| + |
CAMK2G | down-regulates 
phosphorylation
|
HDAC5 |
0.403 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85098 |
Ser259 |
FPLRKTAsEPNLKVR |
Homo sapiens |
|
| pmid |
sentence |
| 11114197 |
Camk phosphorylates serines -259 and -498 in hdac5, which subsequently serve as docking sites for 14-3-3. Our studies suggest that 14-3-3 binding to hdac5 is required for camk-dependent disruption of mef2hdac complexes and nuclear export of hdac5, and implicate 14-3-3 as a signal-dependent regulator of muscle cell differentiation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85102 |
Ser498 |
RPLSRTQsSPLPQSP |
Homo sapiens |
|
| pmid |
sentence |
| 11114197 |
Camk phosphorylates serines -259 and -498 in hdac5, which subsequently serve as docking sites for 14-3-3. Our studies suggest that 14-3-3 binding to hdac5 is required for camk-dependent disruption of mef2hdac complexes and nuclear export of hdac5, and implicate 14-3-3 as a signal-dependent regulator of muscle cell differentiation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| + |
PRKD1 | down-regulates activity
phosphorylation
|
HDAC5 |
0.532 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249270 |
Ser259 |
FPLRKTAsEPNLKVR |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 15367659 |
Here, we demonstrate that signaling by protein kinase C (PKC) is sufficient and, in some cases, necessary to drive nuclear export of class II HDAC5 in cardiomyocytes. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
PRKD3 | up-regulates activity 
phosphorylation
|
HDAC5 |
0.268 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275926 |
Ser259 |
FPLRKTAsEPNLKVR |
|
|
| pmid |
sentence |
| 18692497 |
Histone deacetylase (HDAC) 5 and 7, two members of the class II of classical HDAC [62], are in vivo substrates of PKD3 and PKD [63]. In response to a variety of signals, including phorbol esters, T cell receptor engagement, vascular endothelial growth factor and angiotensin stimulation, the activity of HDAC5 and 7 are regulated by a mechanism that involves PKD3 and PKD-mediated phosphorylation of the highly conserved Ser259 and Ser498 residues that are located in N-terminus of class II HDACs [63–67]. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275928 |
Ser498 |
RPLSRTQsSPLPQSP |
|
|
| pmid |
sentence |
| 18692497 |
Histone deacetylase (HDAC) 5 and 7, two members of the class II of classical HDAC [62], are in vivo substrates of PKD3 and PKD [63]. In response to a variety of signals, including phorbol esters, T cell receptor engagement, vascular endothelial growth factor and angiotensin stimulation, the activity of HDAC5 and 7 are regulated by a mechanism that involves PKD3 and PKD-mediated phosphorylation of the highly conserved Ser259 and Ser498 residues that are located in N-terminus of class II HDACs [63–67]. |
|
| Publications: |
2 |
| + |
PRKCA | down-regulates activity
phosphorylation
|
HDAC5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249268 |
Ser259 |
FPLRKTAsEPNLKVR |
Rattus norvegicus |
Cardiac Muscle Fiber |
| pmid |
sentence |
| 15367659 |
We also demonstrate that protein kinase D (PKD), a downstream effector of PKC, directly phosphorylates HDAC5 and stimulates its nuclear export. | Finally, we assessed the ability of PKD to phosphorylate HDAC5 in cells by employing an antibody that specifically recognizes HDAC5 that has been phosphorylated at serine 259. HDAC5 was basally phosphorylated at serine 259, and phosphorylation at this site was dramatically increased by coexpression of constitutively active PKD S/E |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249269 |
Ser498 |
RPLSRTQsSPLPQSP |
Rattus norvegicus |
Cardiac Muscle Fiber |
| pmid |
sentence |
| 15367659 |
We also demonstrate that protein kinase D (PKD), a downstream effector of PKC, directly phosphorylates HDAC5 and stimulates its nuclear export. | Finally, we assessed the ability of PKD to phosphorylate HDAC5 in cells by employing an antibody that specifically recognizes HDAC5 that has been phosphorylated at serine 259. HDAC5 was basally phosphorylated at serine 259, and phosphorylation at this site was dramatically increased by coexpression of constitutively active PKD S/E |
|
| Publications: |
2 |
Organism: |
Rattus Norvegicus |
| + |
PRKCD | down-regulates activity
phosphorylation
|
HDAC5 |
0.359 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260875 |
Ser259 |
FPLRKTAsEPNLKVR |
Homo sapiens |
|
| pmid |
sentence |
| 18332134 |
In this report, we show that VEGF stimulates PKD-dependent phosphorylation of HDAC5 at Ser259/498residues in ECs, which leads to HDAC5 nuclear exclusion and myocyte enhancer factor-2 (MEF2) transcriptional activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260876 |
Ser498 |
RHRPLSRtQSSPLPQ |
Homo sapiens |
|
| pmid |
sentence |
| 18332134 |
In this report, we show that VEGF stimulates PKD-dependent phosphorylation of HDAC5 at Ser259/498residues in ECs, which leads to HDAC5 nuclear exclusion and myocyte enhancer factor-2 (MEF2) transcriptional activation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKD2 | up-regulates activity
phosphorylation
|
HDAC5 |
0.299 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275927 |
Ser259 |
FPLRKTAsEPNLKVR |
|
|
| pmid |
sentence |
| 18692497 |
Histone deacetylase (HDAC) 5 and 7, two members of the class II of classical HDAC [62], are in vivo substrates of PKD3 and PKD [63]. In response to a variety of signals, including phorbol esters, T cell receptor engagement, vascular endothelial growth factor and angiotensin stimulation, the activity of HDAC5 and 7 are regulated by a mechanism that involves PKD3 and PKD-mediated phosphorylation of the highly conserved Ser259 and Ser498 residues that are located in N-terminus of class II HDACs [63–67]. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275929 |
Ser498 |
RPLSRTQsSPLPQSP |
|
|
| pmid |
sentence |
| 18692497 |
Histone deacetylase (HDAC) 5 and 7, two members of the class II of classical HDAC [62], are in vivo substrates of PKD3 and PKD [63]. In response to a variety of signals, including phorbol esters, T cell receptor engagement, vascular endothelial growth factor and angiotensin stimulation, the activity of HDAC5 and 7 are regulated by a mechanism that involves PKD3 and PKD-mediated phosphorylation of the highly conserved Ser259 and Ser498 residues that are located in N-terminus of class II HDACs [63–67]. |
|
| Publications: |
2 |
| + |
CAMK4 | down-regulates
phosphorylation
|
HDAC5 |
0.49 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85106 |
Ser259 |
FPLRKTAsEPNLKVR |
Homo sapiens |
|
| pmid |
sentence |
| 11114197 |
Camk phosphorylates serines -259 and -498 in hdac5, which subsequently serve as docking sites for 14-3-3. Our studies suggest that 14-3-3 binding to hdac5 is required for camk-dependent disruption of mef2hdac complexes and nuclear export of hdac5, and implicate 14-3-3 as a signal-dependent regulator of muscle cell differentiation.Recently, camkiv, a calcium-calmodulindependent protein kinase, was also shown to activate mef2s by dissociating class ii histone deacetylases (e.g., Hdac5) from mef2s, thus relieving the transcriptional repressive effect of hdacs. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236571 |
Ser259 |
FPLRKTAsEPNLKVR |
Homo sapiens |
|
| pmid |
sentence |
| 12058061 |
Recently, camkiv, a calcium-calmodulindependent protein kinase, was also shown to activate mef2s by dissociating class ii histone deacetylases (e.g., Hdac5) from mef2s, thus relieving the transcriptional repressive effect of hdacs. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236575 |
Ser498 |
RPLSRTQsSPLPQSP |
Homo sapiens |
|
| pmid |
sentence |
| 12058061 |
Recently, camkiv, a calcium-calmodulindependent protein kinase, was also shown to activate mef2s by dissociating class ii histone deacetylases (e.g., Hdac5) from mef2s, thus relieving the transcriptional repressive effect of hdacs. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85110 |
Ser498 |
RPLSRTQsSPLPQSP |
Homo sapiens |
|
| pmid |
sentence |
| 11114197 |
Camk phosphorylates serines -259 and -498 in hdac5, which subsequently serve as docking sites for 14-3-3. Our studies suggest that 14-3-3 binding to hdac5 is required for camk-dependent disruption of mef2hdac complexes and nuclear export of hdac5, and implicate 14-3-3 as a signal-dependent regulator of muscle cell differentiation.Recently, camkiv, a calcium-calmodulindependent protein kinase, was also shown to activate mef2s by dissociating class ii histone deacetylases (e.g., Hdac5) from mef2s, thus relieving the transcriptional repressive effect of hdacs. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Muscle, Skeletal Muscle |
| Pathways: | IGF and Myogenesis |
| + |
PRKAA1 | down-regulates
phosphorylation
|
HDAC5 |
0.347 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176479 |
Ser259 |
FPLRKTAsEPNLKVR |
Homo sapiens |
|
| pmid |
sentence |
| 21892142 |
Another recently described set of transcriptional regulators targeted by ampk and its related family members across a range of eukaryotes are the class iia family of histone deacetylases (hdacs) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176483 |
Ser498 |
RPLSRTQsSPLPQSP |
Homo sapiens |
|
| pmid |
sentence |
| 21892142 |
Another recently described set of transcriptional regulators targeted by ampk and its related family members across a range of eukaryotes are the class iia family of histone deacetylases (hdacs) |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CAMK1 | down-regulates
phosphorylation
|
HDAC5 |
0.43 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85018 |
Ser259 |
FPLRKTAsEPNLKVR |
Homo sapiens |
|
| pmid |
sentence |
| 11114197 |
Camk phosphorylates serines -259 and -498 in hdac5, which subsequently serve as docking sites for 14-3-3. Our studies suggest that 14-3-3 binding to hdac5 is required for camk-dependent disruption of mef2hdac complexes and nuclear export of hdac5, and implicate 14-3-3 as a signal-dependent regulator of muscle cell differentiation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85022 |
Ser498 |
RPLSRTQsSPLPQSP |
Homo sapiens |
|
| pmid |
sentence |
| 11114197 |
Camk phosphorylates serines -259 and -498 in hdac5, which subsequently serve as docking sites for 14-3-3. Our studies suggest that 14-3-3 binding to hdac5 is required for camk-dependent disruption of mef2hdac complexes and nuclear export of hdac5, and implicate 14-3-3 as a signal-dependent regulator of muscle cell differentiation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| + |
AMPK | down-regulates
phosphorylation
|
HDAC5 |
0.316 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216596 |
Ser259 |
FPLRKTAsEPNLKVR |
Homo sapiens |
|
| pmid |
sentence |
| 21892142 |
Another recently described set of transcriptional regulators targeted by ampk and its related family members across a range of eukaryotes are the class iia family of histone deacetylases (hdacs) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216550 |
Ser498 |
RPLSRTQsSPLPQSP |
Homo sapiens |
|
| pmid |
sentence |
| 21892142 |
Another recently described set of transcriptional regulators targeted by ampk and its related family members across a range of eukaryotes are the class iia family of histone deacetylases (hdacs) |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
AURKB | down-regulates
phosphorylation
|
HDAC5 |
0.261 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-198650 |
Ser278 |
QKVAERRsSPLLRRK |
Homo sapiens |
|
| pmid |
sentence |
| 22865920 |
We define the precise site of aurb-mediated phosphorylation as a conserved serine within the nuclear localization signals of hdac4, hdac5, and hdac9 at ser265, ser278, and ser242, respectivelyduring mitosis, aurb-mediated phosphorylation may localize class iia hdacs to a phosphorylation gradient at the spindle midzone, permitting temporal and spatial regulatory mechanisms altering hdac protein interactions |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKACA | up-regulates activity
phosphorylation
|
HDAC5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-198658 |
Ser279 |
KVAERRSsPLLRRKD |
Homo sapiens |
|
| pmid |
sentence |
| 22865920 |
PKA/Cdk5-mediated phosphorylation of HDAC5 at Ser279 within the NLS promotes nuclear localization of HDAC5 and interaction with the nuclear corepressor complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DYRK1B | down-regulates activity
phosphorylation
|
HDAC5 |
0.38 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235809 |
Ser279 |
KVAERRSsPLLRRKD |
Mus musculus |
|
| pmid |
sentence |
| 15546868 |
Mirk activated mef2 not through direct phosphorylation of mef2 but by phosphorylation of its inhibitors, the class ii histone deacetylases (hdacs). Mef2 is sequestered by class ii hdacs such as hdac5 and mef2-interacting transcriptional repressor (mitr). Mirk antagonized the inhibition of mef2c by mitr, whereas kinase-inactive mirk was ineffective. Mirk phosphorylates class ii hdacs at a conserved site within the nuclear localization region, reducing their nuclear accumulation in a dose-dependent and kinase-dependent mannermirk phosphorylates hdac5 at ser-279 |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PRKD1 | down-regulates
phosphorylation
|
HDAC5 |
0.532 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-198662 |
Ser498 |
RPLSRTQsSPLPQSP |
Homo sapiens |
|
| pmid |
sentence |
| 22865920 |
When phosphorylated by camk/pkd, class iia hdacs bind 14-3-3 chaperone proteins, which facilitates their nuclear export, thereby relieving hdac-mediated transcriptional repression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
6-(1,3-dioxo-2-benzo[de]isoquinolinyl)-N-hydroxyhexanamide | down-regulates activity
chemical inhibition
|
HDAC5 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258005 |
|
|
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 |
| + |
HDAC5 | down-regulates activity
deacetylation
|
RUNX2 |
0.47 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-227550 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16613856 |
HDAC4 and HDAC5 deacetylate Runx2, allowing the protein to undergo Smurf-mediated degradation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BCOR | up-regulates activity
binding
|
HDAC5 |
0.53 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252238 |
|
|
Homo sapiens |
HEK-293 Cell |
| 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 |
| + |
CUDC-101 | down-regulates activity
chemical inhibition
|
HDAC5 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262261 |
|
|
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 |
| + |
14-3-3 | down-regulates
binding
|
HDAC5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-89444 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12058061 |
In the cytoplasm, 14-3-3 proteins bind the phosphorylated hdac5 and retain it in the cytosol. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Skeletal Muscle |
| + |
N-hydroxy-3-[4-[[2-hydroxyethyl-[2-(1H-indol-3-yl)ethyl]amino]methyl]phenyl]-2-propenamide | down-regulates activity
chemical inhibition
|
HDAC5 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257987 |
|
|
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 |
| + |
HDAC5 | down-regulates
binding
|
MEF2D |
0.698 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-84029 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11062529 |
The histone deacetylase hdac-5, upon dephosphorylation and translocation to the nucleus, directly inactivates mef2, preventing myogenesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | IGF and Myogenesis |
| + |
HDAC5 | down-regulates
deacetylation
|
RUNX2 |
0.47 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-145983 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16613856 |
Hdac4 and hdac5 deacetylate runx2 and lead to a smurf-mediated degradation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-195606 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22298955 |
Hdac4 and hdac5 deacetylate runx2 and lead to a smurf-mediated degradation |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
trichostatin A | down-regulates activity
chemical inhibition
|
HDAC5 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258010 |
|
|
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 |
| + |
HDAC5 | down-regulates
binding
|
MEF2C |
0.684 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-84026 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11062529 |
The histone deacetylase hdac-5, upon dephosphorylation and translocation to the nucleus, directly inactivates mef2, preventing myogenesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | IGF and Myogenesis |
| + |
N-[4-[(hydroxyamino)-oxomethyl]phenyl]carbamic acid [6-(diethylaminomethyl)-2-naphthalenyl]methyl ester | down-regulates activity
chemical inhibition
|
HDAC5 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257969 |
|
|
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 |
| + |
belinostat | down-regulates activity
chemical inhibition
|
HDAC5 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257960 |
|
|
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 |
| + |
BCORL1 | up-regulates activity
binding
|
HDAC5 |
0.451 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259113 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 17379597 |
BCoR-L1 interacts with Class II HDACs, HDAC4, HDAC5, and HDAC7, suggesting that they are involved in its function as transcriptional corepressor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
romidepsin | down-regulates activity
chemical inhibition
|
HDAC5 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257989 |
|
|
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 |
| + |
HDAC5 | down-regulates
binding
|
MEF2A |
0.694 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-84023 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11062529 |
The histone deacetylase hdac-5, upon dephosphorylation and translocation to the nucleus, directly inactivates mef2, preventing myogenesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | IGF and Myogenesis |
| + |
vorinostat | down-regulates activity
chemical inhibition
|
HDAC5 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257947 |
|
|
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 |
3.0
HDAC5
- 
- 