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 |
| ML1481 | def | gene:17575319 | gene:17575781 | Possible molecular chaperone; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | Polypeptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (By similarity). | 0.842 |
| ML1481 | mapB | gene:17575319 | gene:17575417 | Possible molecular chaperone; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | Methionine aminopeptidase; 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. | 0.418 |
| ML1481 | rplI | gene:17575319 | gene:17576548 | Possible molecular chaperone; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | 50S ribosomal protein L9; Binds to the 23S rRNA. | 0.856 |
| ML1481 | rplQ | gene:17575319 | gene:17575808 | Possible molecular chaperone; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | Similar to M. tuberculosis 50S ribosomal protein L17 rplQ Rv3456c SW:RL17_MYCTU (O06323) (180 aa); Fasta score E(): 0, 81.9% identity in 171 aa overlap. Contains Pfam match to entry PF01196 Ribosomal_L17, Ribosomal protein L17. | 0.878 |
| ML1481 | rplU | gene:17575319 | gene:17575305 | Possible molecular chaperone; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | 50S ribosomal protein L21; This protein binds to 23S rRNA in the presence of protein L20; Belongs to the bacterial ribosomal protein bL21 family. | 0.883 |
| ML1481 | rplV | gene:17575319 | gene:17575706 | Possible molecular chaperone; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | 50S ribosomal protein L22; This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity). | 0.906 |
| ML1481 | rpsF | gene:17575319 | gene:17576551 | Possible molecular chaperone; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | 30S ribosomal protein S6; Binds together with S18 to 16S ribosomal RNA. | 0.875 |
| ML1481 | rpsP | gene:17575319 | gene:17575459 | Possible molecular chaperone; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | Highly similar to many 30s ribosomal proteins (S16) including: Bacillus subtilis SW:RS16_BACSU (P21474) (89 aa); Fasta score E(): 2.1e-10, 45.1% identity in 82 aa overlap and Mycobacterium tuberculosis SW:RS16_MYCTU (Q10795) (162 aa); Fasta score E(): 0, 82.5% identity in 160 aa overlap. Contains Pfam match to entry PF00886 Ribosomal_S16, Ribosomal protein S16. Contains PS00732 Ribosomal protein S16 signature; Belongs to the bacterial ribosomal protein bS16 family. | 0.834 |
| ML1481 | rpsT | gene:17575319 | gene:17574425 | Possible molecular chaperone; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | 30S ribosomal protein S20; Binds directly to 16S ribosomal RNA. | 0.812 |
| def | ML1481 | gene:17575781 | gene:17575319 | Polypeptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (By similarity). | Possible molecular chaperone; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.842 |
| def | mapA | gene:17575781 | gene:17575679 | Polypeptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (By similarity). | Probable methionine aminopeptidase; 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. | 0.838 |
| def | mapB | gene:17575781 | gene:17575417 | Polypeptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (By similarity). | Methionine aminopeptidase; 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. | 0.864 |
| def | rplI | gene:17575781 | gene:17576548 | Polypeptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (By similarity). | 50S ribosomal protein L9; Binds to the 23S rRNA. | 0.828 |
| def | rplQ | gene:17575781 | gene:17575808 | Polypeptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (By similarity). | Similar to M. tuberculosis 50S ribosomal protein L17 rplQ Rv3456c SW:RL17_MYCTU (O06323) (180 aa); Fasta score E(): 0, 81.9% identity in 171 aa overlap. Contains Pfam match to entry PF01196 Ribosomal_L17, Ribosomal protein L17. | 0.926 |
| def | rplU | gene:17575781 | gene:17575305 | Polypeptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (By similarity). | 50S ribosomal protein L21; This protein binds to 23S rRNA in the presence of protein L20; Belongs to the bacterial ribosomal protein bL21 family. | 0.842 |
| def | rplV | gene:17575781 | gene:17575706 | Polypeptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (By similarity). | 50S ribosomal protein L22; This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity). | 0.958 |
| def | rpsF | gene:17575781 | gene:17576551 | Polypeptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (By similarity). | 30S ribosomal protein S6; Binds together with S18 to 16S ribosomal RNA. | 0.858 |
| def | rpsP | gene:17575781 | gene:17575459 | Polypeptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (By similarity). | Highly similar to many 30s ribosomal proteins (S16) including: Bacillus subtilis SW:RS16_BACSU (P21474) (89 aa); Fasta score E(): 2.1e-10, 45.1% identity in 82 aa overlap and Mycobacterium tuberculosis SW:RS16_MYCTU (Q10795) (162 aa); Fasta score E(): 0, 82.5% identity in 160 aa overlap. Contains Pfam match to entry PF00886 Ribosomal_S16, Ribosomal protein S16. Contains PS00732 Ribosomal protein S16 signature; Belongs to the bacterial ribosomal protein bS16 family. | 0.835 |
| def | rpsT | gene:17575781 | gene:17574425 | Polypeptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (By similarity). | 30S ribosomal protein S20; Binds directly to 16S ribosomal RNA. | 0.825 |
| mapA | def | gene:17575679 | gene:17575781 | Probable methionine aminopeptidase; 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. | Polypeptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (By similarity). | 0.838 |
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