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 |
| AEA67977.1 | AEA67979.1 | PSEBR_a1766 | PSEBR_a1768 | Liporotein ABC transporter, permease component. | Liporotein ABC transporter, permease component. | 0.957 |
| AEA67977.1 | lolA | PSEBR_a1766 | PSEBR_a3562 | Liporotein ABC transporter, permease component. | Conserved hypothetical protein; 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). | 0.846 |
| AEA67977.1 | lolD | PSEBR_a1766 | PSEBR_a1767 | Liporotein ABC transporter, permease component. | Liporotein ABC transporter, ATP-binding component; Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner. | 0.990 |
| AEA67977.1 | macB | PSEBR_a1766 | PSEBR_a3909 | Liporotein ABC transporter, permease component. | Macrolide ABC transporter, ATP-binding/permease components; 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. | 0.848 |
| AEA67979.1 | AEA67977.1 | PSEBR_a1768 | PSEBR_a1766 | Liporotein ABC transporter, permease component. | Liporotein ABC transporter, permease component. | 0.957 |
| AEA67979.1 | lolA | PSEBR_a1768 | PSEBR_a3562 | Liporotein ABC transporter, permease component. | Conserved hypothetical protein; 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). | 0.842 |
| AEA67979.1 | lolD | PSEBR_a1768 | PSEBR_a1767 | Liporotein ABC transporter, permease component. | Liporotein ABC transporter, ATP-binding component; Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner. | 0.983 |
| AEA67979.1 | macB | PSEBR_a1768 | PSEBR_a3909 | Liporotein ABC transporter, permease component. | Macrolide ABC transporter, ATP-binding/permease components; 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. | 0.848 |
| AEA70096.1 | lolA | PSEBR_a3744 | PSEBR_a3562 | Putative ABC transporter, permease component. | Conserved hypothetical protein; 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). | 0.616 |
| AEA70096.1 | lolD | PSEBR_a3744 | PSEBR_a1767 | Putative ABC transporter, permease component. | Liporotein ABC transporter, ATP-binding component; Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner. | 0.693 |
| AEA70096.1 | macB | PSEBR_a3744 | PSEBR_a3909 | Putative ABC transporter, permease component. | Macrolide ABC transporter, ATP-binding/permease components; 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. | 0.848 |
| AEA71480.1 | lolD | PSEBR_a5048 | PSEBR_a1767 | Putative ABC transporter, permease component. | Liporotein ABC transporter, ATP-binding component; Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner. | 0.664 |
| AEA71480.1 | macB | PSEBR_a5048 | PSEBR_a3909 | Putative ABC transporter, permease component. | Macrolide ABC transporter, ATP-binding/permease components; 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. | 0.848 |
| AEA72077.1 | lolD | PSEBR_a5547 | PSEBR_a1767 | Putative ABC transporter, permease component. | Liporotein ABC transporter, ATP-binding component; Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner. | 0.638 |
| AEA72077.1 | macB | PSEBR_a5547 | PSEBR_a3909 | Putative ABC transporter, permease component. | Macrolide ABC transporter, ATP-binding/permease components; 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. | 0.848 |
| lolA | AEA67977.1 | PSEBR_a3562 | PSEBR_a1766 | Conserved hypothetical protein; 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). | Liporotein ABC transporter, permease component. | 0.846 |
| lolA | AEA67979.1 | PSEBR_a3562 | PSEBR_a1768 | Conserved hypothetical protein; 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). | Liporotein ABC transporter, permease component. | 0.842 |
| lolA | AEA70096.1 | PSEBR_a3562 | PSEBR_a3744 | Conserved hypothetical protein; 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). | Putative ABC transporter, permease component. | 0.616 |
| lolA | lolD | PSEBR_a3562 | PSEBR_a1767 | Conserved hypothetical protein; 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). | Liporotein ABC transporter, ATP-binding component; Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner. | 0.678 |
| lolA | macB | PSEBR_a3562 | PSEBR_a3909 | Conserved hypothetical protein; 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 ABC transporter, ATP-binding/permease components; 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. | 0.558 |
page 1 of 3