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 |
| CBL57098.1 | CBL57100.1 | PFREUD_16000 | PFREUD_16020 | Short-chain dehydrogenases of various substrate specificities. | 5.2 Protein of unknown function similar to proteins from other organisms. | 0.472 |
| CBL57098.1 | glnE | PFREUD_16000 | PFREUD_16010 | Short-chain dehydrogenases of various substrate specificities. | Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory regi [...] | 0.799 |
| CBL57100.1 | CBL57098.1 | PFREUD_16020 | PFREUD_16000 | 5.2 Protein of unknown function similar to proteins from other organisms. | Short-chain dehydrogenases of various substrate specificities. | 0.472 |
| CBL57100.1 | glnE | PFREUD_16020 | PFREUD_16010 | 5.2 Protein of unknown function similar to proteins from other organisms. | Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory regi [...] | 0.752 |
| glnE | CBL57098.1 | PFREUD_16010 | PFREUD_16000 | Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory regi [...] | Short-chain dehydrogenases of various substrate specificities. | 0.799 |
| glnE | CBL57100.1 | PFREUD_16010 | PFREUD_16020 | Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory regi [...] | 5.2 Protein of unknown function similar to proteins from other organisms. | 0.752 |