Search Results
Overview
| Uniprot ID | Q01780 |
|---|---|
| Protein Name | Exosome complex component 10 |
| Gene Name | EXOSC10 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 178 | TFRLLHAKNIIRPQL |
| 592 | EVAAGVKKSGPLPSA |
| 710 | APVSQAAKFDPSTKI |
| 733 | LAQVQVQKDSKEAVK |
| 835 | FAGNSKSKVSSQFDP |
| 844 | SSQFDPNKQTPSGKK |
| 857 | KKCIAAKKIKQSVGN |
| 859 | CIAAKKIKQSVGNKS |
| 873 | SMSFPTGKSDRGFRY |
Function
Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. EXOSC10 is required for nucleolar localization of C1D and probably mediates the association of MTREX, C1D and MPHOSPH6 with the RNA exosome involved in the maturation of 5.8S rRNA. Plays a role in the recruitment of replication protein A complex (RPA) and RAD51 to DNA double-strand breaks caused by irradiation, contributing to DNA repair by homologous recombination (PubMed:25632158, PubMed:31086179). Regulates levels of damage-induced RNAs in order to prevent DNA-RNA hybrid formation at DNA double-strand breaks and limit DNA end resection after damage (PubMed:31086179). Plays a role in oocyte development, maturation and survival (By similarity). Required for normal testis development and mitotic division of spermatogonia (By similarity). Plays a role in proper embryo development (By similarity). Required for global protein translation (PubMed:26857222, PubMed:36912080). Required for cell proliferation (PubMed:36912080). Regulates metabolism of C9orf72-derived repeat RNA that can be translated into toxic dipeptide repeat proteins (PubMed:32830871)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Biological Process | GO:0071028 | nuclear mRNA surveillance |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0000791 | euchromatin |
| Cellular Component | GO:0000178 | exosome (RNase complex) |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0000176 | nuclear exosome (RNase complex) |
| Cellular Component | GO:0005730 | nucleolus |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0032040 | small-subunit processome |
| Molecular Function | GO:0000175 | 3'-5'-RNA exonuclease activity |
| Molecular Function | GO:0046872 | metal ion binding |
| Molecular Function | GO:0000166 | nucleotide binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0004532 | RNA exonuclease activity |
| Molecular Function | GO:0003727 | single-stranded RNA binding |
| Molecular Function | GO:0070034 | telomerase RNA binding |
| Biological Process | GO:0071034 | CUT catabolic process |
| Biological Process | GO:0006281 | DNA repair |
| Biological Process | GO:0000467 | exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) |
| Biological Process | GO:0071044 | histone mRNA catabolic process |
| Biological Process | GO:0000460 | maturation of 5.8S rRNA |
| Biological Process | GO:0032211 | negative regulation of telomere maintenance via telomerase |
| Biological Process | GO:0071040 | nuclear polyadenylation-dependent antisense transcript catabolic process |
| Biological Process | GO:0071039 | nuclear polyadenylation-dependent CUT catabolic process |
| Biological Process | GO:0071035 | nuclear polyadenylation-dependent rRNA catabolic process |
| Biological Process | GO:0071036 | nuclear polyadenylation-dependent snoRNA catabolic process |
| Biological Process | GO:0071037 | nuclear polyadenylation-dependent snRNA catabolic process |
| Biological Process | GO:0000956 | nuclear-transcribed mRNA catabolic process |
| Biological Process | GO:0000184 | nuclear-transcribed mRNA catabolic process, nonsense-mediated decay |
| Biological Process | GO:0071051 | poly(A)-dependent snoRNA 3'-end processing |
| Biological Process | GO:1904872 | regulation of telomerase RNA localization to Cajal body |
| Biological Process | GO:0042274 | ribosomal small subunit biogenesis |
| Biological Process | GO:0006401 | RNA catabolic process |
| Biological Process | GO:0006396 | RNA processing |
| Biological Process | GO:0006364 | rRNA processing |
| Biological Process | GO:0071038 | TRAMP-dependent tRNA surveillance pathway |
Reference
[1] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.
[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.