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SERPINE2 protein (human) - STRING interaction network
"SERPINE2" - Glia-derived nexin in Homo sapiens
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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SERPINE2Glia-derived nexin; Serine protease inhibitor with activity toward thrombin, trypsin, and urokinase. Promotes neurite extension by inhibiting thrombin. Binds heparin; Belongs to the serpin family (409 aa)    
Predicted Functional Partners:
PLAU
Urokinase-type plasminogen activator; Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin (431 aa)
       
  0.986
F2
Prothrombin; 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 (622 aa)
     
  0.986
PLAT
Tissue-type plasminogen activator; Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events. Plays a direct role in facilitating neuronal migration (562 aa)
     
  0.979
PLAUR
Urokinase plasminogen activator surface receptor; Acts as a receptor for urokinase plasminogen activator. Plays a role in localizing and promoting plasmin formation. Mediates the proteolysis-independent signal transduction activation effects of U-PA. It is subject to negative-feedback regulation by U-PA which cleaves it into an inactive form; CD molecules (335 aa)
         
  0.958
F11
Coagulation factor XI; Factor XI triggers the middle phase of the intrinsic pathway of blood coagulation by activating factor IX (625 aa)
       
  0.934
VWF
Von Willebrand factor; Important in the maintenance of hemostasis, it promotes adhesion of platelets to the sites of vascular injury by forming a molecular bridge between sub-endothelial collagen matrix and platelet-surface receptor complex GPIb-IX-V. Also acts as a chaperone for coagulation factor VIII, delivering it to the site of injury, stabilizing its heterodimeric structure and protecting it from premature clearance from plasma; Endogenous ligands (2813 aa)
         
  0.928
F10
Coagulation factor X; 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; Gla domain containing (488 aa)
     
  0.923
SERPINE1
Plasminogen activator inhibitor 1; Serine protease inhibitor. This inhibitor acts as ’bait’ for tissue plasminogen activator, urokinase, protein C and matriptase-3/TMPRSS7. Its rapid interaction with PLAT may function as a major control point in the regulation of fibrinolysis; Serpin peptidase inhibitors (402 aa)
   
 
0.916
F13A1
Coagulation factor XIII A chain; Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl- epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin (732 aa)
         
  0.914
F8
Coagulation factor VIII; Factor VIII, along with calcium and phospholipid, acts as a cofactor for F9/factor IXa when it converts F10/factor X to the activated form, factor Xa; Belongs to the multicopper oxidase family (2351 aa)
         
  0.912
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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