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 proteins in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| hly | lip2 | SAOUHSC_01121 | SAOUHSC_00300 | 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. | Lipase precursor. | 0.594 |
| hly | plc | SAOUHSC_01121 | SAOUHSC_00051 | 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. | 1-phosphatidylinositol phosphodiesterase precursor, putative; Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates. Potential virulence factor (By similarity). | 0.422 |
| hly | splA | SAOUHSC_01121 | SAOUHSC_01942 | 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. | Serine protease SplA. | 0.494 |
| hly | splB | SAOUHSC_01121 | SAOUHSC_01941 | 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. | Serine protease SplB; Serine protease that cleaves specifically after the sequence Trp-Glu-Leu-Gln; Belongs to the peptidase S1B family. | 0.425 |
| hly | sspA | SAOUHSC_01121 | SAOUHSC_00988 | 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. | Glutamyl endopeptidase precursor, putative; Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobu [...] | 0.594 |
| hly | sspB | SAOUHSC_01121 | SAOUHSC_00987 | 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. | Cysteine protease precursor, putative; Cysteine protease that plays an important role in the inhibition of host innate immune response. Degrades host elastin, fibrogen, fibronectin and kininogen. Blocks phagocytosis of opsonised S. aureus by neutrophils and monocytes by inducing their death in a proteolytic activity-dependent manner. Decreases surface expression of the 'don't eat me' signal CD31 on neutrophils. Cleaves host galectin- 3/LGALS3, thereby inhibiting the neutrophil-activating ability of the lectin. | 0.549 |
| lip2 | hly | SAOUHSC_00300 | SAOUHSC_01121 | Lipase precursor. | 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. | 0.594 |
| lip2 | splA | SAOUHSC_00300 | SAOUHSC_01942 | Lipase precursor. | Serine protease SplA. | 0.513 |
| lip2 | splB | SAOUHSC_00300 | SAOUHSC_01941 | Lipase precursor. | Serine protease SplB; Serine protease that cleaves specifically after the sequence Trp-Glu-Leu-Gln; Belongs to the peptidase S1B family. | 0.441 |
| lip2 | splC | SAOUHSC_00300 | SAOUHSC_01939 | Lipase precursor. | Serine protease SplC. | 0.468 |
| lip2 | sspA | SAOUHSC_00300 | SAOUHSC_00988 | Lipase precursor. | Glutamyl endopeptidase precursor, putative; Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobu [...] | 0.522 |
| lip2 | sspB | SAOUHSC_00300 | SAOUHSC_00987 | Lipase precursor. | Cysteine protease precursor, putative; Cysteine protease that plays an important role in the inhibition of host innate immune response. Degrades host elastin, fibrogen, fibronectin and kininogen. Blocks phagocytosis of opsonised S. aureus by neutrophils and monocytes by inducing their death in a proteolytic activity-dependent manner. Decreases surface expression of the 'don't eat me' signal CD31 on neutrophils. Cleaves host galectin- 3/LGALS3, thereby inhibiting the neutrophil-activating ability of the lectin. | 0.520 |
| lip2 | sspC | SAOUHSC_00300 | SAOUHSC_00986 | Lipase precursor. | Cysteine protease, putative; Specifically inhibits the cysteine protease staphopain B (SspB) by blocking the active site of the enzyme. Probably required to protect cytoplasmic proteins from being degraded by prematurely activated/folded prostaphopain B. Also involved in growth capacity, viability and bacterial morphology; Belongs to the protease inhibitor I57 (SspC) family. | 0.461 |
| plc | hly | SAOUHSC_00051 | SAOUHSC_01121 | 1-phosphatidylinositol phosphodiesterase precursor, putative; Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates. Potential virulence factor (By similarity). | 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. | 0.422 |
| plc | sspA | SAOUHSC_00051 | SAOUHSC_00988 | 1-phosphatidylinositol phosphodiesterase precursor, putative; Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates. Potential virulence factor (By similarity). | Glutamyl endopeptidase precursor, putative; Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobu [...] | 0.423 |
| plc | sspB | SAOUHSC_00051 | SAOUHSC_00987 | 1-phosphatidylinositol phosphodiesterase precursor, putative; Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates. Potential virulence factor (By similarity). | Cysteine protease precursor, putative; Cysteine protease that plays an important role in the inhibition of host innate immune response. Degrades host elastin, fibrogen, fibronectin and kininogen. Blocks phagocytosis of opsonised S. aureus by neutrophils and monocytes by inducing their death in a proteolytic activity-dependent manner. Decreases surface expression of the 'don't eat me' signal CD31 on neutrophils. Cleaves host galectin- 3/LGALS3, thereby inhibiting the neutrophil-activating ability of the lectin. | 0.579 |
| plc | sspC | SAOUHSC_00051 | SAOUHSC_00986 | 1-phosphatidylinositol phosphodiesterase precursor, putative; Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates. Potential virulence factor (By similarity). | Cysteine protease, putative; Specifically inhibits the cysteine protease staphopain B (SspB) by blocking the active site of the enzyme. Probably required to protect cytoplasmic proteins from being degraded by prematurely activated/folded prostaphopain B. Also involved in growth capacity, viability and bacterial morphology; Belongs to the protease inhibitor I57 (SspC) family. | 0.870 |
| scpA | scpB | SAOUHSC_01589 | SAOUHSC_01588 | Conserved hypothetical protein; Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpB that pull DNA away from mid-cell into both cell halves. | Conserved hypothetical protein; Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpA that pull DNA away from mid-cell into both cell halves. | 0.999 |
| scpA | splA | SAOUHSC_01589 | SAOUHSC_01942 | Conserved hypothetical protein; Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpB that pull DNA away from mid-cell into both cell halves. | Serine protease SplA. | 0.509 |
| scpA | sspA | SAOUHSC_01589 | SAOUHSC_00988 | Conserved hypothetical protein; Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpB that pull DNA away from mid-cell into both cell halves. | Glutamyl endopeptidase precursor, putative; Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobu [...] | 0.749 |
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