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 |
| ALO36857.1 | ALO36858.1 | UZ73_00460 | UZ73_00465 | Antibiotic resistance protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Disulfide bond formation protein DsbB; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.820 |
| ALO36857.1 | ALO40333.1 | UZ73_00460 | UZ73_08830 | Antibiotic resistance protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Glutamate synthase subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.414 |
| ALO36857.1 | glnD | UZ73_00460 | UZ73_00455 | Antibiotic resistance protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Bifunctional uridylyltransferase/uridylyl-removing protein; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), 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 metabolism. | 0.853 |
| ALO36857.1 | map | UZ73_00460 | UZ73_00450 | Antibiotic resistance protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.782 |
| ALO36858.1 | ALO36857.1 | UZ73_00465 | UZ73_00460 | Disulfide bond formation protein DsbB; Derived by automated computational analysis using gene prediction method: Protein Homology. | Antibiotic resistance protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.820 |
| ALO36858.1 | glnD | UZ73_00465 | UZ73_00455 | Disulfide bond formation protein DsbB; Derived by automated computational analysis using gene prediction method: Protein Homology. | Bifunctional uridylyltransferase/uridylyl-removing protein; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), 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 metabolism. | 0.906 |
| ALO36858.1 | map | UZ73_00465 | UZ73_00450 | Disulfide bond formation protein DsbB; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.816 |
| ALO40333.1 | ALO36857.1 | UZ73_08830 | UZ73_00460 | Glutamate synthase subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology. | Antibiotic resistance protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.414 |
| ALO40333.1 | glnD | UZ73_08830 | UZ73_00455 | Glutamate synthase subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology. | Bifunctional uridylyltransferase/uridylyl-removing protein; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), 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 metabolism. | 0.700 |
| glnD | ALO36857.1 | UZ73_00455 | UZ73_00460 | Bifunctional uridylyltransferase/uridylyl-removing protein; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), 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 metabolism. | Antibiotic resistance protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.853 |
| glnD | ALO36858.1 | UZ73_00455 | UZ73_00465 | Bifunctional uridylyltransferase/uridylyl-removing protein; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), 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 metabolism. | Disulfide bond formation protein DsbB; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.906 |
| glnD | ALO40333.1 | UZ73_00455 | UZ73_08830 | Bifunctional uridylyltransferase/uridylyl-removing protein; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), 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 metabolism. | Glutamate synthase subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.700 |
| glnD | map | UZ73_00455 | UZ73_00450 | Bifunctional uridylyltransferase/uridylyl-removing protein; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), 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 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; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.883 |
| map | ALO36857.1 | UZ73_00450 | UZ73_00460 | 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; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | Antibiotic resistance protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.782 |
| map | ALO36858.1 | UZ73_00450 | UZ73_00465 | 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; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | Disulfide bond formation protein DsbB; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.816 |
| map | glnD | UZ73_00450 | UZ73_00455 | 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; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | Bifunctional uridylyltransferase/uridylyl-removing protein; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), 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 metabolism. | 0.883 |