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 |
| ABD30228.1 | clfA | SAOUHSC_01114 | SAOUHSC_00812 | Fibrinogen-binding protein. | Clumping factor; Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen c [...] | 0.741 |
| ABD30228.1 | clfB | SAOUHSC_01114 | SAOUHSC_02963 | Fibrinogen-binding protein. | Clumping factor B, putative; Cell surface-associated protein implicated in virulence by promoting bacterial attachment to both alpha- and beta-chains of human fibrinogen and inducing the formation of bacterial clumps. Partly responsible for mediating bacterial attachment to the highly keratinized squamous epithelial cells from the nasal cavity via an interaction with cytokeratin K10 (K10). Also promotes bacterial attachment to cultured keratinocytes, possibly through an interaction with cytokeratin K10. Binds mouse cytokeratin K10. Activates human platelet aggregation; Belongs to the s [...] | 0.707 |
| ABD30228.1 | ebpS | SAOUHSC_01114 | SAOUHSC_01501 | Fibrinogen-binding protein. | Elastin binding protein; Promotes binding of soluble elastin peptides and tropoelastin to S.aureus cells although it is not able to promote bacterial adherence to immobilized elastin and, therefore, is not a microbial surface component recognizing adhesive matrix molecule (MSCRAMM). May be involved in sensing the environment or in nutrient transport, since its loss caused a growth defect. | 0.708 |
| ABD30228.1 | eno | SAOUHSC_01114 | SAOUHSC_00799 | Fibrinogen-binding protein. | Enolase; Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis; Belongs to the enolase family. | 0.687 |
| ABD30228.1 | fnbA | SAOUHSC_01114 | SAOUHSC_02803 | Fibrinogen-binding protein. | Fibronectin-binding protein precursor, putative; Possesses multiple, substituting fibronectin (Fn) binding regions, each capable of conferring adherence to both soluble and immobilized forms of Fn. This confers to S.aureus the ability to invade endothelial cells both in vivo and in vitro, without requiring additional factors, although in a slow and inefficient way through actin rearrangements in host cells. This invasion process is mediated by integrin alpha-5/beta-1. Promotes bacterial attachment to both soluble and immobilized forms of fibrinogen (Fg) by means of a unique binding sit [...] | 0.611 |
| ABD30228.1 | hly | SAOUHSC_01114 | SAOUHSC_01121 | Fibrinogen-binding protein. | Alpha-hemolysin precursor; Alpha-toxin binds to the membrane of eukaryotic cells resulting in the release of low-molecular weight molecules and leading to an eventual osmotic lysis. Inhibits host neutrophil chemotaxis to the lesion region (Probable). Heptamer oligomerization and pore formation is required for lytic activity (By similarity). Belongs to the aerolysin family. | 0.529 |
| ABD30228.1 | sasG | SAOUHSC_01114 | SAOUHSC_02798 | Fibrinogen-binding protein. | Conserved hypothetical protein; Promotes adhesion of bacterial cells to human squamous nasal epithelial cells, a phenomenon which is likely to be important in nasal colonization. Forms short, extremely dense and thin fibrils all over the bacterial surface. Does not bind to either buccal cells or non- differentiated keratinocytes. Promotes cellular aggregation leading to biofilm formation. | 0.434 |
| clfA | ABD30228.1 | SAOUHSC_00812 | SAOUHSC_01114 | Clumping factor; Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen c [...] | Fibrinogen-binding protein. | 0.741 |
| clfA | clfB | SAOUHSC_00812 | SAOUHSC_02963 | Clumping factor; Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen c [...] | Clumping factor B, putative; Cell surface-associated protein implicated in virulence by promoting bacterial attachment to both alpha- and beta-chains of human fibrinogen and inducing the formation of bacterial clumps. Partly responsible for mediating bacterial attachment to the highly keratinized squamous epithelial cells from the nasal cavity via an interaction with cytokeratin K10 (K10). Also promotes bacterial attachment to cultured keratinocytes, possibly through an interaction with cytokeratin K10. Binds mouse cytokeratin K10. Activates human platelet aggregation; Belongs to the s [...] | 0.733 |
| clfA | ebh | SAOUHSC_00812 | SAOUHSC_01447 | Clumping factor; Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen c [...] | Conserved hypothetical protein; Promotes bacterial attachment to both soluble and immobilized forms of fibronectin (Fn), in a dose-dependent and saturable manner. | 0.711 |
| clfA | ebpS | SAOUHSC_00812 | SAOUHSC_01501 | Clumping factor; Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen c [...] | Elastin binding protein; Promotes binding of soluble elastin peptides and tropoelastin to S.aureus cells although it is not able to promote bacterial adherence to immobilized elastin and, therefore, is not a microbial surface component recognizing adhesive matrix molecule (MSCRAMM). May be involved in sensing the environment or in nutrient transport, since its loss caused a growth defect. | 0.889 |
| clfA | eno | SAOUHSC_00812 | SAOUHSC_00799 | Clumping factor; Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen c [...] | Enolase; Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis; Belongs to the enolase family. | 0.751 |
| clfA | fnbA | SAOUHSC_00812 | SAOUHSC_02803 | Clumping factor; Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen c [...] | Fibronectin-binding protein precursor, putative; Possesses multiple, substituting fibronectin (Fn) binding regions, each capable of conferring adherence to both soluble and immobilized forms of Fn. This confers to S.aureus the ability to invade endothelial cells both in vivo and in vitro, without requiring additional factors, although in a slow and inefficient way through actin rearrangements in host cells. This invasion process is mediated by integrin alpha-5/beta-1. Promotes bacterial attachment to both soluble and immobilized forms of fibrinogen (Fg) by means of a unique binding sit [...] | 0.901 |
| clfA | hlb | SAOUHSC_00812 | SAOUHSC_02240 | Clumping factor; Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen c [...] | Truncated beta-hemolysin; Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture. Beta-hemolysin is a phospholipase C with specific activity toward sphingomyelins. Has a high specificity for sphingomyelin, hydrolyzes lysophosphatidylcholine at a much lower rate, but has no activity towards phosphatidylcholine, phosphatidylethanolamine, or phosphatidylserine; Belongs to the neutral sphingomyelinase family. | 0.675 |
| clfA | hly | SAOUHSC_00812 | SAOUHSC_01121 | Clumping factor; Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen c [...] | Alpha-hemolysin precursor; Alpha-toxin binds to the membrane of eukaryotic cells resulting in the release of low-molecular weight molecules and leading to an eventual osmotic lysis. Inhibits host neutrophil chemotaxis to the lesion region (Probable). Heptamer oligomerization and pore formation is required for lytic activity (By similarity). Belongs to the aerolysin family. | 0.753 |
| clfA | isdB | SAOUHSC_00812 | SAOUHSC_01079 | Clumping factor; Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen c [...] | Neurofilament protein; Cell wall-anchored surface receptor that extracts heme from oxidized metHb to enable growth on hemoglobin as a sole iron source. Rapidly extracts heme from hemoglobin and transfers it to IsdA or IsdC, which then relays it to the membrane transporter/IsdEF for internalization. Promotes also resistance to hydrogen peroxide and killing by neutrophils; Belongs to the IsdB family. | 0.751 |
| clfA | sasG | SAOUHSC_00812 | SAOUHSC_02798 | Clumping factor; Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen c [...] | Conserved hypothetical protein; Promotes adhesion of bacterial cells to human squamous nasal epithelial cells, a phenomenon which is likely to be important in nasal colonization. Forms short, extremely dense and thin fibrils all over the bacterial surface. Does not bind to either buccal cells or non- differentiated keratinocytes. Promotes cellular aggregation leading to biofilm formation. | 0.777 |
| clfB | ABD30228.1 | SAOUHSC_02963 | SAOUHSC_01114 | Clumping factor B, putative; Cell surface-associated protein implicated in virulence by promoting bacterial attachment to both alpha- and beta-chains of human fibrinogen and inducing the formation of bacterial clumps. Partly responsible for mediating bacterial attachment to the highly keratinized squamous epithelial cells from the nasal cavity via an interaction with cytokeratin K10 (K10). Also promotes bacterial attachment to cultured keratinocytes, possibly through an interaction with cytokeratin K10. Binds mouse cytokeratin K10. Activates human platelet aggregation; Belongs to the s [...] | Fibrinogen-binding protein. | 0.707 |
| clfB | clfA | SAOUHSC_02963 | SAOUHSC_00812 | Clumping factor B, putative; Cell surface-associated protein implicated in virulence by promoting bacterial attachment to both alpha- and beta-chains of human fibrinogen and inducing the formation of bacterial clumps. Partly responsible for mediating bacterial attachment to the highly keratinized squamous epithelial cells from the nasal cavity via an interaction with cytokeratin K10 (K10). Also promotes bacterial attachment to cultured keratinocytes, possibly through an interaction with cytokeratin K10. Binds mouse cytokeratin K10. Activates human platelet aggregation; Belongs to the s [...] | Clumping factor; Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen c [...] | 0.733 |
| clfB | ebh | SAOUHSC_02963 | SAOUHSC_01447 | Clumping factor B, putative; Cell surface-associated protein implicated in virulence by promoting bacterial attachment to both alpha- and beta-chains of human fibrinogen and inducing the formation of bacterial clumps. Partly responsible for mediating bacterial attachment to the highly keratinized squamous epithelial cells from the nasal cavity via an interaction with cytokeratin K10 (K10). Also promotes bacterial attachment to cultured keratinocytes, possibly through an interaction with cytokeratin K10. Binds mouse cytokeratin K10. Activates human platelet aggregation; Belongs to the s [...] | Conserved hypothetical protein; Promotes bacterial attachment to both soluble and immobilized forms of fibronectin (Fn), in a dose-dependent and saturable manner. | 0.712 |
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