node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Y73B6BL.12 | png-1 | Y73B6BL.12.1 | F56G4.5.1 | Thioredoxin; Belongs to the thioredoxin family. | Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase; Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta- aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native protein [...] | 0.767 |
Y73B6BL.12 | rps-30 | Y73B6BL.12.1 | C26F1.4.3 | Thioredoxin; Belongs to the thioredoxin family. | 40S ribosomal protein S30; Belongs to the eukaryotic ribosomal protein eS30 family. | 0.498 |
cdc-48.2 | cup-2 | C41C4.8.2 | F25D7.1.1 | 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 [...] | 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. | 0.960 |
cdc-48.2 | hrdl-1 | C41C4.8.2 | F26E4.11.1 | 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 [...] | E3 ubiquitin-protein ligase hrd-like protein 1; Proposed to have a role in neuroprotection. | 0.883 |
cdc-48.2 | png-1 | C41C4.8.2 | F56G4.5.1 | 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 [...] | Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase; Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta- aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native protein [...] | 0.862 |
cdc-48.2 | rad-23 | C41C4.8.2 | ZK20.3.2 | 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 [...] | Uncharacterized protein. | 0.818 |
cdc-48.2 | rps-30 | C41C4.8.2 | C26F1.4.3 | 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 [...] | 40S ribosomal protein S30; Belongs to the eukaryotic ribosomal protein eS30 family. | 0.437 |
cdc-48.2 | rpt-2 | C41C4.8.2 | F29G9.5.1 | 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 [...] | Probable 26S proteasome regulatory subunit 4; The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity). May play a role in the degradation of microtubule severing protein mei-1. | 0.787 |
cdc-48.2 | ubql-1 | C41C4.8.2 | F15C11.2a.1 | 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 [...] | Ubiquilin; May play a role in the ER-associated protein degradation pathway (ERAD) possibly via its interaction with ER-localized proteins ubxn-4 and cdc-48.1 and/or cdc48.2, providing a link between the polyubiquitinated ERAD substrates and the proteasome. Also plays an important role in the regulation of other protein degradation mechanisms and pathways including ubiquitin-proteasome system (UPS) and autophagy (By similarity). Mediates the proteasomal targeting of misfolded or accumulated proteins for degradation by binding (via UBA domain) to their polyubiquitin chains and by intera [...] | 0.743 |
cdc-48.2 | ubxn-1 | C41C4.8.2 | F23C8.4.2 | 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 [...] | 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. | 0.996 |
cdc-48.2 | ufd-2 | C41C4.8.2 | T05H10.5b.1 | 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 [...] | 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 [...] | 0.920 |
cup-2 | cdc-48.2 | F25D7.1.1 | C41C4.8.2 | 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. | 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 [...] | 0.960 |
cup-2 | hrdl-1 | F25D7.1.1 | F26E4.11.1 | 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. | E3 ubiquitin-protein ligase hrd-like protein 1; Proposed to have a role in neuroprotection. | 0.991 |
cup-2 | png-1 | F25D7.1.1 | F56G4.5.1 | 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. | Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase; Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta- aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native protein [...] | 0.877 |
cup-2 | rad-23 | F25D7.1.1 | ZK20.3.2 | 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. | Uncharacterized protein. | 0.883 |
cup-2 | rpt-2 | F25D7.1.1 | F29G9.5.1 | 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. | Probable 26S proteasome regulatory subunit 4; The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity). May play a role in the degradation of microtubule severing protein mei-1. | 0.809 |
cup-2 | ubxn-1 | F25D7.1.1 | F23C8.4.2 | 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. | 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. | 0.936 |
cup-2 | ufd-2 | F25D7.1.1 | T05H10.5b.1 | 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. | 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 [...] | 0.567 |
hrdl-1 | cdc-48.2 | F26E4.11.1 | C41C4.8.2 | E3 ubiquitin-protein ligase hrd-like protein 1; Proposed to have a role in neuroprotection. | 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 [...] | 0.883 |
hrdl-1 | cup-2 | F26E4.11.1 | F25D7.1.1 | E3 ubiquitin-protein ligase hrd-like protein 1; Proposed to have a role in neuroprotection. | 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 |