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 |
| cbbL | ccmK | Synpcc7942_1426 | Synpcc7942_1421 | Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit; RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. | Putative carboxysome assembly protein; May be involved in the formation of the carboxysome, a polyhedral inclusion where RuBisCO is sequestered. | 0.911 |
| cbbL | ccmM | Synpcc7942_1426 | Synpcc7942_1423 | Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit; RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. | Carbonate dehydratase; The presence of two potential DNA-binding regions suggests this protein may be a transcriptional regulator. | 0.999 |
| cbbL | chlB | Synpcc7942_1426 | Synpcc7942_1838 | Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit; RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. | Light-independent protochlorophyllide reductase, B subunit; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. | 0.460 |
| cbbL | chlL | Synpcc7942_1426 | Synpcc7942_1419 | Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit; RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. | Light-independent protochlorophyllide reductase, iron-sulfur ATP-binding protein; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP. | 0.571 |
| cbbL | chlN | Synpcc7942_1426 | Synpcc7942_1420 | Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit; RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. | Light-independent protochlorophyllide reductase, N subunit; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. | 0.517 |
| cbbL | glnB | Synpcc7942_1426 | Synpcc7942_0321 | Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit; RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. | Nitrogen regulatory protein P-II; P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I- phosphate, the transcriptional activator of glnA. When P-II is phosphorylated, these events are reversed. In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is phosphorylated which allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme; Belongs to the P(II) protein family. | 0.409 |
| cbiA | chlB | Synpcc7942_1855 | Synpcc7942_1838 | Cobyrinate a,c-diamide synthase; Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source; Belongs to the CobB/CbiA family. | Light-independent protochlorophyllide reductase, B subunit; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. | 0.523 |
| cbiA | chlL | Synpcc7942_1855 | Synpcc7942_1419 | Cobyrinate a,c-diamide synthase; Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source; Belongs to the CobB/CbiA family. | Light-independent protochlorophyllide reductase, iron-sulfur ATP-binding protein; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP. | 0.485 |
| cbiA | chlN | Synpcc7942_1855 | Synpcc7942_1420 | Cobyrinate a,c-diamide synthase; Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source; Belongs to the CobB/CbiA family. | Light-independent protochlorophyllide reductase, N subunit; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. | 0.407 |
| ccmK | cbbL | Synpcc7942_1421 | Synpcc7942_1426 | Putative carboxysome assembly protein; May be involved in the formation of the carboxysome, a polyhedral inclusion where RuBisCO is sequestered. | Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit; RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. | 0.911 |
| ccmK | ccmM | Synpcc7942_1421 | Synpcc7942_1423 | Putative carboxysome assembly protein; May be involved in the formation of the carboxysome, a polyhedral inclusion where RuBisCO is sequestered. | Carbonate dehydratase; The presence of two potential DNA-binding regions suggests this protein may be a transcriptional regulator. | 0.962 |
| ccmK | chlL | Synpcc7942_1421 | Synpcc7942_1419 | Putative carboxysome assembly protein; May be involved in the formation of the carboxysome, a polyhedral inclusion where RuBisCO is sequestered. | Light-independent protochlorophyllide reductase, iron-sulfur ATP-binding protein; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP. | 0.663 |
| ccmK | chlN | Synpcc7942_1421 | Synpcc7942_1420 | Putative carboxysome assembly protein; May be involved in the formation of the carboxysome, a polyhedral inclusion where RuBisCO is sequestered. | Light-independent protochlorophyllide reductase, N subunit; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. | 0.702 |
| ccmM | cbbL | Synpcc7942_1423 | Synpcc7942_1426 | Carbonate dehydratase; The presence of two potential DNA-binding regions suggests this protein may be a transcriptional regulator. | Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit; RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. | 0.999 |
| ccmM | ccmK | Synpcc7942_1423 | Synpcc7942_1421 | Carbonate dehydratase; The presence of two potential DNA-binding regions suggests this protein may be a transcriptional regulator. | Putative carboxysome assembly protein; May be involved in the formation of the carboxysome, a polyhedral inclusion where RuBisCO is sequestered. | 0.962 |
| chlB | cbbL | Synpcc7942_1838 | Synpcc7942_1426 | Light-independent protochlorophyllide reductase, B subunit; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. | Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit; RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. | 0.460 |
| chlB | cbiA | Synpcc7942_1838 | Synpcc7942_1855 | Light-independent protochlorophyllide reductase, B subunit; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. | Cobyrinate a,c-diamide synthase; Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source; Belongs to the CobB/CbiA family. | 0.523 |
| chlB | chlL | Synpcc7942_1838 | Synpcc7942_1419 | Light-independent protochlorophyllide reductase, B subunit; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. | Light-independent protochlorophyllide reductase, iron-sulfur ATP-binding protein; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP. | 0.999 |
| chlB | chlN | Synpcc7942_1838 | Synpcc7942_1420 | Light-independent protochlorophyllide reductase, B subunit; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. | Light-independent protochlorophyllide reductase, N subunit; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. | 0.999 |
| chlL | cbbL | Synpcc7942_1419 | Synpcc7942_1426 | Light-independent protochlorophyllide reductase, iron-sulfur ATP-binding protein; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP. | Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit; RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. | 0.571 |
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