| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Apoh | F10 | ENSRNOP00000004756 | ENSRNOP00000026677 | Beta-2-glycoprotein 1; Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells. | Activated factor Xa heavy chain; Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting; Belongs to the peptidase S1 family. | 0.429 |
| Apoh | F2 | ENSRNOP00000004756 | ENSRNOP00000022233 | Beta-2-glycoprotein 1; Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells. | Activation peptide fragment 1; Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing; Belongs to the peptidase S1 family. | 0.962 |
| Apoh | Fga | ENSRNOP00000004756 | ENSRNOP00000060007 | Beta-2-glycoprotein 1; Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells. | Fibrinogen alpha chain; Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re- epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it [...] | 0.868 |
| Apoh | Fgb | ENSRNOP00000004756 | ENSRNOP00000009813 | Beta-2-glycoprotein 1; Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells. | Fibrinogen beta chain; Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re- epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However subsequent studies have shown that it i [...] | 0.785 |
| Apoh | Fgg | ENSRNOP00000004756 | ENSRNOP00000032735 | Beta-2-glycoprotein 1; Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells. | Fibrinogen gamma chain; Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), polymerizes to form an insoluble fibrin matrix. Has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re- epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhan [...] | 0.941 |
| Apoh | Plg | ENSRNOP00000004756 | ENSRNOP00000023370 | Beta-2-glycoprotein 1; Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells. | Plasmin heavy chain A, short form; Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invas [...] | 0.883 |
| Apoh | Serpinc1 | ENSRNOP00000004756 | ENSRNOP00000003748 | Beta-2-glycoprotein 1; Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells. | Serine (Or cysteine) peptidase inhibitor, clade C (Antithrombin), member 1; Belongs to the serpin family. | 0.943 |
| Apoh | Serpind1 | ENSRNOP00000004756 | ENSRNOP00000074639 | Beta-2-glycoprotein 1; Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells. | Heparin cofactor 2; Thrombin inhibitor activated by the glycosaminoglycans, heparin or dermatan sulfate. In the presence of the latter, HC-II becomes the predominant thrombin inhibitor in place of antithrombin III (AT) (By similarity). | 0.670 |
| Apoh | Serping1 | ENSRNOP00000004756 | ENSRNOP00000009817 | Beta-2-glycoprotein 1; Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells. | Plasma protease C1 inhibitor; Activation of the C1 complex is under control of the C1- inhibitor. It forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases. May play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. Very efficient inhibitor of FXIIa. Inhibits chymotrypsin and kallikrein (By similarity). | 0.413 |
| F10 | Apoh | ENSRNOP00000026677 | ENSRNOP00000004756 | Activated factor Xa heavy chain; Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting; Belongs to the peptidase S1 family. | Beta-2-glycoprotein 1; Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells. | 0.429 |
| F10 | F2 | ENSRNOP00000026677 | ENSRNOP00000022233 | Activated factor Xa heavy chain; Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting; Belongs to the peptidase S1 family. | Activation peptide fragment 1; Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing; Belongs to the peptidase S1 family. | 0.974 |
| F10 | Fga | ENSRNOP00000026677 | ENSRNOP00000060007 | Activated factor Xa heavy chain; Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting; Belongs to the peptidase S1 family. | Fibrinogen alpha chain; Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re- epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it [...] | 0.558 |
| F10 | Fgg | ENSRNOP00000026677 | ENSRNOP00000032735 | Activated factor Xa heavy chain; Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting; Belongs to the peptidase S1 family. | Fibrinogen gamma chain; Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), polymerizes to form an insoluble fibrin matrix. Has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re- epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhan [...] | 0.500 |
| F10 | Plg | ENSRNOP00000026677 | ENSRNOP00000023370 | Activated factor Xa heavy chain; Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting; Belongs to the peptidase S1 family. | Plasmin heavy chain A, short form; Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invas [...] | 0.516 |
| F10 | Serpinc1 | ENSRNOP00000026677 | ENSRNOP00000003748 | Activated factor Xa heavy chain; Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting; Belongs to the peptidase S1 family. | Serine (Or cysteine) peptidase inhibitor, clade C (Antithrombin), member 1; Belongs to the serpin family. | 0.911 |
| F10 | Serpind1 | ENSRNOP00000026677 | ENSRNOP00000074639 | Activated factor Xa heavy chain; Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting; Belongs to the peptidase S1 family. | Heparin cofactor 2; Thrombin inhibitor activated by the glycosaminoglycans, heparin or dermatan sulfate. In the presence of the latter, HC-II becomes the predominant thrombin inhibitor in place of antithrombin III (AT) (By similarity). | 0.617 |
| F10 | Serping1 | ENSRNOP00000026677 | ENSRNOP00000009817 | Activated factor Xa heavy chain; Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting; Belongs to the peptidase S1 family. | Plasma protease C1 inhibitor; Activation of the C1 complex is under control of the C1- inhibitor. It forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases. May play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. Very efficient inhibitor of FXIIa. Inhibits chymotrypsin and kallikrein (By similarity). | 0.429 |
| F2 | Apoh | ENSRNOP00000022233 | ENSRNOP00000004756 | Activation peptide fragment 1; Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing; Belongs to the peptidase S1 family. | Beta-2-glycoprotein 1; Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells. | 0.962 |
| F2 | F10 | ENSRNOP00000022233 | ENSRNOP00000026677 | Activation peptide fragment 1; Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing; Belongs to the peptidase S1 family. | Activated factor Xa heavy chain; Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting; Belongs to the peptidase S1 family. | 0.974 |
| F2 | Fga | ENSRNOP00000022233 | ENSRNOP00000060007 | Activation peptide fragment 1; Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing; Belongs to the peptidase S1 family. | Fibrinogen alpha chain; Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re- epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it [...] | 0.993 |