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 |
| PV09_00284 | PV09_01028 | A0A0D2AS74 | A0A0D2AN09 | Purine nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. | Metallophos domain-containing protein. | 0.705 |
| PV09_00284 | PV09_03661 | A0A0D2AS74 | A0A0D2B1A8 | Purine nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. | ENDO3c domain-containing protein. | 0.683 |
| PV09_00284 | PV09_04355 | A0A0D2AS74 | A0A0D1YVB1 | Purine nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. | Uncharacterized protein. | 0.705 |
| PV09_00284 | PV09_04967 | A0A0D2AS74 | A0A0D2ACC5 | Purine nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. | Uncharacterized protein; Belongs to the 5'-nucleotidase family. | 0.830 |
| PV09_00284 | PV09_09430 | A0A0D2AS74 | A0A0D1YDK0 | Purine nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. | S-methyl-5'-thioadenosine phosphorylase; Catalyzes the reversible phosphorylation of S-methyl-5'- thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates. | 0.540 |
| PV09_01028 | PV09_00284 | A0A0D2AN09 | A0A0D2AS74 | Metallophos domain-containing protein. | Purine nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. | 0.705 |
| PV09_01028 | PV09_03661 | A0A0D2AN09 | A0A0D2B1A8 | Metallophos domain-containing protein. | ENDO3c domain-containing protein. | 0.613 |
| PV09_01028 | PV09_09430 | A0A0D2AN09 | A0A0D1YDK0 | Metallophos domain-containing protein. | S-methyl-5'-thioadenosine phosphorylase; Catalyzes the reversible phosphorylation of S-methyl-5'- thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates. | 0.694 |
| PV09_01740 | PV09_01799 | A0A0D1XYD8 | A0A0D1XYL5 | DNA polymerase. | Endo/exonuclease/phosphatase domain-containing protein. | 0.721 |
| PV09_01740 | PV09_01800 | A0A0D1XYD8 | A0A0D2AMB0 | DNA polymerase. | Uncharacterized protein. | 0.682 |
| PV09_01740 | PV09_03661 | A0A0D1XYD8 | A0A0D2B1A8 | DNA polymerase. | ENDO3c domain-containing protein. | 0.522 |
| PV09_01740 | PV09_04211 | A0A0D1XYD8 | A0A0D1XQX4 | DNA polymerase. | Endo/exonuclease/phosphatase domain-containing protein. | 0.660 |
| PV09_01740 | PV09_05649 | A0A0D1XYD8 | A0A0D2A8W1 | DNA polymerase. | AP_endonuc_2 domain-containing protein. | 0.771 |
| PV09_01799 | PV09_01740 | A0A0D1XYL5 | A0A0D1XYD8 | Endo/exonuclease/phosphatase domain-containing protein. | DNA polymerase. | 0.721 |
| PV09_01799 | PV09_03661 | A0A0D1XYL5 | A0A0D2B1A8 | Endo/exonuclease/phosphatase domain-containing protein. | ENDO3c domain-containing protein. | 0.776 |
| PV09_01799 | PV09_05649 | A0A0D1XYL5 | A0A0D2A8W1 | Endo/exonuclease/phosphatase domain-containing protein. | AP_endonuc_2 domain-containing protein. | 0.955 |
| PV09_01800 | PV09_01740 | A0A0D2AMB0 | A0A0D1XYD8 | Uncharacterized protein. | DNA polymerase. | 0.682 |
| PV09_01800 | PV09_03661 | A0A0D2AMB0 | A0A0D2B1A8 | Uncharacterized protein. | ENDO3c domain-containing protein. | 0.776 |
| PV09_01800 | PV09_05649 | A0A0D2AMB0 | A0A0D2A8W1 | Uncharacterized protein. | AP_endonuc_2 domain-containing protein. | 0.955 |
| PV09_03661 | PV09_00284 | A0A0D2B1A8 | A0A0D2AS74 | ENDO3c domain-containing protein. | Purine nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. | 0.683 |
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