node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
C44H4.6 | R03D7.5 | C44H4.6.1 | R03D7.5a.1 | Protein kinase domain-containing protein; Belongs to the protein kinase superfamily. | Putative serine/threonine-protein kinase R03D7.5; Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. | 0.909 |
C44H4.6 | gsk-3 | C44H4.6.1 | Y18D10A.5.1 | Protein kinase domain-containing protein; Belongs to the protein kinase superfamily. | Glycogen synthase kinase-3; Phosphorylates oma-1, a regulator of the oocyte-to-embryo transition, enabling its degradation. Phosphorylates skn-1, preventing it from accumulating in nuclei and thus inhibiting phase II gene expression in the oxidative stress defense. Involved in mesendoderm specification and mitotic spindle orientation in EMS blastomeres. Thought to be a branch point in these processes as proteins downstream are not required. Negatively regulates Wnt signaling in vulval precursor cells and acts as a Wnt-independent repressor of med-1 and med-2 in the C lineage inhibiting [...] | 0.904 |
R03D7.5 | C44H4.6 | R03D7.5a.1 | C44H4.6.1 | Putative serine/threonine-protein kinase R03D7.5; Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. | Protein kinase domain-containing protein; Belongs to the protein kinase superfamily. | 0.909 |
R03D7.5 | gsk-3 | R03D7.5a.1 | Y18D10A.5.1 | Putative serine/threonine-protein kinase R03D7.5; Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. | Glycogen synthase kinase-3; Phosphorylates oma-1, a regulator of the oocyte-to-embryo transition, enabling its degradation. Phosphorylates skn-1, preventing it from accumulating in nuclei and thus inhibiting phase II gene expression in the oxidative stress defense. Involved in mesendoderm specification and mitotic spindle orientation in EMS blastomeres. Thought to be a branch point in these processes as proteins downstream are not required. Negatively regulates Wnt signaling in vulval precursor cells and acts as a Wnt-independent repressor of med-1 and med-2 in the C lineage inhibiting [...] | 0.900 |
acy-1 | acy-2 | F17C8.1.1 | C10F3.3.1 | Adenylyl CYclase. | Adenylyl CYclase; Belongs to the adenylyl cyclase class-4/guanylyl cyclase family. | 0.484 |
acy-1 | acy-3 | F17C8.1.1 | C44F1.5.2 | Adenylyl CYclase. | Adenylyl CYclase. | 0.463 |
acy-2 | acy-1 | C10F3.3.1 | F17C8.1.1 | Adenylyl CYclase; Belongs to the adenylyl cyclase class-4/guanylyl cyclase family. | Adenylyl CYclase. | 0.484 |
acy-3 | acy-1 | C44F1.5.2 | F17C8.1.1 | Adenylyl CYclase. | Adenylyl CYclase. | 0.463 |
crt-1 | gpd-1 | Y38A10A.5.2 | T09F3.3.2 | Calreticulin; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle (By similarity). This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). Probably by controlling the folding of extracellular matrix protein unc-52/Perlecan, may play a role in the formation of fibrous organelles, a hemidesmosome-like structure attaching muscles to the epidermis. Protects dopaminergic neurons against oxidative stress-induced neurodegen [...] | Glyceraldehyde-3-phosphate dehydrogenase 1. | 0.498 |
crt-1 | gpd-2 | Y38A10A.5.2 | K10B3.8.2 | Calreticulin; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle (By similarity). This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). Probably by controlling the folding of extracellular matrix protein unc-52/Perlecan, may play a role in the formation of fibrous organelles, a hemidesmosome-like structure attaching muscles to the epidermis. Protects dopaminergic neurons against oxidative stress-induced neurodegen [...] | Glyceraldehyde-3-phosphate dehydrogenase 2. | 0.507 |
crt-1 | gpd-3 | Y38A10A.5.2 | K10B3.7.2 | Calreticulin; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle (By similarity). This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). Probably by controlling the folding of extracellular matrix protein unc-52/Perlecan, may play a role in the formation of fibrous organelles, a hemidesmosome-like structure attaching muscles to the epidermis. Protects dopaminergic neurons against oxidative stress-induced neurodegen [...] | Glyceraldehyde-3-phosphate dehydrogenase 3. | 0.485 |
crt-1 | gpd-4 | Y38A10A.5.2 | F33H1.2.2 | Calreticulin; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle (By similarity). This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). Probably by controlling the folding of extracellular matrix protein unc-52/Perlecan, may play a role in the formation of fibrous organelles, a hemidesmosome-like structure attaching muscles to the epidermis. Protects dopaminergic neurons against oxidative stress-induced neurodegen [...] | Glyceraldehyde-3-phosphate dehydrogenase 4. | 0.494 |
gpd-1 | crt-1 | T09F3.3.2 | Y38A10A.5.2 | Glyceraldehyde-3-phosphate dehydrogenase 1. | Calreticulin; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle (By similarity). This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). Probably by controlling the folding of extracellular matrix protein unc-52/Perlecan, may play a role in the formation of fibrous organelles, a hemidesmosome-like structure attaching muscles to the epidermis. Protects dopaminergic neurons against oxidative stress-induced neurodegen [...] | 0.498 |
gpd-1 | gpd-2 | T09F3.3.2 | K10B3.8.2 | Glyceraldehyde-3-phosphate dehydrogenase 1. | Glyceraldehyde-3-phosphate dehydrogenase 2. | 0.409 |
gpd-1 | gpd-3 | T09F3.3.2 | K10B3.7.2 | Glyceraldehyde-3-phosphate dehydrogenase 1. | Glyceraldehyde-3-phosphate dehydrogenase 3. | 0.618 |
gpd-1 | gpd-4 | T09F3.3.2 | F33H1.2.2 | Glyceraldehyde-3-phosphate dehydrogenase 1. | Glyceraldehyde-3-phosphate dehydrogenase 4. | 0.824 |
gpd-1 | gsk-3 | T09F3.3.2 | Y18D10A.5.1 | Glyceraldehyde-3-phosphate dehydrogenase 1. | Glycogen synthase kinase-3; Phosphorylates oma-1, a regulator of the oocyte-to-embryo transition, enabling its degradation. Phosphorylates skn-1, preventing it from accumulating in nuclei and thus inhibiting phase II gene expression in the oxidative stress defense. Involved in mesendoderm specification and mitotic spindle orientation in EMS blastomeres. Thought to be a branch point in these processes as proteins downstream are not required. Negatively regulates Wnt signaling in vulval precursor cells and acts as a Wnt-independent repressor of med-1 and med-2 in the C lineage inhibiting [...] | 0.435 |
gpd-2 | crt-1 | K10B3.8.2 | Y38A10A.5.2 | Glyceraldehyde-3-phosphate dehydrogenase 2. | Calreticulin; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle (By similarity). This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). Probably by controlling the folding of extracellular matrix protein unc-52/Perlecan, may play a role in the formation of fibrous organelles, a hemidesmosome-like structure attaching muscles to the epidermis. Protects dopaminergic neurons against oxidative stress-induced neurodegen [...] | 0.507 |
gpd-2 | gpd-1 | K10B3.8.2 | T09F3.3.2 | Glyceraldehyde-3-phosphate dehydrogenase 2. | Glyceraldehyde-3-phosphate dehydrogenase 1. | 0.409 |
gpd-2 | gpd-3 | K10B3.8.2 | K10B3.7.2 | Glyceraldehyde-3-phosphate dehydrogenase 2. | Glyceraldehyde-3-phosphate dehydrogenase 3. | 0.966 |