Search Results
Overview
| Uniprot ID | O95453 |
|---|---|
| Protein Name | Poly(A)-specific ribonuclease PARN |
| Gene Name | PARN |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 168 | YVSPNTSKCPVTIPE |
| 525 | EEKQIKRKWTEDSWK |
| 566 | TAPSTVGKRNLSPSQ |
| 616 | KKLKRMKKELSPAGS |
Function
3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence certain maternal mRNAs translationally during oocyte maturation and early embryonic development. Interacts with both the 3'-end poly(A) tail and the 5'-end cap structure during degradation, the interaction with the cap structure being required for an efficient degradation of poly(A) tails. Involved in nonsense-mediated mRNA decay, a critical process of selective degradation of mRNAs that contain premature stop codons. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly via its interaction with KHSRP. Probably mediates the removal of poly(A) tails of AREs mRNAs, which constitutes the first step of destabilization (PubMed:10882133, PubMed:11359775, PubMed:12748283, PubMed:15175153, PubMed:9736620). Also able to recognize and trim poly(A) tails of microRNAs such as MIR21 and H/ACA box snoRNAs (small nucleolar RNAs) leading to microRNAs degradation or snoRNA increased stability (PubMed:22442037, PubMed:25049417)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0098978 | glutamatergic synapse |
| Cellular Component | GO:0016607 | nuclear speck |
| Cellular Component | GO:0005730 | nucleolus |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0098794 | postsynapse |
| Molecular Function | GO:0000175 | 3'-5'-RNA exonuclease activity |
| Molecular Function | GO:0043169 | cation binding |
| Molecular Function | GO:0046872 | metal ion binding |
| Molecular Function | GO:0003730 | mRNA 3'-UTR binding |
| Molecular Function | GO:0004518 | nuclease activity |
| Molecular Function | GO:0004535 | poly(A)-specific ribonuclease activity |
| Molecular Function | GO:0019901 | protein kinase binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0070034 | telomerase RNA binding |
| Biological Process | GO:0000495 | box H/ACA sno(s)RNA 3'-end processing |
| Biological Process | GO:0007292 | female gamete generation |
| Biological Process | GO:0180035 | lncRNA processing |
| Biological Process | GO:0010587 | miRNA catabolic process |
| Biological Process | GO:0000184 | nuclear-transcribed mRNA catabolic process, nonsense-mediated decay |
| Biological Process | GO:0000289 | nuclear-transcribed mRNA poly(A) tail shortening |
| Biological Process | GO:0071051 | poly(A)-dependent snoRNA 3'-end processing |
| Biological Process | GO:0032212 | positive regulation of telomere maintenance via telomerase |
| Biological Process | GO:1990431 | priRNA 3'-end processing |
| Biological Process | GO:1904872 | regulation of telomerase RNA localization to Cajal body |
| Biological Process | GO:0009451 | RNA modification |
| Biological Process | GO:1990432 | siRNA 3'-end processing |
| Biological Process | GO:0090669 | telomerase RNA stabilization |
Reference
[1] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.
[2] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.