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [histone H3]-L-lysine | - |
Saccharomyces cerevisiae ATCC 204508 | CoA + [histone H3]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [histone H3]-L-lysine14 | - |
Homo sapiens | CoA + [histone H3]-N6-acetyl-L-lysine14 | - |
? | |
| acetyl-CoA + [histone H3]-L-lysine14 | - |
Saccharomyces cerevisiae | CoA + [histone H3]-N6-acetyl-L-lysine14 | - |
? | |
| acetyl-CoA + [histone H3]-L-lysine14 | - |
Saccharomyces cerevisiae ATCC 204508 | CoA + [histone H3]-N6-acetyl-L-lysine14 | - |
? | |
| acetyl-CoA + [histone H3]-L-lysine18 | - |
Homo sapiens | CoA + [histone H3]-N6-acetyl-L-lysine18 | - |
? | |
| acetyl-CoA + [histone H3]-L-lysine23 | - |
Saccharomyces cerevisiae | CoA + [histone H3]-N6-acetyl-L-lysine23 | - |
? | |
| acetyl-CoA + [histone H3]-L-lysine23 | - |
Saccharomyces cerevisiae ATCC 204508 | CoA + [histone H3]-N6-acetyl-L-lysine23 | - |
? | |
| acetyl-CoA + [histone H3]-L-lysine56 | - |
Saccharomyces cerevisiae | CoA + [histone H3]-N6-acetyl-L-lysine56 | - |
? | |
| acetyl-CoA + [histone H3]-L-lysine56 | - |
Saccharomyces cerevisiae ATCC 204508 | CoA + [histone H3]-N6-acetyl-L-lysine56 | - |
? | |
| acetyl-CoA + [histone H3]-L-lysine9 | - |
Homo sapiens | CoA + [histone H3]-N6-acetyl-L-lysine9 | - |
? | |
| acetyl-CoA + [histone H3]-L-lysine9 | - |
Saccharomyces cerevisiae | CoA + [histone H3]-N6-acetyl-L-lysine9 | - |
? | |
| acetyl-CoA + [histone H3]-L-lysine9 | - |
Saccharomyces cerevisiae ATCC 204508 | CoA + [histone H3]-N6-acetyl-L-lysine9 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine | - |
Saccharomyces cerevisiae | CoA + [histone H4]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine | - |
Homo sapiens | CoA + [histone H4]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine | - |
Drosophila melanogaster | CoA + [histone H4]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine | - |
Saccharomyces cerevisiae ATCC 204508 | CoA + [histone H4]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine12 | - |
Homo sapiens | CoA + [histone H4]-N6-acetyl-L-lysine12 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine12 | - |
Saccharomyces cerevisiae | CoA + [histone H4]-N6-acetyl-L-lysine12 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine12 | - |
Drosophila melanogaster | CoA + [histone H4]-N6-acetyl-L-lysine12 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine12 | - |
Saccharomyces cerevisiae ATCC 204508 | CoA + [histone H4]-N6-acetyl-L-lysine12 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine16 | - |
Homo sapiens | CoA + [histone H4]-N6-acetyl-L-lysine16 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine16 | - |
Drosophila melanogaster | CoA + [histone H4]-N6-acetyl-L-lysine16 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine16 | main substrate | Homo sapiens | CoA + [histone H4]-N6-acetyl-L-lysine16 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine16 | main substrate | Drosophila melanogaster | CoA + [histone H4]-N6-acetyl-L-lysine16 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine5 | - |
Homo sapiens | CoA + [histone H4]-N6-acetyl-L-lysine5 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine5 | - |
Saccharomyces cerevisiae | CoA + [histone H4]-N6-acetyl-L-lysine5 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine5 | - |
Drosophila melanogaster | CoA + [histone H4]-N6-acetyl-L-lysine5 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine5 | - |
Saccharomyces cerevisiae ATCC 204508 | CoA + [histone H4]-N6-acetyl-L-lysine5 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine8 | - |
Homo sapiens | CoA + [histone H4]-N6-acetyl-L-lysine8 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine8 | - |
Saccharomyces cerevisiae | CoA + [histone H4]-N6-acetyl-L-lysine8 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine8 | - |
Drosophila melanogaster | CoA + [histone H4]-N6-acetyl-L-lysine8 | - |
? | |
| acetyl-CoA + [histone H4]-L-lysine8 | - |
Saccharomyces cerevisiae ATCC 204508 | CoA + [histone H4]-N6-acetyl-L-lysine8 | - |
? | |
| acetyl-CoA + [NFkappaB]-L-lysine | - |
Homo sapiens | CoA + [NFkappaB]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [p27]-L-lysine | - |
Homo sapiens | CoA + [p27]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [p53]-L-lysine | - |
Homo sapiens | CoA + [p53]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [p53]-L-lysine | - |
Drosophila melanogaster | CoA + [p53]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [p53]-L-lysine120 | - |
Homo sapiens | CoA + [p53]-N6-acetyl-L-lysine120 | - |
? | |
| acetyl-CoA + [p53]-L-lysine120 | - |
Drosophila melanogaster | CoA + [p53]-N6-acetyl-L-lysine120 | - |
? | |
| acetyl-CoA + [PGC-1alpha]-L-lysine | - |
Homo sapiens | CoA + [PGC-1alpha]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [PGC-1]-L-lysine | - |
Homo sapiens | CoA + [PGC-1]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [PTEN]-L-lysine | acetylation of the oncosuppressor protein PTEN on two lysine residues (Lys125 and Lys128) | Homo sapiens | CoA + [PTEN]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [STAT3]-L-lysine | - |
Homo sapiens | CoA + [STAT3]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [TIP5]-L-lysine | - |
Homo sapiens | CoA + [TIP5]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [TIP5]-L-lysine | - |
Drosophila melanogaster | CoA + [TIP5]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [TRRAP]-L-lysine | - |
Homo sapiens | CoA + [TRRAP]-N6-acetyl-L-lysine | - |
? | |
| acetyl-CoA + [TRRAP]-L-lysine | - |
Drosophila melanogaster | CoA + [TRRAP]-N6-acetyl-L-lysine | - |
? | |
| additional information | high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview | Saccharomyces cerevisiae | ? | - |
- |
|
| additional information | high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14 | Homo sapiens | ? | - |
- |
|
| additional information | high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Hpa3 also acts as D-amino-acid N-acetyltransferase, EC 2.3.1.36 | Saccharomyces cerevisiae | ? | - |
- |
|
| additional information | Nut1 is a mediator of RNA polymerase II transcription subunit 5, that also has histone acetylase activity | Saccharomyces cerevisiae | ? | - |
- |
|
| additional information | Rtt109 has a low catalytic efficiency in isolation, but it is much more active when associated with the histone chaperones Asf1 and Vps75. The two chaperones also determine substrate specificity, with the preferred substrate being H3K56 when Rtt109 is associated with Asf1, whereas H3K9 and H3K23 are acetylated when in complex with Vps75 | Saccharomyces cerevisiae | ? | - |
- |
|
| additional information | Tip60 preferentially catalyzes acetylation of histone H4 | Homo sapiens | ? | - |
- |
|
| additional information | high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Hpa3 also acts as D-amino-acid N-acetyltransferase, EC 2.3.1.36 | Saccharomyces cerevisiae ATCC 204508 | ? | - |
- |
|
| additional information | Nut1 is a mediator of RNA polymerase II transcription subunit 5, that also has histone acetylase activity | Saccharomyces cerevisiae ATCC 204508 | ? | - |
- |
|
| additional information | high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview | Saccharomyces cerevisiae ATCC 204508 | ? | - |
- |
|
| additional information | Rtt109 has a low catalytic efficiency in isolation, but it is much more active when associated with the histone chaperones Asf1 and Vps75. The two chaperones also determine substrate specificity, with the preferred substrate being H3K56 when Rtt109 is associated with Asf1, whereas H3K9 and H3K23 are acetylated when in complex with Vps75 | Saccharomyces cerevisiae ATCC 204508 | ? | - |
- |
|
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AIB1 | - |
Homo sapiens |
| Cbp | - |
Homo sapiens |
| circadian locomoter output cycles protein kaput | UniProt | Homo sapiens |
| CLOCK | - |
Homo sapiens |
| CREBBP | - |
Homo sapiens |
| ELP3 | - |
Homo sapiens |
| Gcn5 | - |
Homo sapiens |
| Gcn5 related N-acetyltransferase | - |
Homo sapiens |
| Gcn5 related N-acetyltransferase | - |
Saccharomyces cerevisiae |
| GNAT | - |
Homo sapiens |
| GNAT | - |
Saccharomyces cerevisiae |
| GTF3C4 | - |
Homo sapiens |
| HBO1 | - |
Homo sapiens |
| Hpa2 | - |
Saccharomyces cerevisiae |
| Hpa3 | - |
Saccharomyces cerevisiae |
| KAT | - |
Homo sapiens |
| KAT | - |
Saccharomyces cerevisiae |
| KAT | - |
Drosophila melanogaster |
| KAT10 | - |
Saccharomyces cerevisiae |
| KAT11 | - |
Saccharomyces cerevisiae |
| KAT12 | - |
Homo sapiens |
| KAT13A | - |
Homo sapiens |
| KAT13B | - |
Homo sapiens |
| KAT13C | - |
Homo sapiens |
| KAT13D | - |
Homo sapiens |
| Kat2A | - |
Homo sapiens |
| Kat2b | - |
Homo sapiens |
| KAT3A | - |
Homo sapiens |
| KAT3B | - |
Homo sapiens |
| KAT4 | - |
Homo sapiens |
| KAT4 | - |
Saccharomyces cerevisiae |
| KAT4 | - |
Drosophila melanogaster |
| KAT5 | - |
Homo sapiens |
| KAT5 | - |
Drosophila melanogaster |
| KAT6A | - |
Homo sapiens |
| KAT6B | - |
Homo sapiens |
| KAT7 | - |
Homo sapiens |
| KAT8 | - |
Homo sapiens |
| KAT8 | - |
Drosophila melanogaster |
| KAT9 | - |
Homo sapiens |
| lysine acetyltransferase | - |
Homo sapiens |
| lysine acetyltransferase | - |
Saccharomyces cerevisiae |
| lysine acetyltransferase | - |
Drosophila melanogaster |
| Mof | - |
Homo sapiens |
| Mof | - |
Drosophila melanogaster |
| More | also cf. EC 2.7.11.1 | Homo sapiens |
| More | also cf. EC 2.7.11.1 | Drosophila melanogaster |
| More | cf. EC 2.3.1.36 | Saccharomyces cerevisiae |
| Morf | - |
Homo sapiens |
| MOZ | - |
Homo sapiens |
| Myb-binding protein 1A | UniProt | Homo sapiens |
| MYBBP1A | - |
Homo sapiens |
| MYST | - |
Homo sapiens |
| MYST | - |
Drosophila melanogaster |
| MYST1 | - |
Homo sapiens |
| MYST1 | - |
Drosophila melanogaster |
| MYST2 | - |
Homo sapiens |
| MYST3 | - |
Homo sapiens |
| MYST4 | - |
Homo sapiens |
| NCoA-1 | UniProt | Homo sapiens |
| NCoA-3 | UniProt | Homo sapiens |
| nuclear receptor coactivator 1 | UniProt | Homo sapiens |
| nuclear receptor coactivator 3 | UniProt | Homo sapiens |
| Nut1 | - |
Saccharomyces cerevisiae |
| p160 | - |
Homo sapiens |
| p300 | - |
Homo sapiens |
| PCAF | - |
Homo sapiens |
| regulator of Ty1 transposition protein 109 | UniProt | Saccharomyces cerevisiae |
| Rtt109 | - |
Saccharomyces cerevisiae |
| SRC1 | - |
Homo sapiens |
| SRC3 | - |
Homo sapiens |
| TAF | - |
Homo sapiens |
| TAF | - |
Saccharomyces cerevisiae |
| TAF | - |
Drosophila melanogaster |
| TBP1 | - |
Homo sapiens |
| TBP1 | - |
Saccharomyces cerevisiae |
| TBP1 | - |
Drosophila melanogaster |
| TFIIIC90 | - |
Homo sapiens |
| Tip60 | - |
Homo sapiens |
| Tip60 | - |
Drosophila melanogaster |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| acetyl-CoA | - |
Homo sapiens | |
| acetyl-CoA | - |
Saccharomyces cerevisiae | |
| acetyl-CoA | - |
Drosophila melanogaster | |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.46 | - |
C646 | pH and temperature not specified in the publication | Homo sapiens | |
IC50 Value
| IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
|---|---|---|---|---|---|
| 0.0000026 | - |
pH and temperature not specified in the publication | Homo sapiens | A-485 | |
| 0.0000098 | - |
pH and temperature not specified in the publication | Homo sapiens | A-485 | |
| 0.000011 | - |
pH and temperature not specified in the publication | Homo sapiens | NK13650A | |
| 0.000022 | - |
pH and temperature not specified in the publication | Homo sapiens | NK13650B | |
| 0.00007 | - |
pH and temperature not specified in the publication | Homo sapiens | peptide conjugate Boc-C5-CoA | |
| 0.0003 | - |
pH and temperature not specified in the publication | Homo sapiens | peptide conjugate H3-CoA-20 | |
| 0.0005 | - |
pH and temperature not specified in the publication | Homo sapiens | Lys-CoA | |
| 0.0011 | - |
pH and temperature not specified in the publication | Homo sapiens | EML425 | |
| 0.0016 | - |
pH and temperature not specified in the publication | Homo sapiens | C646 | |
| 0.0016 | 0.00974 | pH and temperature not specified in the publication | Homo sapiens | PU139 | |
| 0.002 | - |
pH and temperature not specified in the publication | Homo sapiens | Plumbagin | |
| 0.002 | - |
pH and temperature not specified in the publication | Homo sapiens | NU9056 | |
| 0.002 | 0.128 | pH and temperature not specified in the publication | Homo sapiens | L002 | |
| 0.00249 | - |
pH and temperature not specified in the publication | Homo sapiens | PU139 | |
| 0.0029 | - |
pH and temperature not specified in the publication | Homo sapiens | EML425 | |
| 0.0041 | - |
pH and temperature not specified in the publication | Homo sapiens | N-[5-[(5-[[5-([4-[(5-[[5-([5-[(5-[[3-(dimethylamino)propyl]carbamoyl]-1-methyl-1H-pyrrol-3-yl)carbamoyl]-1-methyl-1H-pyrrol-3-yl]carbamoyl)-1-methyl-1H-pyrrol-3-yl]carbamoyl]-1-methyl-1H-pyrrol-3-yl)amino]-4-oxobutyl]carbamoyl)-1-methyl-1H-pyrrol-3-yl]carbamoyl]-1-methyl-1H-pyrrol-3-yl)carbamoyl]-1-methyl-1H-pyrrol-3-yl]-4-[(N-[[2-(2-[4-[(4Z)-4-[[5-(2,3-dimethyl-6-nitrophenyl)furan-2-yl]methylidene]-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl]benzamido]ethoxy)ethoxy]acetyl]-beta-alanyl)amino]-1-methyl-1H-pyrrole-2-carboxamide | |
| 0.005 | - |
pH and temperature not specified in the publication | Homo sapiens | garcinol | |
| 0.00534 | - |
pH and temperature not specified in the publication | Homo sapiens | PU139 | |
| 0.00662 | - |
pH and temperature not specified in the publication | Homo sapiens | peptide conjugate H4-K16-CoA | |
| 0.007 | - |
pH and temperature not specified in the publication | Homo sapiens | garcinol | |
| 0.0072 | - |
pH and temperature not specified in the publication | Homo sapiens | embelin | |
| 0.00839 | - |
pH and temperature not specified in the publication | Homo sapiens | PU139 | |
| 0.0097 | - |
pH and temperature not specified in the publication | Homo sapiens | 4-amino-1-naphthol | |
| 0.01759 | - |
pH and temperature not specified in the publication | Homo sapiens | peptide conjugate H4-K16-CoA | |
| 0.025 | - |
pH and temperature not specified in the publication | Homo sapiens | curcumin | |
| 0.03 | - |
pH and temperature not specified in the publication | Homo sapiens | epigallocatechin-3-gallate | |
| 0.0339 | - |
pH and temperature not specified in the publication | Homo sapiens | L002 | |
| 0.0347 | - |
pH and temperature not specified in the publication | Homo sapiens | L002 | |
| 0.043 | 0.348 | pH and temperature not specified in the publication | Homo sapiens | anacardic acid | |
| 0.043 | 0.064 | pH and temperature not specified in the publication | Drosophila melanogaster | anacardic acid | |
| 0.05 | - |
pH and temperature not specified in the publication | Homo sapiens | epigallocatechin-3-gallate | |
| 0.0575 | - |
pH and temperature not specified in the publication | Homo sapiens | ethyl 2-methyl-6-([5-[(prop-2-yn-1-yl)amino]pentyl]oxy)quinoline-3-carboxylate | |
| 0.06 | - |
pH and temperature not specified in the publication | Homo sapiens | epigallocatechin-3-gallate | |
| 0.07 | - |
pH and temperature not specified in the publication | Homo sapiens | epigallocatechin-3-gallate | |
| 0.1 | - |
pH and temperature not specified in the publication | Homo sapiens | MB-3 | |
| 0.2 | - |
pH and temperature not specified in the publication | Homo sapiens | Lys-CoA | |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Homo sapiens | Tip60 is downregulated in breast cancer | down |
| Drosophila melanogaster | Tip60 is downregulated in breast cancer | down |
| Homo sapiens | Gcn5 is upregulated in human malignancies including non-small-cell lung cancer (NSCLC), colon cancer, and glioma | up |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme belongs to the components of transcription factor complexes | Homo sapiens |
| evolution | the enzyme belongs to the MYST family. The MYST family takes its name from the first identified members: (MOZ, KAT6A), Ybf2 (Sas3, KAT6), something about silencing (Sas2, KAT8) and Tat-interacting protein (Tip60, KAT5). To date, five human KATs have been identified in this family: MOZ, MOZ related factor (MORF, KAT6B), Tip60, HAT bound to ORC1 (HBO1, KAT7) and males absent on the first (MOF, KAT8 or MYST 1), the functional orthologue of yeast's Sas2. The defining feature of MYST family is the presence of the highly conserved MYST domain. MYST enzymes possess a highly-conserved acetyl-CoA-binding motif A within the catalytic domain. Additionally, some family members have also structural features in common with one another, such as chromodomains or plant homeodomain-linked zinc fingers. The members of this family utilize a double displacement (or ping-pong) catalytic mechanism. Autoacetylation is an important process in modulating the activity of MYST family members | Homo sapiens |
| evolution | the enzyme belongs to the MYST family. The MYST family takes its name from the first identified members: (MOZ, KAT6A), Ybf2 (Sas3, KAT6), something about silencing (Sas2, KAT8) and Tat-interacting protein (Tip60, KAT5). To date, five human KATs have been identified in this family: MOZ, MOZ related factor (MORF, KAT6B), Tip60, HAT bound to ORC1 (HBO1, KAT7) and males absent on the first (MOF, KAT8 or MYST 1), the functional orthologue of yeast's Sas2. The defining feature of MYST family is the presence of the highly conserved MYST domain. MYST enzymes possess a highly-conserved acetyl-CoA-binding motif A within the catalytic domain. Additionally, some family members have also structural features in common with one another, such as chromodomains or plant homeodomain-linked zinc fingers. The members of this family utilize a double displacement (or ping-pong) catalytic mechanism. Autoacetylation is an important process in modulating the activity of MYST family members | Drosophila melanogaster |
| evolution | the enzyme belongs to the nuclear receptors coactivators | Homo sapiens |
| evolution | the enzyme belongs to the nuclear receptors coactivators. Fungal enzyme Rtt109 shows low sequence similarity to members of other KAT families. It is comparable to p300 in terms of its tertiary structure, but has a different catalytic mechanism | Saccharomyces cerevisiae |
| evolution | the enzyme TAF1/TBP belongs to the components of transcription factor complexes | Homo sapiens |
| evolution | the enzyme TAF1/TBP belongs to the components of transcription factor complexes | Saccharomyces cerevisiae |
| evolution | the enzyme TAF1/TBP belongs to the components of transcription factor complexes | Drosophila melanogaster |
| evolution | the KATs belong to the enzyme families Gcn5 (KAT2A), PCAF (p300/CBP associated factor, KAT2B), Elp3 (KAT9), Hpa2 (KAT10), Hpa3, and Nut1. The common feature is the presence of four conserved 15-33 amino acid motifs indicated as A, B, C and D, in addition to various chromo- and bromodomains that can bind methylated or acetylated lysines, respectively. The A motif is the most conserved and contains the R/Q-X-X-G-X-G/A sequence that is essential for acetyl-CoA recognition and binding. Despite the structural similarities that characterize an enzyme family, the N- and C-terminal domains are quite different, and allow each enzyme to be specific for a particular substrate | Homo sapiens |
| evolution | the KATs belong to the enzyme families Gcn5 (KAT2A), PCAF (p300/CBP associated factor, KAT2B), Elp3 (KAT9), Hpa2 (KAT10), Hpa3, and Nut1. The common feature is the presence of four conserved 15-33 amino acid motifs indicated as A, B, C and D, in addition to various chromo- and bromodomains that can bind methylated or acetylated lysines, respectively. The A motif is the most conserved and contains the R/Q-X-X-G-X-G/A sequence that is essential for acetyl-CoA recognition and binding. Despite the structural similarities that characterize an enzyme family, the N- and C-terminal domains are quite different, and allow each enzyme to be specific for a particular substrate | Saccharomyces cerevisiae |
| evolution | the KATs belong to the enzyme families Gcn5 (KAT2A), PCAF (p300/CBP associated factor, KAT2B), Elp3 (KAT9), Hpa2 (KAT10), Hpa3, and Nut1. The common feature is the presence of four conserved 15-33 amino acid motifs indicated as A, B, C and D, in addition to various chromo- and bromodomains that can bind methylated or acetylated lysines, respectively. The A motif is the most conserved and contains the R/Q-X-X-G-X-G/A sequence that is essential for acetyl-CoA recognition and binding. Despite the structural similarities that characterize an enzyme family, the N- and C-terminal domains are quite different, and allow each enzyme to be specific for a particular substrate. A characterizing feature of p300/CBP family is the presence of a loop, called the L1 loop, which connects an alpha-helix (alpha4) and a beta-sheet (beta5), and is part of the lysine and acetyl-CoA binding site | Homo sapiens |
| evolution | the KATs belong to the enzyme families Gcn5 (KAT2A), PCAF (p300/CBP associated factor, KAT2B), Elp3 (KAT9), Hpa2 (KAT10), Hpa3, and Nut1. The common feature is the presence of four conserved 15-33 amino acid motifs indicated as A, B, C and D, in addition to various chromo- and bromodomains that can bind methylated or acetylated lysines, respectively. The A motif is the most conserved and contains the R/Q-X-X-G-X-G/A sequence that is essential for acetyl-CoA recognition and binding. Despite the structural similarities that characterize an enzyme family, the N- and C-terminal domains are quite different, and allow each enzyme to be specific for a particular substrate. A characterizing feature of p300/CBP family is the presence of a loop, called the L1 loop, which connects an alpha-helix (alpha4) and a beta-sheet (beta5), and is part of the lysine and acetyl-CoA binding site. Enzyme CBP is implicated in Rubinstein-Taybi syndrome and inflammation and mutated in lung, colon and ovarian carcinomas. The enzyme forms fusion proteins in acute myeloid leukemia | Homo sapiens |
| malfunction | HBO1 misregulation is linked to uncontrolled proliferation | Homo sapiens |
| malfunction | Myst3 forms fusion proteins in acute myeloid leukemia | Homo sapiens |
| malfunction | Myst4 forms fusion proteins in acute myeloid leukemia | Homo sapiens |
| malfunction | the dysregulation of the enzyme activity is implicated in many human pathologies such as cancer, neurological and inflammatory disorders | Homo sapiens |
| malfunction | the dysregulation of the enzyme activity is implicated in many human pathologies such as cancer, neurological and inflammatory disorders. An aberrant activity of Gcn5 can lead to uncontrolled cell cycle progression | Homo sapiens |
| malfunction | the dysregulation of the enzyme activity is implicated in many human pathologies such as cancer, neurological and inflammatory disorders. PCAF knockdown blocks the growth of urothelial cancer cells and reduces their invasive ability | Homo sapiens |
| metabolism | PCAF and Gcn5-mediated acetylation can be implicated in type 2 diabetes | Homo sapiens |
| additional information | mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis | Homo sapiens |
| additional information | mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis | Saccharomyces cerevisiae |
| additional information | mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis | Drosophila melanogaster |
| additional information | mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r) | Homo sapiens |
| additional information | mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Rtt109 with bound acetyl-CoA (PDB ID 3qm0) | Saccharomyces cerevisiae |
| additional information | mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2) | Homo sapiens |
| additional information | mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer | Homo sapiens |
| additional information | mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs) | Homo sapiens |
| physiological function | lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts | Homo sapiens |
| physiological function | lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts | Saccharomyces cerevisiae |
| physiological function | lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. Enzyme CBP is implicated in Rubinstein-Taybi syndrome and inflammation, and forms fusion proteins in acute myeloid leukemia | Homo sapiens |
| physiological function | lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. Enzyme CLOCK is a regulator of circadian rhythm | Homo sapiens |
| physiological function | lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. Enzyme p300 is implicated in inflammation, esophageal squamous cell and hepatocellular carcinoma, and it forms fusion proteins in acute myeloid leukemia. The acetylase activity regulated by autoacetylation | Homo sapiens |
| physiological function | lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. Enzyme SCR1 is involved in steroid-related transcription through pre-initiation complex formation stabilization. SRC1 KAT activity is primarily specific for histones H3 and H4, and is a consequence of ligand binding to steroid receptors. This is thought to be a mechanism by which steroid receptors and their co-activators enhance formation of a stable pre-initiation complex, thereby increasing transcription of the target genes | Homo sapiens |
| physiological function | lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. GCN5 is upregulated in non-small cell lung carcinoma, colon cancer, and glioma, and implicated in type 2 diabetes and AIDS. Gcn5 is essential in the activation and stabilization of the tumor suppressor p53. It acetylates peroxisome proliferator-activated receptor gamma co-activator 1alpha (PGC-1alpha), a co-activator which plays a central role in hepatic gluconeogenesis. PGC-1alpha acetylation triggers its degradation, leading to a decrease in blood and hepatic glucose output. In non-small-cell lung cancer (NSCLC), Gcn5 promotes cell proliferation by regulating the expression of cell cycle proteins cyclin D1, E1 and E2F1. In colon cancer tissues, Gcn5 overexpression is found to be dependent on both the cell cycle protein E2F1 and the oncogene c-myc | Homo sapiens |
| physiological function | lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. MYST enzymes have their acetylase activity regulated by autoacetylation. Tip60 activates the machinery for DNA repair | Drosophila melanogaster |
| physiological function | lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. MYST enzymes have their acetylase activity regulated by autoacetylation. Tip60 activates the machinery for DNA repair. It is involved in numerous activities such as transcription, DNA damage cellular response, apoptosis and it has been reported to regulate p53 through acetylation at Lys120 | Homo sapiens |
| physiological function | lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. PCAF acetylates the cyclin-dependent kinase inhibitor p27 leading to its degradation and facilitating cell cycle progression. PCAF is essential in the activation and stabilization of the tumor suppressor p53. It acetylates peroxisome proliferator-activated receptor gamma co-activator 1alpha (PGC-1alpha), a co-activator which plays a central role in hepatic gluconeogenesis. PGC-1alpha acetylation triggers its degradation, leading to a decrease in blood and hepatic glucose output. PCAF catalyzes the acetylation of the oncosuppressor protein PTEN on two lysine residues (Lys125 and Lys128), thereby promoting cell cycle blocking in the G1 phase after growth factor stimulation. A critical function of PCAF is the acetylation of connexin 43, which is linked to cardiac dystrophy. PCAF catalyzes the acetylation of the oncosuppressor protein PTEN on two lysine residues (Lys125 and Lys128), thereby promoting cell cycle blocking in the G1 phase after growth factor stimulation. PCAF is implicated in urothelial cancer, type 2 diabetes and cardiac dystrophy | Homo sapiens |
| physiological function | lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. Rtt109 has a low catalytic efficiency in isolation, but it is much more active when associated with the histone chaperones Asf1 and Vps75. The two chaperones also determine substrate specificity, with the preferred substrate being H3K56 when Rtt109 is associated with Asf1, whereas H3K9 and H3K23 are acetylated when in complex with Vps75 | Saccharomyces cerevisiae |
| physiological function | lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. TAF1 is a regulatory element in hormone-related transcriptional processes | Homo sapiens |
| physiological function | lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. TAF1 is a regulatory element in hormone-related transcriptional processes | Drosophila melanogaster |
| physiological function | lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. The enzyme is a regulatory element in hormone-related transcriptional processes. It is required for RNA polymerase III transcription | Homo sapiens |
| physiological function | lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. The MYST protein HBO1/MYST2 preferentially catalyzes the acetylation of histone H4. MYST enzymes have their acetylase activity regulated by autoacetylation. Enzyme HBO1/MYST2 is involved in regulation of DNA replication, since it interacts with proteins of the origin of replication complex (ORC1). HBO1 is involved in DNA replication | Homo sapiens |
| physiological function | lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. The MYST protein MOF catalyzes the acetylation of p53 at lysine120, which helps to discriminate cell-cycle arrest and apoptotic functions. MYST enzymes have their acetylase activity regulated by autoacetylation | Drosophila melanogaster |
| physiological function | lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. The MYST protein MOF catalyzes the acetylation of p53 at lysine120, which helps to discriminate cell-cycle arrest and apoptotic functions. MYST enzymes have their acetylase activity regulated by autoacetylation. MYST1/MOF is associated with tumor growth of oral tongue squamous cell carcinoma | Homo sapiens |
| physiological function | lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. The MYST protein MORF catalyzes the acetylation of histone H3 at Lys14. MYST enzymes have their acetylase activity regulated by autoacetylation | Homo sapiens |
| physiological function | lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. The MYST protein MOZ catalyzes the acetylation of histone H3 at Lys14. MYST enzymes have their acetylase activity regulated by autoacetylation | Homo sapiens |
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