node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
atf-6 | cnx-1 | F45E6.2.1 | ZK632.6a.1 | BZIP domain-containing protein. | Calnexin; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity). Required for embryogenesis and larval development under heat and ER stress conditions. May be important for germ cell development. Involved in neuronal necrotic cell death. | 0.822 |
atf-6 | dnj-29 | F45E6.2.1 | Y63D3A.6b.2 | BZIP domain-containing protein. | J domain-containing protein. | 0.592 |
atf-6 | ero-1 | F45E6.2.1 | Y105E8B.8c.2 | BZIP domain-containing protein. | Endoplasmic reticulum oxidoreductin-1; Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes pdi-1, the enzyme catalyzing protein disulfide formation, in order to allow pdi-1 to sustain additional rounds of disulfide formation. Following pdi reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell (By similarity). | 0.722 |
atf-6 | hsp-3 | F45E6.2.1 | C15H9.6a.5 | BZIP domain-containing protein. | Heat shock 70 kDa protein C; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. | 0.755 |
atf-6 | hsp-4 | F45E6.2.1 | F43E2.8a.2 | BZIP domain-containing protein. | Endoplasmic reticulum chaperone BiP homolog; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Required for ER dynamics during the first embryonic cell divisions. Specifically, controls ER transition into sheet-like structures at the onset of mitosis, possibly by regulating homotypic membrane fusion. Belongs to the heat shock protein 70 family. | 0.837 |
atf-6 | ire-1 | F45E6.2.1 | C41C4.4a.1 | BZIP domain-containing protein. | Serine/threonine-protein kinase/endoribonuclease ire-1; Senses unfolded proteins in the lumen of the endoplasmic reticulum via its N-terminal domain which leads to enzyme auto- activation. The active endoribonuclease domain splices xbp-1 precursor mRNA to produce the mature form which then induces transcription of UPR target genes. Unfolded protein response (UPR) transcriptional activation by ire-1, as well as translational attenuation by pek-1 in a complementary pathway, maintains ER homeostasis. Regulates the transcriptional up-regulation of nucleoside-diphosphatase apy-1 upon ER str [...] | 0.694 |
atf-6 | sel-11 | F45E6.2.1 | F55A11.3.1 | BZIP 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 [...] | 0.641 |
atf-6 | xbp-1 | F45E6.2.1 | R74.3a.1 | BZIP domain-containing protein. | BZIP domain-containing protein. | 0.995 |
cnx-1 | atf-6 | ZK632.6a.1 | F45E6.2.1 | Calnexin; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity). Required for embryogenesis and larval development under heat and ER stress conditions. May be important for germ cell development. Involved in neuronal necrotic cell death. | BZIP domain-containing protein. | 0.822 |
cnx-1 | dnj-29 | ZK632.6a.1 | Y63D3A.6b.2 | Calnexin; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity). Required for embryogenesis and larval development under heat and ER stress conditions. May be important for germ cell development. Involved in neuronal necrotic cell death. | J domain-containing protein. | 0.775 |
cnx-1 | ero-1 | ZK632.6a.1 | Y105E8B.8c.2 | Calnexin; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity). Required for embryogenesis and larval development under heat and ER stress conditions. May be important for germ cell development. Involved in neuronal necrotic cell death. | Endoplasmic reticulum oxidoreductin-1; Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes pdi-1, the enzyme catalyzing protein disulfide formation, in order to allow pdi-1 to sustain additional rounds of disulfide formation. Following pdi reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell (By similarity). | 0.778 |
cnx-1 | hrdl-1 | ZK632.6a.1 | F26E4.11.1 | Calnexin; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity). Required for embryogenesis and larval development under heat and ER stress conditions. May be important for germ cell development. Involved in neuronal necrotic cell death. | E3 ubiquitin-protein ligase hrd-like protein 1; Proposed to have a role in neuroprotection. | 0.406 |
cnx-1 | hsp-3 | ZK632.6a.1 | C15H9.6a.5 | Calnexin; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity). Required for embryogenesis and larval development under heat and ER stress conditions. May be important for germ cell development. Involved in neuronal necrotic cell death. | Heat shock 70 kDa protein C; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. | 0.929 |
cnx-1 | hsp-4 | ZK632.6a.1 | F43E2.8a.2 | Calnexin; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity). Required for embryogenesis and larval development under heat and ER stress conditions. May be important for germ cell development. Involved in neuronal necrotic cell death. | Endoplasmic reticulum chaperone BiP homolog; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Required for ER dynamics during the first embryonic cell divisions. Specifically, controls ER transition into sheet-like structures at the onset of mitosis, possibly by regulating homotypic membrane fusion. Belongs to the heat shock protein 70 family. | 0.924 |
cnx-1 | ire-1 | ZK632.6a.1 | C41C4.4a.1 | Calnexin; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity). Required for embryogenesis and larval development under heat and ER stress conditions. May be important for germ cell development. Involved in neuronal necrotic cell death. | Serine/threonine-protein kinase/endoribonuclease ire-1; Senses unfolded proteins in the lumen of the endoplasmic reticulum via its N-terminal domain which leads to enzyme auto- activation. The active endoribonuclease domain splices xbp-1 precursor mRNA to produce the mature form which then induces transcription of UPR target genes. Unfolded protein response (UPR) transcriptional activation by ire-1, as well as translational attenuation by pek-1 in a complementary pathway, maintains ER homeostasis. Regulates the transcriptional up-regulation of nucleoside-diphosphatase apy-1 upon ER str [...] | 0.580 |
cnx-1 | sel-11 | ZK632.6a.1 | F55A11.3.1 | Calnexin; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity). Required for embryogenesis and larval development under heat and ER stress conditions. May be important for germ cell development. Involved in neuronal necrotic cell death. | 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 [...] | 0.506 |
cnx-1 | xbp-1 | ZK632.6a.1 | R74.3a.1 | Calnexin; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity). Required for embryogenesis and larval development under heat and ER stress conditions. May be important for germ cell development. Involved in neuronal necrotic cell death. | BZIP domain-containing protein. | 0.918 |
dnj-29 | atf-6 | Y63D3A.6b.2 | F45E6.2.1 | J domain-containing protein. | BZIP domain-containing protein. | 0.592 |
dnj-29 | cnx-1 | Y63D3A.6b.2 | ZK632.6a.1 | J domain-containing protein. | Calnexin; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity). Required for embryogenesis and larval development under heat and ER stress conditions. May be important for germ cell development. Involved in neuronal necrotic cell death. | 0.775 |
dnj-29 | ero-1 | Y63D3A.6b.2 | Y105E8B.8c.2 | J domain-containing protein. | Endoplasmic reticulum oxidoreductin-1; Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes pdi-1, the enzyme catalyzing protein disulfide formation, in order to allow pdi-1 to sustain additional rounds of disulfide formation. Following pdi reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell (By similarity). | 0.754 |