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 |
| AFM24343.1 | AFM24344.1 | Desti_1632 | Desti_1633 | PFAM: Adenylate and Guanylate cyclase catalytic domain; HAMP domain. | PFAM: Nitroreductase family; TIGRFAM: SagB-type dehydrogenase domain. | 0.787 |
| AFM24343.1 | hppA | Desti_1632 | Desti_1631 | PFAM: Adenylate and Guanylate cyclase catalytic domain; HAMP domain. | Vacuolar-type H(+)-translocating pyrophosphatase; Proton pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for proton movement across the membrane. Generates a proton motive force. | 0.494 |
| AFM24344.1 | AFM24343.1 | Desti_1633 | Desti_1632 | PFAM: Nitroreductase family; TIGRFAM: SagB-type dehydrogenase domain. | PFAM: Adenylate and Guanylate cyclase catalytic domain; HAMP domain. | 0.787 |
| AFM24344.1 | hppA | Desti_1633 | Desti_1631 | PFAM: Nitroreductase family; TIGRFAM: SagB-type dehydrogenase domain. | Vacuolar-type H(+)-translocating pyrophosphatase; Proton pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for proton movement across the membrane. Generates a proton motive force. | 0.474 |
| hppA | AFM24343.1 | Desti_1631 | Desti_1632 | Vacuolar-type H(+)-translocating pyrophosphatase; Proton pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for proton movement across the membrane. Generates a proton motive force. | PFAM: Adenylate and Guanylate cyclase catalytic domain; HAMP domain. | 0.494 |
| hppA | AFM24344.1 | Desti_1631 | Desti_1633 | Vacuolar-type H(+)-translocating pyrophosphatase; Proton pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for proton movement across the membrane. Generates a proton motive force. | PFAM: Nitroreductase family; TIGRFAM: SagB-type dehydrogenase domain. | 0.474 |
| hppA | pfp | Desti_1631 | Desti_2703 | Vacuolar-type H(+)-translocating pyrophosphatase; Proton pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for proton movement across the membrane. Generates a proton motive force. | 6-phosphofructokinase; Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. | 0.426 |
| pfp | hppA | Desti_2703 | Desti_1631 | 6-phosphofructokinase; Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. | Vacuolar-type H(+)-translocating pyrophosphatase; Proton pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for proton movement across the membrane. Generates a proton motive force. | 0.426 |