node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
C18B12.6 | C26D10.6 | C18B12.6.1 | C26D10.6a.1 | Uncharacterized protein. | Uncharacterized protein. | 0.855 |
C18B12.6 | R151.6 | C18B12.6.1 | R151.6.1 | Uncharacterized 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. | 0.919 |
C26D10.6 | C18B12.6 | C26D10.6a.1 | C18B12.6.1 | Uncharacterized protein. | Uncharacterized protein. | 0.855 |
C26D10.6 | F48E8.4 | C26D10.6a.1 | F48E8.4.1 | Uncharacterized protein. | PRKCSH domain-containing protein. | 0.810 |
C26D10.6 | R151.6 | C26D10.6a.1 | R151.6.1 | Uncharacterized 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. | 0.922 |
C26D10.6 | Y105E8A.2 | C26D10.6a.1 | Y105E8A.2.1 | Uncharacterized protein. | Uncharacterized protein. | 0.810 |
C26D10.6 | cdc-48.1 | C26D10.6a.1 | C06A1.1.1 | Uncharacterized 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 [...] | 0.603 |
C26D10.6 | cdc-48.2 | C26D10.6a.1 | C41C4.8.2 | Uncharacterized 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 [...] | 0.603 |
C26D10.6 | chs-2 | C26D10.6a.1 | F48A11.1c.1 | Uncharacterized protein. | Chitin synthase chs-2; May be involved in chitin synthesis in the pharynx during larval development; Belongs to the chitin synthase family. Class IV subfamily. | 0.662 |
C26D10.6 | cup-2 | C26D10.6a.1 | F25D7.1.1 | Uncharacterized 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. | 0.921 |
C26D10.6 | hrdl-1 | C26D10.6a.1 | F26E4.11.1 | Uncharacterized protein. | E3 ubiquitin-protein ligase hrd-like protein 1; Proposed to have a role in neuroprotection. | 0.807 |
C26D10.6 | sel-11 | C26D10.6a.1 | F55A11.3.1 | Uncharacterized 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 [...] | 0.807 |
F48E8.4 | C26D10.6 | F48E8.4.1 | C26D10.6a.1 | PRKCSH domain-containing protein. | Uncharacterized protein. | 0.810 |
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 | hrdl-1 | F48E8.4.1 | F26E4.11.1 | PRKCSH domain-containing protein. | E3 ubiquitin-protein ligase hrd-like protein 1; Proposed to have a role in neuroprotection. | 0.809 |
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 |