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 |
| R151.6 | cup-2 | R151.6.1 | F25D7.1.1 | Derlin-2; May be required for the degradation process of some specific misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Its precise function remains unclear, but its ability to complement der1 mutations in C.cerevisiae, suggests a similar function in the degradation of ER misfolded proteins. | Derlin-1; Specifically required for the degradation process of misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Belongs to the derlin family. | 0.991 |
| R151.6 | erl-1 | R151.6.1 | C42C1.15.1 | Derlin-2; May be required for the degradation process of some specific misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Its precise function remains unclear, but its ability to complement der1 mutations in C.cerevisiae, suggests a similar function in the degradation of ER misfolded proteins. | Erlin. | 0.577 |
| R151.6 | marc-6 | R151.6.1 | F55A3.1.1 | Derlin-2; May be required for the degradation process of some specific misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Its precise function remains unclear, but its ability to complement der1 mutations in C.cerevisiae, suggests a similar function in the degradation of ER misfolded proteins. | RING-CH-type domain-containing protein. | 0.673 |
| R151.6 | rnf-5 | R151.6.1 | C16C10.7a.1 | Derlin-2; May be required for the degradation process of some specific misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Its precise function remains unclear, but its ability to complement der1 mutations in C.cerevisiae, suggests a similar function in the degradation of ER misfolded proteins. | E3 ubiquitin ligase rnf-5; E3 ubiquitin ligase that plays a role in the maintenance of muscle cell boundaries and muscle dense bodies, which establish the adhesion sites of the muscle cells to the extracellular matrix. Ubiquitinates the LIM domain protein unc-95, thereby regulating its dislocalization from muscle dense bodies and weakening the link between the muscle cells and the hypodermis. Regulation of unc-95 dissociation from muscle dense bodies by ubiquitination plays an important role in ecdysis during molting. Plays a role in the cessation of distal tip cell migration at the en [...] | 0.769 |
| R151.6 | sel-1 | R151.6.1 | F45D3.5.2 | Derlin-2; May be required for the degradation process of some specific misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Its precise function remains unclear, but its ability to complement der1 mutations in C.cerevisiae, suggests a similar function in the degradation of ER misfolded proteins. | Suppressor/Enhancer of Lin-12. | 0.994 |
| R151.6 | ubq-2 | R151.6.1 | ZK1010.1.1 | Derlin-2; May be required for the degradation process of some specific misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Its precise function remains unclear, but its ability to complement der1 mutations in C.cerevisiae, suggests a similar function in the degradation of ER misfolded proteins. | Ubiquitin-60S ribosomal protein L40; [Ubiquitin]: exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is invol [...] | 0.499 |
| T16G12.6 | ccdc-55 | T16G12.6.1 | C16C10.6.1 | Xpo1 domain-containing protein. | Nuclear speckle splicing regulatory protein 1 homolog; Required for the cessation of distal tip cell migration at the end of larval morphogenesis; Belongs to the NSRP1 family. | 0.425 |
| T16G12.6 | rnf-5 | T16G12.6.1 | C16C10.7a.1 | Xpo1 domain-containing protein. | E3 ubiquitin ligase rnf-5; E3 ubiquitin ligase that plays a role in the maintenance of muscle cell boundaries and muscle dense bodies, which establish the adhesion sites of the muscle cells to the extracellular matrix. Ubiquitinates the LIM domain protein unc-95, thereby regulating its dislocalization from muscle dense bodies and weakening the link between the muscle cells and the hypodermis. Regulation of unc-95 dissociation from muscle dense bodies by ubiquitination plays an important role in ecdysis during molting. Plays a role in the cessation of distal tip cell migration at the en [...] | 0.702 |
| ccdc-55 | T16G12.6 | C16C10.6.1 | T16G12.6.1 | Nuclear speckle splicing regulatory protein 1 homolog; Required for the cessation of distal tip cell migration at the end of larval morphogenesis; Belongs to the NSRP1 family. | Xpo1 domain-containing protein. | 0.425 |
| ccdc-55 | rnf-121 | C16C10.6.1 | C16C10.5.1 | Nuclear speckle splicing regulatory protein 1 homolog; Required for the cessation of distal tip cell migration at the end of larval morphogenesis; Belongs to the NSRP1 family. | RING finger protein 121; Required for the cessation of distal tip cell migration at the end of larval morphogenesis; Belongs to the RNF121 family. | 0.974 |
| ccdc-55 | rnf-5 | C16C10.6.1 | C16C10.7a.1 | Nuclear speckle splicing regulatory protein 1 homolog; Required for the cessation of distal tip cell migration at the end of larval morphogenesis; Belongs to the NSRP1 family. | E3 ubiquitin ligase rnf-5; E3 ubiquitin ligase that plays a role in the maintenance of muscle cell boundaries and muscle dense bodies, which establish the adhesion sites of the muscle cells to the extracellular matrix. Ubiquitinates the LIM domain protein unc-95, thereby regulating its dislocalization from muscle dense bodies and weakening the link between the muscle cells and the hypodermis. Regulation of unc-95 dissociation from muscle dense bodies by ubiquitination plays an important role in ecdysis during molting. Plays a role in the cessation of distal tip cell migration at the en [...] | 0.708 |
| cup-2 | R151.6 | F25D7.1.1 | R151.6.1 | Derlin-1; Specifically required for the degradation process of misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Belongs to the derlin family. | Derlin-2; May be required for the degradation process of some specific misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Its precise function remains unclear, but its ability to complement der1 mutations in C.cerevisiae, suggests a similar function in the degradation of ER misfolded proteins. | 0.991 |
| cup-2 | erl-1 | F25D7.1.1 | C42C1.15.1 | Derlin-1; Specifically required for the degradation process of misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Belongs to the derlin family. | Erlin. | 0.591 |
| cup-2 | marc-6 | F25D7.1.1 | F55A3.1.1 | Derlin-1; Specifically required for the degradation process of misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Belongs to the derlin family. | RING-CH-type domain-containing protein. | 0.784 |
| cup-2 | rnf-121 | F25D7.1.1 | C16C10.5.1 | Derlin-1; Specifically required for the degradation process of misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Belongs to the derlin family. | RING finger protein 121; Required for the cessation of distal tip cell migration at the end of larval morphogenesis; Belongs to the RNF121 family. | 0.488 |
| cup-2 | rnf-5 | F25D7.1.1 | C16C10.7a.1 | Derlin-1; Specifically required for the degradation process of misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Belongs to the derlin family. | E3 ubiquitin ligase rnf-5; E3 ubiquitin ligase that plays a role in the maintenance of muscle cell boundaries and muscle dense bodies, which establish the adhesion sites of the muscle cells to the extracellular matrix. Ubiquitinates the LIM domain protein unc-95, thereby regulating its dislocalization from muscle dense bodies and weakening the link between the muscle cells and the hypodermis. Regulation of unc-95 dissociation from muscle dense bodies by ubiquitination plays an important role in ecdysis during molting. Plays a role in the cessation of distal tip cell migration at the en [...] | 0.823 |
| cup-2 | sel-1 | F25D7.1.1 | F45D3.5.2 | Derlin-1; Specifically required for the degradation process of misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Belongs to the derlin family. | Suppressor/Enhancer of Lin-12. | 0.991 |
| cup-2 | ubq-2 | F25D7.1.1 | ZK1010.1.1 | Derlin-1; Specifically required for the degradation process of misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Belongs to the derlin family. | Ubiquitin-60S ribosomal protein L40; [Ubiquitin]: exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is invol [...] | 0.499 |
| erl-1 | R151.6 | C42C1.15.1 | R151.6.1 | Erlin. | Derlin-2; May be required for the degradation process of some specific misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Its precise function remains unclear, but its ability to complement der1 mutations in C.cerevisiae, suggests a similar function in the degradation of ER misfolded proteins. | 0.577 |
| erl-1 | cup-2 | C42C1.15.1 | F25D7.1.1 | Erlin. | Derlin-1; Specifically required for the degradation process of misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Belongs to the derlin family. | 0.591 |
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