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 |
| ACPL_1169 | ACPL_1172 | ACPL_1169 | ACPL_1172 | Ribonuclease Z; Metal-dependent hydrolases of the beta-lactamase superfamily III. | Nucleoside-triphosphatase; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family. | 0.667 |
| ACPL_1169 | rph | ACPL_1169 | ACPL_1171 | Ribonuclease Z; Metal-dependent hydrolases of the beta-lactamase superfamily III. | Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. | 0.870 |
| ACPL_1172 | ACPL_1169 | ACPL_1172 | ACPL_1169 | Nucleoside-triphosphatase; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family. | Ribonuclease Z; Metal-dependent hydrolases of the beta-lactamase superfamily III. | 0.667 |
| ACPL_1172 | rph | ACPL_1172 | ACPL_1171 | Nucleoside-triphosphatase; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family. | Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. | 0.990 |
| ACPL_1374 | ACPL_7089 | ACPL_1374 | ACPL_7089 | Ribonucleases G and E. | Ribonuclease D. | 0.571 |
| ACPL_1374 | rnr | ACPL_1374 | ACPL_1561 | Ribonucleases G and E. | Exoribonuclease R. | 0.649 |
| ACPL_1374 | rph | ACPL_1374 | ACPL_1171 | Ribonucleases G and E. | Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. | 0.843 |
| ACPL_7089 | ACPL_1374 | ACPL_7089 | ACPL_1374 | Ribonuclease D. | Ribonucleases G and E. | 0.571 |
| ACPL_7089 | rnr | ACPL_7089 | ACPL_1561 | Ribonuclease D. | Exoribonuclease R. | 0.954 |
| ACPL_7089 | rph | ACPL_7089 | ACPL_1171 | Ribonuclease D. | Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. | 0.972 |
| ACPL_7089 | rpsA | ACPL_7089 | ACPL_1832 | Ribonuclease D. | Ribosomal protein S1. | 0.951 |
| ACPL_7089 | rpsD | ACPL_7089 | ACPL_1799 | Ribonuclease D. | 30S ribosomal protein S4; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit. | 0.957 |
| ACPL_7089 | rpsD-2 | ACPL_7089 | ACPL_810 | Ribonuclease D. | 30S ribosomal protein S4; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit. | 0.957 |
| dnaG | dnaG-2 | ACPL_1453 | ACPL_5940 | DNA primase; RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. | DNA primase (bacterial type). | 0.926 |
| dnaG | rph | ACPL_1453 | ACPL_1171 | DNA primase; RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. | Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. | 0.846 |
| dnaG-2 | dnaG | ACPL_5940 | ACPL_1453 | DNA primase (bacterial type). | DNA primase; RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. | 0.926 |
| dnaG-2 | rph | ACPL_5940 | ACPL_1171 | DNA primase (bacterial type). | Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. | 0.846 |
| rnr | ACPL_1374 | ACPL_1561 | ACPL_1374 | Exoribonuclease R. | Ribonucleases G and E. | 0.649 |
| rnr | ACPL_7089 | ACPL_1561 | ACPL_7089 | Exoribonuclease R. | Ribonuclease D. | 0.954 |
| rnr | rph | ACPL_1561 | ACPL_1171 | Exoribonuclease R. | Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. | 0.985 |
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