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 |
| ADH7 | SERPINB11 | ENSP00000420269 | ENSP00000485532 | All-trans-retinol dehydrogenase [NAD(+)] ADH7; Catalyzes the NAD-dependent oxidation of all-trans-retinol, alcohol, and omega-hydroxy fatty acids and their derivatives. Oxidizes preferentially all trans-retinol, all-trans-4-hydroxyretinol, 9-cis- retinol, 2-hexenol, and long chain omega-hydroxy fatty acids such as juniperic acid. In vitro can also catalyzes the NADH-dependent reduction of all-trans- retinal and aldehydes and their derivatives. Reduces preferentially all trans- retinal, all-trans-4-oxoretinal and hexanal. Catalyzes in the oxidative direction with higher efficiency. Ther [...] | Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change. | 0.491 |
| CBWD3 | SERPINB11 | ENSP00000353295 | ENSP00000485532 | COBW domain containing 3. | Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change. | 0.420 |
| CPE | SERPINB11 | ENSP00000386104 | ENSP00000485532 | Carboxypeptidase E; Sorting receptor that directs prohormones to the regulated secretory pathway. Acts also as a prohormone processing enzyme in neuro/endocrine cells, removing dibasic residues from the C-terminal end of peptide hormone precursors after initial endoprotease cleavage. Belongs to the peptidase M14 family. | Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change. | 0.461 |
| DNLZ | SERPINB11 | ENSP00000360803 | ENSP00000485532 | DNL-type zinc finger protein; May function as a co-chaperone towards HSPA9/mortalin which, by itself, is prone to self-aggregation. | Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change. | 0.468 |
| KLK14 | SERPINB11 | ENSP00000375678 | ENSP00000485532 | Kallikrein-14; Serine-type endopeptidase with a dual trypsin-like and chymotrypsin-like substrate specificity. May activate/inactivate the proteinase-activated receptors F2R, F2RL1 and F2RL3 and other kallikreins including KLK1, KLK3, KLK5 and KLK11. May function in seminal clot liquefaction through direct cleavage of the semenogelin SEMG1 and SEMG2 and activation of KLK3. May function through desmoglein DSG1 cleavage in epidermal desquamation a process by which the most superficial corneocytes are shed from the skin surface. May be involved in several aspects of tumor progression incl [...] | Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change. | 0.485 |
| NFASC | SERPINB11 | ENSP00000344786 | ENSP00000485532 | Neurofascin; Cell adhesion, ankyrin-binding protein which may be involved in neurite extension, axonal guidance, synaptogenesis, myelination and neuron-glial cell interactions. | Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change. | 0.401 |
| S100A12 | SERPINB11 | ENSP00000357726 | ENSP00000485532 | Protein S100-A12; S100A12 is a calcium-, zinc- and copper-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. Its proinflammatory activity involves recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to receptor for advanced glycation endproducts (AGER). Binding to AGER activates the MAP-kinase and NF- kappa-B signaling pathways leadi [...] | Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change. | 0.400 |
| SERPINB11 | ADH7 | ENSP00000485532 | ENSP00000420269 | Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change. | All-trans-retinol dehydrogenase [NAD(+)] ADH7; Catalyzes the NAD-dependent oxidation of all-trans-retinol, alcohol, and omega-hydroxy fatty acids and their derivatives. Oxidizes preferentially all trans-retinol, all-trans-4-hydroxyretinol, 9-cis- retinol, 2-hexenol, and long chain omega-hydroxy fatty acids such as juniperic acid. In vitro can also catalyzes the NADH-dependent reduction of all-trans- retinal and aldehydes and their derivatives. Reduces preferentially all trans- retinal, all-trans-4-oxoretinal and hexanal. Catalyzes in the oxidative direction with higher efficiency. Ther [...] | 0.491 |
| SERPINB11 | CBWD3 | ENSP00000485532 | ENSP00000353295 | Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change. | COBW domain containing 3. | 0.420 |
| SERPINB11 | CPE | ENSP00000485532 | ENSP00000386104 | Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change. | Carboxypeptidase E; Sorting receptor that directs prohormones to the regulated secretory pathway. Acts also as a prohormone processing enzyme in neuro/endocrine cells, removing dibasic residues from the C-terminal end of peptide hormone precursors after initial endoprotease cleavage. Belongs to the peptidase M14 family. | 0.461 |
| SERPINB11 | DNLZ | ENSP00000485532 | ENSP00000360803 | Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change. | DNL-type zinc finger protein; May function as a co-chaperone towards HSPA9/mortalin which, by itself, is prone to self-aggregation. | 0.468 |
| SERPINB11 | KLK14 | ENSP00000485532 | ENSP00000375678 | Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change. | Kallikrein-14; Serine-type endopeptidase with a dual trypsin-like and chymotrypsin-like substrate specificity. May activate/inactivate the proteinase-activated receptors F2R, F2RL1 and F2RL3 and other kallikreins including KLK1, KLK3, KLK5 and KLK11. May function in seminal clot liquefaction through direct cleavage of the semenogelin SEMG1 and SEMG2 and activation of KLK3. May function through desmoglein DSG1 cleavage in epidermal desquamation a process by which the most superficial corneocytes are shed from the skin surface. May be involved in several aspects of tumor progression incl [...] | 0.485 |
| SERPINB11 | NFASC | ENSP00000485532 | ENSP00000344786 | Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change. | Neurofascin; Cell adhesion, ankyrin-binding protein which may be involved in neurite extension, axonal guidance, synaptogenesis, myelination and neuron-glial cell interactions. | 0.401 |
| SERPINB11 | S100A12 | ENSP00000485532 | ENSP00000357726 | Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change. | Protein S100-A12; S100A12 is a calcium-, zinc- and copper-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. Its proinflammatory activity involves recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to receptor for advanced glycation endproducts (AGER). Binding to AGER activates the MAP-kinase and NF- kappa-B signaling pathways leadi [...] | 0.400 |
| SERPINB11 | ZC2HC1C | ENSP00000485532 | ENSP00000435550 | Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change. | Zinc finger C2HC-type containing 1C; Belongs to the ZC2HC1 family. | 0.432 |
| SERPINB11 | ZNF799 | ENSP00000485532 | ENSP00000411084 | Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change. | Zinc finger protein 799; May be involved in transcriptional regulation. | 0.479 |
| ZC2HC1C | SERPINB11 | ENSP00000435550 | ENSP00000485532 | Zinc finger C2HC-type containing 1C; Belongs to the ZC2HC1 family. | Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change. | 0.432 |
| ZNF799 | SERPINB11 | ENSP00000411084 | ENSP00000485532 | Zinc finger protein 799; May be involved in transcriptional regulation. | Serpin B11; Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change. | 0.479 |