| + |
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 |
| + |
F2 | up-regulates activity 
cleavage,
|
F5 |
0.877 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263631 |
Arg1046 |
HHAPLSPrTFHPLRS |
in vitro |
|
| pmid |
sentence |
| 10026263 |
Thrombin is considered the physiological activator of factor V and is the most potent activator, catalyzing the cleavage of three peptide bonds at Arg709, Arg1018, and Arg1545 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263632 |
Arg737 |
LAAALGIrSFRNSSL |
in vitro |
|
| pmid |
sentence |
| 10026263 |
Thrombin is considered the physiological activator of factor V and is the most potent activator, catalyzing the cleavage of three peptide bonds at Arg709, Arg1018, and Arg1545 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263530 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29880919 |
Thrombin also activates the cofactors FVIII (to FVIIIa) and FV (to FVa) and activates platelets such that they provide a procoagulant membrane surface to which these proteins then bind |
|
| Publications: |
3 |
Organism: |
In Vitro, Homo Sapiens |
| Tissue: |
Blood Plasma |
| + |
Factor FVIIa:TF | down-regulates activity
cleavage
|
F5 |
0.496 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263645 |
Arg1046 |
HHAPLSPrTFHPLRS |
in vitro |
|
| pmid |
sentence |
| 10026263 |
Factor VIIa/tissue factor generates a form of factor V with unchanged specific activity, resistance to activation by thrombin, and increased sensitivity to activated protein C| In this study, we found that TF/VIIa was able to cleave multiple peptide bonds in the coagulation cofactor, factor V. SDS-PAGE analysis and sequencing indicated the factor V was cleaved at Arg679, Arg709, Arg1018, and Arg1192 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263648 |
Arg1220 |
LSPELIQrNLSPALG |
in vitro |
|
| pmid |
sentence |
| 10026263 |
Thrombin is considered the physiological activator of factor V and is the most potent activator, catalyzing the cleavage of three peptide bonds at Arg709, Arg1018, and Arg1545 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263647 |
Arg707 |
ESTVMATrKMHDRLE |
in vitro |
|
| pmid |
sentence |
| 10026263 |
Thrombin is considered the physiological activator of factor V and is the most potent activator, catalyzing the cleavage of three peptide bonds at Arg709, Arg1018, and Arg1545 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263646 |
Arg737 |
LAAALGIrSFRNSSL |
in vitro |
|
| pmid |
sentence |
| 10026263 |
Thrombin is considered the physiological activator of factor V and is the most potent activator, catalyzing the cleavage of three peptide bonds at Arg709, Arg1018, and Arg1545 |
|
| Publications: |
4 |
Organism: |
In Vitro |
| + |
PROC | down-regulates activity
cleavage
|
F5 |
0.583 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263628 |
Arg334 |
KNCPKKTrNLKKITR |
in vitro |
|
| pmid |
sentence |
| 7989361 |
The mechanism of inactivation of human factor V and human factor Va by activated protein C|Membrane-bound human factor V (250 nM) is cleaved by APC (2.5 nM) to give M(r) = 200,000, 70,000, 45,000, and 30,000 fragments and an M(r) = 22/20,000 doublet. These fragments are released after four sequential cleavages of the membrane-bound procofactor at Arg306, Arg506, Arg679, and Lys994. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263629 |
Arg534 |
KSRSLDRrGIQRAAD |
in vitro |
|
| pmid |
sentence |
| 7989361 |
The mechanism of inactivation of human factor V and human factor Va by activated protein C|Membrane-bound human factor V (250 nM) is cleaved by APC (2.5 nM) to give M(r) = 200,000, 70,000, 45,000, and 30,000 fragments and an M(r) = 22/20,000 doublet. These fragments are released after four sequential cleavages of the membrane-bound procofactor at Arg306, Arg506, Arg679, and Lys994. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263630 |
Arg707 |
ESTVMATrKMHDRLE |
in vitro |
|
| pmid |
sentence |
| 7989361 |
The mechanism of inactivation of human factor V and human factor Va by activated protein C|Membrane-bound human factor V (250 nM) is cleaved by APC (2.5 nM) to give M(r) = 200,000, 70,000, 45,000, and 30,000 fragments and an M(r) = 22/20,000 doublet. These fragments are released after four sequential cleavages of the membrane-bound procofactor at Arg306, Arg506, Arg679, and Lys994. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263627 |
Lys1022 |
GGKSRLKkSQFLIKT |
in vitro |
|
| pmid |
sentence |
| 7989361 |
The mechanism of inactivation of human factor V and human factor Va by activated protein C|Membrane-bound human factor V (250 nM) is cleaved by APC (2.5 nM) to give M(r) = 200,000, 70,000, 45,000, and 30,000 fragments and an M(r) = 22/20,000 doublet. These fragments are released after four sequential cleavages of the membrane-bound procofactor at Arg306, Arg506, Arg679, and Lys994. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263528 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29880919 |
Activated protein C (APC), which cleaves and inactivates both FVIIIa and FVa, thereby shutting down both the tenase and prothrombinase complexes |
|
| Publications: |
5 |
Organism: |
In Vitro, Homo Sapiens |
| Tissue: |
Blood Plasma |
| + |
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 |
| + |
CSNK2A1 | down-regulates activity
phosphorylation
|
F5 |
0.311 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250862 |
Ser692 |
IPDDDEDsYEIFEPP |
in vitro |
|
| pmid |
sentence |
| 9525959 |
Factor Va, the essential cofactor for prothrombinase, is phosphorylated on the acidic COOH terminus of the heavy chain of the cofactor, at Ser692, by a platelet membrane-associated casein kinase II (CKII). | The phosphorylated cofactor has increased susceptibility to inactivation by activated protein C, since phosphorylated factor Va was found to be inactivated approximately 3-fold faster than its native counterpart. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
F5 | form complex 
binding
|
Factor Va-Xa |
0.765 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263558 |
|
|
in vitro |
|
| pmid |
sentence |
| 2026608 |
The binding of factor Xa to factor Va in the presence of Ca2+ ions and phospholipid is fundamental for the activation of prothrombin to thrombin. |Regardless of which protein was labeled, a factor Xa-Va complex (s20,w = 9.8) was formed. The interaction is specific and reversible. I |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
F5
- 
- 