| + |
F2 | up-regulates activity 
cleavage
|
F8 |
0.747 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263639 |
Arg1708 |
EDENQSPrSFQKKTR |
in vitro |
|
| pmid |
sentence |
| 10350471 |
Activation of factor VIII by thrombin occurs via limited proteolysis at R372, R740, and R1689. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263640 |
Arg391 |
SPSFIQIrSVAKKHP |
in vitro |
|
| pmid |
sentence |
| 10350471 |
Activation of factor VIII by thrombin occurs via limited proteolysis at R372, R740, and R1689. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263641 |
Arg759 |
KNNAIEPrSFSQNSR |
in vitro |
|
| pmid |
sentence |
| 10350471 |
Activation of factor VIII by thrombin occurs via limited proteolysis at R372, R740, and R1689. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
Factor FVIIa:TF | down-regulates activity 
cleavage
|
F8 |
0.475 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263643 |
Arg355 |
CPEEPQLrMKNNEEA |
in vitro |
|
| pmid |
sentence |
| 10350471 |
N-Terminal sequencing along with time courses of proteolysis indicated that VIIa-TF/PL cleaved factor VIII first at R740, followed by concomitant cleavage at R336 and R372. |hus, heavy chain cleavage of factor VIII by VIIa-TF/PL produces an inactive factor VIII cofactor no longer capable of activation by thrombin. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263642 |
Arg391 |
SPSFIQIrSVAKKHP |
in vitro |
|
| pmid |
sentence |
| 10350471 |
N-Terminal sequencing along with time courses of proteolysis indicated that VIIa-TF/PL cleaved factor VIII first at R740, followed by concomitant cleavage at R336 and R372. |hus, heavy chain cleavage of factor VIII by VIIa-TF/PL produces an inactive factor VIII cofactor no longer capable of activation by thrombin. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263644 |
Arg759 |
KNNAIEPrSFSQNSR |
in vitro |
|
| pmid |
sentence |
| 10350471 |
N-Terminal sequencing along with time courses of proteolysis indicated that VIIa-TF/PL cleaved factor VIII first at R740, followed by concomitant cleavage at R336 and R372. |hus, heavy chain cleavage of factor VIII by VIIa-TF/PL produces an inactive factor VIII cofactor no longer capable of activation by thrombin. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
CSNK2A3 | down-regulates activity
phosphorylation
|
F8 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263649 |
Ser1656 |
GRTERLCsQNPPVLK |
in vitro |
|
| pmid |
sentence |
| 8427963 |
Our findings suggest that phosphorylation of factors Va and VIIIa by a platelet casein kinase II-like kinase may downregulate the activity of the two cofactors.| Recombinant human factor VIII also showed incorporation of radioactivity in the presence of purified casein kinase II at the acidic NH2-terminal portion of factor VIII light chain (residues 1648 through 1689). Based on all the considerations reported above Se1657 is the most likely candidate within this region capable of incorporation of radioactivity |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
VWF | up-regulates quantity by stabilization 
|
F8 |
0.783 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261865 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32644488 |
VWF plays a crucial role in hemostasis through platelet adhesion facilitation and coagulation factor VIII stabilization |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
VWF | up-regulates activity
binding
|
F8 |
0.783 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251967 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23020315 |
Binding of FVIII to VWF is needed to maintain appropriate plasma levels, as FVIII plasma levels and half-life are remarkably reduced in the absence of VWF |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
F8 | form complex 
binding
|
Factor VIIIa-IXa |
0.758 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263553 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 25769543 |
The present data point to key roles of FVIII and FIX in FX activation at the site of a platelet thrombus by supporting: (i) thrombin generation, (ii) thrombus growth and platelet phosphatidylserine exposure, and (iii) fibrin formation at the platelet surface. The likely mechanism is that tenase activity via FVIIIa and FIXa, which is confined to the sites of platelet thrombi, generates FXa that directly catalyzes the conversion of prothrombin into thrombin. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Blood Plasma |
3.0
F8
- 
- 