node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Ambp | C9 | ENSRNOP00000009248 | ENSRNOP00000018545 | Alpha-1-microglobulin/bikunin precursor; Protein AMBP; Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin, and lysosomal granulocytic elastase. Inhibits calcium oxalate crystallization (By similarity); In the N-terminal section; belongs to the calycin superfamily. Lipocalin family | Complement component 9; Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. C9 is the pore-forming subunit of the MAC | 0.828 |
Ambp | F2 | ENSRNOP00000009248 | ENSRNOP00000022233 | Alpha-1-microglobulin/bikunin precursor; Protein AMBP; Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin, and lysosomal granulocytic elastase. Inhibits calcium oxalate crystallization (By similarity); In the N-terminal section; belongs to the calycin superfamily. Lipocalin family | Coagulation factor ii (thrombin); 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 | 0.868 |
Ambp | Fga | ENSRNOP00000009248 | ENSRNOP00000060007 | Alpha-1-microglobulin/bikunin precursor; Protein AMBP; Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin, and lysosomal granulocytic elastase. Inhibits calcium oxalate crystallization (By similarity); In the N-terminal section; belongs to the calycin superfamily. Lipocalin 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 [...] | 0.927 |
Ambp | Fgb | ENSRNOP00000009248 | ENSRNOP00000050663 | Alpha-1-microglobulin/bikunin precursor; Protein AMBP; Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin, and lysosomal granulocytic elastase. Inhibits calcium oxalate crystallization (By similarity); In the N-terminal section; belongs to the calycin superfamily. Lipocalin family | 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 is [...] | 0.876 |
Ambp | Fgg | ENSRNOP00000009248 | ENSRNOP00000032735 | Alpha-1-microglobulin/bikunin precursor; Protein AMBP; Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin, and lysosomal granulocytic elastase. Inhibits calcium oxalate crystallization (By similarity); In the N-terminal section; belongs to the calycin superfamily. Lipocalin 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 [...] | 0.950 |
Ambp | Plg | ENSRNOP00000009248 | ENSRNOP00000023370 | Alpha-1-microglobulin/bikunin precursor; Protein AMBP; Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin, and lysosomal granulocytic elastase. Inhibits calcium oxalate crystallization (By similarity); In the N-terminal section; belongs to the calycin superfamily. Lipocalin family | Plasminogen; 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 invasion may be modulated b [...] | 0.946 |
Ambp | Serpina5 | ENSRNOP00000009248 | ENSRNOP00000013138 | Alpha-1-microglobulin/bikunin precursor; Protein AMBP; Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin, and lysosomal granulocytic elastase. Inhibits calcium oxalate crystallization (By similarity); In the N-terminal section; belongs to the calycin superfamily. Lipocalin family | Serine (or cysteine) peptidase inhibitor, clade a, member 5; Serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 5; Belongs to the serpin family | 0.548 |
Ambp | Serpinc1 | ENSRNOP00000009248 | ENSRNOP00000003748 | Alpha-1-microglobulin/bikunin precursor; Protein AMBP; Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin, and lysosomal granulocytic elastase. Inhibits calcium oxalate crystallization (By similarity); In the N-terminal section; belongs to the calycin superfamily. Lipocalin family | Serine (or cysteine) peptidase inhibitor, clade c (antithrombin), member 1; Serpin peptidase inhibitor, clade C (antithrombin), member 1; Belongs to the serpin family | 0.881 |
C9 | Ambp | ENSRNOP00000018545 | ENSRNOP00000009248 | Complement component 9; Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. C9 is the pore-forming subunit of the MAC | Alpha-1-microglobulin/bikunin precursor; Protein AMBP; Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin, and lysosomal granulocytic elastase. Inhibits calcium oxalate crystallization (By similarity); In the N-terminal section; belongs to the calycin superfamily. Lipocalin family | 0.828 |
C9 | F2 | ENSRNOP00000018545 | ENSRNOP00000022233 | Complement component 9; Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. C9 is the pore-forming subunit of the MAC | Coagulation factor ii (thrombin); 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 | 0.441 |
C9 | Fga | ENSRNOP00000018545 | ENSRNOP00000060007 | Complement component 9; Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. C9 is the pore-forming subunit of the MAC | 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 [...] | 0.924 |
C9 | Fgb | ENSRNOP00000018545 | ENSRNOP00000050663 | Complement component 9; Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. C9 is the pore-forming subunit of the MAC | 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 is [...] | 0.925 |
C9 | Fgg | ENSRNOP00000018545 | ENSRNOP00000032735 | Complement component 9; Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. C9 is the pore-forming subunit of the MAC | 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 [...] | 0.922 |
C9 | Plg | ENSRNOP00000018545 | ENSRNOP00000023370 | Complement component 9; Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. C9 is the pore-forming subunit of the MAC | Plasminogen; 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 invasion may be modulated b [...] | 0.932 |
C9 | Serpinc1 | ENSRNOP00000018545 | ENSRNOP00000003748 | Complement component 9; Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. C9 is the pore-forming subunit of the MAC | Serine (or cysteine) peptidase inhibitor, clade c (antithrombin), member 1; Serpin peptidase inhibitor, clade C (antithrombin), member 1; Belongs to the serpin family | 0.758 |
F13b | F2 | ENSRNOP00000016944 | ENSRNOP00000022233 | Coagulation factor XIII, B polypeptide | Coagulation factor ii (thrombin); 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 | 0.953 |
F13b | Fga | ENSRNOP00000016944 | ENSRNOP00000060007 | Coagulation factor XIII, B polypeptide | 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 [...] | 0.989 |
F13b | Fgb | ENSRNOP00000016944 | ENSRNOP00000050663 | Coagulation factor XIII, B polypeptide | 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 is [...] | 0.986 |
F13b | Fgg | ENSRNOP00000016944 | ENSRNOP00000032735 | Coagulation factor XIII, B polypeptide | 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 [...] | 0.990 |
F13b | Plg | ENSRNOP00000016944 | ENSRNOP00000023370 | Coagulation factor XIII, B polypeptide | Plasminogen; 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 invasion may be modulated b [...] | 0.547 |