| + |
CASP1 | up-regulates activity 
cleavage
|
PSEN2 |
0.325 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261747 |
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-261748 |
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 |
| + |
CASP1 | up-regulates activity
cleavage
|
PSEN1 |
0.395 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261755 |
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 |
| + |
CASP1 | down-regulates activity 
cleavage
|
RNF31 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272192 |
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-272193 |
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 |
| + |
CASP1 | form complex 
binding
|
NLRC4 inflammasome |
0.707 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256402 |
|
|
|
|
| pmid |
sentence |
| 30288079 |
Canonical inflammasomes form activation platforms for caspase-1. Their assembly depends on some dedicated cytosolic PRRs from the nucleotide-binding domain leucin-rich repeat (NLR) family including NLR and pyrin domain containing receptor 1 (NLRP1), NLRP3, and NLR and caspase recruitment domain containing receptor 4 (NLRC4); the AIM2-like receptors (ALR) family including absent in melanoma 2 (AIM2); or the tripartite motif (TRIM) family including pyrin. |
|
| Publications: |
1 |
| + |
RNF31 | up-regulates activity
polyubiquitination
|
CASP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272191 |
|
|
Homo sapiens |
HaCaT II-4 Cell |
| pmid |
sentence |
| 32122970 |
HOIP forms a constitutive interaction with caspase-1 and mediates the linear ubiquitination of the CARD pro-domain. Upon engagement of apoptosis, caspase-1 and caspase-8 cleave HOIP at Asp-348 and Asp-387, limiting the ability of LUBAC to ubiquitinate substrates. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CASP1 | form complex
binding
|
AIM2 inflammasome |
0.784 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256400 |
|
|
|
|
| pmid |
sentence |
| 30288079 |
Canonical inflammasomes form activation platforms for caspase-1. Their assembly depends on some dedicated cytosolic PRRs from the nucleotide-binding domain leucin-rich repeat (NLR) family including NLR and pyrin domain containing receptor 1 (NLRP1), NLRP3, and NLR and caspase recruitment domain containing receptor 4 (NLRC4); the AIM2-like receptors (ALR) family including absent in melanoma 2 (AIM2); or the tripartite motif (TRIM) family including pyrin. |
|
| Publications: |
1 |
| + |
CASP1 | up-regulates activity
binding
|
SPHK2 |
0.252 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268831 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 20197547 |
Our data so far indicated colocalization of SphK2 with caspase-1 at the plasma membrane after induction of apoptosis.These observations supported caspase-1–dependent cleavage of SphK2 at its N-terminus as a prerequisite for its release. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CASP1 | form complex
binding
|
Caspase 1 complex |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256386 |
|
|
|
|
| pmid |
sentence |
| 7721861 |
The interleukin-1 beta-converting enzyme is a heterodimeric cysteine protease that is produced as a 45-kDa precursor. The full-length precursor form of the enzyme was expressed in Escherichia coli as insoluble inclusion bodies. Following solubilization and refolding of the 45-kDa protein, autoproteolytic conversion to a heterodimeric form containing 10- and 20-kDa subunits was observed. |
|
| Publications: |
1 |
| + |
CASP1 | form complex
binding
|
Pyrin inflammasome |
0.729 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256412 |
|
|
|
|
| pmid |
sentence |
| 30288079 |
Canonical inflammasomes form activation platforms for caspase-1. Their assembly depends on some dedicated cytosolic PRRs from the nucleotide-binding domain leucin-rich repeat (NLR) family including NLR and pyrin domain containing receptor 1 (NLRP1), NLRP3, and NLR and caspase recruitment domain containing receptor 4 (NLRC4); the AIM2-like receptors (ALR) family including absent in melanoma 2 (AIM2); or the tripartite motif (TRIM) family including pyrin. |
|
| Publications: |
1 |
| + |
CASP1 | form complex
binding
|
NLRP1 inflammasome |
0.792 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256406 |
|
|
|
|
| pmid |
sentence |
| 30288079 |
Canonical inflammasomes form activation platforms for caspase-1. Their assembly depends on some dedicated cytosolic PRRs from the nucleotide-binding domain leucin-rich repeat (NLR) family including NLR and pyrin domain containing receptor 1 (NLRP1), NLRP3, and NLR and caspase recruitment domain containing receptor 4 (NLRC4); the AIM2-like receptors (ALR) family including absent in melanoma 2 (AIM2); or the tripartite motif (TRIM) family including pyrin. |
|
| Publications: |
1 |
| + |
VX-765 | down-regulates
chemical inhibition
|
CASP1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-207770 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CASP1 | form complex
binding
|
NLRP3 inflammasome |
0.756 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256409 |
|
|
|
|
| pmid |
sentence |
| 30288079 |
Canonical inflammasomes form activation platforms for caspase-1. Their assembly depends on some dedicated cytosolic PRRs from the nucleotide-binding domain leucin-rich repeat (NLR) family including NLR and pyrin domain containing receptor 1 (NLRP1), NLRP3, and NLR and caspase recruitment domain containing receptor 4 (NLRC4); the AIM2-like receptors (ALR) family including absent in melanoma 2 (AIM2); or the tripartite motif (TRIM) family including pyrin. |
|
| Publications: |
1 |
3.0
CASP1
- 
- 