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 |
| CAPN10 | RNPEP | ENSP00000375844 | ENSP00000295640 | Calpain-10; Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. May play a role in insulin- stimulated glucose uptake; Belongs to the peptidase C2 family. | Aminopeptidase B; Exopeptidase which selectively removes arginine and/or lysine residues from the N-terminus of several peptide substrates including Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(-1)-Lys(0)- somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene B4 (LTB-4) (By similarity). | 0.764 |
| CPB1 | RNPEP | ENSP00000417222 | ENSP00000295640 | Carboxypeptidase B1; Belongs to the peptidase M14 family. | Aminopeptidase B; Exopeptidase which selectively removes arginine and/or lysine residues from the N-terminus of several peptide substrates including Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(-1)-Lys(0)- somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene B4 (LTB-4) (By similarity). | 0.551 |
| DNPEP | DPP3 | ENSP00000431076 | ENSP00000440502 | Aspartyl aminopeptidase; Aminopeptidase with specificity towards an acidic amino acid at the N-terminus. Likely to play an important role in intracellular protein and peptide metabolism. | Dipeptidyl peptidase 3; Cleaves and degrades bioactive peptides, including angiotensin, Leu-enkephalin and Met-enkephalin. Also cleaves Arg-Arg-beta-naphthylamide (in vitro). | 0.546 |
| DNPEP | ENPEP | ENSP00000431076 | ENSP00000265162 | Aspartyl aminopeptidase; Aminopeptidase with specificity towards an acidic amino acid at the N-terminus. Likely to play an important role in intracellular protein and peptide metabolism. | Glutamyl aminopeptidase; Regulates central hypertension through its calcium-modulated preference to cleave N-terminal acidic residues from peptides such as angiotensin II. | 0.711 |
| DNPEP | LAP3 | ENSP00000431076 | ENSP00000226299 | Aspartyl aminopeptidase; Aminopeptidase with specificity towards an acidic amino acid at the N-terminus. Likely to play an important role in intracellular protein and peptide metabolism. | Cytosol aminopeptidase; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides; Belongs to the peptidase M17 family. | 0.727 |
| DNPEP | PGPEP1 | ENSP00000431076 | ENSP00000269919 | Aspartyl aminopeptidase; Aminopeptidase with specificity towards an acidic amino acid at the N-terminus. Likely to play an important role in intracellular protein and peptide metabolism. | Pyroglutamyl-peptidase 1; Removes 5-oxoproline from various penultimate amino acid residues except L-proline. | 0.608 |
| DNPEP | PREP | ENSP00000431076 | ENSP00000499089 | Aspartyl aminopeptidase; Aminopeptidase with specificity towards an acidic amino acid at the N-terminus. Likely to play an important role in intracellular protein and peptide metabolism. | Prolyl endopeptidase; Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long; Belongs to the peptidase S9A family. | 0.537 |
| DNPEP | RNPEP | ENSP00000431076 | ENSP00000295640 | Aspartyl aminopeptidase; Aminopeptidase with specificity towards an acidic amino acid at the N-terminus. Likely to play an important role in intracellular protein and peptide metabolism. | Aminopeptidase B; Exopeptidase which selectively removes arginine and/or lysine residues from the N-terminus of several peptide substrates including Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(-1)-Lys(0)- somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene B4 (LTB-4) (By similarity). | 0.764 |
| DPP3 | DNPEP | ENSP00000440502 | ENSP00000431076 | Dipeptidyl peptidase 3; Cleaves and degrades bioactive peptides, including angiotensin, Leu-enkephalin and Met-enkephalin. Also cleaves Arg-Arg-beta-naphthylamide (in vitro). | Aspartyl aminopeptidase; Aminopeptidase with specificity towards an acidic amino acid at the N-terminus. Likely to play an important role in intracellular protein and peptide metabolism. | 0.546 |
| DPP3 | PREP | ENSP00000440502 | ENSP00000499089 | Dipeptidyl peptidase 3; Cleaves and degrades bioactive peptides, including angiotensin, Leu-enkephalin and Met-enkephalin. Also cleaves Arg-Arg-beta-naphthylamide (in vitro). | Prolyl endopeptidase; Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long; Belongs to the peptidase S9A family. | 0.646 |
| DPP3 | RNPEP | ENSP00000440502 | ENSP00000295640 | Dipeptidyl peptidase 3; Cleaves and degrades bioactive peptides, including angiotensin, Leu-enkephalin and Met-enkephalin. Also cleaves Arg-Arg-beta-naphthylamide (in vitro). | Aminopeptidase B; Exopeptidase which selectively removes arginine and/or lysine residues from the N-terminus of several peptide substrates including Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(-1)-Lys(0)- somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene B4 (LTB-4) (By similarity). | 0.640 |
| ENPEP | DNPEP | ENSP00000265162 | ENSP00000431076 | Glutamyl aminopeptidase; Regulates central hypertension through its calcium-modulated preference to cleave N-terminal acidic residues from peptides such as angiotensin II. | Aspartyl aminopeptidase; Aminopeptidase with specificity towards an acidic amino acid at the N-terminus. Likely to play an important role in intracellular protein and peptide metabolism. | 0.711 |
| ENPEP | LAP3 | ENSP00000265162 | ENSP00000226299 | Glutamyl aminopeptidase; Regulates central hypertension through its calcium-modulated preference to cleave N-terminal acidic residues from peptides such as angiotensin II. | Cytosol aminopeptidase; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides; Belongs to the peptidase M17 family. | 0.549 |
| ENPEP | PGPEP1 | ENSP00000265162 | ENSP00000269919 | Glutamyl aminopeptidase; Regulates central hypertension through its calcium-modulated preference to cleave N-terminal acidic residues from peptides such as angiotensin II. | Pyroglutamyl-peptidase 1; Removes 5-oxoproline from various penultimate amino acid residues except L-proline. | 0.419 |
| ENPEP | PREP | ENSP00000265162 | ENSP00000499089 | Glutamyl aminopeptidase; Regulates central hypertension through its calcium-modulated preference to cleave N-terminal acidic residues from peptides such as angiotensin II. | Prolyl endopeptidase; Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long; Belongs to the peptidase S9A family. | 0.554 |
| ENPEP | RNPEP | ENSP00000265162 | ENSP00000295640 | Glutamyl aminopeptidase; Regulates central hypertension through its calcium-modulated preference to cleave N-terminal acidic residues from peptides such as angiotensin II. | Aminopeptidase B; Exopeptidase which selectively removes arginine and/or lysine residues from the N-terminus of several peptide substrates including Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(-1)-Lys(0)- somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene B4 (LTB-4) (By similarity). | 0.495 |
| LAP3 | DNPEP | ENSP00000226299 | ENSP00000431076 | Cytosol aminopeptidase; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides; Belongs to the peptidase M17 family. | Aspartyl aminopeptidase; Aminopeptidase with specificity towards an acidic amino acid at the N-terminus. Likely to play an important role in intracellular protein and peptide metabolism. | 0.727 |
| LAP3 | ENPEP | ENSP00000226299 | ENSP00000265162 | Cytosol aminopeptidase; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides; Belongs to the peptidase M17 family. | Glutamyl aminopeptidase; Regulates central hypertension through its calcium-modulated preference to cleave N-terminal acidic residues from peptides such as angiotensin II. | 0.549 |
| LAP3 | PGPEP1 | ENSP00000226299 | ENSP00000269919 | Cytosol aminopeptidase; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides; Belongs to the peptidase M17 family. | Pyroglutamyl-peptidase 1; Removes 5-oxoproline from various penultimate amino acid residues except L-proline. | 0.489 |
| LAP3 | PREP | ENSP00000226299 | ENSP00000499089 | Cytosol aminopeptidase; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides; Belongs to the peptidase M17 family. | Prolyl endopeptidase; Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long; Belongs to the peptidase S9A family. | 0.525 |
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