node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
1700113H08Rik | Ttll3 | ENSMUSP00000130852 | ENSMUSP00000032414 | RIKEN cDNA 1700113H08 gene. | Tubulin monoglycylase TTLL3; Monoglycylase which modifies alpha- and beta-tubulin, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Involved in the side-chain initiation step of the glycylation reaction by adding a single glycine chain to generate monoglycine side chains. Not involved in elongation step of the polyglycylation reaction. | 0.473 |
Agtpbp1 | Ttll3 | ENSMUSP00000022040 | ENSMUSP00000032414 | Cytosolic carboxypeptidase 1; Metallocarboxypeptidase that mediates deglutamylation of target proteins. Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation in proteins such as tubulins. Also removes gene-encoded polyglutamates from the carboxy-terminus of target proteins such as MYLK. Acts as a long-chain deglutamylase and specifically shortens long polyglutamate chains, while it is not able to remove the branching point glutamate, a process catalyzed by AGBL5/CCP5. Deglutamylation plays a key role in cerebellar Purkinje cell dif [...] | Tubulin monoglycylase TTLL3; Monoglycylase which modifies alpha- and beta-tubulin, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Involved in the side-chain initiation step of the glycylation reaction by adding a single glycine chain to generate monoglycine side chains. Not involved in elongation step of the polyglycylation reaction. | 0.529 |
Agtpbp1 | Ttll5 | ENSMUSP00000022040 | ENSMUSP00000048809 | Cytosolic carboxypeptidase 1; Metallocarboxypeptidase that mediates deglutamylation of target proteins. Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation in proteins such as tubulins. Also removes gene-encoded polyglutamates from the carboxy-terminus of target proteins such as MYLK. Acts as a long-chain deglutamylase and specifically shortens long polyglutamate chains, while it is not able to remove the branching point glutamate, a process catalyzed by AGBL5/CCP5. Deglutamylation plays a key role in cerebellar Purkinje cell dif [...] | Tubulin polyglutamylase TTLL5; Polyglutamylase which preferentially modifies alpha-tubulin. Involved in the side-chain initiation step of the polyglutamylation reaction rather than in the elongation step. Required for CCSAP localization to both spindle and cilia microtubules (By similarity). Increases the effects of NCOA2 in glucocorticoid receptor-mediated repression and induction and in androgen receptor-mediated induction (By similarity). Belongs to the tubulin--tyrosine ligase family. | 0.647 |
Agtpbp1 | Ttll7 | ENSMUSP00000022040 | ENSMUSP00000043753 | Cytosolic carboxypeptidase 1; Metallocarboxypeptidase that mediates deglutamylation of target proteins. Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation in proteins such as tubulins. Also removes gene-encoded polyglutamates from the carboxy-terminus of target proteins such as MYLK. Acts as a long-chain deglutamylase and specifically shortens long polyglutamate chains, while it is not able to remove the branching point glutamate, a process catalyzed by AGBL5/CCP5. Deglutamylation plays a key role in cerebellar Purkinje cell dif [...] | Tubulin polyglutamylase TTLL7; Polyglutamylase which preferentially modifies beta-tubulin. Mediates both ATP- dependent initiation and elongation of polyglutamylation of microtubules. Required for neurite growth; responsible for the strong increase in tubulin polyglutamylation during postnatal neuronal maturation ; Belongs to the tubulin--tyrosine ligase family. | 0.564 |
Atat1 | Ttll3 | ENSMUSP00000056383 | ENSMUSP00000032414 | Alpha-tubulin N-acetyltransferase 1; Specifically acetylates 'Lys-40' in alpha-tubulin 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 on dyn [...] | Tubulin monoglycylase TTLL3; Monoglycylase which modifies alpha- and beta-tubulin, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Involved in the side-chain initiation step of the glycylation reaction by adding a single glycine chain to generate monoglycine side chains. Not involved in elongation step of the polyglycylation reaction. | 0.451 |
Atat1 | Ttll5 | ENSMUSP00000056383 | ENSMUSP00000048809 | Alpha-tubulin N-acetyltransferase 1; Specifically acetylates 'Lys-40' in alpha-tubulin 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 on dyn [...] | Tubulin polyglutamylase TTLL5; Polyglutamylase which preferentially modifies alpha-tubulin. Involved in the side-chain initiation step of the polyglutamylation reaction rather than in the elongation step. Required for CCSAP localization to both spindle and cilia microtubules (By similarity). Increases the effects of NCOA2 in glucocorticoid receptor-mediated repression and induction and in androgen receptor-mediated induction (By similarity). Belongs to the tubulin--tyrosine ligase family. | 0.607 |
Atat1 | Ttll7 | ENSMUSP00000056383 | ENSMUSP00000043753 | Alpha-tubulin N-acetyltransferase 1; Specifically acetylates 'Lys-40' in alpha-tubulin 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 on dyn [...] | Tubulin polyglutamylase TTLL7; Polyglutamylase which preferentially modifies beta-tubulin. Mediates both ATP- dependent initiation and elongation of polyglutamylation of microtubules. Required for neurite growth; responsible for the strong increase in tubulin polyglutamylation during postnatal neuronal maturation ; Belongs to the tubulin--tyrosine ligase family. | 0.459 |
Ccdc74a | Ttll3 | ENSMUSP00000049541 | ENSMUSP00000032414 | Coiled-coil domain-containing 74A. | Tubulin monoglycylase TTLL3; Monoglycylase which modifies alpha- and beta-tubulin, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Involved in the side-chain initiation step of the glycylation reaction by adding a single glycine chain to generate monoglycine side chains. Not involved in elongation step of the polyglycylation reaction. | 0.528 |
Dcp1a | Dcp1b | ENSMUSP00000022535 | ENSMUSP00000108397 | mRNA-decapping enzyme 1A; Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Contributes to the transactivation of target genes after stimulation by TGFB1 (By similarity). | mRNA-decapping enzyme 1B; May play a role in the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. May remove the 7- methyl guanine cap structure from mRNA molecules, yielding a 5'- phosphorylated mRNA fragment and 7m-GDP (By similarity); Belongs to the DCP1 family. | 0.973 |
Dcp1a | Dcp2 | ENSMUSP00000022535 | ENSMUSP00000025350 | mRNA-decapping enzyme 1A; Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Contributes to the transactivation of target genes after stimulation by TGFB1 (By similarity). | m7GpppN-mRNA hydrolase; Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay (By similarity). Plays a role in replication-dependent histone mRNA degradation (By similarity). Has higher activity towards mRNAs that lack a poly(A) tail. Has no activity towards a cap structure lacking an RNA moiety. | 0.999 |
Dcp1a | Ttll3 | ENSMUSP00000022535 | ENSMUSP00000032414 | mRNA-decapping enzyme 1A; Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Contributes to the transactivation of target genes after stimulation by TGFB1 (By similarity). | Tubulin monoglycylase TTLL3; Monoglycylase which modifies alpha- and beta-tubulin, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Involved in the side-chain initiation step of the glycylation reaction by adding a single glycine chain to generate monoglycine side chains. Not involved in elongation step of the polyglycylation reaction. | 0.461 |
Dcp1a | Ttll5 | ENSMUSP00000022535 | ENSMUSP00000048809 | mRNA-decapping enzyme 1A; Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Contributes to the transactivation of target genes after stimulation by TGFB1 (By similarity). | Tubulin polyglutamylase TTLL5; Polyglutamylase which preferentially modifies alpha-tubulin. Involved in the side-chain initiation step of the polyglutamylation reaction rather than in the elongation step. Required for CCSAP localization to both spindle and cilia microtubules (By similarity). Increases the effects of NCOA2 in glucocorticoid receptor-mediated repression and induction and in androgen receptor-mediated induction (By similarity). Belongs to the tubulin--tyrosine ligase family. | 0.471 |
Dcp1b | Dcp1a | ENSMUSP00000108397 | ENSMUSP00000022535 | mRNA-decapping enzyme 1B; May play a role in the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. May remove the 7- methyl guanine cap structure from mRNA molecules, yielding a 5'- phosphorylated mRNA fragment and 7m-GDP (By similarity); Belongs to the DCP1 family. | mRNA-decapping enzyme 1A; Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Contributes to the transactivation of target genes after stimulation by TGFB1 (By similarity). | 0.973 |
Dcp1b | Dcp2 | ENSMUSP00000108397 | ENSMUSP00000025350 | mRNA-decapping enzyme 1B; May play a role in the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. May remove the 7- methyl guanine cap structure from mRNA molecules, yielding a 5'- phosphorylated mRNA fragment and 7m-GDP (By similarity); Belongs to the DCP1 family. | m7GpppN-mRNA hydrolase; Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay (By similarity). Plays a role in replication-dependent histone mRNA degradation (By similarity). Has higher activity towards mRNAs that lack a poly(A) tail. Has no activity towards a cap structure lacking an RNA moiety. | 0.986 |
Dcp1b | Ttll3 | ENSMUSP00000108397 | ENSMUSP00000032414 | mRNA-decapping enzyme 1B; May play a role in the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. May remove the 7- methyl guanine cap structure from mRNA molecules, yielding a 5'- phosphorylated mRNA fragment and 7m-GDP (By similarity); Belongs to the DCP1 family. | Tubulin monoglycylase TTLL3; Monoglycylase which modifies alpha- and beta-tubulin, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Involved in the side-chain initiation step of the glycylation reaction by adding a single glycine chain to generate monoglycine side chains. Not involved in elongation step of the polyglycylation reaction. | 0.469 |
Dcp1b | Ttll5 | ENSMUSP00000108397 | ENSMUSP00000048809 | mRNA-decapping enzyme 1B; May play a role in the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. May remove the 7- methyl guanine cap structure from mRNA molecules, yielding a 5'- phosphorylated mRNA fragment and 7m-GDP (By similarity); Belongs to the DCP1 family. | Tubulin polyglutamylase TTLL5; Polyglutamylase which preferentially modifies alpha-tubulin. Involved in the side-chain initiation step of the polyglutamylation reaction rather than in the elongation step. Required for CCSAP localization to both spindle and cilia microtubules (By similarity). Increases the effects of NCOA2 in glucocorticoid receptor-mediated repression and induction and in androgen receptor-mediated induction (By similarity). Belongs to the tubulin--tyrosine ligase family. | 0.465 |
Dcp2 | Dcp1a | ENSMUSP00000025350 | ENSMUSP00000022535 | m7GpppN-mRNA hydrolase; Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay (By similarity). Plays a role in replication-dependent histone mRNA degradation (By similarity). Has higher activity towards mRNAs that lack a poly(A) tail. Has no activity towards a cap structure lacking an RNA moiety. | mRNA-decapping enzyme 1A; Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Contributes to the transactivation of target genes after stimulation by TGFB1 (By similarity). | 0.999 |
Dcp2 | Dcp1b | ENSMUSP00000025350 | ENSMUSP00000108397 | m7GpppN-mRNA hydrolase; Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay (By similarity). Plays a role in replication-dependent histone mRNA degradation (By similarity). Has higher activity towards mRNAs that lack a poly(A) tail. Has no activity towards a cap structure lacking an RNA moiety. | mRNA-decapping enzyme 1B; May play a role in the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. May remove the 7- methyl guanine cap structure from mRNA molecules, yielding a 5'- phosphorylated mRNA fragment and 7m-GDP (By similarity); Belongs to the DCP1 family. | 0.986 |
Dcp2 | Ttll3 | ENSMUSP00000025350 | ENSMUSP00000032414 | m7GpppN-mRNA hydrolase; Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay (By similarity). Plays a role in replication-dependent histone mRNA degradation (By similarity). Has higher activity towards mRNAs that lack a poly(A) tail. Has no activity towards a cap structure lacking an RNA moiety. | Tubulin monoglycylase TTLL3; Monoglycylase which modifies alpha- and beta-tubulin, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Involved in the side-chain initiation step of the glycylation reaction by adding a single glycine chain to generate monoglycine side chains. Not involved in elongation step of the polyglycylation reaction. | 0.494 |
Dcp2 | Ttll5 | ENSMUSP00000025350 | ENSMUSP00000048809 | m7GpppN-mRNA hydrolase; Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay (By similarity). Plays a role in replication-dependent histone mRNA degradation (By similarity). Has higher activity towards mRNAs that lack a poly(A) tail. Has no activity towards a cap structure lacking an RNA moiety. | Tubulin polyglutamylase TTLL5; Polyglutamylase which preferentially modifies alpha-tubulin. Involved in the side-chain initiation step of the polyglutamylation reaction rather than in the elongation step. Required for CCSAP localization to both spindle and cilia microtubules (By similarity). Increases the effects of NCOA2 in glucocorticoid receptor-mediated repression and induction and in androgen receptor-mediated induction (By similarity). Belongs to the tubulin--tyrosine ligase family. | 0.498 |