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 |
| llmg_0944 | pepDB | llmg_0944 | llmg_0943 | Putative secreted protein. | PepDB protein; High confidence in function and specificity. | 0.512 |
| papL | pepDB | llmg_0942 | llmg_0943 | poly(A) polymerase; Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. | PepDB protein; High confidence in function and specificity. | 0.531 |
| pepDB | llmg_0944 | llmg_0943 | llmg_0944 | PepDB protein; High confidence in function and specificity. | Putative secreted protein. | 0.512 |
| pepDB | papL | llmg_0943 | llmg_0942 | PepDB protein; High confidence in function and specificity. | poly(A) polymerase; Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. | 0.531 |
| pepDB | pepM | llmg_0943 | llmg_0577 | PepDB protein; High confidence in function and specificity. | PepM protein; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.631 |
| pepDB | pepN | llmg_0943 | llmg_0319 | PepDB protein; High confidence in function and specificity. | PepN protein; Aminopeptidase with broad substrate specificity to several peptides. It has more affinity for oligopeptides than for dipeptides. It plays an essential role in the metabolism, it may be involved in nitrogen supply or protein turnover. | 0.479 |
| pepDB | pepT | llmg_0943 | llmg_1994 | PepDB protein; High confidence in function and specificity. | Peptidase T; Cleaves the N-terminal amino acid of tripeptides. Has a broad specificity for tripeptides with no clear preference for a particular tripeptide. Tripeptides with proline in the second position are an exception and are not hydrolyzed. Does not hydrolyze dipeptides, tetrapeptides, or oligopeptides (By similarity). | 0.596 |
| pepDB | pepV | llmg_0943 | llmg_1706 | PepDB protein; High confidence in function and specificity. | Dipeptidase; High confidence in function and specificity. | 0.572 |
| pepDB | pepXP | llmg_0943 | llmg_2328 | PepDB protein; High confidence in function and specificity. | X-prolyl dipeptidyl aminopeptidase; Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline; Belongs to the peptidase S15 family. | 0.561 |
| pepM | pepDB | llmg_0577 | llmg_0943 | PepM protein; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | PepDB protein; High confidence in function and specificity. | 0.631 |
| pepM | pepN | llmg_0577 | llmg_0319 | PepM protein; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | PepN protein; Aminopeptidase with broad substrate specificity to several peptides. It has more affinity for oligopeptides than for dipeptides. It plays an essential role in the metabolism, it may be involved in nitrogen supply or protein turnover. | 0.970 |
| pepM | pepT | llmg_0577 | llmg_1994 | PepM protein; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | Peptidase T; Cleaves the N-terminal amino acid of tripeptides. Has a broad specificity for tripeptides with no clear preference for a particular tripeptide. Tripeptides with proline in the second position are an exception and are not hydrolyzed. Does not hydrolyze dipeptides, tetrapeptides, or oligopeptides (By similarity). | 0.967 |
| pepM | pepV | llmg_0577 | llmg_1706 | PepM protein; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | Dipeptidase; High confidence in function and specificity. | 0.929 |
| pepM | pepXP | llmg_0577 | llmg_2328 | PepM protein; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | X-prolyl dipeptidyl aminopeptidase; Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline; Belongs to the peptidase S15 family. | 0.922 |
| pepN | pepDB | llmg_0319 | llmg_0943 | PepN protein; Aminopeptidase with broad substrate specificity to several peptides. It has more affinity for oligopeptides than for dipeptides. It plays an essential role in the metabolism, it may be involved in nitrogen supply or protein turnover. | PepDB protein; High confidence in function and specificity. | 0.479 |
| pepN | pepM | llmg_0319 | llmg_0577 | PepN protein; Aminopeptidase with broad substrate specificity to several peptides. It has more affinity for oligopeptides than for dipeptides. It plays an essential role in the metabolism, it may be involved in nitrogen supply or protein turnover. | PepM protein; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.970 |
| pepN | pepT | llmg_0319 | llmg_1994 | PepN protein; Aminopeptidase with broad substrate specificity to several peptides. It has more affinity for oligopeptides than for dipeptides. It plays an essential role in the metabolism, it may be involved in nitrogen supply or protein turnover. | Peptidase T; Cleaves the N-terminal amino acid of tripeptides. Has a broad specificity for tripeptides with no clear preference for a particular tripeptide. Tripeptides with proline in the second position are an exception and are not hydrolyzed. Does not hydrolyze dipeptides, tetrapeptides, or oligopeptides (By similarity). | 0.966 |
| pepN | pepV | llmg_0319 | llmg_1706 | PepN protein; Aminopeptidase with broad substrate specificity to several peptides. It has more affinity for oligopeptides than for dipeptides. It plays an essential role in the metabolism, it may be involved in nitrogen supply or protein turnover. | Dipeptidase; High confidence in function and specificity. | 0.932 |
| pepN | pepXP | llmg_0319 | llmg_2328 | PepN protein; Aminopeptidase with broad substrate specificity to several peptides. It has more affinity for oligopeptides than for dipeptides. It plays an essential role in the metabolism, it may be involved in nitrogen supply or protein turnover. | X-prolyl dipeptidyl aminopeptidase; Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline; Belongs to the peptidase S15 family. | 0.984 |
| pepT | pepDB | llmg_1994 | llmg_0943 | Peptidase T; Cleaves the N-terminal amino acid of tripeptides. Has a broad specificity for tripeptides with no clear preference for a particular tripeptide. Tripeptides with proline in the second position are an exception and are not hydrolyzed. Does not hydrolyze dipeptides, tetrapeptides, or oligopeptides (By similarity). | PepDB protein; High confidence in function and specificity. | 0.596 |
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