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 | 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-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 | ufd-1 | F48E8.4.1 | F19B6.2a.2 | PRKCSH domain-containing protein. | 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 [...] | 0.433 |
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 | hrdl-1 | R151.6.1 | F26E4.11.1 | 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-like protein 1; Proposed to have a role in neuroprotection. | 0.971 |
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 | 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 | 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 |
Y105E8A.2 | F48E8.4 | Y105E8A.2.1 | F48E8.4.1 | Uncharacterized protein. | PRKCSH domain-containing protein. | 0.800 |