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 proteins in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| APP | CLU | ENSCAFP00000012583 | ENSCAFP00000034804 | Gamma-secretase C-terminal fragment 57; Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions (By similarity). Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb (By similarity). Couples to apoptosis-inducing pathways such as those medi [...] | Clusterin alpha chain; Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself (By similarity). Binding to cell surface receptors triggers internalization of the chaperone-client complex and [...] | 0.907 |
| APP | LCN2 | ENSCAFP00000012583 | ENSCAFP00000029769 | Gamma-secretase C-terminal fragment 57; Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions (By similarity). Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb (By similarity). Couples to apoptosis-inducing pathways such as those medi [...] | Lipocalin 2; Belongs to the calycin superfamily. Lipocalin family. | 0.729 |
| APP | LOC607874 | ENSCAFP00000012583 | ENSCAFP00000036304 | Gamma-secretase C-terminal fragment 57; Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions (By similarity). Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb (By similarity). Couples to apoptosis-inducing pathways such as those medi [...] | Cystatin domain-containing protein. | 0.443 |
| APP | MMP9 | ENSCAFP00000012583 | ENSCAFP00000035167 | Gamma-secretase C-terminal fragment 57; Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions (By similarity). Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb (By similarity). Couples to apoptosis-inducing pathways such as those medi [...] | Matrix metalloproteinase-9; Could play a role in bone osteoclastic resorption. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments (By similarity). | 0.456 |
| CAMP | LCN2 | ENSCAFP00000019004 | ENSCAFP00000029769 | Cathelicidin antimicrobial peptide. | Lipocalin 2; Belongs to the calycin superfamily. Lipocalin family. | 0.782 |
| CAMP | MMP9 | ENSCAFP00000019004 | ENSCAFP00000035167 | Cathelicidin antimicrobial peptide. | Matrix metalloproteinase-9; Could play a role in bone osteoclastic resorption. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments (By similarity). | 0.466 |
| CD28 | LCN2 | ENSCAFP00000052654 | ENSCAFP00000029769 | CD28 molecule. | Lipocalin 2; Belongs to the calycin superfamily. Lipocalin family. | 0.762 |
| CLU | APP | ENSCAFP00000034804 | ENSCAFP00000012583 | Clusterin alpha chain; Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself (By similarity). Binding to cell surface receptors triggers internalization of the chaperone-client complex and [...] | Gamma-secretase C-terminal fragment 57; Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions (By similarity). Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb (By similarity). Couples to apoptosis-inducing pathways such as those medi [...] | 0.907 |
| CLU | FN1 | ENSCAFP00000034804 | ENSCAFP00000066679 | Clusterin alpha chain; Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself (By similarity). Binding to cell surface receptors triggers internalization of the chaperone-client complex and [...] | Fibronectin; Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts (By similarity). | 0.583 |
| CLU | LCN2 | ENSCAFP00000034804 | ENSCAFP00000029769 | Clusterin alpha chain; Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself (By similarity). Binding to cell surface receptors triggers internalization of the chaperone-client complex and [...] | Lipocalin 2; Belongs to the calycin superfamily. Lipocalin family. | 0.720 |
| CLU | LOC607874 | ENSCAFP00000034804 | ENSCAFP00000036304 | Clusterin alpha chain; Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself (By similarity). Binding to cell surface receptors triggers internalization of the chaperone-client complex and [...] | Cystatin domain-containing protein. | 0.794 |
| FN1 | CLU | ENSCAFP00000066679 | ENSCAFP00000034804 | Fibronectin; Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts (By similarity). | Clusterin alpha chain; Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself (By similarity). Binding to cell surface receptors triggers internalization of the chaperone-client complex and [...] | 0.583 |
| FN1 | LCN2 | ENSCAFP00000066679 | ENSCAFP00000029769 | Fibronectin; Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts (By similarity). | Lipocalin 2; Belongs to the calycin superfamily. Lipocalin family. | 0.781 |
| FN1 | MMP9 | ENSCAFP00000066679 | ENSCAFP00000035167 | Fibronectin; Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts (By similarity). | Matrix metalloproteinase-9; Could play a role in bone osteoclastic resorption. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments (By similarity). | 0.448 |
| HAMP | LCN2 | ENSCAFP00000010474 | ENSCAFP00000029769 | Hepcidin; Seems to act as a signaling molecule involved in the maintenance of iron homeostasis. Seems to be required in conjunction with HFE to regulate both intestinal iron absorption and iron storage in macrophages. May also have antimicrobial activity (By similarity). Belongs to the hepcidin family. | Lipocalin 2; Belongs to the calycin superfamily. Lipocalin family. | 0.863 |
| LCN2 | APP | ENSCAFP00000029769 | ENSCAFP00000012583 | Lipocalin 2; Belongs to the calycin superfamily. Lipocalin family. | Gamma-secretase C-terminal fragment 57; Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions (By similarity). Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb (By similarity). Couples to apoptosis-inducing pathways such as those medi [...] | 0.729 |
| LCN2 | CAMP | ENSCAFP00000029769 | ENSCAFP00000019004 | Lipocalin 2; Belongs to the calycin superfamily. Lipocalin family. | Cathelicidin antimicrobial peptide. | 0.782 |
| LCN2 | CD28 | ENSCAFP00000029769 | ENSCAFP00000052654 | Lipocalin 2; Belongs to the calycin superfamily. Lipocalin family. | CD28 molecule. | 0.762 |
| LCN2 | CLU | ENSCAFP00000029769 | ENSCAFP00000034804 | Lipocalin 2; Belongs to the calycin superfamily. Lipocalin family. | Clusterin alpha chain; Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself (By similarity). Binding to cell surface receptors triggers internalization of the chaperone-client complex and [...] | 0.720 |
| LCN2 | FN1 | ENSCAFP00000029769 | ENSCAFP00000066679 | Lipocalin 2; Belongs to the calycin superfamily. Lipocalin family. | Fibronectin; Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts (By similarity). | 0.781 |
page 1 of 2