node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Ankrd60 | Lrrc63 | ENSMUSP00000113291 | ENSMUSP00000022574 | Ankyrin repeat domain 60. | Leucine-rich repeat-containing protein 63. | 0.815 |
Ankrd60 | Ttll8 | ENSMUSP00000113291 | ENSMUSP00000104996 | Ankyrin repeat domain 60. | Protein monoglycylase TTLL8; Monoglycylase which modifies both tubulin and non-tubulin proteins, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues of target proteins. Monoglycylates tubulin, with a preference for alpha-tubulin toward beta-tubulin. Has the ability to modify non-tubulin proteins such as ANP32A, ANP32B, SET and NCL. 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. | 0.620 |
Atat1 | Ttll8 | ENSMUSP00000056383 | ENSMUSP00000104996 | 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 [...] | Protein monoglycylase TTLL8; Monoglycylase which modifies both tubulin and non-tubulin proteins, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues of target proteins. Monoglycylates tubulin, with a preference for alpha-tubulin toward beta-tubulin. Has the ability to modify non-tubulin proteins such as ANP32A, ANP32B, SET and NCL. 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. | 0.458 |
Ccdc149 | Ttll8 | ENSMUSP00000062411 | ENSMUSP00000104996 | Coiled-coil domain-containing 149. | Protein monoglycylase TTLL8; Monoglycylase which modifies both tubulin and non-tubulin proteins, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues of target proteins. Monoglycylates tubulin, with a preference for alpha-tubulin toward beta-tubulin. Has the ability to modify non-tubulin proteins such as ANP32A, ANP32B, SET and NCL. 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 |
Ccdc149 | Zfp775 | ENSMUSP00000062411 | ENSMUSP00000145192 | Coiled-coil domain-containing 149. | Zinc finger protein 775; May be involved in transcriptional regulation; Belongs to the krueppel C2H2-type zinc-finger protein family. | 0.489 |
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 | Ttll8 | ENSMUSP00000022535 | ENSMUSP00000104996 | 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). | Protein monoglycylase TTLL8; Monoglycylase which modifies both tubulin and non-tubulin proteins, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues of target proteins. Monoglycylates tubulin, with a preference for alpha-tubulin toward beta-tubulin. Has the ability to modify non-tubulin proteins such as ANP32A, ANP32B, SET and NCL. 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. | 0.460 |
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 | Ttll8 | ENSMUSP00000108397 | ENSMUSP00000104996 | 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. | Protein monoglycylase TTLL8; Monoglycylase which modifies both tubulin and non-tubulin proteins, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues of target proteins. Monoglycylates tubulin, with a preference for alpha-tubulin toward beta-tubulin. Has the ability to modify non-tubulin proteins such as ANP32A, ANP32B, SET and NCL. 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. | 0.460 |
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 | Ttll8 | ENSMUSP00000025350 | ENSMUSP00000104996 | 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. | Protein monoglycylase TTLL8; Monoglycylase which modifies both tubulin and non-tubulin proteins, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues of target proteins. Monoglycylates tubulin, with a preference for alpha-tubulin toward beta-tubulin. Has the ability to modify non-tubulin proteins such as ANP32A, ANP32B, SET and NCL. 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 |
Lrrc63 | Ankrd60 | ENSMUSP00000022574 | ENSMUSP00000113291 | Leucine-rich repeat-containing protein 63. | Ankyrin repeat domain 60. | 0.815 |
Lrrc63 | Ttll8 | ENSMUSP00000022574 | ENSMUSP00000104996 | Leucine-rich repeat-containing protein 63. | Protein monoglycylase TTLL8; Monoglycylase which modifies both tubulin and non-tubulin proteins, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues of target proteins. Monoglycylates tubulin, with a preference for alpha-tubulin toward beta-tubulin. Has the ability to modify non-tubulin proteins such as ANP32A, ANP32B, SET and NCL. 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. | 0.714 |
Ttll8 | Ankrd60 | ENSMUSP00000104996 | ENSMUSP00000113291 | Protein monoglycylase TTLL8; Monoglycylase which modifies both tubulin and non-tubulin proteins, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues of target proteins. Monoglycylates tubulin, with a preference for alpha-tubulin toward beta-tubulin. Has the ability to modify non-tubulin proteins such as ANP32A, ANP32B, SET and NCL. 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. | Ankyrin repeat domain 60. | 0.620 |
Ttll8 | Atat1 | ENSMUSP00000104996 | ENSMUSP00000056383 | Protein monoglycylase TTLL8; Monoglycylase which modifies both tubulin and non-tubulin proteins, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues of target proteins. Monoglycylates tubulin, with a preference for alpha-tubulin toward beta-tubulin. Has the ability to modify non-tubulin proteins such as ANP32A, ANP32B, SET and NCL. 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. | 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 [...] | 0.458 |
Ttll8 | Ccdc149 | ENSMUSP00000104996 | ENSMUSP00000062411 | Protein monoglycylase TTLL8; Monoglycylase which modifies both tubulin and non-tubulin proteins, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues of target proteins. Monoglycylates tubulin, with a preference for alpha-tubulin toward beta-tubulin. Has the ability to modify non-tubulin proteins such as ANP32A, ANP32B, SET and NCL. 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. | Coiled-coil domain-containing 149. | 0.469 |
Ttll8 | Dcp1a | ENSMUSP00000104996 | ENSMUSP00000022535 | Protein monoglycylase TTLL8; Monoglycylase which modifies both tubulin and non-tubulin proteins, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues of target proteins. Monoglycylates tubulin, with a preference for alpha-tubulin toward beta-tubulin. Has the ability to modify non-tubulin proteins such as ANP32A, ANP32B, SET and NCL. 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. | 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). | 0.460 |