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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: UTP:RNA uridylyltransferase 1

UniprotKB/SwissProt ID: O64642 (O64642)

Gene Name: URT1

Organism: Arabidopsis thaliana (Mouse-ear cress)

Function: UTP:RNA uridylyltransferase with a marked preference for uridine polymerization and a distributive activity for the first added nucleotides (PubMed:23748567, PubMed:25928405). Uridylates oligo(A)-tailed mRNAs to prevent 3' to 5' ribonucleotytic attacks (PubMed:23748567). Reduces the accumulation of oligo(A)-tailed mRNAs (PubMed:33637717). Prevents the accumulation of excessively deadenylated mRNAs to avoid siRNA biogenesis (PubMed:26972004, PubMed:33637717). Uridylation repairs deadenylated extremities to restore the size distribution observed for non-uridylated oligo(A) tails (PubMed:26972004). Can prevent the 3' trimming of mRNAs still engaged on polysomes (PubMed:23748567). Acts synergistically with HESO1 in unmethylated miRNA uridylation, leading to their degradation (PubMed:25928341). URT1 and HESO1 prefer substrates with different 3' end nucleotides and act cooperatively to tail different forms of the same miRNAs (PubMed:25928405). URT1 and HESO1 act sequentially, with URT1 mono-uridylating the miRNAs followed by their further uridylation by HESO1 (PubMed:25928405). URT1 and HESO1 are involved in the uridylation and clearance of RISC-generated 5' mRNA fragments (PubMed:30364210). Has no effect on uridylation of heterochromatic siRNAs (PubMed:25928341). Able to act on AGO1-bound miRNAs and the uridylated species stay associated with AGO1 (PubMed:25928405). Acts as post-transcriptional gene silencing (PTGS) suppressor (PubMed:31076735)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Cytoplasm, P-body

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR054708 MTPAP-like_central
IPR043519 NT_sf
IPR002058 PAP_assoc

The S-nitrosylation sites of O64642

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 705 RRVGNDRHLI C IEDPFETSHD