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 |
| EEF59999.1 | EEF61098.1 | Cflav_PD3058 | Cflav_PD3815 | TIGRFAM: glutamine synthetase, type I; PFAM: glutamine synthetase catalytic region; glutamine synthetase beta-Grasp; KEGG: ade:Adeh_4252 L-glutamine synthetase. | (Glutamate--ammonia-ligase) adenylyltransferase; 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 region of GlnE binds the signal tra [...] | 0.695 |
| EEF59999.1 | EEF61099.1 | Cflav_PD3058 | Cflav_PD3816 | TIGRFAM: glutamine synthetase, type I; PFAM: glutamine synthetase catalytic region; glutamine synthetase beta-Grasp; KEGG: ade:Adeh_4252 L-glutamine synthetase. | (Glutamate--ammonia-ligase) adenylyltransferase; 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 region of GlnE binds the signal tra [...] | 0.690 |
| EEF61098.1 | EEF59999.1 | Cflav_PD3815 | Cflav_PD3058 | (Glutamate--ammonia-ligase) adenylyltransferase; 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 region of GlnE binds the signal tra [...] | TIGRFAM: glutamine synthetase, type I; PFAM: glutamine synthetase catalytic region; glutamine synthetase beta-Grasp; KEGG: ade:Adeh_4252 L-glutamine synthetase. | 0.695 |
| EEF61098.1 | EEF61099.1 | Cflav_PD3815 | Cflav_PD3816 | (Glutamate--ammonia-ligase) adenylyltransferase; 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 region of GlnE binds the signal tra [...] | (Glutamate--ammonia-ligase) adenylyltransferase; 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 region of GlnE binds the signal tra [...] | 0.644 |
| EEF61098.1 | EEF61100.1 | Cflav_PD3815 | Cflav_PD3817 | (Glutamate--ammonia-ligase) adenylyltransferase; 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 region of GlnE binds the signal tra [...] | KEGG: gur:Gura_3835 hypothetical protein. | 0.497 |
| EEF61098.1 | EEF61230.1 | Cflav_PD3815 | Cflav_PD3947 | (Glutamate--ammonia-ligase) adenylyltransferase; 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 region of GlnE binds the signal tra [...] | TIGRFAM: glutamine synthetase, type I; PFAM: glutamine synthetase catalytic region; KEGG: min:Minf_1203 glutamine synthetase. | 0.698 |
| EEF61098.1 | EEF61231.1 | Cflav_PD3815 | Cflav_PD3948 | (Glutamate--ammonia-ligase) adenylyltransferase; 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 region of GlnE binds the signal tra [...] | PFAM: glutamine synthetase beta-Grasp; KEGG: bba:Bd0267 hypothetical protein. | 0.626 |
| EEF61098.1 | EEF62248.1 | Cflav_PD3815 | Cflav_PD4883 | (Glutamate--ammonia-ligase) adenylyltransferase; 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 region of GlnE binds the signal tra [...] | TIGRFAM: glutamine synthetase, type I; PFAM: glutamine synthetase catalytic region; glutamine synthetase beta-Grasp; KEGG: min:Minf_1203 glutamine synthetase. | 0.684 |
| EEF61098.1 | EEF63192.1 | Cflav_PD3815 | Cflav_PD5827 | (Glutamate--ammonia-ligase) adenylyltransferase; 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 region of GlnE binds the signal tra [...] | KEGG: sfu:Sfum_2963 ATP-dependent helicase HrpA; TIGRFAM: ATP-dependent helicase HrpA; PFAM: helicase domain protein; helicase-associated domain protein; protein of unknown function DUF1605; SMART: DEAD-like helicases. | 0.422 |
| EEF61098.1 | glnD | Cflav_PD3815 | Cflav_PD1494 | (Glutamate--ammonia-ligase) adenylyltransferase; 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 region of GlnE binds the signal tra [...] | UTP-GlnB uridylyltransferase, GlnD; 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. | 0.664 |
| EEF61099.1 | EEF59999.1 | Cflav_PD3816 | Cflav_PD3058 | (Glutamate--ammonia-ligase) adenylyltransferase; 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 region of GlnE binds the signal tra [...] | TIGRFAM: glutamine synthetase, type I; PFAM: glutamine synthetase catalytic region; glutamine synthetase beta-Grasp; KEGG: ade:Adeh_4252 L-glutamine synthetase. | 0.690 |
| EEF61099.1 | EEF61098.1 | Cflav_PD3816 | Cflav_PD3815 | (Glutamate--ammonia-ligase) adenylyltransferase; 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 region of GlnE binds the signal tra [...] | (Glutamate--ammonia-ligase) adenylyltransferase; 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 region of GlnE binds the signal tra [...] | 0.644 |
| EEF61099.1 | EEF61100.1 | Cflav_PD3816 | Cflav_PD3817 | (Glutamate--ammonia-ligase) adenylyltransferase; 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 region of GlnE binds the signal tra [...] | KEGG: gur:Gura_3835 hypothetical protein. | 0.762 |
| EEF61099.1 | EEF61230.1 | Cflav_PD3816 | Cflav_PD3947 | (Glutamate--ammonia-ligase) adenylyltransferase; 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 region of GlnE binds the signal tra [...] | TIGRFAM: glutamine synthetase, type I; PFAM: glutamine synthetase catalytic region; KEGG: min:Minf_1203 glutamine synthetase. | 0.694 |
| EEF61099.1 | EEF61231.1 | Cflav_PD3816 | Cflav_PD3948 | (Glutamate--ammonia-ligase) adenylyltransferase; 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 region of GlnE binds the signal tra [...] | PFAM: glutamine synthetase beta-Grasp; KEGG: bba:Bd0267 hypothetical protein. | 0.617 |
| EEF61099.1 | EEF62248.1 | Cflav_PD3816 | Cflav_PD4883 | (Glutamate--ammonia-ligase) adenylyltransferase; 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 region of GlnE binds the signal tra [...] | TIGRFAM: glutamine synthetase, type I; PFAM: glutamine synthetase catalytic region; glutamine synthetase beta-Grasp; KEGG: min:Minf_1203 glutamine synthetase. | 0.679 |
| EEF61099.1 | EEF63192.1 | Cflav_PD3816 | Cflav_PD5827 | (Glutamate--ammonia-ligase) adenylyltransferase; 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 region of GlnE binds the signal tra [...] | KEGG: sfu:Sfum_2963 ATP-dependent helicase HrpA; TIGRFAM: ATP-dependent helicase HrpA; PFAM: helicase domain protein; helicase-associated domain protein; protein of unknown function DUF1605; SMART: DEAD-like helicases. | 0.465 |
| EEF61099.1 | glnD | Cflav_PD3816 | Cflav_PD1494 | (Glutamate--ammonia-ligase) adenylyltransferase; 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 region of GlnE binds the signal tra [...] | UTP-GlnB uridylyltransferase, GlnD; 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. | 0.691 |
| EEF61100.1 | EEF61098.1 | Cflav_PD3817 | Cflav_PD3815 | KEGG: gur:Gura_3835 hypothetical protein. | (Glutamate--ammonia-ligase) adenylyltransferase; 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 region of GlnE binds the signal tra [...] | 0.497 |
| EEF61100.1 | EEF61099.1 | Cflav_PD3817 | Cflav_PD3816 | KEGG: gur:Gura_3835 hypothetical protein. | (Glutamate--ammonia-ligase) adenylyltransferase; 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 region of GlnE binds the signal tra [...] | 0.762 |
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