| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Ahsg | F2 | ENSRNOP00000073898 | ENSRNOP00000022233 | Alpha-2-HS-glycoprotein; Could inhibit both insulin-receptor tyrosine kinase activity and insulin-stimulated receptor autophosphorylation and, concomitantly, antagonize the mitogenic effect of the hormone in cultured rat hepatoma 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. | 0.971 |
| Ahsg | Fga | ENSRNOP00000073898 | ENSRNOP00000060007 | Alpha-2-HS-glycoprotein; Could inhibit both insulin-receptor tyrosine kinase activity and insulin-stimulated receptor autophosphorylation and, concomitantly, antagonize the mitogenic effect of the hormone in cultured rat hepatoma 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 [...] | 0.960 |
| Ahsg | Fgb | ENSRNOP00000073898 | ENSRNOP00000009813 | Alpha-2-HS-glycoprotein; Could inhibit both insulin-receptor tyrosine kinase activity and insulin-stimulated receptor autophosphorylation and, concomitantly, antagonize the mitogenic effect of the hormone in cultured rat hepatoma 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 [...] | 0.844 |
| Ahsg | Fgg | ENSRNOP00000073898 | ENSRNOP00000032735 | Alpha-2-HS-glycoprotein; Could inhibit both insulin-receptor tyrosine kinase activity and insulin-stimulated receptor autophosphorylation and, concomitantly, antagonize the mitogenic effect of the hormone in cultured rat hepatoma 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 [...] | 0.918 |
| Ahsg | Kng1 | ENSRNOP00000073898 | ENSRNOP00000069578 | Alpha-2-HS-glycoprotein; Could inhibit both insulin-receptor tyrosine kinase activity and insulin-stimulated receptor autophosphorylation and, concomitantly, antagonize the mitogenic effect of the hormone in cultured rat hepatoma cells. | Kininogen-1 heavy chain; (1) Kininogens are inhibitors of thiol proteases; (2) HMW- kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII; (3) HMW-kininogen inhibits the thrombin- and plasmin-induced aggregation of thrombocytes; (4) the active peptide bradykinin that is released from HMW-kininogen shows a variety of physiological effects: (4A) influence in smooth muscle contraction, (4B) induction of hypotension, (4C) natriuresis and diuresis, (4D) decrease in blood glucose level, (4E) it is a mediator of [...] | 0.805 |
| Ahsg | Serpinc1 | ENSRNOP00000073898 | ENSRNOP00000003748 | Alpha-2-HS-glycoprotein; Could inhibit both insulin-receptor tyrosine kinase activity and insulin-stimulated receptor autophosphorylation and, concomitantly, antagonize the mitogenic effect of the hormone in cultured rat hepatoma cells. | Serine (Or cysteine) peptidase inhibitor, clade C (Antithrombin), member 1; Belongs to the serpin family. | 0.850 |
| Ahsg | Serpind1 | ENSRNOP00000073898 | ENSRNOP00000074639 | Alpha-2-HS-glycoprotein; Could inhibit both insulin-receptor tyrosine kinase activity and insulin-stimulated receptor autophosphorylation and, concomitantly, antagonize the mitogenic effect of the hormone in cultured rat hepatoma 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). | 0.652 |
| Ahsg | Serpinf2 | ENSRNOP00000073898 | ENSRNOP00000004322 | Alpha-2-HS-glycoprotein; Could inhibit both insulin-receptor tyrosine kinase activity and insulin-stimulated receptor autophosphorylation and, concomitantly, antagonize the mitogenic effect of the hormone in cultured rat hepatoma cells. | Serpin family F member 2; Belongs to the serpin family. | 0.740 |
| F13b | F2 | ENSRNOP00000075643 | ENSRNOP00000022233 | Coagulation factor XIII B chain. | 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. | 0.861 |
| F13b | Fga | ENSRNOP00000075643 | ENSRNOP00000060007 | 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 [...] | 0.956 |
| F13b | Fgb | ENSRNOP00000075643 | ENSRNOP00000009813 | Coagulation factor XIII B chain. | 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 [...] | 0.856 |
| F13b | Fgg | ENSRNOP00000075643 | ENSRNOP00000032735 | Coagulation factor XIII B chain. | 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 [...] | 0.896 |
| F13b | Kng1 | ENSRNOP00000075643 | ENSRNOP00000069578 | Coagulation factor XIII B chain. | Kininogen-1 heavy chain; (1) Kininogens are inhibitors of thiol proteases; (2) HMW- kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII; (3) HMW-kininogen inhibits the thrombin- and plasmin-induced aggregation of thrombocytes; (4) the active peptide bradykinin that is released from HMW-kininogen shows a variety of physiological effects: (4A) influence in smooth muscle contraction, (4B) induction of hypotension, (4C) natriuresis and diuresis, (4D) decrease in blood glucose level, (4E) it is a mediator of [...] | 0.525 |
| F13b | Serpinc1 | ENSRNOP00000075643 | ENSRNOP00000003748 | Coagulation factor XIII B chain. | Serine (Or cysteine) peptidase inhibitor, clade C (Antithrombin), member 1; Belongs to the serpin family. | 0.761 |
| F13b | Serpind1 | ENSRNOP00000075643 | ENSRNOP00000074639 | Coagulation factor XIII B chain. | 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). | 0.844 |
| F13b | Serpinf2 | ENSRNOP00000075643 | ENSRNOP00000004322 | Coagulation factor XIII B chain. | Serpin family F member 2; Belongs to the serpin family. | 0.765 |
| F2 | Ahsg | ENSRNOP00000022233 | ENSRNOP00000073898 | 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. | Alpha-2-HS-glycoprotein; Could inhibit both insulin-receptor tyrosine kinase activity and insulin-stimulated receptor autophosphorylation and, concomitantly, antagonize the mitogenic effect of the hormone in cultured rat hepatoma cells. | 0.971 |
| F2 | F13b | ENSRNOP00000022233 | ENSRNOP00000075643 | 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. | Coagulation factor XIII B chain. | 0.861 |
| 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 [...] | 0.999 |
| F2 | Fgb | ENSRNOP00000022233 | ENSRNOP00000009813 | 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 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 [...] | 0.996 |