| + |
CAPN2 | down-regulates activity 
cleavage
|
F2RL1 |
0.301 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263581 |
Gly71 |
FSASVLTgKLTTVFL |
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-263582 |
Thr45 |
LIGKVDGtSHVTGKG |
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-263583 |
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 |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
MAPK3 | up-regulates 
phosphorylation
|
CAPN2 |
0.547 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-123083 |
Ser50 |
GTLFQDPsFPAIPSA |
Homo sapiens |
|
| pmid |
sentence |
| 14993287 |
Epidermal growth factor activates m-calpain (calpain ii), at least in part, by extracellular signal-regulated kinase-mediated phosphorylation.We now show that erk directly phosphorylates and activates m-calpain both in vitro and in vivo. We identified serine 50 as required for epidermal growth factor (egf)-induced calpain activation in vitro and in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK1 | up-regulates
phosphorylation
|
CAPN2 |
0.611 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-123079 |
Ser50 |
GTLFQDPsFPAIPSA |
Homo sapiens |
|
| pmid |
sentence |
| 14993287 |
Epidermal growth factor activates m-calpain (calpain ii), at least in part, by extracellular signal-regulated kinase-mediated phosphorylation.We now show that erk directly phosphorylates and activates m-calpain both in vitro and in vivo. We identified serine 50 as required for epidermal growth factor (egf)-induced calpain activation in vitro and in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKACA | down-regulates
phosphorylation
|
CAPN2 |
0.265 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-116248 |
Thr370 |
GNWRRGStAGGCRNY |
Homo sapiens |
|
| pmid |
sentence |
| 11909964 |
Activation of m-calpain (calpain ii) by epidermal growth factor is limited by protein kinase a phosphorylation of m-calpain.These Data point to a novel mechanism of negative control of calpain activation, direct phosphorylation by pka. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SRC | up-regulates activity
phosphorylation
|
CAPN2 |
0.505 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277598 |
Tyr625 |
RSGTMNSyEMRKALE |
in vitro |
|
| pmid |
sentence |
| 35697802 |
CAPN2 itself was a bone fide substrate of SRC that was primarily phosphorylated at Y625 by SRC and exhibited increased proteolysis activity upon phosphorylation. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CAPN2 | up-regulates activity
cleavage
|
GSK3B |
0.289 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251613 |
|
|
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 25969760 |
Thus, it has been shown that calpain cleaves the inhibitory domain of GSK3 generating two fragments of 40 and 30 kDa. This cleavage enhanced activity of the kinase |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAPN2 | down-regulates activity
cleavage
|
MAPT |
0.445 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251611 |
|
|
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 25969760 |
Besides tau phosphorylation, calpain activation might play a role in tau-mediated neurodegeneration by inducing tau cleavage. In vitro studies have shown that both fetal and adult tau isoforms are rapidly proteolyzed by calpains |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAPN2 | up-regulates activity
cleavage
|
CDK5R1 |
0.545 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251610 |
|
|
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 25969760 |
Calpains also modulate the activity of CDK5. Physiologically, CDK 5 is activated by p35 and its cleaved product p25. The latter has a longer half life than p35 and therefore it is a more potent activator of CDK5. The cleavage of p35 to p25 is mediated by calpain |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAPN2 | up-regulates activity
cleavage
|
CDK5/CDK5R1 |
0.551 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251608 |
|
|
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 25969760 |
Calpains also modulate the activity of CDK5. Physiologically, CDK 5 is activated by p35 and its cleaved product p25. The latter has a longer half life than p35 and therefore it is a more potent activator of CDK5. The cleavage of p35 to p25 is mediated by calpain |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAPN2 | up-regulates activity
cleavage
|
GSK3A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251612 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25969760 |
Thus, it has been shown that calpain cleaves the inhibitory domain of GSK3 generating two fragments of 40 and 30 kDa. This cleavage enhanced activity of the kinase |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAST | down-regulates activity
binding
|
CAPN2 |
0.901 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251609 |
|
|
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 25969760 |
In addition to Ca2+, calpastatin has a key role in the regulation of calpain. Calpastatin, a heat-stable protein ranging from ~70 to ~140 kDa of apparent molecular weight depending on the cell type, is considered a specific endogenous inhibitor of calpains|The calpastatin molecule contains four inhibitory units [75–77]. Each of these units binds to one calpain molecule [75–77]. Therefore, the ratio calpain/calpastatin plays a key role in the regulation of calpain activity [78–80]. The inhibitory effect of calpastatin requires Ca2+-dependent high-affinity binding to three sites of calpain |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERK1/2 | up-regulates
phosphorylation
|
CAPN2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270179 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14993287 |
Epidermal growth factor activates m-calpain (calpain ii), at least in part, by extracellular signal-regulated kinase-mediated phosphorylation.We now show that erk directly phosphorylates and activates m-calpain both in vitro and in vivo. We identified serine 50 as required for epidermal growth factor (egf)-induced calpain activation in vitro and in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Gbeta | up-regulates
phosphorylation
|
CAPN2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270078 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14993287 |
Epidermal growth factor activates m-calpain (calpain ii), at least in part, by extracellular signal-regulated kinase-mediated phosphorylation.We now show that erk directly phosphorylates and activates m-calpain both in vitro and in vivo. We identified serine 50 as required for epidermal growth factor (egf)-induced calpain activation in vitro and in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CAPN2
- 
- 