| + |
ERK1/2 | up-regulates quantity by stabilization 
phosphorylation
|
BCL2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244501 |
Ser70 |
RDPVARTsPLQTPAA |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 10677502 |
Erk1 and erk2 directly phosphorylate bcl2 exclusively at ser-70. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244505 |
Ser87 |
AAAGPALsPVPPVVH |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 10669763 |
The results of this study reveal the following novel findings: destruction of the three putative MAP kinase sites at positions 56, 74, and 87 results in ubiquitination and subsequent degradation of the protein. Progressive inactivation of these MAP kinase sites revealed that Bcl-2 stability is mainly regulated by phosphorylation at Thr74 and Ser87, with Ser87 phosphorylation playing a predominant role. TNF-α or the MAP kinase-specific inhibitor PD98059 diminishes Ser87 phosphorylation of Bcl-2 in vivo, while activated ERK2 induces phosphorylation of Bcl-2 in vivo and in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244610 |
Thr56 |
FSSQPGHtPHPAASR |
Homo sapiens |
|
| pmid |
sentence |
| 10669763 |
The results of this study reveal the following novel findings: destruction of the three putative MAP kinase sites at positions 56, 74, and 87 results in ubiquitination and subsequent degradation of the protein. Progressive inactivation of these MAP kinase sites revealed that Bcl-2 stability is mainly regulated by phosphorylation at Thr74 and Ser87. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244494 |
Thr74 |
ARTSPLQtPAAPGAA |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 10669763 |
The results of this study reveal the following novel findings: destruction of the three putative MAP kinase sites at positions 56, 74, and 87 results in ubiquitination and subsequent degradation of the protein. Progressive inactivation of these MAP kinase sites revealed that Bcl-2 stability is mainly regulated by phosphorylation at Thr74 and Ser87, with Ser87 phosphorylation playing a predominant role. TNF-α or the MAP kinase-specific inhibitor PD98059 diminishes Ser87 phosphorylation of Bcl-2 in vivo, while activated ERK2 induces phosphorylation of Bcl-2 in vivo and in vitro. |
|
| Publications: |
4 |
Organism: |
Chlorocebus Aethiops, Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, BCR-ABL in AML, FLT3 in AML, KIT in AML, AML_TRIPLETS, COVID-19 Causal Network, Colorectal Carcinoma, FLT3-ITD signaling, Inhibition of Apoptosis, Malignant Melanoma, Triple mutant AML, NPM1_new, Non-small-cell lung cancer (NSCLC), SARS-CoV MAPK PERTURBATION |
| + |
PPP2R5B | down-regulates 
dephosphorylation
|
BCL2 |
0.308 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-181559 |
Ser70 |
RDPVARTsPLQTPAA |
Homo sapiens |
|
| pmid |
sentence |
| 18845789 |
Pp2a directly interacts with the bh4 domain of bcl2 as a docking site to potentially bridge pp2a to bcl2's flexible loop domain containing the target serine 70 phosphorylation site. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK8 | up-regulates
phosphorylation
|
BCL2 |
0.567 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-72125 |
Ser70 |
RDPVARTsPLQTPAA |
Homo sapiens |
|
| pmid |
sentence |
| 10567572 |
G(2)/m-phase cells proved more susceptible to death signals, and phosphorylation of bcl-2 appeared to be responsible, as a ser70ala substitution restored resistance to apoptosis. We noted that ask1 and jnk1 were normally activated at g(2)/m phase, and jnk was capable of phosphorylating bcl-2.. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179088 |
Ser70 |
RDPVARTsPLQTPAA |
Homo sapiens |
|
| pmid |
sentence |
| 18570871 |
Together, our findings demonstrate that jnk1-mediated multisite phosphorylation of bcl-2 stimulates starvation-induced autophagy by disrupting the bcl-2/beclin 1 complex. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, COVID-19 Causal Network |
| + |
MAPK3 | up-regulates
phosphorylation
|
BCL2 |
0.544 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-74935 |
Ser70 |
RDPVARTsPLQTPAA |
Homo sapiens |
|
| pmid |
sentence |
| 10669763 |
Erk1 and erk2 directly phosphorylate bcl2 exclusively at ser-70 p44mapk/extracellular signal-regulated kinase 1 (erk1) and p42 mapk/erk2 are activated by il-3, colocalize with mitochondrial bcl2, and can directly phosphorylate bcl2 on ser-70 in a stauro-resistant manner both in vitro and in vivo molecular association. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
JNK | up-regulates activity
phosphorylation
|
BCL2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261133 |
Ser70 |
RDPVARTsPLQTPAA |
in vitro |
|
| pmid |
sentence |
| 11323415 |
JNK1 directly phosphorylates Bcl2 at Ser70 in vitro and co-localizes with Bcl2 in mitochondrial membranes in vivo. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | COVID-19 Causal Network, FLT3-ITD signaling, SARS-CoV MAPK PERTURBATION |
| + |
MAPK1 | up-regulates quantity by stabilization
phosphorylation
|
BCL2 |
0.535 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-219217 |
Ser70 |
RDPVARTsPLQTPAA |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 10677502 |
Erk1 and erk2 directly phosphorylate bcl2 exclusively at ser-70. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-74919 |
Ser70 |
RDPVARTsPLQTPAA |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 10669763 |
Phosphorylation of the map kinase sites in bcl-2, thr56, thr74, and ser87, is sufficient to inhibit tnf--induced degradation. p44mapk/extracellular signal-regulated kinase 1 (erk1) and p42 mapk/erk2 are activated by il-3, colocalize with mitochondrial bcl2, and can directly phosphorylate bcl2 on ser-70 in a stauro-resistant manner both_ in vitro_ and_ in vivo. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-74931 |
Ser87 |
AAAGPALsPVPPVVH |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 10669763 |
Phosphorylation of the map kinase sites in bcl-2, thr56, thr74, and ser87, is sufficient to inhibit tnf--induced degradation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-74923 |
Thr56 |
FSSQPGHtPHPAASR |
Homo sapiens |
|
| pmid |
sentence |
| 10669763 |
Phosphorylation of the map kinase sites in bcl-2, thr56, thr74, and ser87, is sufficient to inhibit tnf--induced degradation. p44mapk/extracellular signal-regulated kinase 1 (erk1) and p42 mapk/erk2 are activated by il-3, colocalize with mitochondrial bcl2, and can directly phosphorylate bcl2 on ser-70 in a stauro-resistant manner both_ in vitro_ and_ in vivo. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-74927 |
Thr74 |
ARTSPLQtPAAPGAA |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 10669763 |
In endothelial cells, tumor necrosis factor alpha (tnf-alpha) induces dephosphorylation and subsequent ubiquitin-dependent degradation of the antiapoptotic protein bcl-2. Here, we investigate the role of different putative phosphorylation sites to facilitate bcl-2 degradation |
|
| Publications: |
5 |
Organism: |
Chlorocebus Aethiops, Homo Sapiens |
| + |
PRKCA | up-regulates
phosphorylation
|
BCL2 |
0.354 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-60120 |
Ser70 |
RDPVARTsPLQTPAA |
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 9738012 |
Purified pkca can efficiently and directly phosphorylate bcl2 at serine 70 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP2CA | up-regulates activity
dephosphorylation
|
BCL2 |
0.459 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248624 |
Ser87 |
AAAGPALsPVPPVVH |
Homo sapiens |
|
| pmid |
sentence |
| 15225643 |
The phosphorylation of Bcl-2 resulted in a reduction in anti-apoptotic function, implying that dephosphorylation promoted the anti-apoptotic activity of Bcl-2 protein in human tumor cell lines. Thus, the present findings suggest that ERK and PP2A are physiological regulators of Bcl-2 phosphorylation, and these enzymes exert an influence on the anti-apoptotic function of Bcl-2.phosphorylation of Bcl2 at Ser70 is proposed to be a dynamic process regulated by the sequential action of an agonist-activated Bcl2 kinase and PP2A. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network |
| + |
PPP2CB | up-regulates activity
dephosphorylation
|
BCL2 |
0.372 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248589 |
Ser87 |
AAAGPALsPVPPVVH |
Homo sapiens |
|
| pmid |
sentence |
| 15225643 |
The phosphorylation of Bcl-2 resulted in a reduction in anti-apoptotic function, implying that dephosphorylation promoted the anti-apoptotic activity of Bcl-2 protein in human tumor cell lines. Thus, the present findings suggest that ERK and PP2A are physiological regulators of Bcl-2 phosphorylation, and these enzymes exert an influence on the anti-apoptotic function of Bcl-2.phosphorylation of Bcl2 at Ser70 is proposed to be a dynamic process regulated by the sequential action of an agonist-activated Bcl2 kinase and PP2A. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
p38 | down-regulates activity
phosphorylation
|
BCL2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260450 |
Ser87 |
AAAGPALsPVPPVVH |
Homo sapiens |
|
| pmid |
sentence |
| 19336399 |
The protein's reduced antiapoptotic capacity was related to phosphorylation of its threonine 56 and serine 87 residues by virally activated p38mapk |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, SARS-COV APOPTOSIS, SARS-CoV MAPK PERTURBATION |
| + |
MAPK14 | down-regulates activity
phosphorylation
|
BCL2 |
0.338 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-184936 |
Ser87 |
AAAGPALsPVPPVVH |
Homo sapiens |
|
| pmid |
sentence |
| 19336399 |
The protein's reduced antiapoptotic capacity was related to phosphorylation of its threonine 56 and serine 87 residues by virally activated p38mapk |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-146786 |
Thr56 |
FSSQPGHtPHPAASR |
Homo sapiens |
|
| pmid |
sentence |
| 16714293 |
Bcl-2 phosphorylation by p38 mapkin this study, we identify, by using mass spectrometry techniques and specific anti-phosphopeptide antibodies, ser(87) and thr(56) as the bcl-2 residues phosphorylated by p38 mapk and show that phosphorylation of these residues is always associated with a decrease in the antiapoptotic potential of bcl-2 protein. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | FLT3-ITD signaling |
| + |
MAPK8 | down-regulates activity
phosphorylation
|
BCL2 |
0.567 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-48038 |
Ser87 |
AAAGPALsPVPPVVH |
Homo sapiens |
|
| pmid |
sentence |
| 10567572 |
Jnk1-mediated phosphorylation of bcl-2 regulates starvation-induced autophagy. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179092 |
Ser87 |
AAAGPALsPVPPVVH |
Homo sapiens |
|
| pmid |
sentence |
| 18570871 |
Jnk1-mediated phosphorylation of bcl-2 regulates starvation-induced autophagy. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, COVID-19 Causal Network |
| + |
CDK1 | up-regulates activity
phosphorylation
|
BCL2 |
0.35 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-76837 |
Thr56 |
FSSQPGHtPHPAASR |
Homo sapiens |
|
| pmid |
sentence |
| 10766756 |
Using synthetic peptides and mutant cell lines, we identified threonine 56, one of two consensus sites for cdc2 within the bcl-2 sequence, as a residue phosphorylated by cdc2. Mutation at threonine 56 abrogated the cell cycle inhibitory effect of bcl-2 without affecting anti-apoptotic function.Taken together, our present findings indicate that phosphorylation of bcl-2 at threonine 56 by cdc2 is required for bcl-2-mediated cell cycle inhibition, which may have some roles during mitosis in the normal cell cycle. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, KIT in AML |
| + |
MAPK3 | up-regulates quantity by stabilization
phosphorylation
|
BCL2 |
0.544 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-74939 |
Thr56 |
FSSQPGHtPHPAASR |
Homo sapiens |
|
| pmid |
sentence |
| 10669763 |
Phosphorylation of the map kinase sites in bcl-2, thr56, thr74, and ser87, is sufficient to inhibit tnf--induced degradation. p44mapk/extracellular signal-regulated kinase 1 (erk1) and p42 mapk/erk2 are activated by il-3, colocalize with mitochondrial bcl2, and can directly phosphorylate bcl2 on ser-70 in a stauro-resistant manner both_ in vitro_ and_ in vivo. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-74943 |
Thr74 |
ARTSPLQtPAAPGAA |
Homo sapiens |
|
| pmid |
sentence |
| 10669763 |
The results of this study reveal the following novel findings: destruction of the three putative MAP kinase sites at positions 56, 74, and 87 results in ubiquitination and subsequent degradation of the protein. Progressive inactivation of these MAP kinase sites revealed that Bcl-2 stability is mainly regulated by phosphorylation at Thr74 and Ser87, with Ser87 phosphorylation playing a predominant role. TNF-α or the MAP kinase-specific inhibitor PD98059 diminishes Ser87 phosphorylation of Bcl-2 in vivo, while activated ERK2 induces phosphorylation of Bcl-2 in vivo and in vitro. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
MAPK8 | down-regulates
phosphorylation
|
BCL2 |
0.567 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179096 |
Thr69 |
SRDPVARtSPLQTPA |
Homo sapiens |
|
| pmid |
sentence |
| 18570871 |
Together, our findings demonstrate that jnk1-mediated multisite phosphorylation of bcl-2 stimulates starvation-induced autophagy by disrupting the bcl-2/beclin 1 complex. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-72361 |
Thr69 |
SRDPVARtSPLQTPA |
Homo sapiens |
|
| pmid |
sentence |
| 10567572 |
G(2)/m-phase cells proved more susceptible to death signals, and phosphorylation of bcl-2 appeared to be responsible, as a ser70ala substitution restored resistance to apoptosis. We noted that ask1 and jnk1 were normally activated at g(2)/m phase, and jnk was capable of phosphorylating bcl-2.. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-72364 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10567572 |
Jnk was capable of phosphorylating bcl-2. Phosphorylation of bcl-2 inactivates the molecule |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, COVID-19 Causal Network |
| + |
4-[4-[[2-(4-chlorophenyl)-5,5-dimethyl-1-cyclohexenyl]methyl]-1-piperazinyl]-N-[4-[[(2R)-4-(4-morpholinyl)-1-(phenylthio)butan-2-yl]amino]-3-(trifluoromethylsulfonyl)phenyl]sulfonylbenzamide | down-regulates
chemical inhibition
|
BCL2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-200460 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23336025 |
Bcl-2 inhibitors physically antagonize their anti-apoptotic actions to create a synergistic effect. Numerous compounds have been specifically developed or identified as bcl-2 inhibitors. These compounds include abt-737 and abt-263, obatoclax, gossypol. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-189150 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
BCL2 | down-regulates
binding
|
BECN1 |
0.732 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-156941 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17643073 |
In mammalian cells, the antiapoptotic protein, bcl-2, binds to beclin 1 during nonstarvation conditions and inhibits its autophagy function. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179084 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18570871 |
In mammalian cells, the antiapoptotic protein, bcl-2, binds to beclin 1 during nonstarvation conditions and inhibits its autophagy function. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-154477 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17446862 |
In mammalian cells, the antiapoptotic protein, bcl-2, binds to beclin 1 during nonstarvation conditions and inhibits its autophagy function. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Pathways: | Autophagy |
| + |
CREB1 | up-regulates quantity by expression 
transcriptional regulation
|
BCL2 |
0.442 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-43927 |
|
|
Homo sapiens |
B-lymphocyte, RAMOS Cell |
| pmid |
sentence |
| 8816467 |
Induction of bcl-2 expression by phosphorylated CREB proteins during B-cell activation and rescue from apoptosis |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-76558 |
|
|
Rattus norvegicus |
PC-12 Cell |
| pmid |
sentence |
| 10753867 |
Creb activity by akt signaling leads to increased bcl-2 promoter activity and cell survival. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, Rattus Norvegicus |
| Pathways: | COVID-19 Causal Network, FLT3-ITD signaling, Inhibition of Apoptosis, Malignant Melanoma, SARS-CoV MAPK PERTURBATION |
| + |
BBC3 | down-regulates activity
binding
|
BCL2 |
0.651 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109506 |
|
|
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 11463392 |
Puma localizes to the mitochondria, interacts with bcl-2, and function to induce cytochrome c release |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-133808 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15694340 |
Only bimbh3 and bbc3 had comparable strong affinitiesfor all the prosurvival proteins. The members that promote cell survival, including mammalian bcl-2, bcl-xl,bcl-w, mcl-1, and a1. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Death Receptor Signaling, Mitochondrial Control of Apoptosis |
| + |
N-[4-(2-tert-butylphenyl)sulfonylphenyl]-2,3,4-trihydroxy-5-[(2-propan-2-ylphenyl)methyl]benzamide | down-regulates
chemical inhibition
|
BCL2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-207459 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HMOX1 | up-regulates quantity by expression
transcriptional regulation
|
BCL2 |
0.252 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256303 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26722274 |
The results of the present study indicated that knockdown of HMOX-1 significantly enhanced doxorubicin-induced apoptosis and downregulated the expression of Bcl-2 and Bcl-xL in breast cancer cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SOD1 | up-regulates activity
binding
|
BCL2 |
0.491 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262799 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15233914 |
Familial amyotrophic lateral sclerosis (ALS)-linked mutations in the copper-zinc superoxide dismutase (SOD1) gene cause motor neuron death in about 3% of ALS cases. While the wild-type (wt) protein is anti-apoptotic, mutant SOD1 promotes apoptosis.|We now demonstrate that both wt and mutant SOD1 bind the anti-apoptotic protein Bcl-2, providing evidence of a direct link between SOD1 and an apoptotic pathway. This interaction is evident in vitro and in vivo in mouse and human spinal cord.|These findings provide new insights into the anti-apoptotic function of SOD1 and suggest that entrapment of Bcl-2 by large SOD1 aggregates may deplete motor neurons of this anti-apoptotic protein. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Spinal Cord |
| Pathways: | Autophagy |
| + |
BCL2 | down-regulates activity 
|
CYCS |
0.633 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-99063 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 12624108 |
Bcl-2 blocked the release of mitochondrial cytochrome c |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Alzheimer, COVID-19 Causal Network, Death Receptor Signaling, Mitochondrial Control of Apoptosis, SARS-COV APOPTOSIS |
| + |
NOTCH1 | up-regulates quantity by expression
transcriptional regulation
|
BCL2 |
0.266 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149730 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 16990763 |
Other notch target genes identi__ed in the thymoma cell line were dtx1 (gene for deltex1), i__-202, i__-204, i__-d3, adam19 (meltrinb).24 a number of other genes have been reported as being notch targets, including notch1 itself,28 nrarp in xenopus embryos,29 bcl2 in thymoma cells,30 ccnd1 (gene for cyclin d1) in a kidney cell line,31 dkn1a (gene for cyclindependent kinase inhibitor 1a (p21, cip1)) in keratinocytes32 and tcf3 (gene for e2a). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, FLT3-ITD signaling |
| + |
BCL2 | down-regulates
binding
|
BAK1 |
0.664 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-152980 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17289999 |
Bax is held in check by mcl1, bcl-2, and either bcl2l1 or bcl2l2, or by all four. They bind a primed conformer of bak or bax bax/bak are kept in check by the pro-survival bcl-2 family members and also proposes that for apoptotic death to occur, all pro-survival bcl-2-like proteins present within a given cell need to be neutralised by bh3-only proteins, thereby derepressing bax/bak |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-55546 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9463381 |
Bcl-2 bind to bax or five other pro-apoptotic relatives (bak, bad, bik, bid or bim) |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, MLL fusion protein in AML, Malignant Melanoma, Non-small-cell lung cancer (NSCLC) |
| + |
BCL2 | down-regulates
|
DIABLO |
0.476 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-88885 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14585074 |
Bcl- confers protection to apoptosis by interference with bax/bak-mediated release of the pro-apoptotic mitochodrial factors smac/diablo and htra2/omi |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Death Receptor Signaling |
| + |
RHOXF1 | up-regulates quantity by expression
transcriptional regulation
|
BCL2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268957 |
|
|
|
|
| pmid |
sentence |
| 23317270 |
ShRNA knock down of RHOXF1 resulted in significantly decreased BCL2 expression in both cell lines but no change in CASP8 expression. |
|
| Publications: |
1 |
| + |
Gbeta | up-regulates
phosphorylation
|
BCL2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270064 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10669763 |
Erk1 and erk2 directly phosphorylate bcl2 exclusively at ser-70 p44mapk/extracellular signal-regulated kinase 1 (erk1) and p42 mapk/erk2 are activated by il-3, colocalize with mitochondrial bcl2, and can directly phosphorylate bcl2 on ser-70 in a stauro-resistant manner both in vitro and in vivo molecular association. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RBM10 | down-regulates quantity by repression
transcriptional regulation
|
BCL2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259151 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30403180 |
In this study, we report that RBM10 acts as a tumor suppressor in osteosarcoma via the inhibition of cell growth, cell migration and invasion and the induction of cell apoptosis by inhibiting Bcl-2, activating caspase-3, and producing TNF-α. We also found that RBM10 overexpression significantly inhibited the expression of Bcl-2 and induced the expression of caspase-3 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMAD3 | down-regulates quantity by repression
transcriptional regulation
|
BCL2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256294 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16766264 |
This protection is conferred by Smad3’s ability to promote apoptosis by repressing Bcl-2 transcription in vivo through a GC-rich element in the Bcl-2 promoter. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, Colorectal Carcinoma |
| + |
BCL2 | down-regulates
|
Cell_death |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256637 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 1286168 |
Bcl-2 functions to inhibit apoptosis in a variety of in vitro and in vivo experiments, suggesting interference with a central mechanism of apoptosis |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TP53 | down-regulates activity
binding
|
BCL2 |
0.742 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-99712 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19007744 |
Mechanistic insights into the mitochondrial function of wtp53 came when it was realized that mitochondrially translocated p53 interacts directly with members of the Bcl-2 family, which are central in governing the induction of mitochondrial outer membrane permeabilization. In response to stress, wtp53 interacts with and neutralizes the anti-apoptotic members Bcl-xL and Bcl-2. This interaction stimulates MOMP and subsequent apoptosis |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, DNMT3A in AML, KIT in AML, miRNA in AML, AML_TRIPLETS, Colorectal Carcinoma, FLT3-ITD signaling, Mitochondrial Control of Apoptosis, Malignant Melanoma, Triple mutant AML, NPM1_new, Non-small-cell lung cancer (NSCLC), p53 in cancer |
| + |
NR4A3 | down-regulates activity
binding
|
BCL2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259399 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30455429 |
NR4A3 physically interacted with an anti-apoptotic Bcl-2 protein hence sequestering it from blunting apoptosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TP53 | down-regulates quantity by repression
transcriptional regulation
|
BCL2 |
0.742 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271677 |
|
|
|
|
| pmid |
sentence |
| 10329733 |
P53 suppresses the activation of the Bcl-2 promoter by the Brn-3a POU family transcription factor. |
|
| Publications: |
1 |
| Pathways: | Acute Myeloid Leukemia, DNMT3A in AML, KIT in AML, miRNA in AML, AML_TRIPLETS, Colorectal Carcinoma, FLT3-ITD signaling, Mitochondrial Control of Apoptosis, Malignant Melanoma, Triple mutant AML, NPM1_new, Non-small-cell lung cancer (NSCLC), p53 in cancer |
| + |
NOXA1 | down-regulates activity
|
BCL2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-209684 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19879762 |
BH3-only proteins containing only a single BH domain and including Puma, Noxa, Bid and Bad as well as other factors are particularly important for such neutralisation, binding and regulating the anti-apoptotic Bcl-2 proteins to promote apoptosis |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Mitochondrial Control of Apoptosis |
| + |
Obatoclax mesylate | down-regulates
chemical inhibition
|
BCL2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-194952 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
A5/b1 integrin | up-regulates quantity
|
BCL2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253310 |
|
|
|
|
| pmid |
sentence |
| 15721307 |
Previous reports indicated that the prosurvival signal mediated through α5β1-fibronectin interactions was due to increased Bcl-2 levels |
|
| Publications: |
1 |
| + |
MYCT1 | down-regulates quantity by repression
transcriptional regulation
|
BCL2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261735 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30283340 |
MYCT1 overexpression significantly inhibited cell proliferation, arrested cell cycle at G0/G1 phase, and downregulated the expression of cyclins D and E. Moreover, MYCT1 overexpression triggered apoptosis in AML cells, which was accompanied by enhanced cleavage of caspase-3 and -9, upregulated expression of B-cell lymphoma 2 (Bcl-2)-associated X protein (Bax), and downregulated Bcl-2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NOTCH | up-regulates quantity by expression
transcriptional regulation
|
BCL2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254344 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 16990763 |
Addition of jag-1 peptide induced ikkalpha mediated nf-kappab activation, as well as increased ppargamma expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia |
| + |
Obatoclax | down-regulates
chemical inhibition
|
BCL2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-200478 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23336025 |
Bcl-2 inhibitors physically antagonize their anti-apoptotic actions to create a synergistic effect. Numerous compounds have been specifically developed or identified as bcl-2 inhibitors. These compounds include abt-737 and abt-263, obatoclax, gossypol. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BCL2L11 | down-regulates
binding
|
BCL2 |
0.812 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-133823 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15694340 |
Bim can induce apoptosis by interacting with anti-apoptotic members of the bcl2 family, including bcl2, bcl-xl and mcl-1.. Bim binds prosurvival proteins comparably. The members that promote cell survival, including mammalian bcl-2, bcl-xl,bcl-w, mcl-1, and a1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, Inhibition of Apoptosis, Mitochondrial Control of Apoptosis, SARS-COV APOPTOSIS |
| + |
BAX | down-regulates activity
binding
|
BCL2 |
0.622 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249612 |
|
|
|
|
| pmid |
sentence |
| 8358790 |
Bax shows extensive amino acid homology with Bcl-2 and forms homodimers and heterodimers with Bcl-2 in vivo. When Bax predominates, programed cell death is accelerated, and the death repressor activity of Bcl-2 is countered. |
|
| Publications: |
1 |
| Pathways: | Alzheimer, Acute Myeloid Leukemia, MLL fusion protein in AML, COVID-19 Causal Network, Death Receptor Signaling, FLT3-ITD signaling, Inhibition of Apoptosis, Mitochondrial Control of Apoptosis, Malignant Melanoma, p53 in cancer, SARS-COV APOPTOSIS |
| + |
gossypol | down-regulates
chemical inhibition
|
BCL2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-200469 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23336025 |
Bcl-2 inhibitors physically antagonize their anti-apoptotic actions to create a synergistic effect. Numerous compounds have been specifically developed or identified as bcl-2 inhibitors. These compounds include abt-737 and abt-263, obatoclax, gossypol. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GLI1/GLI2 | up-regulates quantity by expression
transcriptional regulation
|
BCL2 |
0.385 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269211 |
|
|
Homo sapiens |
PANC-1 Cell |
| pmid |
sentence |
| 32766732 |
GLI1 and GLI2 were shown to co-immunoprecipitate in PANC1 pancreatic cancer cells and RMS13 rhabdomyosarcoma cells.|Chromatin immunoprecipitation showed that GLI1 and GLI2 occupied the same regions at the BCL2, MYCN and CCND1 promoters. Furthermore, depletion of GLI1 inhibited GLI2 occupancy at these promoters, suggesting that GLI1/GLI2 interaction is required for the recruitment of GLI2 to these sites. | RNAi knockdown of either GLI1 or GLI2 inhibited expression of many well-characterized GLI target genes (BCL2, MYCN, PTCH2, IL7 and CCND1) in PANC1 cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DOT1L | up-regulates quantity by expression
transcriptional regulation
|
BCL2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255880 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27856324 |
Previously, we found that MLL-AF4 binds to the BCL-2 gene and directly activates it through DOT1L recruitment and increased H3K79me2/3 levels. MLL-AF4 directly controls the active transcription of both BCL-2 and MCL-1 […]. Of all the BCL-2 family members, only BCL-2 and MCL-1 are directly activated by MLL-AF4. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, MLL fusion protein in AML |
| + |
CD27 | up-regulates quantity by expression
transcriptional regulation
|
BCL2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-93317 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12324477 |
Cd40 ligation up-regulated bcl-2 and bcl-xl as much as 9.7- (p < 0.01) and 6.8-fold (p < 0.01), respectively (fig. 2, b and c). Under similar conditions, cd27 ligation also up-regulated bcl-2 and bcl-xl as much as 5.0- (p < 0.01) and 3.9-fold (p < 0.01), respectively. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GH1 | up-regulates quantity by expression
transcriptional regulation
|
BCL2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261628 |
|
|
Homo sapiens |
MCF-10A Cell |
| pmid |
sentence |
| 15665309 |
Autocrine hGH increased the transcription and subsequent mRNA level and protein expression of c-Myc, Cyclin D1, and Bcl-2 in human mammary epithelial cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MITF | up-regulates quantity by expression
transcriptional regulation
|
BCL2 |
0.457 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249618 |
|
|
|
|
| pmid |
sentence |
| 12086670 |
MITF directly occupies the BCL2 promoter in vivo and this suggest that BCL2 may be a direct transcriptional target of MITF |
|
| Publications: |
1 |
| Pathways: | Malignant Melanoma |
| + |
BCL2L11 | down-regulates activity
binding
|
BCL2 |
0.812 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178676 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 18498746 |
We show that mutation of the phosphorylation site Thr-112 causes decreased binding of Bim to the antiapoptotic protein Bcl2 and can increase cell survival. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-133820 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15694340 |
Apoptosis is initiated when Bcl-2 and its prosurvival relatives are engaged by proapoptotic BH3-only proteins via interaction of its BH3 domain with a groove on the Bcl-2-like proteins. These interactions have been considered promiscuous, but our analysis of the affinity of eight BH3 peptides for five Bcl-2-like proteins has revealed that the interactions vary over 10,000-fold in affinity, and accordingly, only certain protein pairs associate inside cells. Bim and Puma potently engaged all the prosurvival proteins comparably. Bad, however, bound tightly to Bcl-2, Bcl-xL, and Bcl-w but only weakly to A1 and not to Mcl-1. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, Inhibition of Apoptosis, Mitochondrial Control of Apoptosis, SARS-COV APOPTOSIS |
| + |
CDK1 | down-regulates activity
phosphorylation
|
BCL2 |
0.35 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267987 |
|
|
Homo sapiens |
KB-3-1 Cell |
| pmid |
sentence |
| 19917720 |
Cyclin-Dependent Kinase 1-Mediated Bcl-xL/Bcl-2 Phosphorylation Acts as a Functional Link Coupling Mitotic Arrest and Apoptosis|These findings suggest a model whereby a switch in the duration of CDK1 activation, from transient during mitosis to sustained during mitotic arrest, dramatically increases the extent of Bcl-xL/Bcl-2 phosphorylation, resulting in inactivation of their antiapoptotic function. Thus, phosphorylation of antiapoptotic Bcl-2 proteins acts as a sensor for CDK1 signal duration and as a functional link coupling mitotic arrest to apoptosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, KIT in AML |
| + |
BCL2 | down-regulates
|
Apoptosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249611 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 1286168 |
Bcl-2 functions to inhibit apoptosis in a variety of in vitro and in vivo experiments, suggesting interference with a central mechanism of apoptosis |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Alzheimer, Acute Myeloid Leukemia, BCR-ABL in AML, DNMT3A in AML, FLT3 in AML, KIT in AML, miRNA in AML, MLL fusion protein in AML, AML_TRIPLETS, COVID-19 Causal Network, Colorectal Carcinoma, Death Receptor Signaling, FLT3-ITD signaling, Inhibition of Apoptosis, Mitochondrial Control of Apoptosis, Malignant Melanoma, Triple mutant AML, NPM1_new, p53 in cancer, SARS-COV APOPTOSIS, SARS-CoV MAPK PERTURBATION |
| + |
Obatoclax mesylate | down-regulates activity
chemical inhibition
|
BCL2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262022 |
|
|
in vitro |
|
| pmid |
sentence |
| 23515850 |
Obatoclax and its predecessor analogs bind to BCL-2, BCL-XL, BCL-w, BCL-B, BFL-1, and MCL-1 in vitro |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ABT-737 | down-regulates
chemical inhibition
|
BCL2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-151781 |
|
|
Homo sapiens |
Leukemia Cell, B-lymphocyte, Lymphoma Cell |
| pmid |
sentence |
| 17200714 |
A cell-permeant compound, abt-737, binds with high affinity to bcl2, bcl2l1, and bcl2l2, antagonizes their antiapoptotic function, and induces apoptosis in select human tumor cell lines, primary patient-derived cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-189159 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
BCL2 | down-regulates
|
HTRA2 |
0.254 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-89189 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14585074 |
Bcl- confers protection to apoptosis by interference with bax/bak-mediated release of the pro-apoptotic mitochodrial factors smac/diablo and htra2/omi |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FOXA1 | down-regulates quantity by repression
transcriptional regulation
|
BCL2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161448 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19127412 |
Foxa1 overexpression decreased the expression of bcl2, while foxa1 depletion increased the expression of bcl2 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
venetoclax | down-regulates activity
chemical inhibition
|
BCL2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261938 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23291630 |
Here we report the re-engineering of navitoclax to create a highly potent, orally bioavailable and BCL-2-selective inhibitor, ABT-199. This compound inhibits the growth of BCL-2-dependent tumors in vivo and spares human platelets. These data indicate that selective pharmacological inhibition of BCL-2 shows promise for the treatment of BCL-2-dependent hematological cancers. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BCL2 | down-regulates activity
binding
|
BAX |
0.622 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-36898 |
|
|
Homo sapiens |
B-lymphocyte, Lymphoma Cell |
| pmid |
sentence |
| 8183370 |
Bcl-2 has the unique oncogenic role of extending cell survival by inhibiting a variety of apoptotic deaths. Bcl-2 exerts its action through heterodimerization with bax. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Alzheimer, Acute Myeloid Leukemia, MLL fusion protein in AML, COVID-19 Causal Network, Death Receptor Signaling, FLT3-ITD signaling, Inhibition of Apoptosis, Mitochondrial Control of Apoptosis, Malignant Melanoma, p53 in cancer, SARS-COV APOPTOSIS |
| + |
HRK | down-regulates
binding
|
BCL2 |
0.481 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-47794 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9130713 |
Hrk, physically interacts with the death-repressor proteins bcl2 and bcl2l1. Hrk activates cell death at least in part by interacting with and inhibiting the protection afforded by bcl2 and bcl2l1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BAG1 | up-regulates activity
binding
|
BCL2 |
0.422 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254118 |
|
|
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 7834747 |
Cloning and functional analysis of BAG-1: A novel Bcl-2-binding protein with anti-cell death activity| |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
POLR1H | up-regulates quantity by expression
transcriptional regulation
|
BCL2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259908 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16373708 |
ZNRD1 could significantly up-regulate the expression of P-gp, Bcl-2, and the transcription of the MDR1 gene but not alter the expression of MDR-associated protein, glutathione S-transferase activity, or intracellular glutathione content in leukemia cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NPTX1 | down-regulates quantity
|
BCL2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260412 |
|
|
Homo sapiens |
MHCC-97 Cell, SMMC-7721 Cell |
| pmid |
sentence |
| 31113871 |
We found that the protein levels of BCL2-associated agonist of cell death (BAD) and BCL2-associated X protein (BAX) were increased in NPTX1-overexpressing SMMC-7721 and MHCC-97h cells relative to control cells. In contrast, decreased levels of myeloid cell leukemia sequence 1 (Mcl-1) and B-cell lymphoma-2 (Bcl-2) were found in NPTX1-overexpressing SMMC-7721 and MHCC-97h cells relative to control |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BAD | down-regulates activity
relocalization
|
BCL2 |
0.794 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-133756 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15694340 |
Apoptosis is initiated when Bcl-2 and its prosurvival relatives are engaged by proapoptotic BH3-only proteins via interaction of its BH3 domain with a groove on the Bcl-2-like proteins. These interactions have been considered promiscuous, but our analysis of the affinity of eight BH3 peptides for five Bcl-2-like proteins has revealed that the interactions vary over 10,000-fold in affinity, and accordingly, only certain protein pairs associate inside cells. Bim and Puma potently engaged all the prosurvival proteins comparably. Bad, however, bound tightly to Bcl-2, Bcl-xL, and Bcl-w but only weakly to A1 and not to Mcl-1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, COVID-19 Causal Network, FLT3-ITD signaling, Inhibition of Apoptosis, Mitochondrial Control of Apoptosis, Malignant Melanoma, SARS-COV APOPTOSIS |
3.0
BCL2
