| + |
ELANE | up-regulates activity 
cleavage
|
F2R |
0.441 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263565 |
Ala36 |
PESKATNaTLDPRSF |
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.|Protease-activated receptors (PARs) mediate cell activation after proteolytic cleavage of their extracellular amino terminus |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ELANE | down-regulates activity 
cleavage
|
F5 |
0.373 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263635 |
Ala369 |
DYAPVIPaNMDKKYR |
in vitro |
|
| pmid |
sentence |
| 9242537 |
Human neutrophil elastase activates human factor V but inactivates thrombin-activated human factor V|NH2-terminal sequence analysis of F.Va treated with HNE indicated cleavage at Ala341, Ile508, and Thr1767 under conditions, which the cofactor became inactivated, as measured by prothrombinase activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263636 |
Ile536 |
RSLDRRGiQRAADIE |
in vitro |
|
| pmid |
sentence |
| 9242537 |
Human neutrophil elastase activates human factor V but inactivates thrombin-activated human factor V|NH2-terminal sequence analysis of F.Va treated with HNE indicated cleavage at Ala341, Ile508, and Thr1767 under conditions, which the cofactor became inactivated, as measured by prothrombinase activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263634 |
Thr1795 |
SRSSWRLtSSEMKKS |
in vitro |
|
| pmid |
sentence |
| 9242537 |
Human neutrophil elastase activates human factor V but inactivates thrombin-activated human factor V|NH2-terminal sequence analysis of F.Va treated with HNE indicated cleavage at Ala341, Ile508, and Thr1767 under conditions, which the cofactor became inactivated, as measured by prothrombinase activity. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
ELANE | down-regulates activity
cleavage
|
F2R |
0.441 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263566 |
Ala86 |
PLQKQLPaFISEDAS |
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-263567 |
Val72 |
GLTEYRLvSINKSSP |
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: |
2 |
Organism: |
In Vitro |
| + |
ELANE | up-regulates activity
cleavage
|
F5 |
0.373 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263633 |
Ile1512 |
KEFNPLViVGLSKDG |
in vitro |
|
| pmid |
sentence |
| 9242537 |
Human neutrophil elastase activates human factor V but inactivates thrombin-activated human factor V|NH2-terminal sequence analysis of F.V treated with HNE indicated cleavage at Ile819 and Ile1484 under conditions during which the procofactor expressed enhanced cofactor activity in the prothrombinase complex. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263637 |
Ile847 |
LQPDVTGiRLLSLGA |
in vitro |
|
| pmid |
sentence |
| 9242537 |
Human neutrophil elastase activates human factor V but inactivates thrombin-activated human factor V|NH2-terminal sequence analysis of F.V treated with HNE indicated cleavage at Ile819 and Ile1484 under conditions during which the procofactor expressed enhanced cofactor activity in the prothrombinase complex. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
ELANE | up-regulates activity
cleavage
|
AGT |
0.279 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256313 |
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 |
| + |
ELANE | down-regulates activity
cleavage
|
F2RL1 |
0.404 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263587 |
Thr74 |
SVLTGKLtTVFLPIV |
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-263588 |
Val42 |
GRSLIGKvDGTSHVT |
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-263589 |
Val48 |
KVDGTSHvTGKGVTV |
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-263590 |
Val53 |
SHVTGKGvTVETVFS |
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-263591 |
Val58 |
KGVTVETvFSVDEFS |
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-263592 |
Val76 |
LTGKLTTvFLPIVYT |
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: |
6 |
Organism: |
In Vitro |
| + |
ELANE | down-regulates activity
cleavage
|
SERPIND1 |
0.462 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256510 |
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 |
| + |
LEF1 | up-regulates quantity by expression 
transcriptional regulation
|
ELANE |
0.259 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254550 |
|
|
Homo sapiens |
Bone Marrow Cell |
| pmid |
sentence |
| 14594802 |
We find that LEF-1 and CBFalpha co-activate ELA2 expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CEBPA | up-regulates quantity by expression
transcriptional regulation
|
ELANE |
0.313 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253769 |
|
|
Homo sapiens |
Culture Condition:CD34+ Cell |
| pmid |
sentence |
| 19620402 |
The ELA2 gene promoter is positively regulated by the direct binding of LEF-1 or C/EBPalpha, documenting the role of LEF1 in the diminished ELA2 expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RUNX1 | up-regulates quantity by expression
transcriptional regulation
|
ELANE |
0.325 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254553 |
|
|
Homo sapiens |
Bone Marrow Cell |
| pmid |
sentence |
| 14594802 |
We find that LEF-1 and CBFalpha co-activate ELA2 expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RUNX3 | up-regulates quantity by expression
transcriptional regulation
|
ELANE |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254554 |
|
|
Homo sapiens |
Bone Marrow Cell |
| pmid |
sentence |
| 14594802 |
We find that LEF-1 and CBFalpha co-activate ELA2 expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RUNX2 | up-regulates quantity by expression
transcriptional regulation
|
ELANE |
0.259 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254552 |
|
|
Homo sapiens |
Bone Marrow Cell |
| pmid |
sentence |
| 14594802 |
We find that LEF-1 and CBFalpha co-activate ELA2 expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
ELANE
- 
- 