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 annotation | node2 annotation | score |
| A0A0K0DSU9 | A0A0K0E147 | 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. | 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. | 0.439 |
| A0A0K0DSU9 | A0A0K0E2S9 | 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. | Uncharacterized protein. | 0.537 |
| A0A0K0DSU9 | A0A0K0E643 | 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. | 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. | 0.439 |
| A0A0K0DSU9 | A0A0K0EAV1 | 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. | 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. | 0.439 |
| A0A0K0DTA7 | A0A0K0E2S9 | Rad51 domain-containing protein. | Uncharacterized protein. | 0.497 |
| A0A0K0DTA7 | A0A0K0E373 | Rad51 domain-containing protein. | DNA-(apurinic or apyrimidinic site) lyase; Belongs to the DNA repair enzymes AP/ExoA family. | 0.538 |
| A0A0K0DTA7 | A0A0K0E894 | Rad51 domain-containing protein. | DNA polymerase. | 0.828 |
| A0A0K0DTA7 | A0A0K0E949 | Rad51 domain-containing protein. | UmuC domain-containing protein. | 0.865 |
| A0A0K0DTA7 | A0A0K0EJ34 | Rad51 domain-containing protein. | Uncharacterized protein. | 0.845 |
| A0A0K0DTA7 | A0A0K0END7 | Rad51 domain-containing protein. | UmuC domain-containing protein. | 0.855 |
| A0A0K0E147 | A0A0K0DSU9 | 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. | 0.439 |
| A0A0K0E147 | A0A0K0E2S9 | 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. | 0.537 |
| A0A0K0E2S9 | A0A0K0DSU9 | Uncharacterized 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. | 0.537 |
| A0A0K0E2S9 | A0A0K0DTA7 | Uncharacterized protein. | Rad51 domain-containing protein. | 0.497 |
| A0A0K0E2S9 | A0A0K0E147 | Uncharacterized 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. | 0.537 |
| A0A0K0E2S9 | A0A0K0E373 | Uncharacterized protein. | DNA-(apurinic or apyrimidinic site) lyase; Belongs to the DNA repair enzymes AP/ExoA family. | 0.811 |
| A0A0K0E2S9 | A0A0K0E643 | Uncharacterized 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. | 0.537 |
| A0A0K0E2S9 | A0A0K0E894 | Uncharacterized protein. | DNA polymerase. | 0.507 |
| A0A0K0E2S9 | A0A0K0E949 | Uncharacterized protein. | UmuC domain-containing protein. | 0.502 |
| A0A0K0E2S9 | A0A0K0EAV1 | Uncharacterized 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. | 0.537 |
page 1 of 3