| + |
F10 | up-regulates activity 
cleavage
|
F7 |
0.52 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263523 |
Arg212 |
NASKPQGrIVGGKVC |
Homo sapiens |
|
| pmid |
sentence |
| 12524220 |
The factor VII zymogen is cleaved at arginine 152 by a variety of proteases, including thrombin, factor IXa, factor Xa, and factor VIIa–tissue factor to produce the serine protease factor VIIa. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Blood Plasma |
| Pathways: | Vitamin-K cycle |
| + |
GGCX | up-regulates activity
carboxylation
|
F10 |
0.598 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263664 |
Glu46 |
TRANSFLeEMKKGHL |
in vitro |
|
| pmid |
sentence |
| 9538022 |
This report describes the expression, purification, and characterization of a series of recombinant factor Xa variants bearing aspartate substitutions for each of the glutamate residues which normally undergo gamma-carboxylation. |We have produced fully active recombinant human factor Xa and demonstrated that gla residues 16, 26, and 29 are critical for normal activity of factor Xa.|This observation suggests that, for wild-type r-fX expressed in HEK cells, carboxylation by the gamma-glutamyl carboxylase proceeds to completion once initiated; | 11 amino terminal glutamic acid residues of fX which normally undergo gamma-carboxylation (glas 6, 7, 14, 16, 19, 20, 25, 26, 29, 32, 39). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263665 |
Glu47 |
RANSFLEeMKKGHLE |
in vitro |
|
| pmid |
sentence |
| 9538022 |
This report describes the expression, purification, and characterization of a series of recombinant factor Xa variants bearing aspartate substitutions for each of the glutamate residues which normally undergo gamma-carboxylation. |We have produced fully active recombinant human factor Xa and demonstrated that gla residues 16, 26, and 29 are critical for normal activity of factor Xa.|This observation suggests that, for wild-type r-fX expressed in HEK cells, carboxylation by the gamma-glutamyl carboxylase proceeds to completion once initiated; | 11 amino terminal glutamic acid residues of fX which normally undergo gamma-carboxylation (glas 6, 7, 14, 16, 19, 20, 25, 26, 29, 32, 39). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263666 |
Glu54 |
EMKKGHLeRECMEET |
in vitro |
|
| pmid |
sentence |
| 9538022 |
This report describes the expression, purification, and characterization of a series of recombinant factor Xa variants bearing aspartate substitutions for each of the glutamate residues which normally undergo gamma-carboxylation. |We have produced fully active recombinant human factor Xa and demonstrated that gla residues 16, 26, and 29 are critical for normal activity of factor Xa.|This observation suggests that, for wild-type r-fX expressed in HEK cells, carboxylation by the gamma-glutamyl carboxylase proceeds to completion once initiated; | 11 amino terminal glutamic acid residues of fX which normally undergo gamma-carboxylation (glas 6, 7, 14, 16, 19, 20, 25, 26, 29, 32, 39). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263667 |
Glu56 |
KKGHLEReCMEETCS |
in vitro |
|
| pmid |
sentence |
| 9538022 |
This report describes the expression, purification, and characterization of a series of recombinant factor Xa variants bearing aspartate substitutions for each of the glutamate residues which normally undergo gamma-carboxylation. |We have produced fully active recombinant human factor Xa and demonstrated that gla residues 16, 26, and 29 are critical for normal activity of factor Xa.|This observation suggests that, for wild-type r-fX expressed in HEK cells, carboxylation by the gamma-glutamyl carboxylase proceeds to completion once initiated; | 11 amino terminal glutamic acid residues of fX which normally undergo gamma-carboxylation (glas 6, 7, 14, 16, 19, 20, 25, 26, 29, 32, 39). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263668 |
Glu59 |
HLERECMeETCSYEE |
in vitro |
|
| pmid |
sentence |
| 9538022 |
This report describes the expression, purification, and characterization of a series of recombinant factor Xa variants bearing aspartate substitutions for each of the glutamate residues which normally undergo gamma-carboxylation. |We have produced fully active recombinant human factor Xa and demonstrated that gla residues 16, 26, and 29 are critical for normal activity of factor Xa.|This observation suggests that, for wild-type r-fX expressed in HEK cells, carboxylation by the gamma-glutamyl carboxylase proceeds to completion once initiated; | 11 amino terminal glutamic acid residues of fX which normally undergo gamma-carboxylation (glas 6, 7, 14, 16, 19, 20, 25, 26, 29, 32, 39). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263669 |
Glu60 |
LERECMEeTCSYEEA |
in vitro |
|
| pmid |
sentence |
| 9538022 |
This report describes the expression, purification, and characterization of a series of recombinant factor Xa variants bearing aspartate substitutions for each of the glutamate residues which normally undergo gamma-carboxylation. |We have produced fully active recombinant human factor Xa and demonstrated that gla residues 16, 26, and 29 are critical for normal activity of factor Xa.|This observation suggests that, for wild-type r-fX expressed in HEK cells, carboxylation by the gamma-glutamyl carboxylase proceeds to completion once initiated; | 11 amino terminal glutamic acid residues of fX which normally undergo gamma-carboxylation (glas 6, 7, 14, 16, 19, 20, 25, 26, 29, 32, 39). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263670 |
Glu65 |
MEETCSYeEAREVFE |
in vitro |
|
| pmid |
sentence |
| 9538022 |
This report describes the expression, purification, and characterization of a series of recombinant factor Xa variants bearing aspartate substitutions for each of the glutamate residues which normally undergo gamma-carboxylation. |We have produced fully active recombinant human factor Xa and demonstrated that gla residues 16, 26, and 29 are critical for normal activity of factor Xa.|This observation suggests that, for wild-type r-fX expressed in HEK cells, carboxylation by the gamma-glutamyl carboxylase proceeds to completion once initiated; | 11 amino terminal glutamic acid residues of fX which normally undergo gamma-carboxylation (glas 6, 7, 14, 16, 19, 20, 25, 26, 29, 32, 39). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263671 |
Glu66 |
EETCSYEeAREVFED |
in vitro |
|
| pmid |
sentence |
| 9538022 |
This report describes the expression, purification, and characterization of a series of recombinant factor Xa variants bearing aspartate substitutions for each of the glutamate residues which normally undergo gamma-carboxylation. |We have produced fully active recombinant human factor Xa and demonstrated that gla residues 16, 26, and 29 are critical for normal activity of factor Xa.|This observation suggests that, for wild-type r-fX expressed in HEK cells, carboxylation by the gamma-glutamyl carboxylase proceeds to completion once initiated; | 11 amino terminal glutamic acid residues of fX which normally undergo gamma-carboxylation (glas 6, 7, 14, 16, 19, 20, 25, 26, 29, 32, 39). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263672 |
Glu69 |
CSYEEAReVFEDSDK |
in vitro |
|
| pmid |
sentence |
| 9538022 |
This report describes the expression, purification, and characterization of a series of recombinant factor Xa variants bearing aspartate substitutions for each of the glutamate residues which normally undergo gamma-carboxylation. |We have produced fully active recombinant human factor Xa and demonstrated that gla residues 16, 26, and 29 are critical for normal activity of factor Xa.|This observation suggests that, for wild-type r-fX expressed in HEK cells, carboxylation by the gamma-glutamyl carboxylase proceeds to completion once initiated; | 11 amino terminal glutamic acid residues of fX which normally undergo gamma-carboxylation (glas 6, 7, 14, 16, 19, 20, 25, 26, 29, 32, 39). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263673 |
Glu72 |
EEAREVFeDSDKTNE |
in vitro |
|
| pmid |
sentence |
| 9538022 |
This report describes the expression, purification, and characterization of a series of recombinant factor Xa variants bearing aspartate substitutions for each of the glutamate residues which normally undergo gamma-carboxylation. |We have produced fully active recombinant human factor Xa and demonstrated that gla residues 16, 26, and 29 are critical for normal activity of factor Xa.|This observation suggests that, for wild-type r-fX expressed in HEK cells, carboxylation by the gamma-glutamyl carboxylase proceeds to completion once initiated; | 11 amino terminal glutamic acid residues of fX which normally undergo gamma-carboxylation (glas 6, 7, 14, 16, 19, 20, 25, 26, 29, 32, 39). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263674 |
Glu79 |
EDSDKTNeFWNKYKD |
in vitro |
|
| pmid |
sentence |
| 9538022 |
This report describes the expression, purification, and characterization of a series of recombinant factor Xa variants bearing aspartate substitutions for each of the glutamate residues which normally undergo gamma-carboxylation. |We have produced fully active recombinant human factor Xa and demonstrated that gla residues 16, 26, and 29 are critical for normal activity of factor Xa.|This observation suggests that, for wild-type r-fX expressed in HEK cells, carboxylation by the gamma-glutamyl carboxylase proceeds to completion once initiated; | 11 amino terminal glutamic acid residues of fX which normally undergo gamma-carboxylation (glas 6, 7, 14, 16, 19, 20, 25, 26, 29, 32, 39). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265921 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31226734 |
Thus, vitamin K acts as a cofactor for GGCX via the vitamin K cycle and exerts physiological effects through its regulation of VKDPs [29]. More than 20 VKDPs have been found. Osteocalcin promotes bone formation, and blood coagulation factors II, VII, IX, and X activate blood coagulation. Matrix Gla protein suppresses cardiovascular calcification, and brain-expressed Gas 6 promotes neural differentiation [29]. GGCX is an enzyme that converts glutamic acid (Glu) residues to Gla residues, so that the Gla-containing proteins can exert various physiological actions such as blood coagulation and bone formation. |
|
| Publications: |
12 |
Organism: |
In Vitro, Homo Sapiens |
| Pathways: | Vitamin-K cycle |
| + |
F10 | down-regulates activity 
cleavage
|
APOH |
0.394 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266997 |
Lys336 |
HSSLAFWKTDASDVK |
in vitro |
|
| pmid |
sentence |
| 9596664 |
In the previous study, we found that factor Xa can produce the nicked form by cleaving Lys 317-Thr 318, using recombinant human domain V (r-Domain V). |The cleavage was completely inhibited by plasmin inhibitor (alpha2PI). The nicked form was demonstrated to show reduced affinity for CL with a dissociation constant of one order of magnitude larger than that of the intact beta2GPI. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
Factor FVIIa:TF | up-regulates activity
binding
|
F10 |
0.638 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263543 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32665005 |
During vascular injury, TF is exposed to the blood, where it functions as a cofactor for the circulating zymogen factor VII (FVII). This TF:FVIIa complex can then bind and activate either factor IX (FIX) or factor X (FX), triggering a cascade that generates fibrin and activates platelets, resulting in a hemostatic plug at the site of injury. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Blood Plasma |
| + |
F7 | up-regulates activity
binding
|
F10 |
0.52 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263545 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29880919 |
TF has a high affinity for FVII and enables the trace levels (∼1% of the total FVII) of activated FVII (FVIIa) in the blood to cleave specific sites in the serine proteases FIX and FX, activating them into FIXa and FXa, respectively. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Blood Plasma |
| Pathways: | Vitamin-K cycle |
| + |
BMS-740808 | down-regulates
chemical inhibition
|
F10 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-190488 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SERPINC1 | down-regulates activity
cleavage
|
F10 |
0.872 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264138 |
|
|
|
|
| pmid |
sentence |
| 31030036 |
Antithrombin (AT), a member of the serine protease inhibitor (SERPIN) superfamily, is a major circulating inhibitor of blood coagulation proteases such as factor (F) IIa (known as thrombin), FXa and, to a lesser extent, FIXa, FXIa and FXIIa. SERPINC1, which encodes AT in humans, is located on chromosome 1q25.1 |
|
| Publications: |
1 |
| + |
F10 | up-regulates activity
cleavage
|
F2 |
0.436 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263539 |
|
|
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 |
| Pathways: | Vitamin-K cycle |
| + |
rivaroxaban | down-regulates
chemical inhibition
|
F10 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-206550 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
apixaban | down-regulates
chemical inhibition
|
F10 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-189865 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
betrixaban | down-regulates activity
chemical inhibition
|
F10 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257817 |
|
|
in vitro |
|
| pmid |
sentence |
| 19297154 |
Discovery of betrixaban (PRT054021), N-(5-chloropyridin-2-yl)-2-(4-(N,N-dimethylcarbamimidoyl)benzamido)-5-methoxybenzamide, a highly potent, selective, and orally efficacious factor Xa inhibitor. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
F10 | form complex 
binding
|
Factor Va-Xa |
0.765 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263557 |
|
|
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 |
| + |
edoxaban | down-regulates activity
chemical inhibition
|
F10 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257845 |
|
|
in vitro |
|
| pmid |
sentence |
| 20503967 |
Replacing the chloroindole P1 moiety of 100 with a 5-chloropyridin-2-yloxalamide group provided 101 (edoxaban, DU-176b). Compound 101 is a potent inhibitor of human FXa in vitro (FXa Ki = 0.56 nM), with >10 000-fold selectivity against relevant serine proteases, and demonstrated good anticoagulant activity (PT2× = 0.26 μM) and activity in various animal models of thrombosis, with minimal bleeding |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
Factor VIIIa-IXa | up-regulates activity
cleavage
|
F10 |
0.553 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263538 |
|
|
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
F10
- 
- 