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 |
| EAQ30864.1 | EAQ30865.1 | OS145_03317 | OS145_03322 | Uncharacterized protein containg phosphate binding CYTH domain and associated CHAD domain. | Proline dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | 0.500 |
| EAQ30864.1 | glnE | OS145_03317 | OS145_03312 | Uncharacterized protein containg phosphate binding CYTH domain and associated CHAD domain. | Glutamine synthetase 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 transducti [...] | 0.804 |
| EAQ30865.1 | EAQ30864.1 | OS145_03322 | OS145_03317 | Proline dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | Uncharacterized protein containg phosphate binding CYTH domain and associated CHAD domain. | 0.500 |
| EAQ30865.1 | EAQ30917.1 | OS145_03322 | OS145_11374 | Proline dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | Glutamate synthase, large subunit; COG0067 Glutamate synthase domain 1. | 0.889 |
| EAQ30865.1 | glnA | OS145_03322 | OS145_08988 | Proline dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | COG0174 Glutamine synthetase. | 0.894 |
| EAQ30865.1 | glnE | OS145_03322 | OS145_03312 | Proline dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | Glutamine synthetase 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 transducti [...] | 0.482 |
| EAQ30865.1 | nadE | OS145_03322 | OS145_03593 | Proline dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | NAD(+) synthase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.819 |
| EAQ30865.1 | tyrA | OS145_03322 | OS145_10645 | Proline dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | COG1605 Chorismate mutase. | 0.476 |
| EAQ30917.1 | EAQ30865.1 | OS145_11374 | OS145_03322 | Glutamate synthase, large subunit; COG0067 Glutamate synthase domain 1. | Proline dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | 0.889 |
| EAQ30917.1 | glnA | OS145_11374 | OS145_08988 | Glutamate synthase, large subunit; COG0067 Glutamate synthase domain 1. | COG0174 Glutamine synthetase. | 0.978 |
| EAQ30917.1 | glnD | OS145_11374 | OS145_13084 | Glutamate synthase, large subunit; COG0067 Glutamate synthase domain 1. | UTP:GlnB (protein PII) uridylyltransferase; 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. | 0.715 |
| EAQ30917.1 | glnE | OS145_11374 | OS145_03312 | Glutamate synthase, large subunit; COG0067 Glutamate synthase domain 1. | Glutamine synthetase 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 transducti [...] | 0.667 |
| EAQ30917.1 | nadE | OS145_11374 | OS145_03593 | Glutamate synthase, large subunit; COG0067 Glutamate synthase domain 1. | NAD(+) synthase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.923 |
| EAQ30917.1 | tyrA | OS145_11374 | OS145_10645 | Glutamate synthase, large subunit; COG0067 Glutamate synthase domain 1. | COG1605 Chorismate mutase. | 0.510 |
| EAQ32405.1 | glnE | OS145_00345 | OS145_03312 | Helicase, ATP-dependent; COG1643 HrpA-like helicases. | Glutamine synthetase 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 transducti [...] | 0.525 |
| glnA | EAQ30865.1 | OS145_08988 | OS145_03322 | COG0174 Glutamine synthetase. | Proline dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | 0.894 |
| glnA | EAQ30917.1 | OS145_08988 | OS145_11374 | COG0174 Glutamine synthetase. | Glutamate synthase, large subunit; COG0067 Glutamate synthase domain 1. | 0.978 |
| glnA | glnD | OS145_08988 | OS145_13084 | COG0174 Glutamine synthetase. | UTP:GlnB (protein PII) uridylyltransferase; 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. | 0.528 |
| glnA | glnE | OS145_08988 | OS145_03312 | COG0174 Glutamine synthetase. | Glutamine synthetase 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 transducti [...] | 0.775 |
| glnA | nadE | OS145_08988 | OS145_03593 | COG0174 Glutamine synthetase. | NAD(+) synthase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.613 |
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