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 | 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 | cdc-48.3 | R151.6.1 | K04G2.3.1 | 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. | ATPase family protein 2 homolog; ATP-dependent chaperone which uses the energy provided by ATP hydrolysis to generate mechanical force to disassemble protein complexes (By similarity). Required for various steps of embryonic mitosis including centrosome duplication, spindle assembly, ER dynamics and cell cycle progression. Regulates the stability and activity of kinase air-2, a component of the chromosomal passenger complex (CPC). Inhibits air-2 kinase activity from metaphase to late telophase and negatively regulates air-2 stability during mitotic exit. Controls ER transition into she [...] | 0.914 |
| 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 | npl-4.1 | R151.6.1 | F59E12.4b.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. | Nuclear protein localization protein 4 homolog 1; In association with ufd-1 and ATPase cdc-48.1 and/or cdc- 48.2, involved in the cytoplasmic elimination of misfolded proteins exported from the ER. This pathway, known as ERAD, prevents the activation of the unfolded protein response (UPR) caused by the accumulation of misfolded proteins in the ER. During S phase and in association with ufd-1, cdc-48.1 and/or cdc-48.2 and ubxn-3, ensures the degradation of DNA licensing factor cdt-1 after the initiation of DNA replication and thus the disassembly of the DNA replication CGM helicase comp [...] | 0.911 |
| R151.6 | npl-4.2 | R151.6.1 | F59E12.5b.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. | Nuclear protein localization protein 4 homolog 2; In association with ufd-1 and ATPase cdc-48.1 and/or cdc- 48.2, involved in the cytoplasmic elimination of misfolded proteins exported from the ER. This pathway, known as ERAD, prevents the activation of the unfolded protein response (UPR) caused by the accumulation of misfolded proteins in the ER. During S phase and in association with ufd-1, cdc-48.1 and/or cdc-48.2 and ubxn-3, ensures the degradation of DNA licensing factor cdt-1 after the initiation of DNA replication and thus the disassembly of the DNA replication CGM helicase comp [...] | 0.922 |
| 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 |
| R151.6 | ufd-1 | R151.6.1 | F19B6.2a.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. | Ubiquitin fusion degradation protein 1 homolog; Functions at a post-ubiquitination step in the ubiquitin fusion degradation (UFD) pathway (By similarity). In association with npl-4.1 and/or npl-4.2 and ATPase cdc-48.1 and/or cdc-48.2, involved in the cytoplasmic elimination of misfolded proteins exported from the ER. This pathway, known as ERAD, prevents the activation of the unfolded protein response (UPR) caused by the accumulation of misfolded proteins in the ER. During S phase and in association with npl-4.1 and/or npl-4.2, cdc-48.1 and/or cdc-48.2 and ubxn-3, ensures the degradati [...] | 0.975 |
| R151.6 | ufd-2 | R151.6.1 | T05H10.5b.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 conjugation factor E4 ufd-2; Acts as an E4 ubiquitin ligase mediating the assembly of polyubiquitin chains on substrates ubiquitinated by another E3 ubiquitin ligase. The elongation of preexisting ubiquitin chains preferentially targets ubiquitin 'Lys-29' and 'Lys-48' residues. Also functions as an E3 ligase in conjunction with specific E1 and E2 ligases. Probably by regulating protein ubiquitination at DNA damage repair sites, coordinates DNA double- strand-break repair and apoptosis in the germline. Required for germline apoptosis in response to DNA damage downstream of cep [...] | 0.518 |
| R151.6 | ufd-3 | R151.6.1 | C05C10.6b.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 fusion degradation protein 3 homolog; Plays a role in protein ubiquitination, sorting and degradation through its association with cdc-48.1 and/or cdc-48.2. | 0.679 |
| cdc-48.1 | R151.6 | C06A1.1.1 | R151.6.1 | 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 [...] | 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. | 0.927 |
| cdc-48.1 | cdc-48.2 | C06A1.1.1 | C41C4.8.2 | 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 [...] | 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 [...] | 0.988 |
| cdc-48.1 | cdc-48.3 | C06A1.1.1 | K04G2.3.1 | 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 [...] | ATPase family protein 2 homolog; ATP-dependent chaperone which uses the energy provided by ATP hydrolysis to generate mechanical force to disassemble protein complexes (By similarity). Required for various steps of embryonic mitosis including centrosome duplication, spindle assembly, ER dynamics and cell cycle progression. Regulates the stability and activity of kinase air-2, a component of the chromosomal passenger complex (CPC). Inhibits air-2 kinase activity from metaphase to late telophase and negatively regulates air-2 stability during mitotic exit. Controls ER transition into she [...] | 0.929 |
| cdc-48.1 | cup-2 | C06A1.1.1 | F25D7.1.1 | 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 [...] | 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. | 0.938 |
| cdc-48.1 | npl-4.1 | C06A1.1.1 | F59E12.4b.1 | 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 [...] | Nuclear protein localization protein 4 homolog 1; In association with ufd-1 and ATPase cdc-48.1 and/or cdc- 48.2, involved in the cytoplasmic elimination of misfolded proteins exported from the ER. This pathway, known as ERAD, prevents the activation of the unfolded protein response (UPR) caused by the accumulation of misfolded proteins in the ER. During S phase and in association with ufd-1, cdc-48.1 and/or cdc-48.2 and ubxn-3, ensures the degradation of DNA licensing factor cdt-1 after the initiation of DNA replication and thus the disassembly of the DNA replication CGM helicase comp [...] | 0.990 |
| cdc-48.1 | npl-4.2 | C06A1.1.1 | F59E12.5b.1 | 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 [...] | Nuclear protein localization protein 4 homolog 2; In association with ufd-1 and ATPase cdc-48.1 and/or cdc- 48.2, involved in the cytoplasmic elimination of misfolded proteins exported from the ER. This pathway, known as ERAD, prevents the activation of the unfolded protein response (UPR) caused by the accumulation of misfolded proteins in the ER. During S phase and in association with ufd-1, cdc-48.1 and/or cdc-48.2 and ubxn-3, ensures the degradation of DNA licensing factor cdt-1 after the initiation of DNA replication and thus the disassembly of the DNA replication CGM helicase comp [...] | 0.991 |
| cdc-48.1 | ubq-2 | C06A1.1.1 | ZK1010.1.1 | 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 [...] | 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 [...] | 0.576 |
| cdc-48.1 | ufd-1 | C06A1.1.1 | F19B6.2a.2 | 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 [...] | Ubiquitin fusion degradation protein 1 homolog; Functions at a post-ubiquitination step in the ubiquitin fusion degradation (UFD) pathway (By similarity). In association with npl-4.1 and/or npl-4.2 and ATPase cdc-48.1 and/or cdc-48.2, involved in the cytoplasmic elimination of misfolded proteins exported from the ER. This pathway, known as ERAD, prevents the activation of the unfolded protein response (UPR) caused by the accumulation of misfolded proteins in the ER. During S phase and in association with npl-4.1 and/or npl-4.2, cdc-48.1 and/or cdc-48.2 and ubxn-3, ensures the degradati [...] | 0.996 |
| cdc-48.1 | ufd-2 | C06A1.1.1 | T05H10.5b.1 | 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 [...] | Ubiquitin conjugation factor E4 ufd-2; Acts as an E4 ubiquitin ligase mediating the assembly of polyubiquitin chains on substrates ubiquitinated by another E3 ubiquitin ligase. The elongation of preexisting ubiquitin chains preferentially targets ubiquitin 'Lys-29' and 'Lys-48' residues. Also functions as an E3 ligase in conjunction with specific E1 and E2 ligases. Probably by regulating protein ubiquitination at DNA damage repair sites, coordinates DNA double- strand-break repair and apoptosis in the germline. Required for germline apoptosis in response to DNA damage downstream of cep [...] | 0.981 |
| cdc-48.1 | ufd-3 | C06A1.1.1 | C05C10.6b.1 | 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 [...] | Ubiquitin fusion degradation protein 3 homolog; Plays a role in protein ubiquitination, sorting and degradation through its association with cdc-48.1 and/or cdc-48.2. | 0.917 |
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