node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AHSG | AMBP | ENSOARP00000022056 | ENSOARP00000006566 | Alpha-2-HS-glycoprotein; Belongs to the fetuin family. | Inter-alpha-trypsin inhibitor; This inhibitory fragment, released from native ITI after limited proteolysis with trypsin, contains two homologous domains. Whereas the second domain is a strong inhibitor of trypsin, the first domain interacts weakly with PMN-granulocytic elastase and not at all with pancreatic elastase. | 0.893 |
AHSG | F2 | ENSOARP00000022056 | ENSOARP00000004316 | Alpha-2-HS-glycoprotein; Belongs to the fetuin family. | Uncharacterized protein; Belongs to the peptidase S1 family. | 0.947 |
AHSG | FGA | ENSOARP00000022056 | ENSOARP00000017968 | Alpha-2-HS-glycoprotein; Belongs to the fetuin 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 [...] | 0.932 |
AHSG | FGB | ENSOARP00000022056 | ENSOARP00000000285 | Alpha-2-HS-glycoprotein; Belongs to the fetuin family. | Fibrinogen beta chain. | 0.818 |
AHSG | FGG | ENSOARP00000022056 | ENSOARP00000017896 | Alpha-2-HS-glycoprotein; Belongs to the fetuin family. | Fibrinogen gamma chain. | 0.892 |
AHSG | PLG | ENSOARP00000022056 | ENSOARP00000005065 | Alpha-2-HS-glycoprotein; Belongs to the fetuin 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 [...] | 0.929 |
AHSG | SERPINC1 | ENSOARP00000022056 | ENSOARP00000013845 | Alpha-2-HS-glycoprotein; Belongs to the fetuin family. | Antithrombin-III; Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin (By similarity). | 0.847 |
AHSG | SERPINF2 | ENSOARP00000022056 | ENSOARP00000015112 | Alpha-2-HS-glycoprotein; Belongs to the fetuin family. | Serpin family F member 2; Belongs to the serpin family. | 0.663 |
AMBP | AHSG | ENSOARP00000006566 | ENSOARP00000022056 | Inter-alpha-trypsin inhibitor; This inhibitory fragment, released from native ITI after limited proteolysis with trypsin, contains two homologous domains. Whereas the second domain is a strong inhibitor of trypsin, the first domain interacts weakly with PMN-granulocytic elastase and not at all with pancreatic elastase. | Alpha-2-HS-glycoprotein; Belongs to the fetuin family. | 0.893 |
AMBP | F2 | ENSOARP00000006566 | ENSOARP00000004316 | Inter-alpha-trypsin inhibitor; This inhibitory fragment, released from native ITI after limited proteolysis with trypsin, contains two homologous domains. Whereas the second domain is a strong inhibitor of trypsin, the first domain interacts weakly with PMN-granulocytic elastase and not at all with pancreatic elastase. | Uncharacterized protein; Belongs to the peptidase S1 family. | 0.909 |
AMBP | FGA | ENSOARP00000006566 | ENSOARP00000017968 | Inter-alpha-trypsin inhibitor; This inhibitory fragment, released from native ITI after limited proteolysis with trypsin, contains two homologous domains. Whereas the second domain is a strong inhibitor of trypsin, the first domain interacts weakly with PMN-granulocytic elastase and not at all with pancreatic elastase. | 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 [...] | 0.892 |
AMBP | FGB | ENSOARP00000006566 | ENSOARP00000000285 | Inter-alpha-trypsin inhibitor; This inhibitory fragment, released from native ITI after limited proteolysis with trypsin, contains two homologous domains. Whereas the second domain is a strong inhibitor of trypsin, the first domain interacts weakly with PMN-granulocytic elastase and not at all with pancreatic elastase. | Fibrinogen beta chain. | 0.852 |
AMBP | FGG | ENSOARP00000006566 | ENSOARP00000017896 | Inter-alpha-trypsin inhibitor; This inhibitory fragment, released from native ITI after limited proteolysis with trypsin, contains two homologous domains. Whereas the second domain is a strong inhibitor of trypsin, the first domain interacts weakly with PMN-granulocytic elastase and not at all with pancreatic elastase. | Fibrinogen gamma chain. | 0.808 |
AMBP | PLG | ENSOARP00000006566 | ENSOARP00000005065 | Inter-alpha-trypsin inhibitor; This inhibitory fragment, released from native ITI after limited proteolysis with trypsin, contains two homologous domains. Whereas the second domain is a strong inhibitor of trypsin, the first domain interacts weakly with PMN-granulocytic elastase and not at all with pancreatic elastase. | 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 [...] | 0.867 |
AMBP | SERPINC1 | ENSOARP00000006566 | ENSOARP00000013845 | Inter-alpha-trypsin inhibitor; This inhibitory fragment, released from native ITI after limited proteolysis with trypsin, contains two homologous domains. Whereas the second domain is a strong inhibitor of trypsin, the first domain interacts weakly with PMN-granulocytic elastase and not at all with pancreatic elastase. | Antithrombin-III; Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin (By similarity). | 0.913 |
AMBP | SERPINF2 | ENSOARP00000006566 | ENSOARP00000015112 | Inter-alpha-trypsin inhibitor; This inhibitory fragment, released from native ITI after limited proteolysis with trypsin, contains two homologous domains. Whereas the second domain is a strong inhibitor of trypsin, the first domain interacts weakly with PMN-granulocytic elastase and not at all with pancreatic elastase. | Serpin family F member 2; Belongs to the serpin family. | 0.738 |
F13B | F2 | ENSOARP00000015307 | ENSOARP00000004316 | Coagulation factor XIII B chain. | Uncharacterized protein; Belongs to the peptidase S1 family. | 0.989 |
F13B | FGA | ENSOARP00000015307 | ENSOARP00000017968 | Coagulation factor XIII B chain. | 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 [...] | 0.913 |
F13B | FGB | ENSOARP00000015307 | ENSOARP00000000285 | Coagulation factor XIII B chain. | Fibrinogen beta chain. | 0.745 |
F13B | FGG | ENSOARP00000015307 | ENSOARP00000017896 | Coagulation factor XIII B chain. | Fibrinogen gamma chain. | 0.789 |