Export your current network:
... as a vector graphic:
SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc
... as short tabular text output:
TSV: tab separated values - can be opened in Excel and Cytoscape (lists only one-way edges: A-B)
... as tabular text output:
TSV: tab separated values - can be opened in Excel (lists reciprocal edges: A-B,B-A)
... as an XML summary:
structured XML interaction data, according to the 'PSI-MI' data standard
... protein node degrees:
node degree of proteins in your network (given the current score cut-off)
... network coordinates:
a flat-file format describing the coordinates and colors of nodes in the network
... protein sequences:
MFA: multi-fasta format - containing the aminoacid sequences in the network
... protein annotations:
a tab-delimited file describing the names, domains and descriptions of proteins in your network
... functional annotations:
a tab-delimited file containing all known functional terms of protiens in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| A2M | F2 | ENSBTAP00000006167 | ENSBTAP00000009406 | Alpha-2-macroglobulin; Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the co [...] | 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 (By similarity); Belongs to the peptidase S1 family. | 0.671 |
| A2M | PROC | ENSBTAP00000006167 | ENSBTAP00000065381 | Alpha-2-macroglobulin; Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the co [...] | Vitamin K-dependent protein C heavy chain; Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids. Exerts a protective effect on the endothelial cell barrier function. Belongs to the peptidase S1 family. | 0.928 |
| A2M | SERPINA1 | ENSBTAP00000006167 | ENSBTAP00000065816 | Alpha-2-macroglobulin; Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the co [...] | Alpha-1-antiproteinase; Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Inhibits trypsin, chymotrypsin and plasminogen activator (By similarity); Belongs to the serpin family. | 0.876 |
| A2M | SERPINE1 | ENSBTAP00000006167 | ENSBTAP00000019232 | Alpha-2-macroglobulin; Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the co [...] | Plasminogen activator inhibitor 1; Serine protease inhibitor. Inhibits TMPRSS7. Is a primary inhibitor of tissue-type plasminogen activator (PLAT) and urokinase- type plasminogen activator (PLAU). As PLAT inhibitor, it is required for fibrinolysis down-regulation and is responsible for the controlled degradation of blood clots. As PLAU inhibitor, it is involved in the regulation of cell adhesion and spreading. Acts as a regulator of cell migration, independently of its role as protease inhibitor. It is required for stimulation of keratinocyte migration during cutaneous injury repair. I [...] | 0.579 |
| A2M | SERPINF2 | ENSBTAP00000006167 | ENSBTAP00000027793 | Alpha-2-macroglobulin; Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the co [...] | Alpha-2-antiplasmin; Serine protease inhibitor. The major targets of this inhibitor are plasmin and trypsin, but it also inactivates matriptase- 3/TMPRSS7 and chymotrypsin (By similarity). | 0.734 |
| A2M | THBD | ENSBTAP00000006167 | ENSBTAP00000066029 | Alpha-2-macroglobulin; Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the co [...] | Thrombomodulin; Thrombomodulin is a specific endothelial cell receptor that forms a 1:1 stoichiometric complex with thrombin. This complex is responsible for the conversion of protein C to the activated protein C (protein Ca). Once evolved, protein Ca scissions the activated cofactors of the coagulation mechanism, factor Va and factor VIIIa, and thereby reduces the amount of thrombin generated. | 0.408 |
| F2 | A2M | ENSBTAP00000009406 | ENSBTAP00000006167 | 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 (By similarity); Belongs to the peptidase S1 family. | Alpha-2-macroglobulin; Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the co [...] | 0.671 |
| F2 | F2R | ENSBTAP00000009406 | ENSBTAP00000026902 | 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 (By similarity); Belongs to the peptidase S1 family. | Proteinase-activated receptor 1; High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. | 0.993 |
| F2 | F8 | ENSBTAP00000009406 | ENSBTAP00000036581 | 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 (By similarity); Belongs to the peptidase S1 family. | Coagulation factor VIII; Belongs to the multicopper oxidase family. | 0.959 |
| F2 | PROC | ENSBTAP00000009406 | ENSBTAP00000065381 | 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 (By similarity); Belongs to the peptidase S1 family. | Vitamin K-dependent protein C heavy chain; Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids. Exerts a protective effect on the endothelial cell barrier function. Belongs to the peptidase S1 family. | 0.965 |
| F2 | PROCR | ENSBTAP00000009406 | ENSBTAP00000010911 | 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 (By similarity); Belongs to the peptidase S1 family. | Endothelial protein C receptor; Binds activated protein C. Enhances protein C activation by the thrombin-thrombomodulin complex; plays a role in the protein C pathway controlling blood coagulation. | 0.764 |
| F2 | SERPINA1 | ENSBTAP00000009406 | ENSBTAP00000065816 | 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 (By similarity); Belongs to the peptidase S1 family. | Alpha-1-antiproteinase; Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Inhibits trypsin, chymotrypsin and plasminogen activator (By similarity); Belongs to the serpin family. | 0.764 |
| F2 | SERPINA5 | ENSBTAP00000009406 | ENSBTAP00000005307 | 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 (By similarity); Belongs to the peptidase S1 family. | Plasma serine protease inhibitor; Heparin-dependent serine protease inhibitor acting in body fluids and secretions. Inactivates serine proteases by binding irreversibly to their serine activation site. Involved in the regulation of intravascular and extravascular proteolytic activities. Plays hemostatic roles in the blood plasma. Acts as a procoagulant and proinflammatory factor by inhibiting the anticoagulant activated protein C factor as well as the generation of activated protein C factor by the thrombin/thrombomodulin complex. Acts as an anticoagulant factor by inhibiting blood coa [...] | 0.941 |
| F2 | SERPINE1 | ENSBTAP00000009406 | ENSBTAP00000019232 | 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 (By similarity); Belongs to the peptidase S1 family. | Plasminogen activator inhibitor 1; Serine protease inhibitor. Inhibits TMPRSS7. Is a primary inhibitor of tissue-type plasminogen activator (PLAT) and urokinase- type plasminogen activator (PLAU). As PLAT inhibitor, it is required for fibrinolysis down-regulation and is responsible for the controlled degradation of blood clots. As PLAU inhibitor, it is involved in the regulation of cell adhesion and spreading. Acts as a regulator of cell migration, independently of its role as protease inhibitor. It is required for stimulation of keratinocyte migration during cutaneous injury repair. I [...] | 0.638 |
| F2 | SERPINF2 | ENSBTAP00000009406 | ENSBTAP00000027793 | 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 (By similarity); Belongs to the peptidase S1 family. | Alpha-2-antiplasmin; Serine protease inhibitor. The major targets of this inhibitor are plasmin and trypsin, but it also inactivates matriptase- 3/TMPRSS7 and chymotrypsin (By similarity). | 0.861 |
| F2 | THBD | ENSBTAP00000009406 | ENSBTAP00000066029 | 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 (By similarity); Belongs to the peptidase S1 family. | Thrombomodulin; Thrombomodulin is a specific endothelial cell receptor that forms a 1:1 stoichiometric complex with thrombin. This complex is responsible for the conversion of protein C to the activated protein C (protein Ca). Once evolved, protein Ca scissions the activated cofactors of the coagulation mechanism, factor Va and factor VIIIa, and thereby reduces the amount of thrombin generated. | 0.996 |
| F2R | F2 | ENSBTAP00000026902 | ENSBTAP00000009406 | Proteinase-activated receptor 1; High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. | 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 (By similarity); Belongs to the peptidase S1 family. | 0.993 |
| F2R | PROC | ENSBTAP00000026902 | ENSBTAP00000065381 | Proteinase-activated receptor 1; High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. | Vitamin K-dependent protein C heavy chain; Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids. Exerts a protective effect on the endothelial cell barrier function. Belongs to the peptidase S1 family. | 0.947 |
| F2R | PROCR | ENSBTAP00000026902 | ENSBTAP00000010911 | Proteinase-activated receptor 1; High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. | Endothelial protein C receptor; Binds activated protein C. Enhances protein C activation by the thrombin-thrombomodulin complex; plays a role in the protein C pathway controlling blood coagulation. | 0.867 |
| F2R | THBD | ENSBTAP00000026902 | ENSBTAP00000066029 | Proteinase-activated receptor 1; High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. | Thrombomodulin; Thrombomodulin is a specific endothelial cell receptor that forms a 1:1 stoichiometric complex with thrombin. This complex is responsible for the conversion of protein C to the activated protein C (protein Ca). Once evolved, protein Ca scissions the activated cofactors of the coagulation mechanism, factor Va and factor VIIIa, and thereby reduces the amount of thrombin generated. | 0.732 |
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