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 |
| elaA | panM | b2267 | b3459 | Gnat family putative n-acetyltransferase; Belongs to the UPF0039 (ElaA) family | Pand autocleavage accelerator, panothenate synthesis; Controls both the activation and catalytic activity of PanD in a coenzyme A (CoA)-dependent fashion. Binding of CoA or a derivative to PanZ leads to interaction with PanD, which promotes the processing and activation of pro-PanD, and subsequent substrate-mediated inhibition of the active form of PanD Inhibition of PanD activity is probably the primary metabolic role of PanZ, allowing negative feedback regulation of pantothenate biosynthesis by CoA | 0.738 |
| elaA | yedL | b2267 | b1932 | Gnat family putative n-acetyltransferase; Belongs to the UPF0039 (ElaA) family | Gnat family putative n-acetyltransferase; Belongs to the acetyltransferase family | 0.867 |
| elaA | yhbS | b2267 | b3156 | Gnat family putative n-acetyltransferase; Belongs to the UPF0039 (ElaA) family | Putative acyltransferase with acyl-coa n-acyltransferase domain; Belongs to the acetyltransferase family | 0.823 |
| elaA | yhhY | b2267 | b3441 | Gnat family putative n-acetyltransferase; Belongs to the UPF0039 (ElaA) family | Aminoacyl nucleotide detoxifying acetyltransferase; Catalyzes the N-acetylation of L-phenylalanine and L- methionine using acetyl-CoA as acetyl donor in vitro. Cannot accept L- tyrosine as substrate and propionyl-CoA, succinyl-CoA or (S)- methylmalonyl-CoA as acyl donors . Is also able to acetylate and thus detoxify several nonhydrolyzable aminoacyl adenylates, but not the processed form of the peptide-nucleotide antibiotic microcin C (McC). When overproduced, provides complete resistance to leucyl sulfamoyl adenylate (LSA) and partial resistance to alanyl sulfamoyl adenylate (ASA) and [...] | 0.803 |
| elaA | yiaC | b2267 | b3550 | Gnat family putative n-acetyltransferase; Belongs to the UPF0039 (ElaA) family | Putative acyltransferase with acyl-coa n-acyltransferase domain; N-epsilon-lysine acetyltransferase that catalyzes acetylation of a large number of proteins. Overexpression inhibits motility | 0.877 |
| elaA | yjaB | b2267 | b4012 | Gnat family putative n-acetyltransferase; Belongs to the UPF0039 (ElaA) family | Gnat-family putative n-acetyltransferase; N-epsilon-lysine acetyltransferase that catalyzes acetylation of a large number of proteins . Binds acetyl-CoA | 0.878 |
| elaA | yjdJ | b2267 | b4127 | Gnat family putative n-acetyltransferase; Belongs to the UPF0039 (ElaA) family | annotation not available | 0.872 |
| elaA | yjgM | b2267 | b4256 | Gnat family putative n-acetyltransferase; Belongs to the UPF0039 (ElaA) family | Gnat family putative n-acetyltransferase; Belongs to the acetyltransferase family | 0.890 |
| elaA | ypeA | b2267 | b2434 | Gnat family putative n-acetyltransferase; Belongs to the UPF0039 (ElaA) family | Gnat family putative n-acetyltransferase; Belongs to the acetyltransferase family. YpeA subfamily | 0.871 |
| panM | elaA | b3459 | b2267 | Pand autocleavage accelerator, panothenate synthesis; Controls both the activation and catalytic activity of PanD in a coenzyme A (CoA)-dependent fashion. Binding of CoA or a derivative to PanZ leads to interaction with PanD, which promotes the processing and activation of pro-PanD, and subsequent substrate-mediated inhibition of the active form of PanD Inhibition of PanD activity is probably the primary metabolic role of PanZ, allowing negative feedback regulation of pantothenate biosynthesis by CoA | Gnat family putative n-acetyltransferase; Belongs to the UPF0039 (ElaA) family | 0.738 |
| panM | yedL | b3459 | b1932 | Pand autocleavage accelerator, panothenate synthesis; Controls both the activation and catalytic activity of PanD in a coenzyme A (CoA)-dependent fashion. Binding of CoA or a derivative to PanZ leads to interaction with PanD, which promotes the processing and activation of pro-PanD, and subsequent substrate-mediated inhibition of the active form of PanD Inhibition of PanD activity is probably the primary metabolic role of PanZ, allowing negative feedback regulation of pantothenate biosynthesis by CoA | Gnat family putative n-acetyltransferase; Belongs to the acetyltransferase family | 0.832 |
| panM | yhbS | b3459 | b3156 | Pand autocleavage accelerator, panothenate synthesis; Controls both the activation and catalytic activity of PanD in a coenzyme A (CoA)-dependent fashion. Binding of CoA or a derivative to PanZ leads to interaction with PanD, which promotes the processing and activation of pro-PanD, and subsequent substrate-mediated inhibition of the active form of PanD Inhibition of PanD activity is probably the primary metabolic role of PanZ, allowing negative feedback regulation of pantothenate biosynthesis by CoA | Putative acyltransferase with acyl-coa n-acyltransferase domain; Belongs to the acetyltransferase family | 0.787 |
| panM | yhhY | b3459 | b3441 | Pand autocleavage accelerator, panothenate synthesis; Controls both the activation and catalytic activity of PanD in a coenzyme A (CoA)-dependent fashion. Binding of CoA or a derivative to PanZ leads to interaction with PanD, which promotes the processing and activation of pro-PanD, and subsequent substrate-mediated inhibition of the active form of PanD Inhibition of PanD activity is probably the primary metabolic role of PanZ, allowing negative feedback regulation of pantothenate biosynthesis by CoA | Aminoacyl nucleotide detoxifying acetyltransferase; Catalyzes the N-acetylation of L-phenylalanine and L- methionine using acetyl-CoA as acetyl donor in vitro. Cannot accept L- tyrosine as substrate and propionyl-CoA, succinyl-CoA or (S)- methylmalonyl-CoA as acyl donors . Is also able to acetylate and thus detoxify several nonhydrolyzable aminoacyl adenylates, but not the processed form of the peptide-nucleotide antibiotic microcin C (McC). When overproduced, provides complete resistance to leucyl sulfamoyl adenylate (LSA) and partial resistance to alanyl sulfamoyl adenylate (ASA) and [...] | 0.739 |
| panM | yiaC | b3459 | b3550 | Pand autocleavage accelerator, panothenate synthesis; Controls both the activation and catalytic activity of PanD in a coenzyme A (CoA)-dependent fashion. Binding of CoA or a derivative to PanZ leads to interaction with PanD, which promotes the processing and activation of pro-PanD, and subsequent substrate-mediated inhibition of the active form of PanD Inhibition of PanD activity is probably the primary metabolic role of PanZ, allowing negative feedback regulation of pantothenate biosynthesis by CoA | Putative acyltransferase with acyl-coa n-acyltransferase domain; N-epsilon-lysine acetyltransferase that catalyzes acetylation of a large number of proteins. Overexpression inhibits motility | 0.730 |
| panM | yjaB | b3459 | b4012 | Pand autocleavage accelerator, panothenate synthesis; Controls both the activation and catalytic activity of PanD in a coenzyme A (CoA)-dependent fashion. Binding of CoA or a derivative to PanZ leads to interaction with PanD, which promotes the processing and activation of pro-PanD, and subsequent substrate-mediated inhibition of the active form of PanD Inhibition of PanD activity is probably the primary metabolic role of PanZ, allowing negative feedback regulation of pantothenate biosynthesis by CoA | Gnat-family putative n-acetyltransferase; N-epsilon-lysine acetyltransferase that catalyzes acetylation of a large number of proteins . Binds acetyl-CoA | 0.734 |
| panM | yjdJ | b3459 | b4127 | Pand autocleavage accelerator, panothenate synthesis; Controls both the activation and catalytic activity of PanD in a coenzyme A (CoA)-dependent fashion. Binding of CoA or a derivative to PanZ leads to interaction with PanD, which promotes the processing and activation of pro-PanD, and subsequent substrate-mediated inhibition of the active form of PanD Inhibition of PanD activity is probably the primary metabolic role of PanZ, allowing negative feedback regulation of pantothenate biosynthesis by CoA | annotation not available | 0.827 |
| panM | yjgM | b3459 | b4256 | Pand autocleavage accelerator, panothenate synthesis; Controls both the activation and catalytic activity of PanD in a coenzyme A (CoA)-dependent fashion. Binding of CoA or a derivative to PanZ leads to interaction with PanD, which promotes the processing and activation of pro-PanD, and subsequent substrate-mediated inhibition of the active form of PanD Inhibition of PanD activity is probably the primary metabolic role of PanZ, allowing negative feedback regulation of pantothenate biosynthesis by CoA | Gnat family putative n-acetyltransferase; Belongs to the acetyltransferase family | 0.737 |
| panM | ypeA | b3459 | b2434 | Pand autocleavage accelerator, panothenate synthesis; Controls both the activation and catalytic activity of PanD in a coenzyme A (CoA)-dependent fashion. Binding of CoA or a derivative to PanZ leads to interaction with PanD, which promotes the processing and activation of pro-PanD, and subsequent substrate-mediated inhibition of the active form of PanD Inhibition of PanD activity is probably the primary metabolic role of PanZ, allowing negative feedback regulation of pantothenate biosynthesis by CoA | Gnat family putative n-acetyltransferase; Belongs to the acetyltransferase family. YpeA subfamily | 0.824 |
| yedK | yedL | b1931 | b1932 | Putative sos response-associated peptidase yedk; Sensor of abasic sites in single-stranded DNA (ssDNA) required to preserve genome integrity by promoting error-free repair of abasic sites . Recognizes and binds abasic sites in ssDNA at replication forks and chemically modifies the lesion by forming a covalent cross-link with DNA . May act as a protease: mediates autocatalytic processing of its N-terminal methionine in order to expose the catalytic cysteine (By similarity) | Gnat family putative n-acetyltransferase; Belongs to the acetyltransferase family | 0.877 |
| yedL | elaA | b1932 | b2267 | Gnat family putative n-acetyltransferase; Belongs to the acetyltransferase family | Gnat family putative n-acetyltransferase; Belongs to the UPF0039 (ElaA) family | 0.867 |
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