| + |
CASP3 | down-regulates quantity by destabilization 
cleavage
|
BRCA1 |
0.476 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256326 |
Asp1155 |
ETPDDLLdDGEIKED |
Homo sapiens |
|
| pmid |
sentence |
| 12149654 |
We demonstrate the cleavage and the consequential downregulation of full-length BRCA1 by caspase-3 during UV-induced apoptosis. Finally, mutation of a caspase-3 specific cleavage site (D/A1154) rendered BRCA1 non-cleavable. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CASP3 | down-regulates
cleavage
|
PTCH1 |
0.323 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-199111 |
Asp1405 |
CPGYPETdHGLFEDP |
Homo sapiens |
|
| pmid |
sentence |
| 23074268 |
Like other dependence receptors, ptc1 contains a dependence-as-associated receptor c-terminal motif that is cleaved by caspases at a conserved aspartic acid (asp 1392) in the absence of shh, to expose a proapoptotic domain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CASP3 | down-regulates activity
cleavage
|
PTCH1 |
0.323 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-104585 |
Asp1405 |
CPGYPETdHGLFEDP |
Homo sapiens |
|
| pmid |
sentence |
| 12907805 |
Like other dependence receptors, ptc1 contains a dependence-as-associated receptor c-terminal motif that is cleaved by caspases at a conserved aspartic acid (asp 1392) in the absence of shh, to expose a proapoptotic domain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CASP3 | down-regulates
cleavage
|
IKBKB |
0.367 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-112788 |
Asp242 |
VRQKSEVdIVVSEDL |
Homo sapiens |
|
| pmid |
sentence |
| 11741536 |
Ikappab kinase (ikk) beta was specifically proteolyzed by caspase-3-related caspases at aspartic acid residues 78, 242, 373, and 546 during tumor necrosis factor (tnf)-alpha-induced apoptosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-112792 |
Asp373 |
PATQCISdGKLNEGH |
Homo sapiens |
|
| pmid |
sentence |
| 11741536 |
Ikappab kinase (ikk) beta was specifically proteolyzed by caspase-3-related caspases at aspartic acid residues 78, 242, 373, and 546 during tumor necrosis factor (tnf)-alpha-induced apoptosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-112796 |
Asp546 |
ALQTDIVdLQRSPMG |
Homo sapiens |
|
| pmid |
sentence |
| 11741536 |
Ikappab kinase (ikk) beta was specifically proteolyzed by caspase-3-related caspases at aspartic acid residues 78, 242, 373, and 546 during tumor necrosis factor (tnf)-alpha-induced apoptosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-112800 |
Asp78 |
PNVVAARdVPEGMQN |
Homo sapiens |
|
| pmid |
sentence |
| 11741536 |
Ikappab kinase (ikk) beta was specifically proteolyzed by caspase-3-related caspases at aspartic acid residues 78, 242, 373, and 546 during tumor necrosis factor (tnf)-alpha-induced apoptosis. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
CASP3 | up-regulates 
cleavage
|
GAS2 |
0.448 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-72347 |
Asp278 |
MLQISRVdGKTSPIQ |
Homo sapiens |
|
| pmid |
sentence |
| 10564664 |
We now demonstrate that gas2 is a substrate of caspase-3 but not of caspase-6. Proteolytic processing both in vitro and in vivo is dependent on aspartic residue 279. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CASP3 | down-regulates quantity by destabilization
cleavage
|
GORASP1 |
0.397 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260602 |
Asp317 |
VSGISLLdNSNASVW |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 11815631 |
Together, our results strongly suggest GRASP65 is a specific substrate for caspase-3.|This suggests that GRASP65 cleavage is required for fragmentation of the Golgi ribbon during apoptosis.| we analyzed the sequence in this region and identified three potential cleavage sites as SLLD320S, SFPD375S, and TLPD393G|mutation of all three aspartic acid residues completely blocked cleavage |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260603 |
Asp372 |
EFEVSFLdSPGAQAQ |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 11815631 |
Together, our results strongly suggest GRASP65 is a specific substrate for caspase-3.|This suggests that GRASP65 cleavage is required for fragmentation of the Golgi ribbon during apoptosis.| we analyzed the sequence in this region and identified three potential cleavage sites as SLLD320S, SFPD375S, and TLPD393G|mutation of all three aspartic acid residues completely blocked cleavage |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260604 |
Asp390 |
LPQLTLPdSLTSAAS |
Homo sapiens |
|
| pmid |
sentence |
| 11815631 |
Together, our results strongly suggest GRASP65 is a specific substrate for caspase-3.|This suggests that GRASP65 cleavage is required for fragmentation of the Golgi ribbon during apoptosis.| we analyzed the sequence in this region and identified three potential cleavage sites as SLLD320S, SFPD375S, and TLPD393G|mutation of all three aspartic acid residues completely blocked cleavage |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
CASP3 | up-regulates activity
cleavage
|
PSEN2 |
0.407 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261743 |
Asp326 |
YDPEMEEdSYDSFGE |
in vitro |
|
| pmid |
sentence |
| 10069390 |
In decreasing order of activity, caspase-8, -3, -1, -6 and -7 proteolysed PS2 at the recognition site D326SYD329. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261749 |
Asp329 |
EMEEDSYdSFGEPSY |
in vitro |
|
| pmid |
sentence |
| 10069390 |
In decreasing order of activity, caspase-8, -3, -1, -6 and -7 proteolysed PS2 at the recognition site D326SYD329. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| Pathways: | Alzheimer |
| + |
CASP3 | up-regulates activity
cleavage
|
STK4 |
0.613 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109874 |
Asp326 |
NSEEDEMdSGTMVRA |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 11517310 |
In response to apoptotic stimuli, caspase cleavage of mst1 occurs at asp-326 and asp-349, resulting in the separation of its n-terminal kinase domain from the nes-containing c-terminal domain. Thus, caspase cleavage of mst1 serves two purposes: one is activation of mst1 kinase activity and the other is translocation of mst1 into the nucleus. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109878 |
Asp349 |
RVASTMTdGANTMIE |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 11517310 |
In response to apoptotic stimuli, caspase cleavage of mst1 occurs at asp-326 and asp-349, resulting in the separation of its n-terminal kinase domain from the nes-containing c-terminal domain. Thus, caspase cleavage of mst1 serves two purposes: one is activation of mst1 kinase activity and the other is translocation of mst1 into the nucleus. |
|
| Publications: |
2 |
Organism: |
Chlorocebus Aethiops |
| + |
CASP3 | up-regulates activity
cleavage
|
CASP9 |
0.635 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-133264 |
Asp330 |
LRTFDQLdAISSLPT |
Homo sapiens |
U-937 Cell |
| pmid |
sentence |
| 15657060 |
In turn, casp3 directs feedback cleavage of casp9 at asp-330 to generate p37 and p10 subunits. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-90397 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14585074 |
Active caspase-3 itself is able to process its upstream , caspase-8 and caspase-9, establishing a self-amplifying loop of caspase activation |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, Death Receptor Signaling, Inhibition of Apoptosis, Mitochondrial Control of Apoptosis, Parkinson, SARS-COV APOPTOSIS |
| + |
CASP3 | up-regulates activity
cleavage
|
PSEN1 |
0.457 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261756 |
Asp345 |
EEWEAQRdSHLGPHR |
in vitro |
|
| pmid |
sentence |
| 10069390 |
Remarkably, the caspases acting on PS1 could be subdivided in two groups. One group, containing caspase-8, -6 and -11, cleaved PS1 after residues ENDD329 and to a lesser extent after residues AQRD341. A second group consisting of caspase-3, -7 and -1 acted uniquely on AQRD341. Importantly, these two cleavage sites were also recognized by caspases in the C-terminal PS1 fragment produced by constitutive proteolysis. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | Alzheimer |
| + |
CASP3 | up-regulates activity
cleavage
|
GORASP1 |
0.397 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260613 |
Asp390 |
LPQLTLPdSLTSAAS |
|
|
| pmid |
sentence |
| 17761173 |
In contrast, Caspase‐3 cleavage of GRASP‐1 releases the C‐terminal fragment, which in turn activates JNK signaling by serving as a scaffold protein |
|
| Publications: |
1 |
| + |
CASP3 | down-regulates activity
cleavage
|
GSN |
0.637 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256357 |
Asp403 |
WRDPDQTdGLGLSYL |
Homo sapiens |
|
| pmid |
sentence |
| 9671712 |
We showed that human gelsolin was cleaved during Fas-mediated apoptosis in vivo and that the caspase-3 cleavage site of human gelsolin was at D352 of DQTD352G. gelsolin seems to have dual functions, i.e., it both prevents and, once cleaved, induces cell death. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CASP3 | down-regulates quantity by destabilization
cleavage
|
MYL3 |
0.379 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270593 |
Glu135 |
GTYEDFVeGLRVFDK |
Oryctolagus cuniculus |
Cardiomyocyte Cell Line |
| pmid |
sentence |
| 12186978 |
By sequencing and site-directed mutagenesis, a noncanonical cleavage site for caspase-3 was mapped to the C-terminal DFVE(135)G motif. We demonstrated that vMLC1 cleavage in failing myocardium in vivo is associated with a morphological disruption of the organized vMLC1 staining of sarcomeres, and with a reduction in myocyte contractile performance. |
|
| Publications: |
1 |
Organism: |
Oryctolagus Cuniculus |
| + |
MAPK14 | down-regulates
phosphorylation
|
CASP3 |
0.775 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-122099 |
Ser150 |
FRGDRCRsLTGKPKL |
Homo sapiens |
Neutrophil |
| pmid |
sentence |
| 14970175 |
Consequently, p38-mapk can directly phosphorylate and inhibit the activities of caspase-8 and caspase-3 and thereby hinder neutrophil apoptosis, and, in so doing, regulate the inflammatory response. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | TNF-alpha Signaling |
| + |
PPP2R5B | up-regulates
dephosphorylation
|
CASP3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-131435 |
Ser150 |
FRGDRCRsLTGKPKL |
Homo sapiens |
Neutrophil |
| pmid |
sentence |
| 15569672 |
Dephosphorylation of caspase-3 at ser150 site by pp2a increased caspase-3 activity,which was essential to trigger apoptosis in neutrophils. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HSPB1 | down-regulates 
|
CASP3 |
0.569 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-71869 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10544189 |
Hsp27 overexpression delays poly(adp-ribose)polymerase cleavage and procaspase-3 activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CASP3 | down-regulates quantity by destabilization
cleavage
|
RAD51 |
0.468 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271709 |
|
|
Homo sapiens |
32D Cell |
| pmid |
sentence |
| 11684015 |
The RAD51 protein has been shown to be a substrate for caspase-3|he activated caspase-3 fragments (19 kDa and 17 kDa) and caspase-3 cleaved RAD51 fragment (∼23 kDa) was detected by Western analysis (Figure 3E). Activation of caspase-3 and the signature proteolytic degradation product of RAD51 only occurred in parental 32Dcl3 cells after treatment with cisplatin |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CASP9 | up-regulates activity
cleavage
|
CASP3 |
0.635 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-53582 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 9390557 |
Activated caspase-9 in turn cleaves and activates caspase-3. Mutation of the active site of caspase-9 attenuated the activation of caspase-3 and cellular apoptotic response in vivo, indicating that caspase-9 is the most upstream member of the apoptotic protease cascade. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-133267 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15657060 |
Following autoprocessing in the apoptosome, caspase-9 cleaves and activates caspase-3. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, Death Receptor Signaling, Inhibition of Apoptosis, Mitochondrial Control of Apoptosis, Parkinson, SARS-COV APOPTOSIS |
| + |
CASP3 | up-regulates 
|
Chromatine_condensation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-66860 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10200555 |
Caspase-3 is required for blebbing, chromatin condensation and dna fragmentation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
Pac-1 | up-regulates activity
chemical activation
|
CASP3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262016 |
|
|
in vitro |
|
| pmid |
sentence |
| 16936720 |
Here we report the identification of a small molecule (PAC-1) that directly activates procaspase-3 to caspase-3 in vitro and induces apoptosis in cancerous cells isolated from primary colon tumors in a manner directly proportional to the concentration of procaspase-3 inside these cells. W |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CASP3 | down-regulates activity
cleavage
|
PARP1 |
0.775 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-116178 |
|
|
Mus musculus |
L-929 Cell |
| pmid |
sentence |
| 11907276 |
Caspase-3 cleaves parp-1. During cd95-mediated apoptosis proteolytic inactivation of parp-1 by caspases prevents atp depletion and thereby ensures the execution of the apoptotic process |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | COVID-19 Causal Network, Death Receptor Signaling, Inhibition of Apoptosis, Mitochondrial Control of Apoptosis, SARS-COV APOPTOSIS, TNF-alpha Signaling |
| + |
BIRC5 | down-regulates
binding
|
CASP3 |
0.492 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-72882 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10587640 |
Use of a dominant-negative survivin mutant or antisense survivin complementary dna disrupts a supramolecular assembly of survivin, caspase-3 and the cyclin-dependent-kinase inhibitor p21waf1/cip1 within centrosomes, and results in caspase-dependent cleavage of p21. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-62484 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9850056 |
Survivin binds specifically to caspase-3. Survivin protected from apoptosis induced by overexpression of procaspase-3 and inhibited the processing of these zymogens into active caspases. Survivin, which is commonly expressed in human tumor cell lines, can bind the effector cell death proteases caspase-3 in vitro and inhibits caspase activity |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
XIAP | down-regulates activity
binding
|
CASP3 |
0.94 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-71954 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10548111 |
The linker region located adjacent to the bir2 domain also participates in the binding of xiap to the effector caspases (-3 and -7). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-110837 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11583623 |
Xiap is an endogenous inhibitor of caspase-3 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Death Receptor Signaling, Inhibition of Apoptosis, Parkinson |
| + |
CASP3 | up-regulates activity
cleavage
|
DFFA |
0.754 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-47416 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9108473 |
DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. We have identified and purified from HeLa cytosol a protein that induces DNA fragmentation in coincubated nuclei after it is activated by caspase-3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BCR-ABL | down-regulates activity
|
CASP3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271704 |
|
|
Homo sapiens |
32D Cell |
| pmid |
sentence |
| 11684015 |
BCR/ABL Tyrosine Kinase Enhances Expression of RAD51 by Stimulation of STAT5-Mediated Transactivation and Inhibition of Caspase-3-Dependent Degradation| |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CASP3 | up-regulates
cleavage
|
DFFB |
0.684 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-47419 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9108473 |
Casp3_ cleaves the 45 kda subunit at two sites to generate an active factor that produces_ dna_ fragmentation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CASP3 | up-regulates
|
DNA_fragmentation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-66863 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10200555 |
Caspase-3 is required for blebbing, chromatin condensation and dna fragmentation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
XIAP | down-regulates quantity by destabilization
ubiquitination
|
CASP3 |
0.94 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109243 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11447297 |
Xiap promotes the degradation of active-form caspase-3, but not procaspase-3, in living cells. Both the association of XIAP with caspase-3 and the RING finger domain of XIAP were essential for ubiquitination. XIAP promotes the degradation of caspase-3, which enhances its anti-apoptotic effect. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Death Receptor Signaling, Inhibition of Apoptosis, Parkinson |
| + |
CASP3 | up-regulates
cleavage
|
ROCK1 |
0.733 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-106546 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11283607 |
Rock i is cleaved by casp3 at a conserved detd1113/g sequence and its carboxy-terminal inhibitory domain is removed, resulting in deregulated and constitutive kinase activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STAT3 | up-regulates quantity by expression
transcriptional regulation
|
CASP3 |
0.466 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255335 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 25787076 |
We determined that Stat3 activation increases caspase-3 expression in C2C12 cells. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
CASP3 | down-regulates activity
cleavage
|
AKT1 |
0.608 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252624 |
|
|
in vitro |
|
| pmid |
sentence |
| 10579725 |
P53 can inhibit the survival function of integrins by inducing the caspase-dependent cleavage and inactivation of the serine/threonine kinase akt/pkb;the involvement of caspase 3 in akt/pkb regulation was indicated by the ability of z-devd-fmk, a caspase 3 inhibitor, to block the alpha6beta4-associated reduction in akt/pkb levels in vivo, and by the ability of recombinant caspase 3 to promote the cleavage of akt/pkb in vitro |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | Parkinson |
| + |
CASP3 | up-regulates
cleavage
|
CASP6 |
0.614 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-64179 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9922454 |
Caspase-3 is required for the activation of caspases 6 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, SARS-COV APOPTOSIS |
| + |
BIRC6 | down-regulates
binding
|
CASP3 |
0.467 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-125956 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15200957 |
Bruce binds and thereby inhibits caspases, in particular effector caspase-3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CASP3 | up-regulates
|
Muscle_atrophy |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255336 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 25787076 |
The UPS by itself degrades actomyosin and myofibrillar proteins slowly, but when caspase-3 is activated, it cleaves actomyosin and the myofibrillar proteins to provide substrates for degradation in the UPS . Caspase-3 also can cleave specific subunits of the 19 S proteasome particle, which stimulates the proteolytic activity of the 26S proteasome[...] These results indicate that caspase-3 participates in the muscle proteolysis that is present in tumor-bearing mice |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
RBM10 | down-regulates quantity by repression
transcriptional regulation
|
CASP3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259152 |
|
|
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 |
| + |
Caspase 9 complex | up-regulates activity
cleavage
|
CASP3 |
0.635 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256462 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 9390557 |
Activated caspase-9 in turn cleaves and activates caspase-3. Mutation of the active site of caspase-9 attenuated the activation of caspase-3 and cellular apoptotic response in vivo, indicating that caspase-9 is the most upstream member of the apoptotic protease cascade. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256448 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15657060 |
Following autoprocessing in the apoptosome, caspase-9 cleaves and activates caspase-3. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ING1 | up-regulates quantity by expression
transcriptional regulation
|
CASP3 |
0.259 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254489 |
|
|
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 15662138 |
Ectopic expression of p33ING1b could obviously upregulate p53, p21WAF1 and bax protein levels and activate caspase-3 in taxol-treated U2OS cells. Taken together, our data demonstrate that p33ING1b enhances taxol-induced apoptosis through p53-dependent pathway in human osteosarcoma cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CASP3 | up-regulates activity
cleavage
|
BAD |
0.534 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-126727 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 15231831 |
Casp3 cleaves bad at asp-61. In addition, caspases convert bad(l) into a pro-death fragment that resembles the short splice variant. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, Inhibition of Apoptosis, Mitochondrial Control of Apoptosis, SARS-COV APOPTOSIS |
| + |
CASP3 | up-regulates
cleavage
|
ACIN1 |
0.626 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-70800 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10490026 |
Induces apoptotic chromatin condensation after activation by casp3 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RNF7 | down-regulates activity
ubiquitination
|
CASP3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271448 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23136067 |
SAG (Sensitive to Apoptosis Gene), also known as RBX2 (RING box protein 2), ROC2 (Regulator of Cullins 2), or RNF7 (RING Finger Protein 7), was originally cloned in our laboratory as a redox inducible antioxidant protein and later characterized as the second member of the RBX/ROC RING component of the SCF (SKP1-CUL-F-box Proteins) E3 ubiquitin ligase. by forming a complex with other components of the SCF E3 ligase, SAG promotes ubiquitination and degradation of a number of protein substrates, including c-JUN, DEPTOR, HIF-1α, IκBα, NF1, NOXA, p27, and procaspase-3, thus regulating various signaling pathways and biological processes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Caspase 8 complex | up-regulates activity
cleavage
|
CASP3 |
0.722 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256458 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16964285 |
Casp8 induces apoptosis by directly activating casp3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256451 |
|
|
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 10988287 |
The temporal pattern of caspase-8 cleavage is consistent with the possibility that it may function upstream of caspase-3 during p53-dependent apoptosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256452 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21295084 |
Triggering of the DISC leads to caspase-8 activation. Active caspase-8 cleaves caspase-3 which, in type I cells, leads to cell death induction. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens, Mus Musculus |
| + |
ANXA3 | down-regulates quantity by repression
transcriptional regulation
|
CASP3 |
0.263 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262209 |
|
|
Homo sapiens |
HCT-116 Cell, SW-480 Cell |
| pmid |
sentence |
| 30998268 |
ANXA3 depletion promoted cell apoptosis and upregulated c‐caspase 3 expression in HCT116/Ox and SW480/Ox cells with or without Ox, which is consistent with findings from a preliminary study by Yan et al |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAC-1 | up-regulates
chemical activation
|
CASP3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-198535 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CASP3 | up-regulates
|
Apoptosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-89244 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14585074 |
Caspase-3 is responsible for apoptosis execution |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Alzheimer, COVID-19 Causal Network, Death Receptor Signaling, Inhibition of Apoptosis, Mitochondrial Control of Apoptosis, Parkinson, SARS-COV APOPTOSIS, TNF-alpha Signaling |
| + |
Apoptosome | up-regulates activity
cleavage
|
CASP3 |
0.74 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256472 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 9390557 |
Activated caspase-9 in turn cleaves and activates caspase-3. Mutation of the active site of caspase-9 attenuated the activation of caspase-3 and cellular apoptotic response in vivo, indicating that caspase-9 is the most upstream member of the apoptotic protease cascade. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256471 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15657060 |
Following autoprocessing in the apoptosome, caspase-9 cleaves and activates caspase-3. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Alzheimer |
| + |
CASP3 | up-regulates activity
cleavage
|
GRIPAP1 |
0.416 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260641 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17761173 |
These results suggest that the region of GRASP‐1 downstream of the Caspase‐3‐cleavage site is capable of activating the JNK signaling pathway by enhancing the phosphorylation of JNK. these results suggest that full length GRASP‐1 does not enhance JNK pathway activity, possibly due to the inhibitory effect of the N‐terminal fragment on the C‐terminal fragment. In contrast, Caspase‐3 cleavage of GRASP‐1 releases the C‐terminal fragment, which in turn activates JNK signaling by serving as a scaffold protein. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CASP3 | down-regulates activity
cleavage
|
AKT |
0.646 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-72677 |
|
|
in vitro |
|
| pmid |
sentence |
| 10579725 |
P53 can inhibit the survival function of integrins by inducing the caspase-dependent cleavage and inactivation of the serine/threonine kinase akt/pkb;the involvement of caspase 3 in akt/pkb regulation was indicated by the ability of z-devd-fmk, a caspase 3 inhibitor, to block the alpha6beta4-associated reduction in akt/pkb levels in vivo, and by the ability of recombinant caspase 3 to promote the cleavage of akt/pkb in vitro |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | COVID-19 Causal Network, Inhibition of Apoptosis, SARS-COV APOPTOSIS |
| + |
CASP3 | up-regulates
|
Cell_death |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256638 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14585074 |
Caspase-3 is responsible for apoptosis execution |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CASP3 | down-regulates
cleavage
|
SPTAN1 |
0.673 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-57891 |
|
|
Homo sapiens |
Breast Cancer Cell, HeLa Cell |
| pmid |
sentence |
| 9624143 |
Caspase-3 is required for alpha-fodrin cleavage but dispensable for cleavage of other death substrates in apoptosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CASP8 | up-regulates activity
cleavage
|
CASP3 |
0.722 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-81808 |
|
|
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 10988287 |
The temporal pattern of caspase-8 cleavage is consistent with the possibility that it may function upstream of caspase-3 during p53-dependent apoptosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149420 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16964285 |
Casp8 induces apoptosis by directly activating casp3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-171767 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21295084 |
Triggering of the DISC leads to caspase-8 activation. Active caspase-8 cleaves caspase-3 which, in type I cells, leads to cell death induction. |
|
| Publications: |
3 |
Organism: |
Mus Musculus, Homo Sapiens |
| Pathways: | Alzheimer, COVID-19 Causal Network, Death Receptor Signaling, Mitochondrial Control of Apoptosis, SARS-COV APOPTOSIS, TNF-alpha Signaling |
| + |
CASP3 | down-regulates activity
cleavage
|
KDM4C |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263870 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29207681 |
JMJD2C as a novel substrate for caspase-3 (cysteine-aspartic acid protease-3), and cleavage of JMJD2C by caspase-3 led to inactivation of JMJD2C demethylase activity and elevation of H3K9 methylation levels. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CASP3 | form complex 
binding
|
Caspase 3 complex |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256387 |
|
|
|
|
| pmid |
sentence |
| 15115390 |
Caspases are expressed as inactive proenzymes of 30−50 kDa that include an amino-terminal domain of variable length and sequence that is followed by two domains of conserved sequences: a large subunit (approximately 20 kDa, designated p17 in caspase-3) and a small carboxy-terminal subunit (approximately 10 kDa, designated p12 in caspase-3). Activation is accomplished by proteolytic cleavage between these domains and subsequent assembly of heterotetramers that contain two copies each of the large and small subunits but lack the amino-terminal domains. |
|
| Publications: |
1 |
| + |
CASP3 | up-regulates
|
Membrane_blebbing |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-66866 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10200555 |
Caspase-3 is required for blebbing, chromatin condensation and dna fragmentation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
MYCT1 | up-regulates activity
|
CASP3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261942 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30283340 |
Herein, we observed that overexpression of MYCT1 induced apoptosis in HL-60 and KG-1a cells, and upregulated Bax, downregulated Bcl-2, and enhanced cleavage of caspase-3 and -9. Similar proapoptotic role of MYCT1 was also found in the AML cell xenografts. These results suggest that MYCT1 affects AML cell apoptosis by modulating the endogenous apoptotic pathways. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CASP3 | down-regulates
cleavage
|
GSN |
0.637 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-51652 |
|
|
Homo sapiens |
Neutrophil |
| pmid |
sentence |
| 9323209 |
Caspase-3 mediates cleavage of gelsolin, generating a fragment that severs actin filaments in an unregulated fashion. The cleavage of gelsolin causes cells to round up, detach and undergo nuclear fragmentation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CASP3 | up-regulates quantity by stabilization
cleavage
|
NFKBIA |
0.425 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-51936 |
|
|
in vitro |
|
| pmid |
sentence |
| 9367996 |
The cell-death protease cpp32 (caspase-3) in vitro specifically cleaved chicken and human ikappab-alpha at a conserved asp-ser sequence.Therefore, cleavage of I_B-_ by a CPP32-like protease could create what is sometimes called a super-repressor form of I_B-_ (20). That is, cleavage by CPP32 would block the ability of I_B-_ to undergo signal-induced degradation by removing the sites of signal-induced ubiquitination and by likely disrupting the ability of I_B-_ to become phosphorylated at critical Ser residues. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | COVID-19 Causal Network, Inhibition of Apoptosis, TNF-alpha Signaling |
| + |
CASP3 | down-regulates
cleavage
|
PSIP1 |
0.349 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-180144 |
|
|
Homo sapiens |
Prostate Gland Cancer Cell |
| pmid |
sentence |
| 18708362 |
Ledgf/ p75 has a cooh-terminally truncated splice variant, p52 / during apoptosis, caspase-3 cleaved p52 to generate a p38 fragment that lacked the nh2-terminal pwwp domain and failed to transactivate the hsp27 promoter in reporter assays. However, p38 retained chromatin association properties and repressed the transactivation potential of ledgf/p75 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CASP3 | up-regulates
|
Protein_degradation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255337 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 25787076 |
The UPS by itself degrades actomyosin and myofibrillar proteins slowly, but when caspase-3 is activated, it cleaves actomyosin and the myofibrillar proteins to provide substrates for degradation in the UPS . Caspase-3 also can cleave specific subunits of the 19 S proteasome particle, which stimulates the proteolytic activity of the 26S proteasome[...] These results indicate that caspase-3 participates in the muscle proteolysis that is present in tumor-bearing mice. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
3.0
CASP3
- 
- 