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 |
| amiB | lolA | WC39_04230 | WC39_05615 | N-acetylmuramoyl-L-alanine amidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lipoprotein chaperone; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). | 0.735 |
| amiB | macB_3 | WC39_04230 | WC39_06885 | N-acetylmuramoyl-L-alanine amidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Macrolide transporter; Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides. | 0.528 |
| dsbA_1 | dsbA_2 | WC39_11890 | WC39_09265 | Thiol:disulfide interchange protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Thiol:disulfide interchange protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.900 |
| dsbA_1 | lolA | WC39_11890 | WC39_05615 | Thiol:disulfide interchange protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lipoprotein chaperone; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). | 0.608 |
| dsbA_1 | lptD_3 | WC39_11890 | WC39_04960 | Thiol:disulfide interchange protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | LPS biosynthesis protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.583 |
| dsbA_1 | smpA | WC39_11890 | WC39_07430 | Thiol:disulfide interchange protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Membrane biogenesis protein; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. | 0.606 |
| dsbA_2 | dsbA_1 | WC39_09265 | WC39_11890 | Thiol:disulfide interchange protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Thiol:disulfide interchange protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.900 |
| dsbA_2 | lolA | WC39_09265 | WC39_05615 | Thiol:disulfide interchange protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lipoprotein chaperone; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). | 0.619 |
| dsbA_2 | lptD_3 | WC39_09265 | WC39_04960 | Thiol:disulfide interchange protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | LPS biosynthesis protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.573 |
| dsbA_2 | smpA | WC39_09265 | WC39_07430 | Thiol:disulfide interchange protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Membrane biogenesis protein; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. | 0.538 |
| lolA | amiB | WC39_05615 | WC39_04230 | Lipoprotein chaperone; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). | N-acetylmuramoyl-L-alanine amidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.735 |
| lolA | dsbA_1 | WC39_05615 | WC39_11890 | Lipoprotein chaperone; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). | Thiol:disulfide interchange protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.608 |
| lolA | dsbA_2 | WC39_05615 | WC39_09265 | Lipoprotein chaperone; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). | Thiol:disulfide interchange protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.619 |
| lolA | lolB_2 | WC39_05615 | WC39_07865 | Lipoprotein chaperone; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). | Membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.647 |
| lolA | lolC | WC39_05615 | WC39_03135 | Lipoprotein chaperone; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). | Permease; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.832 |
| lolA | lolD | WC39_05615 | WC39_03140 | Lipoprotein chaperone; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). | ABC transporter ATP-binding protein; Part of the ABC transporter complex LolCDE involved in the translocation of lipoproteins, in an ATP-dependent manner. | 0.824 |
| lolA | lolE_3 | WC39_05615 | WC39_03145 | Lipoprotein chaperone; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). | Outer membrane-specific lipoprotein transporter subunit LolE; Part of the ATP-dependent transport system LolCDE; responsible for the localization of lipoproteins to the periplasmic surface of the outer membrane; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.800 |
| lolA | lptD_3 | WC39_05615 | WC39_04960 | Lipoprotein chaperone; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). | LPS biosynthesis protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.749 |
| lolA | macB_3 | WC39_05615 | WC39_06885 | Lipoprotein chaperone; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). | Macrolide transporter; Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides. | 0.821 |
| lolA | smpA | WC39_05615 | WC39_07430 | Lipoprotein chaperone; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). | Membrane biogenesis protein; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. | 0.615 |
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