| + |
CTSG | up-regulates activity 
cleavage
|
F2R |
0.577 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263561 |
Arg41 |
TNATLDPrSFLLRNP |
in vitro |
|
| pmid |
sentence |
| 10978167 |
PAR1E and PAR2E (10 microM) were incubated in the presence of the different proteases | The enzymes were used at the following concentrations: 0.5 unit/mL thrombin, 2.5 nM trypsin, 20 nM plasmin, 20 nM cathepsin G, 20 nM elastase, 20 nM proteinase 3, and 2 units/mL calpain I and II|Protease-activated receptors (PARs) mediate cell activation after proteolytic cleavage of their extracellular amino terminus.|Protease-activated receptors (PARs) mediate cell activation after proteolytic cleavage of their extracellular amino terminus.|Arg41-Ser42 activation site |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CTSG | up-regulates activity
cleavage
|
C3 |
0.582 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256347 |
Arg748 |
ASHLGLArSNLDEDI |
Homo sapiens |
U-937 Cell |
| pmid |
sentence |
| 1861080 |
Plasma membrane elastase and cathepsin G from U937 cells cleave C3 into C3a- and C3b-like fragments; further incubation leads to C3c- and C3dg-like fragments, as judged from SDS-PAGE analysis of the digests. Sequencing of the C3b-like fragment purified by reverse phase chromatography indicates that initial cleavage of C3 by purified cathepsin G occurs at two positions in the amino-terminal part of the alpha-chain, at a Arg-Ser bond located between residues 748 and 749 and at a Leu-Asp bond between residues 751 and 752. These proteases are, thus, able to generate, on the U937 surface, active fragments of C3, which are likely to be involved in cell-protein and cell-cell interactions. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256348 |
Leu751 |
LGLARSNlDEDIIAE |
Homo sapiens |
U-937 Cell |
| pmid |
sentence |
| 1861080 |
Plasma membrane elastase and cathepsin G from U937 cells cleave C3 into C3a- and C3b-like fragments; further incubation leads to C3c- and C3dg-like fragments, as judged from SDS-PAGE analysis of the digests. Sequencing of the C3b-like fragment purified by reverse phase chromatography indicates that initial cleavage of C3 by purified cathepsin G occurs at two positions in the amino-terminal part of the alpha-chain, at a Arg-Ser bond located between residues 748 and 749 and at a Leu-Asp bond between residues 751 and 752. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CTSG | down-regulates activity 
cleavage
|
F2RL1 |
0.518 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263584 |
Leu38 |
RSSKGRSlIGKVDGT |
in vitro |
|
| pmid |
sentence |
| 10978167 |
PAR1E and PAR2E (10 microM) were incubated in the presence of the different proteases | The enzymes were used at the following concentrations: 0.5 unit/mL thrombin, 2.5 nM trypsin, 20 nM plasmin, 20 nM cathepsin G, 20 nM elastase, 20 nM proteinase 3, and 2 units/mL calpain I and II|Protease-activated receptors (PARs) mediate cell activation after proteolytic cleavage of their extracellular amino terminus.|Mass spectrometry studies of PAR2E predicted activation of PAR2 by trypsin through cleavage at the Arg36-Ser37 site, no effect of thrombin, and inactivation of the receptor by plasmin, calpain and leukocyte elastase, cathepsin G, and proteinase 3 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263585 |
Phe59 |
GVTVETVfSVDEFSA |
in vitro |
|
| pmid |
sentence |
| 10978167 |
PAR1E and PAR2E (10 microM) were incubated in the presence of the different proteases | The enzymes were used at the following concentrations: 0.5 unit/mL thrombin, 2.5 nM trypsin, 20 nM plasmin, 20 nM cathepsin G, 20 nM elastase, 20 nM proteinase 3, and 2 units/mL calpain I and II|Protease-activated receptors (PARs) mediate cell activation after proteolytic cleavage of their extracellular amino terminus.|Mass spectrometry studies of PAR2E predicted activation of PAR2 by trypsin through cleavage at the Arg36-Ser37 site, no effect of thrombin, and inactivation of the receptor by plasmin, calpain and leukocyte elastase, cathepsin G, and proteinase 3 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263586 |
Phe64 |
TVFSVDEfSASVLTG |
in vitro |
|
| pmid |
sentence |
| 10978167 |
PAR1E and PAR2E (10 microM) were incubated in the presence of the different proteases | The enzymes were used at the following concentrations: 0.5 unit/mL thrombin, 2.5 nM trypsin, 20 nM plasmin, 20 nM cathepsin G, 20 nM elastase, 20 nM proteinase 3, and 2 units/mL calpain I and II|Protease-activated receptors (PARs) mediate cell activation after proteolytic cleavage of their extracellular amino terminus.|Mass spectrometry studies of PAR2E predicted activation of PAR2 by trypsin through cleavage at the Arg36-Ser37 site, no effect of thrombin, and inactivation of the receptor by plasmin, calpain and leukocyte elastase, cathepsin G, and proteinase 3 |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
CTSG | up-regulates activity
cleavage
|
AGT |
0.627 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256312 |
Phe41 |
DRVYIHPfHLVIHNE |
in vitro |
|
| pmid |
sentence |
| 11747312 |
Cathepsin G, elastase, and proteinase 3 are serine proteinases released by activated neutrophils. Cathepsin G can cleave angiotensinogen to release angiotensin II, but this activity has not been previously reported for elastase or proteinase 3. In this study we show that elastase and proteinase 3 can release angiotensin I from angiotensinogen and release angiotensin II from angiotensin I and angiotensinogen. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CTSG | down-regulates activity
cleavage
|
F2R |
0.577 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263562 |
Phe43 |
ATLDPRSfLLRNPND |
in vitro |
|
| pmid |
sentence |
| 10978167 |
PAR1E and PAR2E (10 microM) were incubated in the presence of the different proteases | The enzymes were used at the following concentrations: 0.5 unit/mL thrombin, 2.5 nM trypsin, 20 nM plasmin, 20 nM cathepsin G, 20 nM elastase, 20 nM proteinase 3, and 2 units/mL calpain I and II|Protease-activated receptors (PARs) mediate cell activation after proteolytic cleavage of their extracellular amino terminus.|Protease-activated receptors (PARs) mediate cell activation after proteolytic cleavage of their extracellular amino terminus.|Plasmin, calpain and leukocyte elastase, cathepsin G, and proteinase 3 cleaved at multiple sites and would be expected to disable PAR1 by cleaving COOH-terminal to the activation site. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263563 |
Phe55 |
PNDKYEPfWEDEEKN |
in vitro |
|
| pmid |
sentence |
| 10978167 |
PAR1E and PAR2E (10 microM) were incubated in the presence of the different proteases | The enzymes were used at the following concentrations: 0.5 unit/mL thrombin, 2.5 nM trypsin, 20 nM plasmin, 20 nM cathepsin G, 20 nM elastase, 20 nM proteinase 3, and 2 units/mL calpain I and II|Protease-activated receptors (PARs) mediate cell activation after proteolytic cleavage of their extracellular amino terminus.|Protease-activated receptors (PARs) mediate cell activation after proteolytic cleavage of their extracellular amino terminus.|Plasmin, calpain and leukocyte elastase, cathepsin G, and proteinase 3 cleaved at multiple sites and would be expected to disable PAR1 by cleaving COOH-terminal to the activation site. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263564 |
Tyr69 |
NESGLTEyRLVSINK |
in vitro |
|
| pmid |
sentence |
| 10978167 |
PAR1E and PAR2E (10 microM) were incubated in the presence of the different proteases | The enzymes were used at the following concentrations: 0.5 unit/mL thrombin, 2.5 nM trypsin, 20 nM plasmin, 20 nM cathepsin G, 20 nM elastase, 20 nM proteinase 3, and 2 units/mL calpain I and II|Protease-activated receptors (PARs) mediate cell activation after proteolytic cleavage of their extracellular amino terminus.|Protease-activated receptors (PARs) mediate cell activation after proteolytic cleavage of their extracellular amino terminus.|Plasmin, calpain and leukocyte elastase, cathepsin G, and proteinase 3 cleaved at multiple sites and would be expected to disable PAR1 by cleaving COOH-terminal to the activation site. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
CTSG | down-regulates activity
cleavage
|
SERPIND1 |
0.455 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256509 |
Val458 |
QATTVTTvGFMPLST |
in vitro |
|
| pmid |
sentence |
| 2318847 |
Amino acid sequence analysis led to the conclusion that both neutrophil elastase and cathepsin G cleave HC at Ile66, which does not affect HC activity, and at Val439, near the reactive site Leu444, which inactivates HC. |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
CTSG
- 
- 