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 | 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 | ubxn-1 | R151.6.1 | F23C8.4.2 | 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. | UBX domain-containing protein 1; Ubiquitin-binding protein which acts as an adapter for ATPase cdc-48.1 and/or cdc-48.2, conferring substrate specificity. Together with ubxn-2 and ubxn-3, plays a role in hermaphrodite spermatogenesis probably by promoting the degradation of sex determination terminal factor tra-1. | 0.827 |
| R151.6 | ubxn-2 | R151.6.1 | Y94H6A.9a.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. | UBX domain-containing protein 2; Ubiquitin-binding protein which acts as an adapter for ATPase cdc-48.1 and/or cdc-48.2, conferring substrate specificity. Together with ubxn-2 and ubxn-3, plays a role in hermaphrodite spermatogenesis probably by promoting the degradation of sex determination terminal factor tra-1. Probably in association with ATPase cdc-48.1 or/and cdc-48.2, regulates the centrosomal levels of kinase air-1 levels during mitotic progression by promoting air-1 removal from centrosomes in prophase. Also, regulates spindle orientation in the one-cell embryo by controlling [...] | 0.801 |
| R151.6 | ubxn-4 | R151.6.1 | ZK353.8.2 | 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. | UBX domain-containing protein 4; Probably acts as an adapter for ATPase cdc-48.1 and/or cdc- 48.2, conferring substrate specificity. May play a role in the ER- associated protein degradation pathway (ERAD) possibly acting as a platform to recruit both ubql-1 and cdc-48.1 and/or cdc-48.2 to the ER during ERAD. | 0.558 |
| R151.6 | ubxn-6 | R151.6.1 | H06H21.6.1 | 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. | UBX domain-containing protein 6; Probably acts as an adapter for ATPase cdc-48.1 and/or cdc- 48.2, conferring substrate specificity. Involved in the lysosomal clearance of cellular material in diet restricted conditions. | 0.741 |
| 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 |
| atx-3 | cdc-48.1 | F28F8.6.1 | C06A1.1.1 | Ataxin-3 homolog; Acts as chain editing deubiquitinating enzyme that binds and cleaves 'Lys-48'-linked polyubiquitin chains, with a preference for chains containing four or more ubiquitin molecules thereby modulating protein degradation by the ubiquitin-proteasome pathway. Probably by regulating the IGF-1-insulin-like pathway, regulates lifespan. Regulates germline DNA double-strand-break repair and apoptosis in response to DNA damage by recruiting E4 ubiquitin- protein ligase ufd-2 to DNA repair foci. Interacts with key regulators of transcription and represses transcription (By simil [...] | 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 [...] | 0.963 |
| atx-3 | cdc-48.2 | F28F8.6.1 | C41C4.8.2 | Ataxin-3 homolog; Acts as chain editing deubiquitinating enzyme that binds and cleaves 'Lys-48'-linked polyubiquitin chains, with a preference for chains containing four or more ubiquitin molecules thereby modulating protein degradation by the ubiquitin-proteasome pathway. Probably by regulating the IGF-1-insulin-like pathway, regulates lifespan. Regulates germline DNA double-strand-break repair and apoptosis in response to DNA damage by recruiting E4 ubiquitin- protein ligase ufd-2 to DNA repair foci. Interacts with key regulators of transcription and represses transcription (By simil [...] | 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 [...] | 0.971 |
| atx-3 | ubxn-4 | F28F8.6.1 | ZK353.8.2 | Ataxin-3 homolog; Acts as chain editing deubiquitinating enzyme that binds and cleaves 'Lys-48'-linked polyubiquitin chains, with a preference for chains containing four or more ubiquitin molecules thereby modulating protein degradation by the ubiquitin-proteasome pathway. Probably by regulating the IGF-1-insulin-like pathway, regulates lifespan. Regulates germline DNA double-strand-break repair and apoptosis in response to DNA damage by recruiting E4 ubiquitin- protein ligase ufd-2 to DNA repair foci. Interacts with key regulators of transcription and represses transcription (By simil [...] | UBX domain-containing protein 4; Probably acts as an adapter for ATPase cdc-48.1 and/or cdc- 48.2, conferring substrate specificity. May play a role in the ER- associated protein degradation pathway (ERAD) possibly acting as a platform to recruit both ubql-1 and cdc-48.1 and/or cdc-48.2 to the ER during ERAD. | 0.416 |
| atx-3 | ubxn-6 | F28F8.6.1 | H06H21.6.1 | Ataxin-3 homolog; Acts as chain editing deubiquitinating enzyme that binds and cleaves 'Lys-48'-linked polyubiquitin chains, with a preference for chains containing four or more ubiquitin molecules thereby modulating protein degradation by the ubiquitin-proteasome pathway. Probably by regulating the IGF-1-insulin-like pathway, regulates lifespan. Regulates germline DNA double-strand-break repair and apoptosis in response to DNA damage by recruiting E4 ubiquitin- protein ligase ufd-2 to DNA repair foci. Interacts with key regulators of transcription and represses transcription (By simil [...] | UBX domain-containing protein 6; Probably acts as an adapter for ATPase cdc-48.1 and/or cdc- 48.2, conferring substrate specificity. Involved in the lysosomal clearance of cellular material in diet restricted conditions. | 0.568 |
| atx-3 | ufd-1 | F28F8.6.1 | F19B6.2a.2 | Ataxin-3 homolog; Acts as chain editing deubiquitinating enzyme that binds and cleaves 'Lys-48'-linked polyubiquitin chains, with a preference for chains containing four or more ubiquitin molecules thereby modulating protein degradation by the ubiquitin-proteasome pathway. Probably by regulating the IGF-1-insulin-like pathway, regulates lifespan. Regulates germline DNA double-strand-break repair and apoptosis in response to DNA damage by recruiting E4 ubiquitin- protein ligase ufd-2 to DNA repair foci. Interacts with key regulators of transcription and represses transcription (By simil [...] | 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 [...] | 0.786 |
| 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 | atx-3 | C06A1.1.1 | F28F8.6.1 | 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 [...] | Ataxin-3 homolog; Acts as chain editing deubiquitinating enzyme that binds and cleaves 'Lys-48'-linked polyubiquitin chains, with a preference for chains containing four or more ubiquitin molecules thereby modulating protein degradation by the ubiquitin-proteasome pathway. Probably by regulating the IGF-1-insulin-like pathway, regulates lifespan. Regulates germline DNA double-strand-break repair and apoptosis in response to DNA damage by recruiting E4 ubiquitin- protein ligase ufd-2 to DNA repair foci. Interacts with key regulators of transcription and represses transcription (By simil [...] | 0.963 |
| 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 | 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 | ubxn-1 | C06A1.1.1 | F23C8.4.2 | 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 [...] | UBX domain-containing protein 1; Ubiquitin-binding protein which acts as an adapter for ATPase cdc-48.1 and/or cdc-48.2, conferring substrate specificity. Together with ubxn-2 and ubxn-3, plays a role in hermaphrodite spermatogenesis probably by promoting the degradation of sex determination terminal factor tra-1. | 0.997 |
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