Search Results
Overview
| Uniprot ID | P62244 |
|---|---|
| Protein Name | Small ribosomal subunit protein uS8 |
| Gene Name | RPS15A |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 19 | KSINNAEKRGKRQVL |
| 71 | NLTGRLNKCGVISPR |
| 88 | VQLKDLEKWQNNLLP |
Function
Component of the small ribosomal subunit (PubMed:23636399). 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). Required for proper erythropoiesis (PubMed:27909223)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0022626 | cytosolic ribosome |
| Cellular Component | GO:0022627 | cytosolic small ribosomal subunit |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0032040 | small-subunit processome |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0003735 | structural constituent of ribosome |
| Biological Process | GO:0002181 | cytoplasmic translation |
| Biological Process | GO:0045787 | positive regulation of cell cycle |
| Biological Process | GO:0008284 | positive regulation of cell population proliferation |
| Biological Process | GO:0009615 | response to virus |
| Biological Process | GO:0042274 | ribosomal small subunit biogenesis |
| Biological Process | GO:0006412 | translation |
Reference
[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.
[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[4] 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.
[5] 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.