| + |
CASP7 | up-regulates activity 
cleavage
|
PSEN2 |
0.323 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261746 |
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-261751 |
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 |
| + |
CASP7 | up-regulates activity
cleavage
|
PSEN1 |
0.349 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261757 |
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 |
| + |
PAK2 | down-regulates 
phosphorylation
|
CASP7 |
0.357 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173655 |
Ser239 |
WRSPGRGsWFVQALC |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 21555521 |
Pak2 can bind with caspase-7 and phosphorylate caspase-7 at the ser-30, thr-173, and ser-239 sites. Functionally, the phosphorylation of caspase-7 decreases its activity, thereby inhibiting cellular apoptosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173659 |
Ser30 |
DAKPDRSsFVPSLFS |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 21555521 |
Pak2 can bind with caspase-7 and phosphorylate caspase-7 at the ser-30, thr-173, and ser-239 sites. Functionally, the phosphorylation of caspase-7 decreases its activity, thereby inhibiting cellular apoptosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173663 |
Thr173 |
FRGDRCKtLLEKPKL |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 21555521 |
Pak2 can bind with caspase-7 and phosphorylate caspase-7 at the ser-30, thr-173, and ser-239 sites. Functionally, the phosphorylation of caspase-7 decreases its activity, thereby inhibiting cellular apoptosis. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
CASP8 | up-regulates
cleavage
|
CASP7 |
0.723 |
| 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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-159853 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18073771 |
Active caspase-8 then proteolytically processes and activates caspase-7 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
Caspase 8 complex | up-regulates
cleavage
|
CASP7 |
0.723 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256459 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9727491 |
Casp8 can activate downstream caspases like caspase-6, and caspase-7 by directly cleaving them. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256454 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18073771 |
Active caspase-8 then proteolytically processes and activates caspase-7 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
XIAP | down-regulates quantity by destabilization
binding
|
CASP7 |
0.852 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-110840 |
|
|
in vitro |
|
| pmid |
sentence |
| 11583623 |
Xiap is an endogenous inhibitor of caspase-7 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-105732 |
|
|
in vitro |
|
| pmid |
sentence |
| 11257231 |
Our crystal structure of the complex between xiap (linker-bir2) and caspase-7 surprisingly revealed that the linker is the major determinant of binding and inhibition for the caspase. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| Pathways: | Inhibition of Apoptosis |
| + |
CASP7 | down-regulates
cleavage
|
PARP1 |
0.707 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-83703 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11058599 |
Caspase-7 cleaves parp;redundancy exists between the caspase-3 and -7 at the level of parp proteolysis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Inhibition of Apoptosis |
| + |
CASP7 | form complex 
binding
|
Caspase 7 complex |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256394 |
|
|
|
|
| pmid |
sentence |
| 11701129 |
The quaternary structure of caspase-7 comprises two closely associated heterodimers, with each heterodimer consisting of a large and a small subunit. |
|
| Publications: |
1 |
| Pathways: | Inhibition of Apoptosis |
3.0
CASP7
- 
- 