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 |
| b0582 | yaeI | b0582 | b0164 | IS186 transposase; IS, phage, Tn; Transposon-related functions; extrachromosomal; transposon related | Phosphodiesterase with model substrate bis-pnpp; Shows phosphodiesterase activity, hydrolyzing phosphodiester bond in the artificial chromogenic substrate bis-p-nitrophenyl phosphate (bis-pNPP) | 0.487 |
| b0582 | yibA | b0582 | b3594 | IS186 transposase; IS, phage, Tn; Transposon-related functions; extrachromosomal; transposon related | annotation not available | 0.781 |
| b2394 | insL1 | b2394 | b0016 | annotation not available | IS186/IS421 transposase; IS, phage, Tn; Transposon-related functions; extrachromosomal; transposon related | 0.458 |
| b2394 | yaeI | b2394 | b0164 | annotation not available | Phosphodiesterase with model substrate bis-pnpp; Shows phosphodiesterase activity, hydrolyzing phosphodiester bond in the artificial chromogenic substrate bis-p-nitrophenyl phosphate (bis-pNPP) | 0.487 |
| b2394 | yibA | b2394 | b3594 | annotation not available | annotation not available | 0.781 |
| dapD | glnD | b0166 | b0167 | 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; Belongs to the transferase hexapeptide repeat family | Pii uridylyltransferase/uridylyl removing enzyme; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins GlnB and GlnK, in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism | 0.882 |
| dapD | map | b0166 | b0168 | 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; Belongs to the transferase hexapeptide repeat family | Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed | 0.741 |
| dapD | yaeH | b0166 | b0163 | 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; Belongs to the transferase hexapeptide repeat family | DUF3461 domain-containing protein YaeH; Belongs to the UPF0325 family | 0.420 |
| dapD | yaeI | b0166 | b0164 | 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; Belongs to the transferase hexapeptide repeat family | Phosphodiesterase with model substrate bis-pnpp; Shows phosphodiesterase activity, hydrolyzing phosphodiester bond in the artificial chromogenic substrate bis-p-nitrophenyl phosphate (bis-pNPP) | 0.674 |
| glnD | dapD | b0167 | b0166 | Pii uridylyltransferase/uridylyl removing enzyme; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins GlnB and GlnK, in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism | 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; Belongs to the transferase hexapeptide repeat family | 0.882 |
| glnD | map | b0167 | b0168 | Pii uridylyltransferase/uridylyl removing enzyme; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins GlnB and GlnK, in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism | Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed | 0.772 |
| glnD | yaeI | b0167 | b0164 | Pii uridylyltransferase/uridylyl removing enzyme; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins GlnB and GlnK, in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism | Phosphodiesterase with model substrate bis-pnpp; Shows phosphodiesterase activity, hydrolyzing phosphodiester bond in the artificial chromogenic substrate bis-p-nitrophenyl phosphate (bis-pNPP) | 0.601 |
| iceT | yaeI | b2077 | b0164 | Putative citrate/iron-citrate/zinc-citrate efflux transporter; Belongs to the major facilitator superfamily. TCR/Tet family | Phosphodiesterase with model substrate bis-pnpp; Shows phosphodiesterase activity, hydrolyzing phosphodiester bond in the artificial chromogenic substrate bis-p-nitrophenyl phosphate (bis-pNPP) | 0.416 |
| insL1 | b2394 | b0016 | b2394 | IS186/IS421 transposase; IS, phage, Tn; Transposon-related functions; extrachromosomal; transposon related | annotation not available | 0.458 |
| insL1 | yaeI | b0016 | b0164 | IS186/IS421 transposase; IS, phage, Tn; Transposon-related functions; extrachromosomal; transposon related | Phosphodiesterase with model substrate bis-pnpp; Shows phosphodiesterase activity, hydrolyzing phosphodiester bond in the artificial chromogenic substrate bis-p-nitrophenyl phosphate (bis-pNPP) | 0.487 |
| insL1 | yibA | b0016 | b3594 | IS186/IS421 transposase; IS, phage, Tn; Transposon-related functions; extrachromosomal; transposon related | annotation not available | 0.781 |
| map | dapD | b0168 | b0166 | Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed | 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; Belongs to the transferase hexapeptide repeat family | 0.741 |
| map | glnD | b0168 | b0167 | Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed | Pii uridylyltransferase/uridylyl removing enzyme; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins GlnB and GlnK, in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism | 0.772 |
| map | yaeI | b0168 | b0164 | Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed | Phosphodiesterase with model substrate bis-pnpp; Shows phosphodiesterase activity, hydrolyzing phosphodiester bond in the artificial chromogenic substrate bis-p-nitrophenyl phosphate (bis-pNPP) | 0.474 |
| yaeH | dapD | b0163 | b0166 | DUF3461 domain-containing protein YaeH; Belongs to the UPF0325 family | 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; Belongs to the transferase hexapeptide repeat family | 0.420 |
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