| + |
F9 | up-regulates activity 
cleavage
|
F7 |
0.529 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263522 |
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
|
F9 |
0.67 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263686 |
Glu53 |
RYNSGKLeEFVQGNL |
Mus musculus |
|
| pmid |
sentence |
| 11133752 |
The direct gamma-carboxyglutamic acid analysis and the N-terminal sequence analysis of the myotube-synthesized F.IX demonstrate efficient carboxylation at 11 of 12 γ-carboxyglutamic acid residues. |In previous work54 we have demonstrated that the γ-glutamyl carboxylase is present in skeletal muscle, but at a level only 5% to 10% of that found in the liver. This level of enzyme appears to be sufficient to provide full carboxylation of F.IX synthesized in myotubes|Glu 7, 8, 15, 17, 20, 21, 26, 27, 30, 33, and 36 are each less than 10% of the yield at the previous and subsequent cycles. Only a single γ-carboxylated residue, Gla 40, was not assessed by N-terminal sequencing. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263687 |
Glu54 |
YNSGKLEeFVQGNLE |
Mus musculus |
|
| pmid |
sentence |
| 11133752 |
The direct gamma-carboxyglutamic acid analysis and the N-terminal sequence analysis of the myotube-synthesized F.IX demonstrate efficient carboxylation at 11 of 12 γ-carboxyglutamic acid residues. |In previous work54 we have demonstrated that the γ-glutamyl carboxylase is present in skeletal muscle, but at a level only 5% to 10% of that found in the liver. This level of enzyme appears to be sufficient to provide full carboxylation of F.IX synthesized in myotubes|Glu 7, 8, 15, 17, 20, 21, 26, 27, 30, 33, and 36 are each less than 10% of the yield at the previous and subsequent cycles. Only a single γ-carboxylated residue, Gla 40, was not assessed by N-terminal sequencing. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263688 |
Glu61 |
EFVQGNLeRECMEEK |
Mus musculus |
|
| pmid |
sentence |
| 11133752 |
The direct gamma-carboxyglutamic acid analysis and the N-terminal sequence analysis of the myotube-synthesized F.IX demonstrate efficient carboxylation at 11 of 12 γ-carboxyglutamic acid residues. |In previous work54 we have demonstrated that the γ-glutamyl carboxylase is present in skeletal muscle, but at a level only 5% to 10% of that found in the liver. This level of enzyme appears to be sufficient to provide full carboxylation of F.IX synthesized in myotubes|Glu 7, 8, 15, 17, 20, 21, 26, 27, 30, 33, and 36 are each less than 10% of the yield at the previous and subsequent cycles. Only a single γ-carboxylated residue, Gla 40, was not assessed by N-terminal sequencing. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263689 |
Glu63 |
VQGNLEReCMEEKCS |
Mus musculus |
|
| pmid |
sentence |
| 11133752 |
The direct gamma-carboxyglutamic acid analysis and the N-terminal sequence analysis of the myotube-synthesized F.IX demonstrate efficient carboxylation at 11 of 12 γ-carboxyglutamic acid residues. |In previous work54 we have demonstrated that the γ-glutamyl carboxylase is present in skeletal muscle, but at a level only 5% to 10% of that found in the liver. This level of enzyme appears to be sufficient to provide full carboxylation of F.IX synthesized in myotubes|Glu 7, 8, 15, 17, 20, 21, 26, 27, 30, 33, and 36 are each less than 10% of the yield at the previous and subsequent cycles. Only a single γ-carboxylated residue, Gla 40, was not assessed by N-terminal sequencing. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263690 |
Glu66 |
NLERECMeEKCSFEE |
Mus musculus |
|
| pmid |
sentence |
| 11133752 |
The direct gamma-carboxyglutamic acid analysis and the N-terminal sequence analysis of the myotube-synthesized F.IX demonstrate efficient carboxylation at 11 of 12 γ-carboxyglutamic acid residues. |In previous work54 we have demonstrated that the γ-glutamyl carboxylase is present in skeletal muscle, but at a level only 5% to 10% of that found in the liver. This level of enzyme appears to be sufficient to provide full carboxylation of F.IX synthesized in myotubes|Glu 7, 8, 15, 17, 20, 21, 26, 27, 30, 33, and 36 are each less than 10% of the yield at the previous and subsequent cycles. Only a single γ-carboxylated residue, Gla 40, was not assessed by N-terminal sequencing. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263691 |
Glu67 |
LERECMEeKCSFEEA |
Mus musculus |
|
| pmid |
sentence |
| 11133752 |
The direct gamma-carboxyglutamic acid analysis and the N-terminal sequence analysis of the myotube-synthesized F.IX demonstrate efficient carboxylation at 11 of 12 γ-carboxyglutamic acid residues. |In previous work54 we have demonstrated that the γ-glutamyl carboxylase is present in skeletal muscle, but at a level only 5% to 10% of that found in the liver. This level of enzyme appears to be sufficient to provide full carboxylation of F.IX synthesized in myotubes|Glu 7, 8, 15, 17, 20, 21, 26, 27, 30, 33, and 36 are each less than 10% of the yield at the previous and subsequent cycles. Only a single γ-carboxylated residue, Gla 40, was not assessed by N-terminal sequencing. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263692 |
Glu72 |
MEEKCSFeEAREVFE |
Mus musculus |
|
| pmid |
sentence |
| 11133752 |
The direct gamma-carboxyglutamic acid analysis and the N-terminal sequence analysis of the myotube-synthesized F.IX demonstrate efficient carboxylation at 11 of 12 γ-carboxyglutamic acid residues. |In previous work54 we have demonstrated that the γ-glutamyl carboxylase is present in skeletal muscle, but at a level only 5% to 10% of that found in the liver. This level of enzyme appears to be sufficient to provide full carboxylation of F.IX synthesized in myotubes|Glu 7, 8, 15, 17, 20, 21, 26, 27, 30, 33, and 36 are each less than 10% of the yield at the previous and subsequent cycles. Only a single γ-carboxylated residue, Gla 40, was not assessed by N-terminal sequencing. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263693 |
Glu73 |
EEKCSFEeAREVFEN |
Mus musculus |
|
| pmid |
sentence |
| 11133752 |
The direct gamma-carboxyglutamic acid analysis and the N-terminal sequence analysis of the myotube-synthesized F.IX demonstrate efficient carboxylation at 11 of 12 γ-carboxyglutamic acid residues. |In previous work54 we have demonstrated that the γ-glutamyl carboxylase is present in skeletal muscle, but at a level only 5% to 10% of that found in the liver. This level of enzyme appears to be sufficient to provide full carboxylation of F.IX synthesized in myotubes|Glu 7, 8, 15, 17, 20, 21, 26, 27, 30, 33, and 36 are each less than 10% of the yield at the previous and subsequent cycles. Only a single γ-carboxylated residue, Gla 40, was not assessed by N-terminal sequencing. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263694 |
Glu76 |
CSFEEAReVFENTER |
Mus musculus |
|
| pmid |
sentence |
| 11133752 |
The direct gamma-carboxyglutamic acid analysis and the N-terminal sequence analysis of the myotube-synthesized F.IX demonstrate efficient carboxylation at 11 of 12 γ-carboxyglutamic acid residues. |In previous work54 we have demonstrated that the γ-glutamyl carboxylase is present in skeletal muscle, but at a level only 5% to 10% of that found in the liver. This level of enzyme appears to be sufficient to provide full carboxylation of F.IX synthesized in myotubes|Glu 7, 8, 15, 17, 20, 21, 26, 27, 30, 33, and 36 are each less than 10% of the yield at the previous and subsequent cycles. Only a single γ-carboxylated residue, Gla 40, was not assessed by N-terminal sequencing. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263685 |
Glu79 |
EEAREVFeNTERTTE |
Mus musculus |
|
| pmid |
sentence |
| 11133752 |
The direct gamma-carboxyglutamic acid analysis and the N-terminal sequence analysis of the myotube-synthesized F.IX demonstrate efficient carboxylation at 11 of 12 γ-carboxyglutamic acid residues. |In previous work54 we have demonstrated that the γ-glutamyl carboxylase is present in skeletal muscle, but at a level only 5% to 10% of that found in the liver. This level of enzyme appears to be sufficient to provide full carboxylation of F.IX synthesized in myotubes|Glu 7, 8, 15, 17, 20, 21, 26, 27, 30, 33, and 36 are each less than 10% of the yield at the previous and subsequent cycles. Only a single γ-carboxylated residue, Gla 40, was not assessed by N-terminal sequencing. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263695 |
Glu82 |
REVFENTeRTTEFWK |
Mus musculus |
|
| pmid |
sentence |
| 11133752 |
The direct gamma-carboxyglutamic acid analysis and the N-terminal sequence analysis of the myotube-synthesized F.IX demonstrate efficient carboxylation at 11 of 12 γ-carboxyglutamic acid residues. |In previous work54 we have demonstrated that the γ-glutamyl carboxylase is present in skeletal muscle, but at a level only 5% to 10% of that found in the liver. This level of enzyme appears to be sufficient to provide full carboxylation of F.IX synthesized in myotubes|Glu 7, 8, 15, 17, 20, 21, 26, 27, 30, 33, and 36 are each less than 10% of the yield at the previous and subsequent cycles. Only a single γ-carboxylated residue, Gla 40, was not assessed by N-terminal sequencing. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263696 |
Glu86 |
ENTERTTeFWKQYVD |
Mus musculus |
|
| pmid |
sentence |
| 11133752 |
The direct gamma-carboxyglutamic acid analysis and the N-terminal sequence analysis of the myotube-synthesized F.IX demonstrate efficient carboxylation at 11 of 12 γ-carboxyglutamic acid residues. |In previous work54 we have demonstrated that the γ-glutamyl carboxylase is present in skeletal muscle, but at a level only 5% to 10% of that found in the liver. This level of enzyme appears to be sufficient to provide full carboxylation of F.IX synthesized in myotubes|Glu 7, 8, 15, 17, 20, 21, 26, 27, 30, 33, and 36 are each less than 10% of the yield at the previous and subsequent cycles. Only a single γ-carboxylated residue, Gla 40, was not assessed by N-terminal sequencing. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265920 |
|
|
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: |
13 |
Organism: |
Mus Musculus, Homo Sapiens |
| Tissue: |
Skeletal Muscle |
| Pathways: | Vitamin-K cycle |
| + |
F11 | up-regulates activity
cleavage
|
F9 |
0.462 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263537 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20110423 |
Factor XI (FXI) is the zymogen of an enzyme (FXIa) that contributes to hemostasis by activating factor IX.|The characterization of the apple disk structure, and its relationship to the catalytic domain, have provided new insight into the mechanism of FXI activation, the interaction of FXIa with the substrate factor IX, and the binding of FXI to platelets. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Blood Plasma |
| + |
F7 | up-regulates activity
binding
|
F9 |
0.529 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263544 |
|
|
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 |
| + |
CEBPA | up-regulates quantity by expression 
transcriptional regulation
|
F9 |
0.291 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254040 |
|
|
Homo sapiens |
Hep-G2 Cell |
| pmid |
sentence |
| 8075306 |
Transactivation by the CCAAT/enhancer binding protein alpha of the wild-type and mutated factor IX promoter (-192 to +38) resulted in an approximately four-fold and approximately two-fold, respectively, increase of CAT activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SERPINC1 | down-regulates activity 
cleavage
|
F9 |
0.892 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264140 |
|
|
|
|
| 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 |
| + |
F9 | form complex 
binding
|
Factor VIIIa-IXa |
0.758 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263552 |
|
|
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 |
| + |
Factor FVIIa:TF | up-regulates activity
binding
|
F9 |
0.583 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263542 |
|
|
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 |
3.0
F9
- 
- 