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 |
| F48E8.4 | R151.6 | F48E8.4.1 | R151.6.1 | PRKCSH domain-containing protein. | 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. | 0.957 |
| F48E8.4 | Y105E8A.2 | F48E8.4.1 | Y105E8A.2.1 | PRKCSH domain-containing protein. | Uncharacterized protein. | 0.800 |
| F48E8.4 | cdc-48.1 | F48E8.4.1 | C06A1.1.1 | PRKCSH domain-containing protein. | Transitional endoplasmic reticulum ATPase homolog 1; ATP-dependent chaperone which probably uses the energy provided by ATP hydrolysis to generate mechanical force to unfold substrate proteins, disassemble protein complexes, and disaggregate protein aggregates. Can also prevent aggregation of unfolded proteins also in an ATP- independent manner. Targets polyubiquitinated proteins for proteasomal degradation by binding to 'Lys-48'-linked polyubiquitin chains. Involved in the cytoplasmic elimination of misfolded proteins exported from the ER. This pathway, known as ERAD, prevents the act [...] | 0.619 |
| F48E8.4 | cdc-48.2 | F48E8.4.1 | C41C4.8.2 | PRKCSH domain-containing protein. | Transitional endoplasmic reticulum ATPase homolog 2; ATP-dependent chaperone which probably uses the energy provided by ATP hydrolysis to generate mechanical force to unfold substrate proteins, disassemble protein complexes, and disaggregate protein aggregates. However, able to prevent aggregation of unfolded proteins also in an ATP-independent manner. Targets polyubiquitinated proteins for proteasomal degradation by binding to 'Lys-48'-linked polyubiquitin chains. Involved in the cytoplasmic elimination of misfolded proteins exported from the ER. This pathway, known as ERAD, prevents [...] | 0.801 |
| F48E8.4 | cup-2 | F48E8.4.1 | F25D7.1.1 | PRKCSH domain-containing protein. | 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. | 0.957 |
| F48E8.4 | marc-6 | F48E8.4.1 | F55A3.1.1 | PRKCSH domain-containing protein. | RING-CH-type domain-containing protein. | 0.608 |
| F48E8.4 | sel-1 | F48E8.4.1 | F45D3.5.2 | PRKCSH domain-containing protein. | Suppressor/Enhancer of Lin-12. | 0.916 |
| F48E8.4 | sel-11 | F48E8.4.1 | F55A11.3.1 | PRKCSH domain-containing protein. | E3 ubiquitin-protein ligase hrd-1; Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated ubc-7 E2 ligase and transfers it to substrates, promoting their degradation. Component of the endoplasmic reticulum quality control (ERQC) system, which is also called the ER-associated degradation (ERAD) system, involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Also promotes the degradation of normal but naturally short-lived proteins. Protects cells from ER stress-induced apoptosis. Thought to play [...] | 0.900 |
| F48E8.4 | ubc-14 | F48E8.4.1 | Y87G2A.9.1 | PRKCSH domain-containing protein. | UBIQUITIN_CONJUGAT_2 domain-containing protein; Belongs to the ubiquitin-conjugating enzyme family. | 0.428 |
| R151.6 | F48E8.4 | R151.6.1 | F48E8.4.1 | 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. | PRKCSH domain-containing protein. | 0.957 |
| R151.6 | Y105E8A.2 | R151.6.1 | Y105E8A.2.1 | 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. | Uncharacterized protein. | 0.957 |
| R151.6 | cdc-48.1 | R151.6.1 | C06A1.1.1 | 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. | Transitional endoplasmic reticulum ATPase homolog 1; ATP-dependent chaperone which probably uses the energy provided by ATP hydrolysis to generate mechanical force to unfold substrate proteins, disassemble protein complexes, and disaggregate protein aggregates. Can also prevent aggregation of unfolded proteins also in an ATP- independent manner. Targets polyubiquitinated proteins for proteasomal degradation by binding to 'Lys-48'-linked polyubiquitin chains. Involved in the cytoplasmic elimination of misfolded proteins exported from the ER. This pathway, known as ERAD, prevents the act [...] | 0.927 |
| R151.6 | cdc-48.2 | R151.6.1 | C41C4.8.2 | 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. | Transitional endoplasmic reticulum ATPase homolog 2; ATP-dependent chaperone which probably uses the energy provided by ATP hydrolysis to generate mechanical force to unfold substrate proteins, disassemble protein complexes, and disaggregate protein aggregates. However, able to prevent aggregation of unfolded proteins also in an ATP-independent manner. Targets polyubiquitinated proteins for proteasomal degradation by binding to 'Lys-48'-linked polyubiquitin chains. Involved in the cytoplasmic elimination of misfolded proteins exported from the ER. This pathway, known as ERAD, prevents [...] | 0.967 |
| 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 | hmgr-1 | R151.6.1 | F08F8.2.1 | 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. | 3-hydroxy-3-methylglutaryl coenzyme A reductase. | 0.489 |
| 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 | 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 | sel-11 | R151.6.1 | F55A11.3.1 | 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-protein ligase hrd-1; Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated ubc-7 E2 ligase and transfers it to substrates, promoting their degradation. Component of the endoplasmic reticulum quality control (ERQC) system, which is also called the ER-associated degradation (ERAD) system, involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Also promotes the degradation of normal but naturally short-lived proteins. Protects cells from ER stress-induced apoptosis. Thought to play [...] | 0.986 |
| R151.6 | ubc-14 | R151.6.1 | Y87G2A.9.1 | 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_CONJUGAT_2 domain-containing protein; Belongs to the ubiquitin-conjugating enzyme family. | 0.560 |
| Y105E8A.2 | F48E8.4 | Y105E8A.2.1 | F48E8.4.1 | Uncharacterized protein. | PRKCSH domain-containing protein. | 0.800 |
page 1 of 5