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 |
| ADE3 | ADE8 | YGR204W | YDR408C | C-1-tetrahydrofolate synthase, cytoplasmic; Cytoplasmic trifunctional enzyme C1-tetrahydrofolate synthase; involved in single carbon metabolism and required for biosynthesis of purines, thymidylate, methionine, and histidine; null mutation causes auxotrophy for adenine and histidine. | Phosphoribosylglycinamide formyltransferase; Phosphoribosyl-glycinamide transformylase; catalyzes a step in the 'de novo' purine nucleotide biosynthetic pathway. | 0.994 |
| ADE8 | ADE3 | YDR408C | YGR204W | Phosphoribosylglycinamide formyltransferase; Phosphoribosyl-glycinamide transformylase; catalyzes a step in the 'de novo' purine nucleotide biosynthetic pathway. | C-1-tetrahydrofolate synthase, cytoplasmic; Cytoplasmic trifunctional enzyme C1-tetrahydrofolate synthase; involved in single carbon metabolism and required for biosynthesis of purines, thymidylate, methionine, and histidine; null mutation causes auxotrophy for adenine and histidine. | 0.994 |