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Serpina1a Serpina1a Alb Alb Elane Elane Serpina1b Serpina1b Proc Proc Serpina1c Serpina1c Serpina1d Serpina1d Fga Fga Fgb Fgb Pzp Pzp Ahsg Ahsg
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Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
Serpina1aAlpha-1-antitrypsin 1-1; Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Belongs to the serpin family. (436 aa)    
Predicted Functional Partners:
Alb
Serum albumin; Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc (By similarity). Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (By similarity). Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (B [...]
   
  
 0.990
Elane
Neutrophil elastase; Medullasin modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (By similarity). Capable of killing E.coli; probably digests outer membrane protein A (ompA) in E.coli ; Belongs to the peptidase S1 family. Elastase subfamily.
   
 
 0.980
Serpina1b
Alpha-1-antitrypsin 1-2; Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Belongs to the serpin family.
  
  
0.959
Proc
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.
   
 0.946
Serpina1c
Alpha-1-antitrypsin 1-3; Inhibitor of serine proteases. Can inhibit trypsin and chymotrypsin; relatively ineffective against elastase. Belongs to the serpin family.
  
  
0.941
Serpina1d
Alpha-1-antitrypsin 1-4; Inhibitor of serine proteases. Can inhibit trypsin and chymotrypsin; relatively ineffective against elastase. Belongs to the serpin family.
  
  
0.935
Fga
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 i [...]
   
  
 0.906
Fgb
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 [...]
   
 
 0.878
Pzp
Alpha-2-macroglobulin 165 kDa subunit; 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 an [...]
   
  
 0.878
Ahsg
Alpha-2-HS-glycoprotein; Probably involved in differentiation; Belongs to the fetuin family.
   
  
 0.865
Your Current Organism:
Mus musculus
NCBI taxonomy Id: 10090
Other names: LK3 transgenic mice, M. musculus, Mus sp. 129SV, house mouse, mouse, nude mice, transgenic mice
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