Relation Results

Summary

Name F9
Full Name Coagulation factor IX
Synonyms Christmas factor, Plasma thromboplastin component, PTC |
Primary ID P00740
Links - -
Type protein
Relations 20
Pathways Vitamin-K cycle
Function Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active ...
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Type: Score: Layout: SPV 
0.5310.670.4620.8930.7560.5820.290.531F9F7GGCXF11SERPINC1Factor VIIIa-IXaFactor FVIIa:TFCEBPA

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▶Modifications Tables

Relations
Regulator
Mechanism
target
score ℹ
+ F9up-regulates activity img/direct-activation.png cleavage F7 0.531
Identifier Residue Sequence Organism Cell Line
SIGNOR-263522 Arg212 NASKPQGrIVGGKVC Homo sapiens
pmid sentence
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
+ GGCXup-regulates activity img/direct-activation.png carboxylation F9 0.67
Identifier Residue Sequence Organism Cell Line
SIGNOR-263686 Glu53 RYNSGKLeEFVQGNL Mus musculus
pmid sentence
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
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
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
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
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
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
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
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
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
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
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
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
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
+ F11up-regulates activity img/direct-activation.png cleavage F9 0.462
Identifier Residue Sequence Organism Cell Line
SIGNOR-263537 Homo sapiens
pmid sentence
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
+ SERPINC1down-regulates activity img/direct_inhibition.png cleavage F9 0.893
Identifier Residue Sequence Organism Cell Line
SIGNOR-264140
pmid sentence
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
+ F9form complex img/form-complex.png binding Factor VIIIa-IXa 0.756
Identifier Residue Sequence Organism Cell Line
SIGNOR-263552 Mus musculus
pmid sentence
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:TFup-regulates activity img/direct-activation.png binding F9 0.582
Identifier Residue Sequence Organism Cell Line
SIGNOR-263542 Homo sapiens
pmid sentence
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
+ CEBPAup-regulates quantity by expression img/indirect-activation.png transcriptional regulation F9 0.29
Identifier Residue Sequence Organism Cell Line
SIGNOR-254040 Homo sapiens Hep-G2 Cell
pmid sentence
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
+ F7up-regulates activity img/direct-activation.png binding F9 0.531
Identifier Residue Sequence Organism Cell Line
SIGNOR-263544 Homo sapiens
pmid sentence
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
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