| + |
HIPK2 | down-regulates activity 
phosphorylation
|
HDAC3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277568 |
Ser374 |
KMLNHAPsVQIHDVP |
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 34244427 |
Mechanistically, HIPK2 bound and phosphorylated histone deacetylase 3 (HDAC3) at serine 374 to inhibit its enzymatic activity, thus reducing the deacetylation of p65 at lysine 218 to suppress NF-κB activation. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PPP4C | down-regulates activity
dephosphorylation
|
HDAC3 |
0.387 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248548 |
Ser424 |
DHDNDKEsDVEI |
Homo sapiens |
|
| pmid |
sentence |
| 15805470 |
Here we demonstrate that, in addition to protein-protein interactions with NCoR/SMRT, the activity of HDAC3 is regulated by both phosphorylation and dephosphorylation. A protein kinase CK2 phosphoacceptor site in the HDAC3 protein was identified at position Ser424, which is a nonconserved residue among the class I HDACs. Mutation of this residue was found to reduce deacetylase activity.|Significantly, both overexpression and siRNA knock-down approaches, and analysis of cells devoid of PP4c, unequivocally show that HDAC3 activity is inversely proportional to the cellular abundance of PP4(c). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK2A1 | up-regulates activity 
phosphorylation
|
HDAC3 |
0.517 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250889 |
Ser424 |
DHDNDKEsDVEI |
Homo sapiens |
|
| pmid |
sentence |
| 15805470 |
A protein kinase CK2 phosphoacceptor site in the HDAC3 protein was identified at position Ser424, which is a nonconserved residue among the class I HDACs. Mutation of this residue was found to reduce deacetylase activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SRC | up-regulates activity
phosphorylation
|
HDAC3 |
0.394 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277484 |
Tyr325 |
AISEELPySEYFEYF |
in vitro |
|
| pmid |
sentence |
| 30317579 |
C-Src also phosphorylated three tyrosine sites of HDAC3 at tyrosine 325, 328, and 331. Importantly, wild-type c-Src increases HDAC3 activity, but not mutant c-SrcK298M (kinase inactive form). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277485 |
Tyr328 |
EELPYSEyFEYFAPD |
in vitro |
|
| pmid |
sentence |
| 30317579 |
C-Src also phosphorylated three tyrosine sites of HDAC3 at tyrosine 325, 328, and 331. Importantly, wild-type c-Src increases HDAC3 activity, but not mutant c-SrcK298M (kinase inactive form). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277486 |
Tyr331 |
PYSEYFEyFAPDFTL |
in vitro |
|
| pmid |
sentence |
| 30317579 |
C-Src also phosphorylated three tyrosine sites of HDAC3 at tyrosine 325, 328, and 331. Importantly, wild-type c-Src increases HDAC3 activity, but not mutant c-SrcK298M (kinase inactive form). |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
HDAC3 | up-regulates
binding
|
E2F1 |
0.474 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-199961 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23213415 |
Furthermore, smad7 caused hdac-1 bind to e2f-1 to form a ternary complex on chromosomal dna containing an e2f-binding motif and leading to repression in the activity of the e2f target genes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
N-hydroxy-3-[4-[[2-hydroxyethyl-[2-(1H-indol-3-yl)ethyl]amino]methyl]phenyl]-2-propenamide | down-regulates activity
chemical inhibition
|
HDAC3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257924 |
|
|
in vitro |
|
| pmid |
sentence |
| 17868033 |
Our findings suggest that hydroxamic acid-derived compounds such as TSA, NVP-LAQ824, panobinostat, ITF2357, vorinostat and belinostat act as potent pan-HDAC isoform inhibitors. A notable observation was the similarity between belinostat and vorinostat in the biochemical isoform assays; both compounds exhibit similar EC50 values in all but the HDAC8 assay. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257982 |
|
|
in vitro |
|
| pmid |
sentence |
| 20139990 |
Collaboratively, we synthesized and assembled a panel of structurally-diverse small-molecule HDACi 1, 2, 7-20 that comprise most of the relevant literature-reported tool compounds and pharmaceutically developed clinical candidates (Supplementary Fig 3). We next conducted a high-throughput, precise profiling of HDACi potency against all Class I and II enzymes, in a miniaturized dose-ranging format (Supplementary Table 1). |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
N-[4-[(hydroxyamino)-oxomethyl]phenyl]carbamic acid [6-(diethylaminomethyl)-2-naphthalenyl]methyl ester | down-regulates activity
chemical inhibition
|
HDAC3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257966 |
|
|
in vitro |
|
| pmid |
sentence |
| 20139990 |
Collaboratively, we synthesized and assembled a panel of structurally-diverse small-molecule HDACi 1, 2, 7-20 that comprise most of the relevant literature-reported tool compounds and pharmaceutically developed clinical candidates (Supplementary Fig 3). We next conducted a high-throughput, precise profiling of HDACi potency against all Class I and II enzymes, in a miniaturized dose-ranging format (Supplementary Table 1). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257906 |
|
|
in vitro |
|
| pmid |
sentence |
| 17868033 |
Our findings suggest that hydroxamic acid-derived compounds such as TSA, NVP-LAQ824, panobinostat, ITF2357, vorinostat and belinostat act as potent pan-HDAC isoform inhibitors. A notable observation was the similarity between belinostat and vorinostat in the biochemical isoform assays; both compounds exhibit similar EC50 values in all but the HDAC8 assay. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
JWOGUUIOCYMBPV-GMFLJSBRSA-N | down-regulates activity
chemical inhibition
|
HDAC3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257913 |
|
|
in vitro |
|
| pmid |
sentence |
| 17868033 |
Our findings suggest that hydroxamic acid-derived compounds such as TSA, NVP-LAQ824, panobinostat, ITF2357, vorinostat and belinostat act as potent pan-HDAC isoform inhibitors. A notable observation was the similarity between belinostat and vorinostat in the biochemical isoform assays; both compounds exhibit similar EC50 values in all but the HDAC8 assay. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257978 |
|
|
in vitro |
|
| pmid |
sentence |
| 20139990 |
Collaboratively, we synthesized and assembled a panel of structurally-diverse small-molecule HDACi 1, 2, 7-20 that comprise most of the relevant literature-reported tool compounds and pharmaceutically developed clinical candidates (Supplementary Fig 3). We next conducted a high-throughput, precise profiling of HDACi potency against all Class I and II enzymes, in a miniaturized dose-ranging format (Supplementary Table 1). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261128 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17868033 |
Apicidin inhibited rhHDACs 2 and 3 in the nanomolar range. |
|
| Publications: |
3 |
Organism: |
In Vitro, Homo Sapiens |
| + |
belinostat | down-regulates activity
chemical inhibition
|
HDAC3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257746 |
|
|
in vitro |
|
| pmid |
sentence |
| 17868033 |
Our findings suggest that hydroxamic acid-derived compounds such as TSA, NVP-LAQ824, panobinostat, ITF2357, vorinostat and belinostat act as potent pan-HDAC isoform inhibitors. A notable observation was the similarity between belinostat and vorinostat in the biochemical isoform assays; both compounds exhibit similar EC50 values in all but the HDAC8 assay. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257953 |
|
|
in vitro |
|
| pmid |
sentence |
| 20139990 |
Collaboratively, we synthesized and assembled a panel of structurally-diverse small-molecule HDACi 1, 2, 7-20 that comprise most of the relevant literature-reported tool compounds and pharmaceutically developed clinical candidates (Supplementary Fig 3). We next conducted a high-throughput, precise profiling of HDACi potency against all Class I and II enzymes, in a miniaturized dose-ranging format (Supplementary Table 1). |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
HDAC3 | down-regulates quantity by repression
transcriptional regulation
|
CDH1 |
0.26 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275662 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 25726523 |
GATA1 is a new substrate of p21-activated kinase 5 (PAK5), which is phosphorylated on serine 161 and 187 (S161 and S187). GATA1 recruits HDAC3/4 to E-cadherin promoter, which is reduced by GATA1 S161A S187A mutant. These data indicate that phosphorylated GATA1 recruits more HDAC3/4 to promote transcriptional repression of E-cadherin, leading to the EMT of breast cancer cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
romidepsin | down-regulates activity
chemical inhibition
|
HDAC3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257993 |
|
|
in vitro |
|
| pmid |
sentence |
| 20139990 |
Collaboratively, we synthesized and assembled a panel of structurally-diverse small-molecule HDACi 1, 2, 7-20 that comprise most of the relevant literature-reported tool compounds and pharmaceutically developed clinical candidates (Supplementary Fig 3). We next conducted a high-throughput, precise profiling of HDACi potency against all Class I and II enzymes, in a miniaturized dose-ranging format (Supplementary Table 1). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
panobinostat | down-regulates activity
chemical inhibition
|
HDAC3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257749 |
|
|
in vitro |
|
| pmid |
sentence |
| 17868033 |
Our findings suggest that hydroxamic acid-derived compounds such as TSA, NVP-LAQ824, panobinostat, ITF2357, vorinostat and belinostat act as potent pan-HDAC isoform inhibitors. A notable observation was the similarity between belinostat and vorinostat in the biochemical isoform assays; both compounds exhibit similar EC50 values in all but the HDAC8 assay. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
(S)-N-Hydroxy-4-(3-methyl-2-phenylbutanamido)benzamide | down-regulates activity
chemical inhibition
|
HDAC3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262251 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31908417 |
The present study aimed to detect HDAC1 expression in and around ESCC tissues and comprehensively assess the anti-ESCC effects of AR-42, a phenylbutyrate-derived pan-HDAC inhibitor with low nanomolar IC50s against HDACs including HDAC1. AR-42 developed by Chen et al is an orally bioavailable hydroxamate-tethered phenylbutyrate derivative with strong inhibitory activity against class I (HDAC 1, 2, 3 and 8) and class IIb (HDAC 6 and 10) HDACs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CUDC-907 | down-regulates
chemical inhibition
|
HDAC3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-191209 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GATA1 | up-regulates activity
relocalization
|
HDAC3 |
0.53 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275664 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 25726523 |
GATA1 is a new substrate of p21-activated kinase 5 (PAK5), which is phosphorylated on serine 161 and 187 (S161 and S187). GATA1 recruits HDAC3/4 to E-cadherin promoter, which is reduced by GATA1 S161A S187A mutant. These data indicate that phosphorylated GATA1 recruits more HDAC3/4 to promote transcriptional repression of E-cadherin, leading to the EMT of breast cancer cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
N-(2-aminophenyl)-4-[[[4-(3-pyridinyl)-2-pyrimidinyl]amino]methyl]benzamide | down-regulates
chemical inhibition
|
HDAC3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-194551 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
vorinostat | down-regulates activity
chemical inhibition
|
HDAC3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257948 |
|
|
in vitro |
|
| pmid |
sentence |
| 20139990 |
Collaboratively, we synthesized and assembled a panel of structurally-diverse small-molecule HDACi 1, 2, 7-20 that comprise most of the relevant literature-reported tool compounds and pharmaceutically developed clinical candidates (Supplementary Fig 3). We next conducted a high-throughput, precise profiling of HDACi potency against all Class I and II enzymes, in a miniaturized dose-ranging format (Supplementary Table 1). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257916 |
|
|
in vitro |
|
| pmid |
sentence |
| 17868033 |
Our findings suggest that hydroxamic acid-derived compounds such as TSA, NVP-LAQ824, panobinostat, ITF2357, vorinostat and belinostat act as potent pan-HDAC isoform inhibitors. A notable observation was the similarity between belinostat and vorinostat in the biochemical isoform assays; both compounds exhibit similar EC50 values in all but the HDAC8 assay. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
6-(1,3-dioxo-2-benzo[de]isoquinolinyl)-N-hydroxyhexanamide | down-regulates activity
chemical inhibition
|
HDAC3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258002 |
|
|
in vitro |
|
| pmid |
sentence |
| 20139990 |
Collaboratively, we synthesized and assembled a panel of structurally-diverse small-molecule HDACi 1, 2, 7-20 that comprise most of the relevant literature-reported tool compounds and pharmaceutically developed clinical candidates (Supplementary Fig 3). We next conducted a high-throughput, precise profiling of HDACi potency against all Class I and II enzymes, in a miniaturized dose-ranging format (Supplementary Table 1). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
HDAC3 | down-regulates activity
deacetylation
|
YY1 |
0.582 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268837 |
|
|
in vitro |
|
| pmid |
sentence |
| 11486036 |
Previous studies have established that YY1 interacts with histone acetyltransferases p300 and CREB-binding protein (CBP) and histone deacetylase 1 (HDAC1), HDAC2, and HDAC3. Here, we present evidence that the activity of YY1 is regulated through acetylation by p300 and PCAF and through deacetylation by HDACs. YY1 was acetylated in two regions: both p300 and PCAF acetylated the central glycine-lysine-rich domain of residues 170 to 200, and PCAF also acetylated YY1 at the C-terminal DNA-binding zinc finger domain. Acetylation of the central region was required for the full transcriptional repressor activity of YY1 and targeted YY1 for active deacetylation by HDACs. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CCND1 | up-regulates
binding
|
HDAC3 |
0.421 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134056 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15713663 |
Collectively, these studies suggest an important role of cyclin d1 in regulation of ppargamma-mediated adipocyte differentiation through recruitment of hdacs to regulate ppar response element local chromatin structure and ppargamma function. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HDAC3 | up-regulates
binding
|
SMAD7/HDAC1/E2F-1 |
0.445 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217358 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23213415 |
Furthermore, smad7 caused hdac-1 bind to e2f-1 to form a ternary complex on chromosomal dna containing an e2f-binding motif and leading to repression in the activity of the e2f target genes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CUDC-101 | down-regulates activity
chemical inhibition
|
HDAC3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262259 |
|
|
in vitro |
|
| pmid |
sentence |
| 20143778 |
By incorporating histone deacetylase (HDAC) inhibitory functionality into the pharmacophore of the epidermal growth factor receptor (EGFR) and human epidermal growth factor receptor 2 (HER2) inhibitors, we synthesized a novel series of compounds with potent, multiacting HDAC, EGFR, and HER2 inhibition and identified 7-(4-(3-ethynylphenylamino)-7-methoxyquinazolin-6-yloxy)-N-hydroxyheptanamide 8 (CUDC-101) as a drug candidate, which is now in clinical development. 8 displays potent in vitro inhibitory activity against HDAC, EGFR, and HER2 with an IC(50) of 4.4, 2.4, and 15.7 nM, respectively. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
BCL3 | up-regulates
binding
|
HDAC3 |
0.354 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-129804 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15469820 |
We show that bcl-3 is a substrate for the protein kinase gsk3 and that gsk3-mediated bcl-3 phosphorylation, which is inhibited by akt activation, targets its degradation through the proteasome pathway. This phosphorylation modulates its association with hdac1, 3 and 6. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
N-(2-aminophenyl)-4-[[[4-(3-pyridinyl)-2-pyrimidinyl]amino]methyl]benzamide | down-regulates activity
chemical inhibition
|
HDAC3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257932 |
|
|
in vitro |
|
| pmid |
sentence |
| 17868033 |
Our findings suggest that hydroxamic acid-derived compounds such as TSA, NVP-LAQ824, panobinostat, ITF2357, vorinostat and belinostat act as potent pan-HDAC isoform inhibitors. A notable observation was the similarity between belinostat and vorinostat in the biochemical isoform assays; both compounds exhibit similar EC50 values in all but the HDAC8 assay. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257974 |
|
|
in vitro |
|
| pmid |
sentence |
| 20139990 |
Collaboratively, we synthesized and assembled a panel of structurally-diverse small-molecule HDACi 1, 2, 7-20 that comprise most of the relevant literature-reported tool compounds and pharmaceutically developed clinical candidates (Supplementary Fig 3). We next conducted a high-throughput, precise profiling of HDACi potency against all Class I and II enzymes, in a miniaturized dose-ranging format (Supplementary Table 1). |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
HDAC3 | up-regulates quantity by stabilization
deacetylation
|
FASN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267367 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 27758890 |
Overexpression of HA-HDAC3 decreased the acetylation level of endogenous FASN by 35% in HEK293T cells, while the expression of a catalytic inactive mutant HDAC3Y298H (38) failed to reduce FASN acetylation (Fig. 4C). Conversely, HDAC3 knockdown increased the acetylation level of endogenous FASN by >1.5-fold in HEK293T cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
trichostatin A | down-regulates activity
chemical inhibition
|
HDAC3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258012 |
|
|
in vitro |
|
| pmid |
sentence |
| 20139990 |
Collaboratively, we synthesized and assembled a panel of structurally-diverse small-molecule HDACi 1, 2, 7-20 that comprise most of the relevant literature-reported tool compounds and pharmaceutically developed clinical candidates (Supplementary Fig 3). We next conducted a high-throughput, precise profiling of HDACi potency against all Class I and II enzymes, in a miniaturized dose-ranging format (Supplementary Table 1). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257935 |
|
|
in vitro |
|
| pmid |
sentence |
| 17868033 |
Our findings suggest that hydroxamic acid-derived compounds such as TSA, NVP-LAQ824, panobinostat, ITF2357, vorinostat and belinostat act as potent pan-HDAC isoform inhibitors. A notable observation was the similarity between belinostat and vorinostat in the biochemical isoform assays; both compounds exhibit similar EC50 values in all but the HDAC8 assay. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
entinostat | down-regulates
chemical inhibition
|
HDAC3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-191481 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
4-(4-chloro-2-methylphenoxy)-N-hydroxybutanamide | down-regulates
chemical inhibition
|
HDAC3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-191430 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HDAC3 | down-regulates quantity by repression
transcriptional regulation
|
ATP6V0E2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271868 |
|
|
Mus musculus |
Macrophage |
| pmid |
sentence |
| 30375985 |
Consistent with previous data, HDAC3 only bound to the ATP6V0E2 promoter in the presence of ALDH2.|Taken together, our data demonstrate that in the macrophages of LDLR-KO or ALDH2 rs671 mutant, AMPK phosphorylates ALDH2 at T356, which enables its nuclear translocation. Once in the nucleus, ALDH2 binds to HDAC3 and suppresses the transcription and protein expression of ATP6V0E2. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
BCOR | up-regulates activity
binding
|
HDAC3 |
0.317 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252237 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10898795 |
BCoR can interact w Because HDACs appear to be involved in repression by an increasing number of transcriptional repressors, we tested whether BCoR can associate with HDACs. BCoR can interact with HDAC1, HDAC3, and HDAC-B/5 more strongly than with HDAC-A/4, HDAC-C, HDAC-D, and HDAC-E. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
tacedinaline | down-regulates activity
chemical inhibition
|
HDAC3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258007 |
|
|
in vitro |
|
| pmid |
sentence |
| 20139990 |
Collaboratively, we synthesized and assembled a panel of structurally-diverse small-molecule HDACi 1, 2, 7-20 that comprise most of the relevant literature-reported tool compounds and pharmaceutically developed clinical candidates (Supplementary Fig 3). We next conducted a high-throughput, precise profiling of HDACi potency against all Class I and II enzymes, in a miniaturized dose-ranging format (Supplementary Table 1). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
HDAC3 | up-regulates
binding
|
SMAD7 |
0.348 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-199967 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23213415 |
We show here that smad7 can form a complex with endogenous histone deacetylase proteins hdac-1 and hdac-3 in nih 3t3 mouse fibroblast cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
entinostat | down-regulates activity
chemical inhibition
|
HDAC3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257961 |
|
|
in vitro |
|
| pmid |
sentence |
| 20139990 |
Collaboratively, we synthesized and assembled a panel of structurally-diverse small-molecule HDACi 1, 2, 7-20 that comprise most of the relevant literature-reported tool compounds and pharmaceutically developed clinical candidates (Supplementary Fig 3). We next conducted a high-throughput, precise profiling of HDACi potency against all Class I and II enzymes, in a miniaturized dose-ranging format (Supplementary Table 1). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257903 |
|
|
in vitro |
|
| pmid |
sentence |
| 17868033 |
Our findings suggest that hydroxamic acid-derived compounds such as TSA, NVP-LAQ824, panobinostat, ITF2357, vorinostat and belinostat act as potent pan-HDAC isoform inhibitors. A notable observation was the similarity between belinostat and vorinostat in the biochemical isoform assays; both compounds exhibit similar EC50 values in all but the HDAC8 assay. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
ALDH2 | up-regulates activity
binding
|
HDAC3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271867 |
|
|
in vitro |
|
| pmid |
sentence |
| 28056995 |
Consistent with previous data, HDAC3 only bound to the ATP6V0E2 promoter in the presence of ALDH2.|Taken together, our data demonstrate that in the macrophages of LDLR-KO or ALDH2 rs671 mutant, AMPK phosphorylates ALDH2 at T356, which enables its nuclear translocation. Once in the nucleus, ALDH2 binds to HDAC3 and suppresses the transcription and protein expression of ATP6V0E2. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
HDAC3 | up-regulates
binding
|
HDAC1 |
0.512 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-199964 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23213415 |
Furthermore, smad7 caused hdac-1 bind to e2f-1 to form a ternary complex on chromosomal dna containing an e2f-binding motif and leading to repression in the activity of the e2f target genes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
3-[(dimethylamino)methyl]-N-[2-[4-[(hydroxyamino)-oxomethyl]phenoxy]ethyl]-2-benzofurancarboxamide | down-regulates
chemical inhibition
|
HDAC3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203476 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CCAR2 | down-regulates activity
binding
|
HDAC3 |
0.257 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267665 |
|
|
|
|
| pmid |
sentence |
| 26158765 |
Besides SIRT1, CCAR2 inhibits the activity of the histone-modifying enzymes SUV39H1 and HDAC3 [9, 10], thus playing an important role in chromatin structure regulation. |
|
| Publications: |
1 |
| + |
RB1 | up-regulates 
|
HDAC3 |
0.608 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-118839 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14560017 |
We find that active rb mediates histone deacetylation on cyclin a, cdc2, topoisomerase iialfa, and thymidylate synthase promoters. We also demonstrate that this deacetylation is hdac dependent, since the hdac inhibitor trichostatin a (tsa) prevented histone deacetylation at each promoter. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
HDAC3
- 
- 