node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
T04C12.8 | dcap-1 | T04C12.8.2 | Y55F3AM.12.1 | Uncharacterized protein. | mRNA_decap_C domain-containing protein. | 0.918 |
T04C12.8 | dcap-2 | T04C12.8.2 | F52G2.1b.1 | Uncharacterized protein. | mRNA-decapping enzyme 2; RNA-decapping enzyme although it does not bind cap. May contribute to gene regulation in multiple RNA pathways including monomethylguanosine- and trimethylguanosine-capped RNAs. Belongs to the Nudix hydrolase family. DCP2 subfamily. | 0.923 |
T04C12.8 | ttll-5 | T04C12.8.2 | C55A6.2b.1 | Uncharacterized protein. | Tubulin polyglutamylase ttll-5; Polyglutamylase which preferentially modifies alpha-tubulin (By similarity). Involved in the side-chain initiation step of the polyglutamylation reaction rather than in the elongation step (By similarity). Together with ttll-4 and ttll-11, required for male mating. Probably by regulating microtubule stability via the glutamylation of tubulin, negatively regulates axon regrowth after injury in PLM neurons. | 0.756 |
Y18D10A.3 | dcap-1 | Y18D10A.3.1 | Y55F3AM.12.1 | NAD(P)H-hydrate epimerase; Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX; Belongs to the NnrE/AIBP family. | mRNA_decap_C domain-containing protein. | 0.918 |
Y18D10A.3 | dcap-2 | Y18D10A.3.1 | F52G2.1b.1 | NAD(P)H-hydrate epimerase; Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX; Belongs to the NnrE/AIBP family. | mRNA-decapping enzyme 2; RNA-decapping enzyme although it does not bind cap. May contribute to gene regulation in multiple RNA pathways including monomethylguanosine- and trimethylguanosine-capped RNAs. Belongs to the Nudix hydrolase family. DCP2 subfamily. | 0.923 |
Y18D10A.3 | ttll-5 | Y18D10A.3.1 | C55A6.2b.1 | NAD(P)H-hydrate epimerase; Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX; Belongs to the NnrE/AIBP family. | Tubulin polyglutamylase ttll-5; Polyglutamylase which preferentially modifies alpha-tubulin (By similarity). Involved in the side-chain initiation step of the polyglutamylation reaction rather than in the elongation step (By similarity). Together with ttll-4 and ttll-11, required for male mating. Probably by regulating microtubule stability via the glutamylation of tubulin, negatively regulates axon regrowth after injury in PLM neurons. | 0.756 |
ccpp-1 | ccpp-6 | F56H1.5.1 | EEED8.6.1 | Cytosolic carboxypeptidase 1; Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation of proteins such as tubulins (Probable). Via the deglutamylation of tubulin, regulates the localization and velocity of kinesin motors and the structural integrity of microtubules in sensory cilia. In male CEM sensory neurons, regulates the cilia release of bioactive extracellular vesicles. Also regulates microtubule dynamics in uterine muscle cells. | Cytosolic carboxypeptidase 6; Metallocarboxypeptidase that catalyzes the removing of polyglutamate side chains that are present on the gamma-carboxyl group of glutamate residues of tubulin in sensory cilia. Probably via the deglutamylation of tubulin, promotes microtubule stability required for axon regrowth after injury. Also regulates microtubule dynamics in uterine muscle cells. Belongs to the peptidase M14 family. | 0.452 |
ccpp-1 | mec-17 | F56H1.5.1 | F57H12.7a.1 | Cytosolic carboxypeptidase 1; Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation of proteins such as tubulins (Probable). Via the deglutamylation of tubulin, regulates the localization and velocity of kinesin motors and the structural integrity of microtubules in sensory cilia. In male CEM sensory neurons, regulates the cilia release of bioactive extracellular vesicles. Also regulates microtubule dynamics in uterine muscle cells. | Alpha-tubulin N-acetyltransferase 1; Specifically acetylates 'Lys-40' in alpha-tubulin/mec-12 on the lumenal side of microtubules. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Acetylates alpha-tubulin with a slow enzymatic rate, due to a catalytic site that is not optimized for acetyl transfer. Enters the microtubule through each end and diffuses quickly throughout the lumen of microtubules. Acetylates only long/old microtubules because of its slow acetylation rate since it does not have time to act [...] | 0.581 |
ccpp-1 | spas-1 | F56H1.5.1 | C24B5.2c.1 | Cytosolic carboxypeptidase 1; Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation of proteins such as tubulins (Probable). Via the deglutamylation of tubulin, regulates the localization and velocity of kinesin motors and the structural integrity of microtubules in sensory cilia. In male CEM sensory neurons, regulates the cilia release of bioactive extracellular vesicles. Also regulates microtubule dynamics in uterine muscle cells. | Probable spastin homolog spas-1; Severs microtubules, probably in an ATP-dependent fashion. Belongs to the AAA ATPase family. Spastin subfamily. | 0.838 |
ccpp-1 | ttll-11 | F56H1.5.1 | H23L24.3b.1 | Cytosolic carboxypeptidase 1; Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation of proteins such as tubulins (Probable). Via the deglutamylation of tubulin, regulates the localization and velocity of kinesin motors and the structural integrity of microtubules in sensory cilia. In male CEM sensory neurons, regulates the cilia release of bioactive extracellular vesicles. Also regulates microtubule dynamics in uterine muscle cells. | Tubulin polyglutamylase ttll-11; Polyglutamylase which preferentially modifies tubulin. Involved in the side-chain initiation step of the polyglutamylation reaction. By controlling tubulin glutamylation, regulates ciliary specialization and motor-based transport. Promotes the formation of A and B tubule singlets by splaying microtubule doublets in cilia. Together with ttll-4 and 5, required for male mating. [Isoform b]: Specifically promotes tubulin glutamylation in male ciliated CEM, HOB and RnB neurons that release bioactive extracellular vesicles. Regulates the localization of TRP c [...] | 0.942 |
ccpp-1 | ttll-12 | F56H1.5.1 | D2013.9.1 | Cytosolic carboxypeptidase 1; Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation of proteins such as tubulins (Probable). Via the deglutamylation of tubulin, regulates the localization and velocity of kinesin motors and the structural integrity of microtubules in sensory cilia. In male CEM sensory neurons, regulates the cilia release of bioactive extracellular vesicles. Also regulates microtubule dynamics in uterine muscle cells. | Tubulin--tyrosine ligase-like protein 12; Regulates microtubule dynamics in uterine muscle cells. Belongs to the tubulin--tyrosine ligase family. | 0.860 |
ccpp-1 | ttll-5 | F56H1.5.1 | C55A6.2b.1 | Cytosolic carboxypeptidase 1; Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation of proteins such as tubulins (Probable). Via the deglutamylation of tubulin, regulates the localization and velocity of kinesin motors and the structural integrity of microtubules in sensory cilia. In male CEM sensory neurons, regulates the cilia release of bioactive extracellular vesicles. Also regulates microtubule dynamics in uterine muscle cells. | Tubulin polyglutamylase ttll-5; Polyglutamylase which preferentially modifies alpha-tubulin (By similarity). Involved in the side-chain initiation step of the polyglutamylation reaction rather than in the elongation step (By similarity). Together with ttll-4 and ttll-11, required for male mating. Probably by regulating microtubule stability via the glutamylation of tubulin, negatively regulates axon regrowth after injury in PLM neurons. | 0.945 |
ccpp-6 | ccpp-1 | EEED8.6.1 | F56H1.5.1 | Cytosolic carboxypeptidase 6; Metallocarboxypeptidase that catalyzes the removing of polyglutamate side chains that are present on the gamma-carboxyl group of glutamate residues of tubulin in sensory cilia. Probably via the deglutamylation of tubulin, promotes microtubule stability required for axon regrowth after injury. Also regulates microtubule dynamics in uterine muscle cells. Belongs to the peptidase M14 family. | Cytosolic carboxypeptidase 1; Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation of proteins such as tubulins (Probable). Via the deglutamylation of tubulin, regulates the localization and velocity of kinesin motors and the structural integrity of microtubules in sensory cilia. In male CEM sensory neurons, regulates the cilia release of bioactive extracellular vesicles. Also regulates microtubule dynamics in uterine muscle cells. | 0.452 |
ccpp-6 | mec-17 | EEED8.6.1 | F57H12.7a.1 | Cytosolic carboxypeptidase 6; Metallocarboxypeptidase that catalyzes the removing of polyglutamate side chains that are present on the gamma-carboxyl group of glutamate residues of tubulin in sensory cilia. Probably via the deglutamylation of tubulin, promotes microtubule stability required for axon regrowth after injury. Also regulates microtubule dynamics in uterine muscle cells. Belongs to the peptidase M14 family. | Alpha-tubulin N-acetyltransferase 1; Specifically acetylates 'Lys-40' in alpha-tubulin/mec-12 on the lumenal side of microtubules. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Acetylates alpha-tubulin with a slow enzymatic rate, due to a catalytic site that is not optimized for acetyl transfer. Enters the microtubule through each end and diffuses quickly throughout the lumen of microtubules. Acetylates only long/old microtubules because of its slow acetylation rate since it does not have time to act [...] | 0.612 |
ccpp-6 | spas-1 | EEED8.6.1 | C24B5.2c.1 | Cytosolic carboxypeptidase 6; Metallocarboxypeptidase that catalyzes the removing of polyglutamate side chains that are present on the gamma-carboxyl group of glutamate residues of tubulin in sensory cilia. Probably via the deglutamylation of tubulin, promotes microtubule stability required for axon regrowth after injury. Also regulates microtubule dynamics in uterine muscle cells. Belongs to the peptidase M14 family. | Probable spastin homolog spas-1; Severs microtubules, probably in an ATP-dependent fashion. Belongs to the AAA ATPase family. Spastin subfamily. | 0.599 |
ccpp-6 | ttll-11 | EEED8.6.1 | H23L24.3b.1 | Cytosolic carboxypeptidase 6; Metallocarboxypeptidase that catalyzes the removing of polyglutamate side chains that are present on the gamma-carboxyl group of glutamate residues of tubulin in sensory cilia. Probably via the deglutamylation of tubulin, promotes microtubule stability required for axon regrowth after injury. Also regulates microtubule dynamics in uterine muscle cells. Belongs to the peptidase M14 family. | Tubulin polyglutamylase ttll-11; Polyglutamylase which preferentially modifies tubulin. Involved in the side-chain initiation step of the polyglutamylation reaction. By controlling tubulin glutamylation, regulates ciliary specialization and motor-based transport. Promotes the formation of A and B tubule singlets by splaying microtubule doublets in cilia. Together with ttll-4 and 5, required for male mating. [Isoform b]: Specifically promotes tubulin glutamylation in male ciliated CEM, HOB and RnB neurons that release bioactive extracellular vesicles. Regulates the localization of TRP c [...] | 0.586 |
ccpp-6 | ttll-12 | EEED8.6.1 | D2013.9.1 | Cytosolic carboxypeptidase 6; Metallocarboxypeptidase that catalyzes the removing of polyglutamate side chains that are present on the gamma-carboxyl group of glutamate residues of tubulin in sensory cilia. Probably via the deglutamylation of tubulin, promotes microtubule stability required for axon regrowth after injury. Also regulates microtubule dynamics in uterine muscle cells. Belongs to the peptidase M14 family. | Tubulin--tyrosine ligase-like protein 12; Regulates microtubule dynamics in uterine muscle cells. Belongs to the tubulin--tyrosine ligase family. | 0.823 |
ccpp-6 | ttll-5 | EEED8.6.1 | C55A6.2b.1 | Cytosolic carboxypeptidase 6; Metallocarboxypeptidase that catalyzes the removing of polyglutamate side chains that are present on the gamma-carboxyl group of glutamate residues of tubulin in sensory cilia. Probably via the deglutamylation of tubulin, promotes microtubule stability required for axon regrowth after injury. Also regulates microtubule dynamics in uterine muscle cells. Belongs to the peptidase M14 family. | Tubulin polyglutamylase ttll-5; Polyglutamylase which preferentially modifies alpha-tubulin (By similarity). Involved in the side-chain initiation step of the polyglutamylation reaction rather than in the elongation step (By similarity). Together with ttll-4 and ttll-11, required for male mating. Probably by regulating microtubule stability via the glutamylation of tubulin, negatively regulates axon regrowth after injury in PLM neurons. | 0.882 |
dcap-1 | T04C12.8 | Y55F3AM.12.1 | T04C12.8.2 | mRNA_decap_C domain-containing protein. | Uncharacterized protein. | 0.918 |
dcap-1 | Y18D10A.3 | Y55F3AM.12.1 | Y18D10A.3.1 | mRNA_decap_C domain-containing protein. | NAD(P)H-hydrate epimerase; Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX; Belongs to the NnrE/AIBP family. | 0.918 |