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TTL | tubulin tyrosine ligase; Catalyzes the post-translational addition of a tyrosine to the C-terminal end of detyrosinated alpha-tubulin (By similarity) (377 aa) | |||
TTLL2 | tubulin tyrosine ligase-like family, member 2; Probable tubulin polyglutamylase that forms polyglutamate side chains on tubulin. Probably acts when complexed with other proteins (By similarity) (592 aa) | |||
DDX6 | DEAD (Asp-Glu-Ala-Asp) box helicase 6; In the process of mRNA degradation, may play a role in mRNA decapping (483 aa) | |||
XRN1 | 5’-3’ exoribonuclease 1; Major 5’-3’ exoribonuclease involved in mRNA decay. Required for the 5’-3’-processing of the G4 tetraplex-containing DNA and RNA substrates. The kinetic of hydrolysis is faster for G4 RNA tetraplex than for G4 DNA tetraplex and monomeric RNA tetraplex. Binds to RNA and DNA (By similarity). Plays a role in replication-dependent histone mRNA degradation. May act as a tumor suppressor protein in osteogenic sarcoma (OGS) (1706 aa) | |||
TTLL1 | tubulin tyrosine ligase-like family, member 1; Catalytic subunit of the neuronal tubulin polyglutamylase complex. Modifies alpha- and beta-tubulin, generating side chains of glutamate on the gamma-carboxyl groups of specific glutamate residues within the C-terminal tail of alpha- and beta-tubulin (By similarity) (423 aa) | |||
NUDT7 | nudix (nucleoside diphosphate linked moiety X)-type motif 7; Coenzyme A diphosphatase which mediates the cleavage of CoA, CoA esters and oxidized CoA with similar efficiencies, yielding 3’,5’-ADP and the corresponding 4’-phosphopantetheine derivative as products. CoA into 3’,5’-ADP and 4’- phosphopantetheine. Has no activity toward NDP-sugars, CDP- alcohols, (deoxy)nucleoside 5’-triphosphates, nucleoside 5’-di or monophosphates, diadenosine polyphosphates, NAD, NADH, NADP, NADPH or thymidine-5’-monophospho-p-nitrophenyl ester. May be required to eliminate oxidized CoA from peroxisomes, [...] (238 aa) | |||
DCP1B | DCP1 decapping enzyme homolog B (S. cerevisiae); 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) (617 aa) | |||
TTLL5 | tubulin tyrosine ligase-like family, member 5; Polyglutamylase which preferentially modifies alpha- tubulin. Involved in the side-chain initiation step of the polyglutamylation reaction rather than in the elongation step (By similarity). Required for CCSAP localization to both spindle and cilia microtubules. Increases the effects of NCOA2 in glucocorticoid receptor-mediated repression and induction and in androgen receptor-mediated induction (1281 aa) | |||
PATL1 | protein associated with topoisomerase II homolog 1 (yeast); RNA-binding protein involved in deadenylation-dependent decapping of mRNAs, leading to the degradation of mRNAs. Acts as a scaffold protein that connects deadenylation and decapping machinery. Required for cytoplasmic mRNA processing body (P-body) assembly. In case of infection, required for translation and replication of hepatitis C virus (HCV) (770 aa) | |||
NUDT8 | nudix (nucleoside diphosphate linked moiety X)-type motif 8; Probably mediates the hydrolysis of some nucleoside diphosphate derivatives (By similarity) (140 aa) | |||
LSM1 | LSM1 homolog, U6 small nuclear RNA associated (S. cerevisiae); Plays a role in replication-dependent histone mRNA degradation. Binds specifically to the 3’-terminal U-tract of U6 snRNA (133 aa) | |||
NUDT2 | nudix (nucleoside diphosphate linked moiety X)-type motif 2; Asymmetrically hydrolyzes Ap4A to yield AMP and ATP. Plays a major role in maintaining homeostasis (147 aa) | |||
NUDT1 | nudix (nucleoside diphosphate linked moiety X)-type motif 1; Antimutagenic. Acts as a sanitizing enzyme for oxidized nucleotide pools, thus suppressing cell dysfunction and death induced by oxidative stress. Hydrolyzes 8-oxo-dGTP, 8-oxo-dATP and 2-OH-dATP, thus preventing misincorporation of oxidized purine nucleoside triphosphates into DNA and subsequently preventing A-T to C-G and G-C to T-A transversions. Able to hydrolyze also the corresponding ribonucleotides, 2-OH-ATP, 8-oxo-GTP and 8-oxo-ATP. Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA (179 aa) | |||
NUDT10 | nudix (nucleoside diphosphate linked moiety X)-type motif 10; Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being the preferred substrates. The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A. Also able to hydrolyze 5-phosphoribose 1-diphosphate (164 aa) | |||
TTLL9 | tubulin tyrosine ligase-like family, member 9; Probable tubulin polyglutamylase that forms polyglutamate side chains on tubulin. Probably acts when complexed with other proteins (By similarity) (439 aa) | |||
NUDT11 | nudix (nucleoside diphosphate linked moiety X)-type motif 11; Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being the preferred substrates. The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A. Also able to hydrolyze 5-phosphoribose 1-diphosphate (164 aa) | |||
XRN2 | 5’-3’ exoribonuclease 2; Possesses 5’->3’ exoribonuclease activity (By similarity). May promote the termination of transcription by RNA polymerase II. During transcription termination, cleavage at the polyadenylation site liberates a 5’ fragment which is subsequently processed to form the mature mRNA and a 3’ fragment which remains attached to the elongating polymerase. The processive degradation of this 3’ fragment by this protein may promote termination of transcription (950 aa) | |||
TTLL10 | tubulin tyrosine ligase-like family, member 10; Inactive polyglycylase (673 aa) | |||
DCP2 | DCP2 decapping enzyme homolog (S. cerevisiae); 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. Plays a role in replication-dependent histone mRNA degradation. Has higher activity towards mRNAs that lack a poly(A) tail. Has no activity towards a cap structure lacking a RNA moiety (420 aa) | |||
NUDT14 | nudix (nucleoside diphosphate linked moiety X)-type motif 14; Hydrolyzes UDP-glucose to glucose 1-phosphate and UMP and ADP-ribose to ribose 5-phosphate and AMP. The physiological substrate is probably UDP-glucose. Poor activity on other substrates such as ADP-glucose, CDP-glucose, GDP-glucose and GDP- mannose (222 aa) | |||
ENSG00000250151 | ARPC4-TTLL3 readthrough; Functions as actin-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the mother actin filament (625 aa) | |||
TTLL8 | tubulin tyrosine ligase-like family, member 8; 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 [...] (850 aa) | |||
TTLL3 | tubulin tyrosine ligase-like family, member 3; 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 (915 aa) | |||
HELZ2 | helicase with zinc finger 2, transcriptional coactivator; Helicase that acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB and RXRA (2649 aa) | |||
NUDT5 | nudix (nucleoside diphosphate linked moiety X)-type motif 5; Hydrolyzes with similar activities ADP-ribose ADP- mannose, ADP-glucose, 8-oxo-GDP and 8-oxo-dGDP. Can also hydrolyze other nucleotide sugars with low activity. Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA (219 aa) | |||
YJEFN3 | YjeF N-terminal domain containing 3; May play a role in spermiogenesis and oogenesis (299 aa) |