EC Number   |
General Information |
Reference |
|---|
   2.7.7.52 | malfunction |
enzyme deletion increases sensitivity to protein misfolding stress |
-, 762050 |
| 2.7.7.52 | metabolism |
isoform TUT1 catalyzes oligo-uridylylation of U6 small nuclear RNA, which catalyzes mRNA splicing. Oligo-uridylylation of U6 snRNA is required for U6 snRNA maturation, U4/U6-di-snRNP formation, and U6 snRNA recycling during mRNA splicing |
761139 |
| 2.7.7.52 | metabolism |
isoform TUT4 catalyzes mono- or oligo-uridylylation of precursor let-7 (pre-let-7). Let-7 RNA is broadly expressed in somatic cells and regulates cellular proliferation and differentiation. Mono-uridylylation of pre-let-7 by TUT4 promotes subsequent Dicer processing to up-regulate let-7 biogenesis |
761139 |
| 2.7.7.52 | metabolism |
isoform TUT7 catalyzes mono- or oligo-uridylylation of precursor let-7 (pre-let-7). Let-7 RNA is broadly expressed in somatic cells and regulates cellular proliferation and differentiation. Mono-uridylylation of pre-let-7 by TUT7 promotes subsequent Dicer processing to up-regulate let-7 biogenesis |
761139 |
| 2.7.7.52 | metabolism |
the enzyme plays a crucial role as the repressor in the biogenesis pathway of splicing-derived mirtron pre-miRNAs |
762051 |
| 2.7.7.52 | metabolism |
the enzyme uridylates polyadenylated mRNAs to trigger Lsm1-7-mediated decapping of the RNA 5'-end and subsequent degradation by the U-specific exonuclease Dis3L2 |
-, 762050 |
| 2.7.7.52 | metabolism |
the U6 snRNA-specific terminal uridylyltransferase is required for pre-mRNA splicing |
761992 |
| 2.7.7.52 | physiological function |
isoform HESO1, which uridylates most unmethylated miRNAs in vivo, and isoform URT1 which exhibits nucleotidyl transferase activity on unmethylated miRNA, prefer substrates with different 3'-end nucleotides in vitro and act cooperatively to tail different forms of the same miRNAs in vivo. Both HESO1 and URT1 exhibit nucleotidyl transferase activity on AGO1-bound miRNAs. Although the enzymes are able to add long tails to AGO1-bound miRNAs, the tailed miRNAs remain associated with AGO1. Tailing of AGO1-bound miRNA165/6 drastically reduces the slicing activity of AGO1-miR165/6 |
739397 |
| 2.7.7.52 | physiological function |
isoform RET1 adds U tails to gRNAs, rRNAs, and selected mRNAs and contributes U residues into A/U heteropolymers. Isoform RET1's terminal uridylyl transferase activity is required for the nucleolytic processing of gRNA, rRNA, and mRNA precursors. The U tails presence does not affect the stability of gRNAs and rRNAs, while transcript-specific uridylylation triggers 3' to 5' mRNA decay. The minicircle-encoded antisense transcripts, which are stabilized by RET1-catalyzed uridylylation, may direct a nucleolytic cleavage of multicistronic precursors |
723172 |
| 2.7.7.52 | physiological function |
isoform RET2 is an integral component of the RNA editing core complex RECC. Interaction of RET2 with RECC is accomplished via a protein-protein contact between its middle domain and structural subunit MP81. The recombinant RET2 catalyzes a faithful editing on gapped precleaved double-stranded RNA substrates, and this reaction requires an internal monophosphate group at the 5' end of the mRNA 3' cleavage fragment. RET2 processivity is limited to insertion of three U residues. Incorporation into the RECC voids the internal phosphate requirement and allows filling of longer gaps similar to those observed in vivo. Monomeric and RECC-embedded enzymes display a similar bimodal activity, the distributive insertion of a single uracil is followed by a processive extension limited by the number of guiding nucleotides |
722966 |
