+ |
CASP8 | down-regulates activity
cleavage
|
RIPK1 |
0.907 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-71265 |
Asp324 |
RMQSLQLdCVAVPSS |
Homo sapiens |
HEK-293 Cell, MCF-7 Cell, HeLa Cell |
pmid |
sentence |
10521396 |
These results suggested that the aspartic acid at position 324 is the cleavage site of ripk1. In this study we found that receptor-interacting protein (ripk1) is cleaved by casp8 when cells undergo tnf-induced apoptosis. The cleavage of ripk1 abolished its nf-kb inducing ability. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, Death Receptor Signaling, Mitochondrial Control of Apoptosis, TNF-alpha Signaling |
+ |
CASP8 | up-regulates activity
cleavage
|
PSEN2 |
0.338 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261744 |
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-261752 |
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 |
+ |
CASP8 | up-regulates activity
cleavage
|
PSEN1 |
0.376 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261754 |
Asp333 |
DTVAENDdGGFSEEW |
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. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261760 |
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: |
2 |
Organism: |
In Vitro |
Pathways: | Alzheimer |
+ |
CASP8 | down-regulates activity
cleavage
|
RNF31 |
0.321 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272194 |
Asp348 |
GTGGLEPdLARGRWA |
Homo sapiens |
HaCaT II-4 Cell |
pmid |
sentence |
32122970 |
We show that LUBAC interacted with caspase-1 via HOIP and modified its CARD domain with linear polyubiquitin and that depletion of HOIP or Sharpin resulted in heightened caspase-1 activation and cell death in response to inflammasome activation, unlike what is observed in macrophages. Reciprocally, caspase-1, as well as caspase-8, regulated LUBAC activity by proteolytically processing HOIP at Asp-348 and Asp-387 during the execution of cell death. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272195 |
Asp387 |
QPPSLVVdSRDAGIC |
Homo sapiens |
HaCaT II-4 Cell |
pmid |
sentence |
32122970 |
We show that LUBAC interacted with caspase-1 via HOIP and modified its CARD domain with linear polyubiquitin and that depletion of HOIP or Sharpin resulted in heightened caspase-1 activation and cell death in response to inflammasome activation, unlike what is observed in macrophages. Reciprocally, caspase-1, as well as caspase-8, regulated LUBAC activity by proteolytically processing HOIP at Asp-348 and Asp-387 during the execution of cell death. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CASP8 | up-regulates activity
cleavage
|
BID |
0.874 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-59655 |
Asp60 |
GYDELQTdGNRSSHS |
Homo sapiens |
MCF-7 Cell |
pmid |
sentence |
9727492 |
Caspase-8 cleaves bid at aspartic acid residue 60 (asp60) cleavage of bid by casp8 releases its potent proapoptotic activity |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Alzheimer, COVID-19 Causal Network, Death Receptor Signaling, Mitochondrial Control of Apoptosis, SARS-COV APOPTOSIS, TNF-alpha Signaling |
+ |
HECTD3 | down-regulates activity
polyubiquitination
|
CASP8 |
0.342 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272077 |
Lys231 |
KVYQMKSkPRGYCLI |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
24287696 |
HECTD3, a new E3 ubiquitin ligase, interacts with caspase-8 death effector domains and ubiquitinates caspase-8 with K63-linked polyubiquitin chains that do not target caspase-8 for degradation but decrease the caspase-8 activation. HECTD3 ubiquitinates caspase-8 with K63-linked polyubiquitin chains at K215. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PLK1 | down-regulates quantity by destabilization
phosphorylation
|
CASP8 |
0.38 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272989 |
Ser305 |
IYQLMDHsNMDCFIC |
|
|
pmid |
sentence |
24484936 |
By phosphorylating S387 in procaspase-8 Cdk1/cyclin B1 generates a phospho-epitope for the binding of the PBD of Plk1. Subsequently, S305 in procaspase-8 is phosphorylated by Plk1 during mitosis. Using an RNAi-based strategy we could demonstrate that the extrinsic cell death is increased upon Fas-stimulation when endogenous caspase-8 is replaced by a mutant (S305A) mimicking the non-phosphorylated form. Together, our data show that sequential phosphorylation by Cdk1/cyclin B1 and Plk1 decreases the sensitivity of cells toward stimuli of the extrinsic pathway during mitosis. |
|
Publications: |
1 |
+ |
MAPK14 | down-regulates
phosphorylation
|
CASP8 |
0.567 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-122103 |
Ser347 |
FTGLKCPsLAGKPKV |
Homo sapiens |
Neutrophil |
pmid |
sentence |
14970175 |
P38-mapk can directly phosphorylate and inhibit the activities of caspase-8 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | TNF-alpha Signaling |
+ |
CDK1 | down-regulates
phosphorylation
|
CASP8 |
0.37 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-168446 |
Ser387 |
YLEMDLSsPQTRYIP |
Homo sapiens |
|
pmid |
sentence |
20937773 |
In this study, we demonstrate that procaspase-8 is phosphorylated in mitotic cells by cdk1na interference-mediated silencing of cyclin b1 or treatment with the cdk1 inhibitor ro-3306 enhances the fas-mediated activation and processing of procaspase-8 in mitotic cells/cyclin b1 on ser-387 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Breast |
+ |
ERK1/2 | down-regulates
phosphorylation
|
CASP8 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-244509 |
Ser387 |
YLEMDLSsPQTRYIP |
Homo sapiens |
|
pmid |
sentence |
24342355 |
We demonstrate that perk 1/2 can phosphorylate pro-caspase-8 at s387 by knocking-down the endogenous pro-caspase-8 using rnai and replacing it with its non-phosphorylatable counterpart (s387a), a significant increase in caspase-8 activity |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Breast |
Pathways: | COVID-19 Causal Network |
+ |
CyclinB/CDK1 | down-regulates
phosphorylation
|
CASP8 |
0.381 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-216737 |
Ser387 |
YLEMDLSsPQTRYIP |
Homo sapiens |
|
pmid |
sentence |
20937773 |
In this study, we demonstrate that procaspase-8 is phosphorylated in mitotic cells by cdk1na interference-mediated silencing of cyclin b1 or treatment with the cdk1 inhibitor ro-3306 enhances the fas-mediated activation and processing of procaspase-8 in mitotic cells/cyclin b1 on ser-387 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Breast |
+ |
MAPK3 | down-regulates
phosphorylation
|
CASP8 |
0.706 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-203480 |
Ser387 |
YLEMDLSsPQTRYIP |
Homo sapiens |
|
pmid |
sentence |
24342355 |
We demonstrate that perk 1/2 can phosphorylate pro-caspase-8 at s387 by knocking-down the endogenous pro-caspase-8 using rnai and replacing it with its non-phosphorylatable counterpart (s387a), a significant increase in caspase-8 activity |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Breast |
+ |
MAPK1 | down-regulates
phosphorylation
|
CASP8 |
0.749 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-203473 |
Ser387 |
YLEMDLSsPQTRYIP |
Homo sapiens |
|
pmid |
sentence |
24342355 |
We demonstrate that perk 1/2 can phosphorylate pro-caspase-8 at s387 by knocking-down the endogenous pro-caspase-8 using rnai and replacing it with its non-phosphorylatable counterpart (s387a), a significant increase in caspase-8 activity |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Breast |
+ |
RPS6KA3 | down-regulates quantity by destabilization
phosphorylation
|
CASP8 |
0.378 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272997 |
Thr263 |
SIRDRNGtHLDAGAL |
|
|
pmid |
sentence |
21183680 |
The ribosomal S6 kinase 2 (RSK2) is a member of the p90 ribosomal S6 kinase (p90RSK) family of proteins and plays a critical role in proliferation, cell cycle, and cell transformation. Here, we report that RSK2 phosphorylates caspase-8, and Thr-263 was identified as a novel caspase-8 phosphorylation site. In addition, we showed that EGF induces caspase-8 ubiquitination and degradation through the proteasome pathway, and phosphorylation of Thr-263 is associated with caspase-8 stability. |
|
Publications: |
1 |
+ |
PLK3 | up-regulates activity
phosphorylation
|
CASP8 |
0.346 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272995 |
Thr273 |
DAGALTTtFEELHFE |
|
|
pmid |
sentence |
27325299 |
Furthermore, we identify caspase-8 as a new substrate for Plk3. Phosphorylation occurs on T273 and results in stimulation of caspase-8 proapoptotic function. |
|
Publications: |
1 |
+ |
SRC | down-regulates
phosphorylation
|
CASP8 |
0.467 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-146127 |
Tyr380 |
TDSEEQPyLEMDLSS |
Homo sapiens |
|
pmid |
sentence |
16619028 |
Src kinase phosphorylates caspase-8 on tyr380: a novel mechanism of apoptosis suppressionwe identified caspase-8 as a new substrate for src kinase. Phosphorylation occurs on tyr380, situated in the linker region between the large and the small subunits of human procaspase-8, and results in downregulation of caspase-8 proapoptotic function |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PTPN6 | up-regulates activity
dephosphorylation
|
CASP8 |
0.361 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248477 |
Tyr380 |
TDSEEQPyLEMDLSS |
Homo sapiens |
|
pmid |
sentence |
18086677 |
Caspase-8 is tyrosine-phosphorylated in freshly isolated neutrophils but spontaneously dephosphorylates in culture, in association with the progression of constitutive apoptosis. Phosphorylation of caspase-8 on Tyr-310 facilitates its interaction with the Src-homology domain 2 containing tyrosine phosphatase-1 (SHP-1) and enables SHP-1 to dephosphorylate caspase-8, permitting apoptosis to proceed. The non-receptor tyrosine kinase, Lyn, can phosphorylate caspase-8 on Tyr-397 and Tyr-465, rendering it resistant to activational cleavage and inhibiting apoptosis. Exposure to lipopolysaccharide reduces SHP-1 activity and binding to caspase-8, caspase-8 activity, and rates of spontaneous apoptosis. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248478 |
Tyr448 |
TILTEVNyEVSNKDD |
Homo sapiens |
|
pmid |
sentence |
18086677 |
Caspase-8 is tyrosine-phosphorylated in freshly isolated neutrophils but spontaneously dephosphorylates in culture, in association with the progression of constitutive apoptosis. Phosphorylation of caspase-8 on Tyr-310 facilitates its interaction with the Src-homology domain 2 containing tyrosine phosphatase-1 (SHP-1) and enables SHP-1 to dephosphorylate caspase-8, permitting apoptosis to proceed. The non-receptor tyrosine kinase, Lyn, can phosphorylate caspase-8 on Tyr-397 and Tyr-465, rendering it resistant to activational cleavage and inhibiting apoptosis. Exposure to lipopolysaccharide reduces SHP-1 activity and binding to caspase-8, caspase-8 activity, and rates of spontaneous apoptosis. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
LYN | down-regulates activity
phosphorylation
|
CASP8 |
0.317 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272979 |
Tyr380 |
TDSEEQPyLEMDLSS |
|
|
pmid |
sentence |
18086677 |
The non-receptor tyrosine kinase, Lyn, can phosphorylate caspase-8 on Tyr-397 and Tyr-465, rendering it resistant to activational cleavage and inhibiting apoptosis. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272980 |
Tyr448 |
TILTEVNyEVSNKDD |
|
|
pmid |
sentence |
18086677 |
The non-receptor tyrosine kinase, Lyn, can phosphorylate caspase-8 on Tyr-397 and Tyr-465, rendering it resistant to activational cleavage and inhibiting apoptosis. |
|
Publications: |
2 |
+ |
CASP8 | up-regulates activity
cleavage
|
CASP3 |
0.713 |
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. |
|
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. |
|
Publications: |
3 |
Organism: |
Homo Sapiens, Mus Musculus |
Pathways: | Alzheimer, COVID-19 Causal Network, Death Receptor Signaling, Mitochondrial Control of Apoptosis, SARS-COV APOPTOSIS, TNF-alpha Signaling |
+ |
M | up-regulates activity
|
CASP8 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260201 |
|
|
Homo sapiens |
|
pmid |
sentence |
25271362 |
Taken together, our results demonstrated that expression of M-protein causes activation of both caspases 8 and 9 via the PKB/Akt signalling cascades. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, SARS-COV APOPTOSIS |
+ |
FADD | up-regulates activity
binding
|
CASP8 |
0.929 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-112061 |
|
|
Homo sapiens |
|
pmid |
sentence |
11717445 |
Fadd recruits caspase-8 through homotypic interactions of death-effector domains (deds), leading to caspase-8 activation and apoptosis. In turn, fadd recruits the zymogen form of the apoptosis-initiating protease caspase-8, through homophilic interaction of death effector domains. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Alzheimer, COVID-19 Causal Network, Death Receptor Signaling, Mitochondrial Control of Apoptosis, SARS-COV APOPTOSIS, TNF-alpha Signaling |
+ |
CASP8 | up-regulates
|
Apoptosis |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-90612 |
|
|
Homo sapiens |
|
pmid |
sentence |
14585074 |
Downstream of caspase-8 activation, apoptosis induction takes place |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Alzheimer, COVID-19 Causal Network, Death Receptor Signaling, Mitochondrial Control of Apoptosis, SARS-COV APOPTOSIS, TNF-alpha Signaling |
+ |
RIPK1 | up-regulates activity
binding
|
CASP8 |
0.907 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-173432 |
|
|
Homo sapiens |
|
pmid |
sentence |
21525013 |
Degradation of ciaps triggers the release of receptor interacting protein kinase (ripk1) from tnf receptor i (tnfr1) to form a caspase-8 activating complex |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-104255 |
|
|
Homo sapiens |
|
pmid |
sentence |
12887920 |
Tradd and rip1 associate with fadd and caspase-8, forming a cytoplasmic complex |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, Death Receptor Signaling, Mitochondrial Control of Apoptosis, TNF-alpha Signaling |
+ |
CASP6 | up-regulates
cleavage
|
CASP8 |
0.722 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-109411 |
|
|
Homo sapiens |
|
pmid |
sentence |
11455969 |
This pathway can either be ampli?ed By caspase- 8-mediated cleavage of bid and by the downstream, caspase-6- mediated cleavage of caspase-8. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, SARS-COV APOPTOSIS |
+ |
Gbeta | down-regulates
phosphorylation
|
CASP8 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270118 |
|
|
Homo sapiens |
|
pmid |
sentence |
24342355 |
We demonstrate that perk 1/2 can phosphorylate pro-caspase-8 at s387 by knocking-down the endogenous pro-caspase-8 using rnai and replacing it with its non-phosphorylatable counterpart (s387a), a significant increase in caspase-8 activity |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Breast |
+ |
CASP8 | up-regulates
cleavage
|
CASP6 |
0.722 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-59857 |
|
|
Homo sapiens |
|
pmid |
sentence |
9727491 |
Casp8 can activate downstream caspases like caspase-6, and caspase-7 by directly cleaving them. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, SARS-COV APOPTOSIS |
+ |
CASP8 | up-regulates
|
Cell_death |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-256639 |
|
|
Homo sapiens |
|
pmid |
sentence |
14585074 |
Downstream of caspase-8 activation, apoptosis induction takes place |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CASP8 | up-regulates activity
|
CASP9 |
0.59 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-81811 |
|
|
in vitro |
|
pmid |
sentence |
10988287 |
One indirect means through which caspase-8 might regulate caspase-9 activation is through a bcl-2-regulated pathway. |
|
Publications: |
1 |
Organism: |
In Vitro |
Pathways: | COVID-19 Causal Network, Death Receptor Signaling, Mitochondrial Control of Apoptosis, SARS-COV APOPTOSIS |
+ |
CASP8 | up-regulates
binding
|
CASP8AP2 |
0.459 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-152473 |
|
|
Homo sapiens |
|
pmid |
sentence |
17245429 |
The caspase-8-binding protein flice-associated huge protein (flash) would form a molecular complex with caspase-8, thereby presumably activating the mitochondrial apoptosis pathway by regulating caspase-8 activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CASP8 | up-regulates activity
|
CYCS |
0.495 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-68225 |
|
|
Homo sapiens |
JURKAT Cell |
pmid |
sentence |
10364179 |
Caspase-8 triggered rapid cytochrome c release from mitochondria. The effect was indirect. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Alzheimer, COVID-19 Causal Network, Death Receptor Signaling, Mitochondrial Control of Apoptosis, SARS-COV APOPTOSIS |
+ |
CASP8 | up-regulates
cleavage
|
CASP7 |
0.729 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-159853 |
|
|
Homo sapiens |
|
pmid |
sentence |
18073771 |
Active caspase-8 then proteolytically processes and activates caspase-7 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-58118 |
|
|
Homo sapiens |
|
pmid |
sentence |
9727491 |
Casp8 can activate downstream caspases like caspase-6, and caspase-7 by directly cleaving them. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CASP8 | form complex
binding
|
Caspase 8 complex |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-256395 |
|
|
|
|
pmid |
sentence |
10508785 |
Activated caspase-8 (an alpha2beta2 heterotetramer) activates other downstream caspases that are incapable of autocatalytic processing and activation. |The alphabeta dimeric protein associates further to form an alpha2beta2 heterotetramer that appears to be required for catalytic activity. |
|
Publications: |
1 |
+ |
CFLAR | down-regulates activity
binding
|
CASP8 |
0.76 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-61122 |
|
|
Homo sapiens |
|
pmid |
sentence |
9794838 |
Flip can be incorporated into the disc complex and blocks processing and activation of pro-caspase8 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-96402 |
|
|
Homo sapiens |
|
pmid |
sentence |
14585074 |
Flip can be incorporated into the disc complex and blocks processing and activation of pro-caspase8 |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | Death Receptor Signaling |
+ |
BFAR | down-regulates
binding
|
CASP8 |
0.378 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-112585 |
|
|
Homo sapiens |
MCF-7 Cell |
pmid |
sentence |
11733517 |
We also demonstrate that the mitochondrial protein bar, which has been shown to simultaneously bind caspase-8 and bcl-2 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TRADD | up-regulates activity
binding
|
CASP8 |
0.906 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-118591 |
|
|
Homo sapiens |
|
pmid |
sentence |
14585074 |
Tradd recruits caspase-8 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Alzheimer, COVID-19 Causal Network, Death Receptor Signaling, Mitochondrial Control of Apoptosis, SARS-COV APOPTOSIS, TNF-alpha Signaling |
+ |
MAVS | up-regulates
relocalization
|
CASP8 |
0.57 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-143572 |
|
|
Homo sapiens |
|
pmid |
sentence |
16406812 |
Another protein suggested to play a role in caspase-8 translocation to mitochondria is the mitochondrial membrane protein cardif |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network |
+ |
Caspase 6 complex | up-regulates
cleavage
|
CASP8 |
0.722 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-256468 |
|
|
Homo sapiens |
|
pmid |
sentence |
11455969 |
This pathway can either be ampli?ed By caspase- 8-mediated cleavage of bid and by the downstream, caspase-6- mediated cleavage of caspase-8. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |