+ |
SIRT1 | down-regulates
deacetylation
|
EP300 |
0.829 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-182507 |
Lys1020 |
EERSTELkTEIKEEE |
Homo sapiens |
Breast Cancer Cell |
pmid |
sentence |
19047049 |
Sirt1 induces deacetylation and repression of p300 itself (81). Mutational analysis demonstrated that sirt1 repression of p300 involves both lysine 1020 and lysine 1024 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-182511 |
Lys1024 |
TELKTEIkEEEDQPS |
Homo sapiens |
Breast Cancer Cell |
pmid |
sentence |
19047049 |
Sirt1 induces deacetylation and repression of p300 itself (81). Mutational analysis demonstrated that sirt1 repression of p300 involves both lysine 1020 and lysine 1024 |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | Acute Myeloid Leukemia |
+ |
EP300 | up-regulates
acetylation
|
KPNA2 |
0.363 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-128625 |
Lys22 |
HRFKNKGkDSTEMRR |
Homo sapiens |
|
pmid |
sentence |
15342649 |
Ampk triggered the acetylation of importin alpha1 on lys(22), a process dependent on the acetylase activity of p300 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
EP300 | down-regulates activity
acetylation
|
H3-3A |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-170266 |
Lys28 |
LATKAARkSAPSTGG |
Homo sapiens |
|
pmid |
sentence |
21131905 |
These results highlight the substrate and site specificities of hats in cells, demonstrate the distinct roles of gcn5/pcaf- and cbp/p300-mediated histone acetylations in gene activation, and suggest an important role of cbp/p300-mediated h3k18/27ac in nr-dependent transcription. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
EP300 | up-regulates activity
acetylation
|
RELA |
0.814 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-238778 |
Lys310 |
KRTYETFkSIMKKSP |
Homo sapiens |
NCI-H460 Cell |
pmid |
sentence |
15152190 |
Using acetylation assays, p300 was found to effectively acetylate RelA/p65 across the amino-acid region containing 1317 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Acute Myeloid Leukemia |
+ |
EP300 | up-regulates
acetylation
|
TP53 |
0.909 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-84070 |
Lys373 |
SSHLKSKkGQSTSRH |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
11070080 |
P300 acetylates and activates the tumor suppressor p53 after dna damage. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-84074 |
Lys382 |
QSTSRHKkLMFKTEG |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
11070080 |
P300 acetylates and activates the tumor suppressor p53 after dna damage. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | Acute Myeloid Leukemia, p53 in cancer |
+ |
EP300 | up-regulates quantity by stabilization
acetylation
|
SMAD3 |
0.726 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260431 |
Lys378 |
TIRMSFVkGWGAEYR |
Homo sapiens |
|
pmid |
sentence |
16862174 |
Smad proteins are crucial for the intracellular signaling of transforming growth factor-beta (TGF-beta). Upon their receptor-induced activation, Smad proteins are phosphorylated and translocated to the nucleus to activate the transcription of a select set of target genes. Here, we show that the co-activator p300/CBP bound and acetylated Smad3 as well as Smad2 in vivo, and that the acetylation was stimulated by TGF-beta.A major acetylation site of Smad3 by p300/CBP is Lys-378 in the MH2 domain (Smad3C) known to be critical for the regulation of transcriptional activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, Fibrosis, SARS-CoV FIBROSIS |
+ |
EP300 | up-regulates
acetylation
|
DUSP1 |
0.315 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-166581 |
Lys57 |
TIVRRRAkGAMGLEH |
Homo sapiens |
Macrophage |
pmid |
sentence |
20626350 |
A recent report shows that mkp1 may also be regulated by acetylation. When raw macrophages are stimulated with lps, mkp1 becomes acetylated on lys57 by p300 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
EP300 | down-regulates quantity by destabilization
acetylation
|
PCK1 |
0.526 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267604 |
Lys594 |
KEVEDIEkYLEDQVN |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
21726808 |
Acetylation Regulates Gluconeogenesis by Promoting PEPCK1 Degradation via Recruiting the UBR5 Ubiquitin Ligase|P300 Acetylates and Destabilizes PEPCK1|Furthermore, coexpression of P300 increased acetylation levels of wild-type PEPCK1, but not PEPCK13K/R, indicating that P300 acts on these lysine residues of PEPCK1 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267597 |
Lys70 |
EGILRRLkKYDNCWL |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
21726808 |
Acetylation Regulates Gluconeogenesis by Promoting PEPCK1 Degradation via Recruiting the UBR5 Ubiquitin Ligase|P300 Acetylates and Destabilizes PEPCK1|Furthermore, coexpression of P300 increased acetylation levels of wild-type PEPCK1, but not PEPCK13K/R, indicating that P300 acts on these lysine residues of PEPCK1 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267603 |
Lys71 |
GILRRLKkYDNCWLA |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
21726808 |
Acetylation Regulates Gluconeogenesis by Promoting PEPCK1 Degradation via Recruiting the UBR5 Ubiquitin Ligase|P300 Acetylates and Destabilizes PEPCK1|Furthermore, coexpression of P300 increased acetylation levels of wild-type PEPCK1, but not PEPCK13K/R, indicating that P300 acts on these lysine residues of PEPCK1 |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
EP300 | up-regulates
acetylation
|
SMAD7 |
0.476 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-135469 |
Lys64 |
RAGCCLGkAVRGAKG |
Homo sapiens |
|
pmid |
sentence |
15831498 |
Here we present evidence that smad7 interacts with the transcriptional coactivator p300, resulting in acetylation of smad7 on two lysine residues in its n terminus. Acetylation or mutation of these lysine residues stabilizes smad7 and protects it from tgfbeta-induced degradation. we have recently shown that smad7 is acetylated on lysine residues 64 and 70 by p300 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-95165 |
Lys64 |
RAGCCLGkAVRGAKG |
Homo sapiens |
|
pmid |
sentence |
12408818 |
Here we present evidence that smad7 interacts with the transcriptional coactivator p300, resulting in acetylation of smad7 on two lysine residues in its n terminus. Acetylation or mutation of these lysine residues stabilizes smad7 and protects it from tgfbeta-induced degradation. we have recently shown that smad7 is acetylated on lysine residues 64 and 70 by p300 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-95169 |
Lys70 |
GKAVRGAkGHHHPHP |
Homo sapiens |
|
pmid |
sentence |
12408818 |
Here we present evidence that smad7 interacts with the transcriptional coactivator p300, resulting in acetylation of smad7 on two lysine residues in its n terminus. Acetylation or mutation of these lysine residues stabilizes smad7 and protects it from tgfbeta-induced degradation. we have recently shown that smad7 is acetylated on lysine residues 64 and 70 by p300 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-135473 |
Lys70 |
GKAVRGAkGHHHPHP |
Homo sapiens |
|
pmid |
sentence |
15831498 |
Here we present evidence that smad7 interacts with the transcriptional coactivator p300, resulting in acetylation of smad7 on two lysine residues in its n terminus. Acetylation or mutation of these lysine residues stabilizes smad7 and protects it from tgfbeta-induced degradation. we have recently shown that smad7 is acetylated on lysine residues 64 and 70 by p300 |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, Fibrosis, SARS-CoV FIBROSIS |
+ |
CDK1 | down-regulates quantity by destabilization
phosphorylation
|
EP300 |
0.413 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276457 |
Ser1038 |
STSATQSsPAPGQSK |
Homo sapiens |
Lung Cancer Cell |
pmid |
sentence |
24530506 |
In this study, we found that p300 was highly phosphorylated and its level was decreased during mitosis and tumorigenesis. In vitro and in vivo experiments aimed showed that cyclin-dependent kinase 1 (CDK1) and ERK1/2 phosphorylated p300 on Ser1038 and Ser2039. Mutations of Ser1038 and Ser2039 increased p300 protein stability and levels. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276456 |
Ser2039 |
GLGQVGIsPLKPGTV |
Homo sapiens |
Lung Cancer Cell |
pmid |
sentence |
24530506 |
In this study, we found that p300 was highly phosphorylated and its level was decreased during mitosis and tumorigenesis. In vitro and in vivo experiments aimed showed that cyclin-dependent kinase 1 (CDK1) and ERK1/2 phosphorylated p300 on Ser1038 and Ser2039. Mutations of Ser1038 and Ser2039 increased p300 protein stability and levels. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | Acute Myeloid Leukemia |
+ |
ERK1/2 | down-regulates quantity by destabilization
phosphorylation
|
EP300 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276455 |
Ser1038 |
STSATQSsPAPGQSK |
Homo sapiens |
Lung Cancer Cell |
pmid |
sentence |
24530506 |
In this study, we found that p300 was highly phosphorylated and its level was decreased during mitosis and tumorigenesis. In vitro and in vivo experiments aimed showed that cyclin-dependent kinase 1 (CDK1) and ERK1/2 phosphorylated p300 on Ser1038 and Ser2039. Mutations of Ser1038 and Ser2039 increased p300 protein stability and levels. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276458 |
Ser2039 |
GLGQVGIsPLKPGTV |
Homo sapiens |
Lung Cancer Cell |
pmid |
sentence |
24530506 |
In this study, we found that p300 was highly phosphorylated and its level was decreased during mitosis and tumorigenesis. In vitro and in vivo experiments aimed showed that cyclin-dependent kinase 1 (CDK1) and ERK1/2 phosphorylated p300 on Ser1038 and Ser2039. Mutations of Ser1038 and Ser2039 increased p300 protein stability and levels. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | Acute Myeloid Leukemia, FLT3 in AML, COVID-19 Causal Network |
+ |
ATM | up-regulates
phosphorylation
|
EP300 |
0.411 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-165567 |
Ser106 |
GPGQVMAsQAQQSSP |
Homo sapiens |
|
pmid |
sentence |
20471956 |
Atm mediates phosphorylation of p300 in response to dna damageexpression of nonphosphorylatable serine to alanine form of p300 (s106a) destabilized both p300 and nbs1 proteins, after dna damage |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | p53 in cancer |
+ |
AKT2 | up-regulates
phosphorylation
|
EP300 |
0.333 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-148987 |
Ser1834 |
MLRRRMAsMQRTGVV |
Homo sapiens |
|
pmid |
sentence |
16926151 |
We find that suberoylanilide hydroxamic acid stimulates akt activity, which is required to phosphorylate p300 at ser(1834). Akt-mediated phosphorylation of p300 dramatically increases its acetyltransferase activity |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-158627 |
|
|
Homo sapiens |
|
pmid |
sentence |
17964260 |
Akt1 and 2 promote the association of myod with p300 and pcaf acetyltransferases, via direct phosphorylation of p300. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Tissue: |
Muscle |
+ |
AKT1 | up-regulates
phosphorylation
|
EP300 |
0.685 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-148983 |
Ser1834 |
MLRRRMAsMQRTGVV |
Homo sapiens |
|
pmid |
sentence |
16926151 |
We find that suberoylanilide hydroxamic acid stimulates akt activity, which is required to phosphorylate p300 at ser(1834). Akt-mediated phosphorylation of p300 dramatically increases its acetyltransferase activity |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-158624 |
|
|
Homo sapiens |
|
pmid |
sentence |
17964260 |
Akt1 and 2 promote the association of myod with p300 and pcaf acetyltransferases, via direct phosphorylation of p300. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Tissue: |
Muscle |
Pathways: | IGF and Myogenesis |
+ |
AKT | up-regulates
phosphorylation
|
EP300 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-244236 |
Ser1834 |
MLRRRMAsMQRTGVV |
Homo sapiens |
|
pmid |
sentence |
16926151 |
We find that suberoylanilide hydroxamic acid stimulates akt activity, which is required to phosphorylate p300 at ser(1834). Akt-mediated phosphorylation of p300 dramatically increases its acetyltransferase activity |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-244239 |
|
|
Homo sapiens |
|
pmid |
sentence |
17964260 |
Akt1 and 2 promote the association of myod with p300 and pcaf acetyltransferases, via direct phosphorylation of p300. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | Acute Myeloid Leukemia, FLT3 in AML, COVID-19 Causal Network |
+ |
ERK1/2 | up-regulates
phosphorylation
|
EP300 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-244533 |
Ser2279 |
PVQPNPMsPQQHMLP |
Homo sapiens |
|
pmid |
sentence |
17623675 |
Serine residues (ser-2279, ser-2315, and ser-2366) on the c terminus of p300 were the major signaling targets of egf. Furthermore, the c-terminal serine phosphorylation of p300 stimulated its histone acetyltransferase activity these results also constituted the first report identifying the unique p300 phosphorylation sites induced by erk2 in vivo. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-244634 |
Ser2315 |
RSPQPVPsPRPQSQP |
Homo sapiens |
|
pmid |
sentence |
17623675 |
Erk2-mediated c-terminal serine phosphorylation of p300 (ser-2279, ser-2315, and ser-2366) is vital to the regulation of epidermal growth factor-induced keratin 16 gene expression. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-244537 |
Ser2366 |
MEQGHFAsPDQNSML |
Homo sapiens |
|
pmid |
sentence |
17623675 |
Serine residues (ser-2279, ser-2315, and ser-2366) on the c terminus of p300 were the major signaling targets of egf. Furthermore, the c-terminal serine phosphorylation of p300 stimulated its histone acetyltransferase activity these results also constituted the first report identifying the unique p300 phosphorylation sites induced by erk2 in vivo. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
Pathways: | Acute Myeloid Leukemia, FLT3 in AML, COVID-19 Causal Network |
+ |
MAPK1 | up-regulates
phosphorylation
|
EP300 |
0.478 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-156887 |
Ser2279 |
PVQPNPMsPQQHMLP |
Homo sapiens |
|
pmid |
sentence |
17623675 |
Serine residues (ser-2279, ser-2315, and ser-2366) on the c terminus of p300 were the major signaling targets of egf. Furthermore, the c-terminal serine phosphorylation of p300 stimulated its histone acetyltransferase activity these results also constituted the first report identifying the unique p300 phosphorylation sites induced by erk2 in vivo. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-156891 |
Ser2315 |
RSPQPVPsPRPQSQP |
Homo sapiens |
|
pmid |
sentence |
17623675 |
Erk2-mediated c-terminal serine phosphorylation of p300 (ser-2279, ser-2315, and ser-2366) is vital to the regulation of epidermal growth factor-induced keratin 16 gene expression. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-156895 |
Ser2366 |
MEQGHFAsPDQNSML |
Homo sapiens |
|
pmid |
sentence |
17623675 |
Serine residues (ser-2279, ser-2315, and ser-2366) on the c terminus of p300 were the major signaling targets of egf. Furthermore, the c-terminal serine phosphorylation of p300 stimulated its histone acetyltransferase activity these results also constituted the first report identifying the unique p300 phosphorylation sites induced by erk2 in vivo. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
PRKCD | down-regulates
phosphorylation
|
EP300 |
0.374 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-94263 |
Ser89 |
SELLRSGsSPNLNMG |
Homo sapiens |
|
pmid |
sentence |
12379484 |
Inhibition of histone acetyltransferase function of p300 by pkcdeltawe found that pkcdelta but not classical pkc, specifically phosphorylates p300 at serine 89 in vitro and in vivo. This phosphorylation causes inhibition of p300 intrinsic hat activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKAA1 | down-regulates
phosphorylation
|
EP300 |
0.384 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-176637 |
Ser89 |
SELLRSGsSPNLNMG |
Homo sapiens |
Macrophage, Leukemia Cell, Monocyte |
pmid |
sentence |
21940946 |
The mechanism of ampk-mediated anti- inflammation involves the induction of p300 ser89 phosphor- ylation and subsequent inactivation of p300 hat activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPS6KA6 | down-regulates activity
phosphorylation
|
EP300 |
0.255 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275796 |
Ser89 |
SELLRSGsSPNLNMG |
|
|
pmid |
sentence |
34261798 |
Figure 2G shows that Ser89 phosphorylation of p300, an event that inhibits p300’s acetyltransferase activity (13), was decreased in RSK4-silenced A549 and T24 cells. Consequently, RSK4 may regulate the activity of the NFκB pathway by direct phosphorylation of p300, as recombinant RSK4 phosphorylates p300 on Ser89 in vitro |
|
Publications: |
1 |
+ |
EP300 | up-regulates quantity by expression
transcriptional regulation
|
TBXAS1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253906 |
|
|
Homo sapiens |
A-549 Cell |
pmid |
sentence |
14565864 |
We also showed that forced expression of p300 upregulated TXAS gene in a dose-dependent manner. Mutation of NF-E2 site, but not TATA or initiator site, abolished the p300-mediated activation of TXAS gene. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
EP300 | up-regulates
binding
|
SMAD1 |
0.414 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-195582 |
|
|
Homo sapiens |
|
pmid |
sentence |
22298955 |
Ski and snon also prevent smads from binding to the transcriptional coactivator p300/cbp |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-95462 |
|
|
Homo sapiens |
|
pmid |
sentence |
12419246 |
Thus, Ski/SnoN represses TGFβ signaling by multiple mechanisms. In addition to recruitment of a transcriptional repressor complex and dissociation of the transcriptional coactivator p300/CBP from the Smads |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
EP300 | up-regulates quantity by expression
transcriptional regulation
|
CPT1B |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-254260 |
|
|
Chlorocebus aethiops |
COS-1 Cell |
pmid |
sentence |
15199055 |
Furthermore, we show that the muscle carnitine palmitoyltransferase-1 and caveolin-3 promoters are directly regulated by ROR and coactivated by p300 and PGC-1. This study implicates RORs in the control of lipid homeostasis in skeletal muscle. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
PTMS | up-regulates activity
binding
|
EP300 |
0.327 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-268461 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
16150697 |
Macromolecular translocation inhibitor II (MTI-II), which was first identified as an in vitro inhibitor of binding between the highly purified glucocorticoid receptor (GR) and isolated nuclei, is an 11.5-kDa Zn2+-binding protein that is also known as ZnBP or parathymosin. MTI-II Enhances GR-dependent Transcription through Its Acidic Domain. MTI-II Enhances GR-dependent Transcription in Cooperation with SRC-1 and p300 in Vivo. CBP and p300 Coprecipitate with MTI-II in a Glucocorticoid Hormone-dependent Manner. Immunoprecipitation analysis showed that in the presence of glucocorticoid hormone, p300 and CREB-binding protein are coprecipitated with MTI-II. Furthermore, the knockdown of endogenous MTI-II by RNAi reduces the transcriptional activity of GR in cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
USP24 | up-regulates quantity by stabilization
deubiquitination
|
EP300 |
0.275 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275607 |
|
|
Homo sapiens |
A-549 Cell |
pmid |
sentence |
27991932 |
In this study, several cancer-related proteins (Bax, p300, E2F4 and securin) have been proven to be substrates of ubiquitin-specific peptidase 24 (USP24), and relevance has been shown between USP24 and its substrates in samples from clinical lung cancer patients. |Knockdown of USP24 decreases Bax and p300 levels |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
EP300 | down-regulates activity
acetylation
|
Histone H3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265328 |
|
|
Homo sapiens |
|
pmid |
sentence |
21131905 |
These results highlight the substrate and site specificities of hats in cells, demonstrate the distinct roles of gcn5/pcaf- and cbp/p300-mediated histone acetylations in gene activation, and suggest an important role of cbp/p300-mediated h3k18/27ac in nr-dependent transcription. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
EP300 | up-regulates
binding
|
MEF2A |
0.855 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-232165 |
|
|
Homo sapiens |
|
pmid |
sentence |
11796223 |
Once released from associated repressors, MEF2 is bound by the p300 coactivator, which possesses histone acetyltransferase activity. Thus, the net result of CaMK signaling to MEF2 complexes is increased histone acetylation (Ac), which relaxes chromatin and stimulates MEF2 target gene transcription. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | IGF and Myogenesis |
+ |
DTX1 | up-regulates
binding
|
EP300 |
0.389 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-110629 |
|
|
Homo sapiens |
|
pmid |
sentence |
11564735 |
We found that a significant fraction of dtx1 proteins were localized in the nucleus and physically interacted with the transcriptional coactivator p300. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
EP300 | up-regulates quantity by expression
transcriptional regulation
|
KRT16 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253904 |
|
|
Homo sapiens |
|
pmid |
sentence |
12954631 |
these results suggest that Sp1 and AP1 sites in the essential promoter region are critical for EGF response, and Sp1 showed a functional cooperation with c-Jun and coactivators p300/CBP in driving the transcriptional regulation of EGF-induced keratin 16 gene expression. The coactivators p300/CBP could collaborate with Sp1 and c-Jun in the activation of keratin 16 promoter. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MN1 | up-regulates activity
binding
|
EP300 |
0.348 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-256020 |
|
|
in vitro |
|
pmid |
sentence |
12569362 |
Taken together, our results indicate that MN1 is a transcription coactivator rather than a sequence-specific transcription factor, and that it may stimulate RAR/RXR-mediated transcription through interaction with p160 and p300. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
EP300 | up-regulates activity
acetylation
|
TP53 |
0.909 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261496 |
|
|
Homo sapiens |
|
pmid |
sentence |
25545885 |
C-terminal acetylation of p53 by p300/CBP and PCAF promotes an open conformation of p53 by preventing the occlusion of the DNA binding domain by the C-terminal tail. This enhances p53 transcriptional activity, leading to growth arrest and/or apoptosis |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Acute Myeloid Leukemia, p53 in cancer |
+ |
EP300 | up-regulates
binding
|
FLI1 |
0.296 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-202682 |
|
|
Homo sapiens |
|
pmid |
sentence |
24058639 |
P300 promotes the interaction of fli1 with hdac1 and increases the dna binding ability of fli1 through deacetylation of lysine 380 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
EP300 | form complex
binding
|
CDX2/PAX6/P300 |
0.458 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-70960 |
|
|
Homo sapiens |
|
pmid |
sentence |
10506141 |
In the present study, we investigated the interaction of cdx-2 and pax-6 with p300, a co-activator coupled to the basal transcription machinery. In transient transfection-expression experiments, we found that the transactivating effects of cdx-2 and pax-6 on the glucagon gene were greatly enhanced by the additional expression of p300. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
EP300 | up-regulates quantity
acetylation
|
RUNX2 |
0.464 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-195579 |
|
|
Homo sapiens |
|
pmid |
sentence |
22298955 |
Bmp-induced non-smad erk signaling pathway cooperatively regulates osteoblast differentiation, in part, through increasing the stability and transcriptional activity of runx2 or increasing runx2 acetylation by p300. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-167966 |
|
|
Homo sapiens |
|
pmid |
sentence |
20851880 |
These results indicate that Erk signaling increases Runx2 stability and transcriptional activity, partly via increasing p300 protein levels and histone acetyltransferase activity and subsequently increasing Runx2 acetylation by p300 |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
EP300 | down-regulates quantity by destabilization
polyubiquitination
|
TP53 |
0.909 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271418 |
|
|
Homo sapiens |
|
pmid |
sentence |
12690203 |
P53 is stabilized by the binding of p300 to the oncoprotein E1A, suggesting that p300 regulates p53 degradation. Purified p300 exhibited intrinsic ubiquitin ligase activity that was inhibited by E1A. In vitro, p300 with MDM2 catalyzed p53 polyubiquitination, whereas MDM2 catalyzed p53 monoubiquitination. E1A expression caused a decrease in polyubiquitinated but not monoubiquitinated p53 in cells. Thus, generation of the polyubiquitinated forms of p53 that are targeted for proteasome degradation requires the intrinsic ubiquitin ligase activities of MDM2 and p300. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Acute Myeloid Leukemia, p53 in cancer |
+ |
BRD3 | up-regulates activity
binding
|
EP300 |
0.322 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262044 |
|
|
Homo sapiens |
RAW-264.7 Cell |
pmid |
sentence |
28045112 |
Brd3 interacts with both IRF3 and p300, increases p300-mediated acetylation of IRF3, and enhances the association of IRF3 with p300 upon virus infection.|Brd3 enhances p300-mediated acetylation of IRF3 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SKI | down-regulates
binding
|
EP300 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-72664 |
|
|
Homo sapiens |
|
pmid |
sentence |
10575014 |
Smad2/3 interacts with c-ski through its c-terminal mh2 domain in a tgf-beta-dependent mannerc-ski is incorporated in the smad dna binding complex, interferes with the interaction of smad3 with a transcriptional co-activator, p300, and in turn recruits hdac. c-ski is thus a transcriptional co-repressor that links smads to hdac in tgf-beta signaling. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FBXO3 | down-regulates quantity by destabilization
binding
|
EP300 |
0.347 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271742 |
|
|
Homo sapiens |
BOSC-23 Cell |
pmid |
sentence |
18809579 |
O clarify the role of PML in transcription regulation, we purified the PML complex and identified Fbxo3 (Fbx3), Skp1, and Cullin1 as novel components of this complex. Fbx3 formed SCF(Fbx3) ubiquitin ligase and promoted the degradation of HIPK2 and p300 by the ubiquitin-proteasome pathway. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
EP300 | up-regulates
binding
|
MEF2C |
0.73 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-83846 |
|
|
Homo sapiens |
|
pmid |
sentence |
11062529 |
The cofactors grip-1, cbp/p300 and pcaf have hat activity and function as co-activators for mef-2c during myogenesis. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-232159 |
|
|
Homo sapiens |
|
pmid |
sentence |
11796223 |
Once released from associated repressors, MEF2 is bound by the p300 coactivator, which possesses histone acetyltransferase activity. Thus, the net result of CaMK signaling to MEF2 complexes is increased histone acetylation (Ac), which relaxes chromatin and stimulates MEF2 target gene transcription. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | IGF and Myogenesis |
+ |
Cullin 1-RBX1-Skp1 | down-regulates quantity by destabilization
polyubiquitination
|
EP300 |
0.473 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271746 |
|
|
Homo sapiens |
BOSC-23 Cell |
pmid |
sentence |
18809579 |
O clarify the role of PML in transcription regulation, we purified the PML complex and identified Fbxo3 (Fbx3), Skp1, and Cullin1 as novel components of this complex. Fbx3 formed SCF(Fbx3) ubiquitin ligase and promoted the degradation of HIPK2 and p300 by the ubiquitin-proteasome pathway. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
EP300 | up-regulates activity
acetylation
|
EP300 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262045 |
|
|
Homo sapiens |
RAW-264.7 Cell |
pmid |
sentence |
28045112 |
Brd3 interacts with both IRF3 and p300, increases p300-mediated acetylation of IRF3, and enhances the association of IRF3 with p300 upon virus infection.|Brd3 enhances p300-mediated acetylation of IRF3|Importantly, Brd3 promotes the recruitment of IRF3/p300 complex to the promoter of Ifnb1, and increases the acetylation of histone3/histone4 within the Ifnb1 promoter, leading to the enhancement of type I interferon production. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Acute Myeloid Leukemia, FLT3 in AML, COVID-19 Causal Network, Fibrosis, IGF and Myogenesis, p53 in cancer, SARS-CoV FIBROSIS |
+ |
MAML1 | up-regulates
binding, relocalization
|
EP300 |
0.635 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-145057 |
|
|
Homo sapiens |
|
pmid |
sentence |
16530044 |
Maml-1 is preassociated with other components of the transcriptional machinery, such as p300 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-184853 |
|
|
Homo sapiens |
|
pmid |
sentence |
19304754 |
We show that maml1 potentiates p300 autoacetylation and p300 transcriptional activation. Maml1 directly enhances p300 hat activity, and this coincides with the translocation of maml1, p300 and acetylated histones to nuclear bodies. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
NUP98-HOXA9 | up-regulates activity
binding
|
EP300 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261497 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
28630438 |
NUP98-HOXA9 has an activator-repressor role in transcriptional regulation driven by p300 and HDAC1 interactions. The chromosomal translocation t(7;11)(p15, p15), encoding the fusion protein NUP98-HOXA9 (NHA9), is a rare poor risk cytogenetic event in AML associated with a particularly poor prognosis.In summary, NHA9 deregulates the expression of key leukemic genes, including MEIS1-HOXA9-PBX3 complex, through the enhancer binding and the direct interaction of the fusion protein with HDAC and p300 transcriptional regulators. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
EP300 | up-regulates
binding
|
MN1 |
0.348 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-97899 |
|
|
Homo sapiens |
|
pmid |
sentence |
12569362 |
Our results indicate that mn1 is a transcription coactivator rather than a sequence-specific transcription factor, and that it may stimulate rar/rxr-mediated transcription through interaction with p160 and p300. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
EP300 | up-regulates
acetylation
|
MAML1 |
0.635 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-153035 |
|
|
Homo sapiens |
|
pmid |
sentence |
17300219 |
The n-terminal domain of maml1 directly interacts with both p300 and histones, and the p300-maml1 complex specifically acetylates histone h3 and h4 tails in chromatin. Furthermore, p300 acetylates maml1 and evolutionarily conserved lysine residues in the maml1 n-terminus are direct substrates for p300-mediated acetylation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
EP300 | up-regulates quantity by stabilization
acetylation
|
XBP1 (isoform 2) |
0.289 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260429 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
20955178 |
P300 increases the acetylation and protein stability of XBP1s, and enhances its transcriptional activity, whereas SIRT1 deacetylates XBP1s and inhibits its transcriptional activity.. The mRNA encoding the active spliced form of XBP1 (XBP1s) is generated from the unspliced form by IRE1 (inositol-requiring enzyme 1) during the UPR. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network |
+ |
EP300 | up-regulates
acetylation
|
MYOD1 |
0.667 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-81053 |
|
|
Homo sapiens |
|
pmid |
sentence |
10944526 |
Our results provide direct evidence that myod acetylation functionally activates the protein and show that both pcaf and cbp/p300 are candidate enzymes for myod acetylation in vivo. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Muscle |
Pathways: | IGF and Myogenesis |
+ |
EP300 | up-regulates
acetylation
|
PLAGL2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-140947 |
|
|
Homo sapiens |
|
pmid |
sentence |
16207715 |
Plag1 and plagl2 are also regulated by acetylation. They are acetylated and activated by p300 and deacetylated and repressed by hdac7. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
EP300 | form complex
binding
|
RUNX2/EP300 |
0.464 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255418 |
|
|
Rattus norvegicus |
ROS-17/2.8 Cell |
pmid |
sentence |
12697832 |
More interestingly, the bone-specific transcriptionfactor Runx2/Cbfa1 is present in the immunoprecipitated material, strongly indicating that in osteoblastic cells expressing OC, p300 and Runx2/Cbfa1 are components of the same nuclear protein complex. |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
+ |
EP300 | up-regulates
acetylation
|
RELA |
0.814 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-143399 |
|
|
Homo sapiens |
|
pmid |
sentence |
16382138 |
Rela is also acetylated at several sites by p300 and cbp |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Acute Myeloid Leukemia |
+ |
EP300 | up-regulates
binding
|
MEF2D |
0.732 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-232162 |
|
|
Homo sapiens |
|
pmid |
sentence |
11796223 |
Once released from associated repressors, MEF2 is bound by the p300 coactivator, which possesses histone acetyltransferase activity. Thus, the net result of CaMK signaling to MEF2 complexes is increased histone acetylation (Ac), which relaxes chromatin and stimulates MEF2 target gene transcription. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | IGF and Myogenesis |
+ |
EP300 | up-regulates
acetylation
|
PLAG1 |
0.314 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-140915 |
|
|
Homo sapiens |
|
pmid |
sentence |
16207715 |
Plag1 and plagl2 are also regulated by acetylation. They are acetylated and activated by p300 and deacetylated and repressed by hdac7. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CTNNB1 | up-regulates
binding
|
EP300 |
0.693 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-76987 |
|
|
Homo sapiens |
|
pmid |
sentence |
10775268 |
Ctnnb1 forms a ternary complex with lef1 and ep300 that is disrupted by ctnnbip1 binding |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Acute Myeloid Leukemia, FLT3 in AML |
+ |
EP300 | up-regulates quantity by expression
transcriptional regulation
|
ALOX15 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-254097 |
|
|
Homo sapiens |
A-549 Cell |
pmid |
sentence |
12517954 |
IL-4 has been shown to up-regulate 15-lipoxygenase and produce 15(S)-hydroxyeicosatetraenoic acid (15(S)-HETE) in A549 cells via the Janus kinase/STAT6 pathway under coactivation of CREB binding protein/p300. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
EP300 | up-regulates
|
Differentiation |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-229780 |
|
|
Homo sapiens |
|
pmid |
sentence |
20660310 |
Switch to beta-catenin/p300-mediated gene expression is an essential first step in initiating normal cellular differentiation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Acute Myeloid Leukemia, FLT3 in AML |
+ |
EP300 | form complex
binding
|
P300/PCAF |
0.654 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-170273 |
|
|
Homo sapiens |
|
pmid |
sentence |
21131905 |
Histone acetyltransferases (hats) gcn5 and pcaf (gcn5/pcaf) and cbp and p300 (cbp/p300) are transcription co-activators. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TTC5 | up-regulates activity
binding
|
EP300 |
0.544 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262646 |
|
|
Homo sapiens |
U2-OS Cell |
pmid |
sentence |
15448695 |
DNA damage activates ATM kinase which then phosphorylates Strap at Ser 203 (red circles). Phosphorylated Strap is stabilized and undergoes nuclear accumulation where it assembles into a co-activator complex, which includes p300 and cofactors such as JMY |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
EID1 | down-regulates activity
binding
|
EP300 |
0.431 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253379 |
|
|
|
|
pmid |
sentence |
11073989 |
Here, we show that EID-1 is a potent inhibitor of differentiation and link this activity to its ability to inhibit p300 (and the highly related molecule, CREB-binding protein, or CBP) histone acetylation activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253377 |
|
|
|
|
pmid |
sentence |
11073990 |
Inhibition of MyoD may be explained by EID-1's ability to bind and inhibit p300's histone acetylase activity, an essential MyoD coactivator. |
|
Publications: |
2 |
+ |
BRD4 | up-regulates activity
binding
|
EP300 |
0.436 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262064 |
|
|
Homo sapiens |
|
pmid |
sentence |
32544088 |
In this study, we explored the role of Brd4 and its interaction with the p300 acetyltransferase in the regulation of Nox4 and the in vivo efficacy of a BET inhibitor to reverse established age-associated lung fibrosis. |Together, these studies suggest that Brd4 enhances p300-mediated histone acetylation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MDM2 | down-regulates
binding
|
EP300 |
0.675 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-84077 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
11070080 |
Mdm2, a negative-feedback regulator of p53, inhibited p300-mediated p53 acetylation by complexing with these two proteins. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Acute Myeloid Leukemia, p53 in cancer |
+ |
EP300 | up-regulates quantity by expression
transcriptional regulation
|
CAV3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-254259 |
|
|
Chlorocebus aethiops |
COS-1 Cell |
pmid |
sentence |
15199055 |
Furthermore, we show that the muscle carnitine palmitoyltransferase-1 and caveolin-3 promoters are directly regulated by ROR and coactivated by p300 and PGC-1. This study implicates RORs in the control of lipid homeostasis in skeletal muscle. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
EP300 | form complex
binding
|
SMAD2/STAT3/EP300 |
0.674 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255025 |
|
|
Homo sapiens |
|
pmid |
sentence |
26194464 |
Thus, pSmad2L (Ser255) forms complex with p300 and STAT3 to bind to the proximal promoter of the Rorc and Il17a genes. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
BRMS1 | down-regulates quantity by destabilization
ubiquitination
|
EP300 |
0.37 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266408 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
23269275 |
BRMS1 suppresses lung cancer metastases through an E3 ligase function on histone acetyltransferase p300. BRMS1 induces polyubiquitination of p300, resulting in its proteasome-mediated degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
EP300 | form complex
binding
|
CBP/p300 |
0.524 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-110562 |
|
|
Homo sapiens |
|
pmid |
sentence |
11559745 |
P300/cbp proteins: hats for transcriptional bridges and scaffolds |
|
Publications: |
1 |
Organism: |
Homo Sapiens |