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 |
| actA | hly | gene:17592840 | gene:17592838 | Actin-assembly inducing protein precursor; Virulence factor required for host cell microfilament interaction. It induces actin assembly around the bacteria to allow it to move within the cytoplasm. It is involved in the actin polymerization process. It seems to act as a nucleator that induces the reorganization of the actin cytoskeleton. | Listeriolysin O precursor; Sulfhydryl-activated pore-forming toxin, which is a major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Listeriolysin O activates mitogen-activated protein (MAP) kinase activity in host cells, most likely as a result of the permeabilization of the host cell membrane. Also induces a proteasome- independent degradation of U [...] | 0.944 |
| actA | mpl | gene:17592840 | gene:17592839 | Actin-assembly inducing protein precursor; Virulence factor required for host cell microfilament interaction. It induces actin assembly around the bacteria to allow it to move within the cytoplasm. It is involved in the actin polymerization process. It seems to act as a nucleator that induces the reorganization of the actin cytoskeleton. | Zinc metalloproteinase precursor; Probably linked to the pathogenesis of listerial infection; Belongs to the peptidase M4 family. | 0.957 |
| actA | plcA | gene:17592840 | gene:17592837 | Actin-assembly inducing protein precursor; Virulence factor required for host cell microfilament interaction. It induces actin assembly around the bacteria to allow it to move within the cytoplasm. It is involved in the actin polymerization process. It seems to act as a nucleator that induces the reorganization of the actin cytoskeleton. | Phosphatidylinositol-specific phospholipase c; Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates. Important factor in pathogenesis, PI-PLC activity is present only in virulent listeria species. It may participate in the lysis of the phagolysosomal membrane. | 0.939 |
| actA | plcB | gene:17592840 | gene:17592841 | Actin-assembly inducing protein precursor; Virulence factor required for host cell microfilament interaction. It induces actin assembly around the bacteria to allow it to move within the cytoplasm. It is involved in the actin polymerization process. It seems to act as a nucleator that induces the reorganization of the actin cytoskeleton. | Phospholipase C; Important role in the infectious process. May contribute to efficient lysis of the two-membrane vacuoles that surround the bacteria after direct cell-to-cell spread. | 0.974 |
| hly | actA | gene:17592838 | gene:17592840 | Listeriolysin O precursor; Sulfhydryl-activated pore-forming toxin, which is a major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Listeriolysin O activates mitogen-activated protein (MAP) kinase activity in host cells, most likely as a result of the permeabilization of the host cell membrane. Also induces a proteasome- independent degradation of U [...] | Actin-assembly inducing protein precursor; Virulence factor required for host cell microfilament interaction. It induces actin assembly around the bacteria to allow it to move within the cytoplasm. It is involved in the actin polymerization process. It seems to act as a nucleator that induces the reorganization of the actin cytoskeleton. | 0.944 |
| hly | mpl | gene:17592838 | gene:17592839 | Listeriolysin O precursor; Sulfhydryl-activated pore-forming toxin, which is a major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Listeriolysin O activates mitogen-activated protein (MAP) kinase activity in host cells, most likely as a result of the permeabilization of the host cell membrane. Also induces a proteasome- independent degradation of U [...] | Zinc metalloproteinase precursor; Probably linked to the pathogenesis of listerial infection; Belongs to the peptidase M4 family. | 0.962 |
| hly | plcA | gene:17592838 | gene:17592837 | Listeriolysin O precursor; Sulfhydryl-activated pore-forming toxin, which is a major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Listeriolysin O activates mitogen-activated protein (MAP) kinase activity in host cells, most likely as a result of the permeabilization of the host cell membrane. Also induces a proteasome- independent degradation of U [...] | Phosphatidylinositol-specific phospholipase c; Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates. Important factor in pathogenesis, PI-PLC activity is present only in virulent listeria species. It may participate in the lysis of the phagolysosomal membrane. | 0.960 |
| hly | plcB | gene:17592838 | gene:17592841 | Listeriolysin O precursor; Sulfhydryl-activated pore-forming toxin, which is a major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Listeriolysin O activates mitogen-activated protein (MAP) kinase activity in host cells, most likely as a result of the permeabilization of the host cell membrane. Also induces a proteasome- independent degradation of U [...] | Phospholipase C; Important role in the infectious process. May contribute to efficient lysis of the two-membrane vacuoles that surround the bacteria after direct cell-to-cell spread. | 0.948 |
| mpl | actA | gene:17592839 | gene:17592840 | Zinc metalloproteinase precursor; Probably linked to the pathogenesis of listerial infection; Belongs to the peptidase M4 family. | Actin-assembly inducing protein precursor; Virulence factor required for host cell microfilament interaction. It induces actin assembly around the bacteria to allow it to move within the cytoplasm. It is involved in the actin polymerization process. It seems to act as a nucleator that induces the reorganization of the actin cytoskeleton. | 0.957 |
| mpl | hly | gene:17592839 | gene:17592838 | Zinc metalloproteinase precursor; Probably linked to the pathogenesis of listerial infection; Belongs to the peptidase M4 family. | Listeriolysin O precursor; Sulfhydryl-activated pore-forming toxin, which is a major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Listeriolysin O activates mitogen-activated protein (MAP) kinase activity in host cells, most likely as a result of the permeabilization of the host cell membrane. Also induces a proteasome- independent degradation of U [...] | 0.962 |
| mpl | plcA | gene:17592839 | gene:17592837 | Zinc metalloproteinase precursor; Probably linked to the pathogenesis of listerial infection; Belongs to the peptidase M4 family. | Phosphatidylinositol-specific phospholipase c; Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates. Important factor in pathogenesis, PI-PLC activity is present only in virulent listeria species. It may participate in the lysis of the phagolysosomal membrane. | 0.963 |
| mpl | plcB | gene:17592839 | gene:17592841 | Zinc metalloproteinase precursor; Probably linked to the pathogenesis of listerial infection; Belongs to the peptidase M4 family. | Phospholipase C; Important role in the infectious process. May contribute to efficient lysis of the two-membrane vacuoles that surround the bacteria after direct cell-to-cell spread. | 0.957 |
| plcA | actA | gene:17592837 | gene:17592840 | Phosphatidylinositol-specific phospholipase c; Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates. Important factor in pathogenesis, PI-PLC activity is present only in virulent listeria species. It may participate in the lysis of the phagolysosomal membrane. | Actin-assembly inducing protein precursor; Virulence factor required for host cell microfilament interaction. It induces actin assembly around the bacteria to allow it to move within the cytoplasm. It is involved in the actin polymerization process. It seems to act as a nucleator that induces the reorganization of the actin cytoskeleton. | 0.939 |
| plcA | hly | gene:17592837 | gene:17592838 | Phosphatidylinositol-specific phospholipase c; Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates. Important factor in pathogenesis, PI-PLC activity is present only in virulent listeria species. It may participate in the lysis of the phagolysosomal membrane. | Listeriolysin O precursor; Sulfhydryl-activated pore-forming toxin, which is a major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Listeriolysin O activates mitogen-activated protein (MAP) kinase activity in host cells, most likely as a result of the permeabilization of the host cell membrane. Also induces a proteasome- independent degradation of U [...] | 0.960 |
| plcA | mpl | gene:17592837 | gene:17592839 | Phosphatidylinositol-specific phospholipase c; Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates. Important factor in pathogenesis, PI-PLC activity is present only in virulent listeria species. It may participate in the lysis of the phagolysosomal membrane. | Zinc metalloproteinase precursor; Probably linked to the pathogenesis of listerial infection; Belongs to the peptidase M4 family. | 0.963 |
| plcA | plcB | gene:17592837 | gene:17592841 | Phosphatidylinositol-specific phospholipase c; Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates. Important factor in pathogenesis, PI-PLC activity is present only in virulent listeria species. It may participate in the lysis of the phagolysosomal membrane. | Phospholipase C; Important role in the infectious process. May contribute to efficient lysis of the two-membrane vacuoles that surround the bacteria after direct cell-to-cell spread. | 0.984 |
| plcB | actA | gene:17592841 | gene:17592840 | Phospholipase C; Important role in the infectious process. May contribute to efficient lysis of the two-membrane vacuoles that surround the bacteria after direct cell-to-cell spread. | Actin-assembly inducing protein precursor; Virulence factor required for host cell microfilament interaction. It induces actin assembly around the bacteria to allow it to move within the cytoplasm. It is involved in the actin polymerization process. It seems to act as a nucleator that induces the reorganization of the actin cytoskeleton. | 0.974 |
| plcB | hly | gene:17592841 | gene:17592838 | Phospholipase C; Important role in the infectious process. May contribute to efficient lysis of the two-membrane vacuoles that surround the bacteria after direct cell-to-cell spread. | Listeriolysin O precursor; Sulfhydryl-activated pore-forming toxin, which is a major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Listeriolysin O activates mitogen-activated protein (MAP) kinase activity in host cells, most likely as a result of the permeabilization of the host cell membrane. Also induces a proteasome- independent degradation of U [...] | 0.948 |
| plcB | mpl | gene:17592841 | gene:17592839 | Phospholipase C; Important role in the infectious process. May contribute to efficient lysis of the two-membrane vacuoles that surround the bacteria after direct cell-to-cell spread. | Zinc metalloproteinase precursor; Probably linked to the pathogenesis of listerial infection; Belongs to the peptidase M4 family. | 0.957 |
| plcB | plcA | gene:17592841 | gene:17592837 | Phospholipase C; Important role in the infectious process. May contribute to efficient lysis of the two-membrane vacuoles that surround the bacteria after direct cell-to-cell spread. | Phosphatidylinositol-specific phospholipase c; Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates. Important factor in pathogenesis, PI-PLC activity is present only in virulent listeria species. It may participate in the lysis of the phagolysosomal membrane. | 0.984 |