Search Results
Overview
| Uniprot ID | P61254 |
|---|---|
| Protein Name | Large ribosomal subunit protein uL24 |
| Gene Name | RPL26 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 134 | QVGKEKGKYKEETIE |
| 136 | GKEKGKYKEETIEKM |
| 142 | YKEETIEKMQE**** |
| 28 | APSHIRRKIMSSPLS |
| 51 | VRSMPIRKDDEVQVV |
| 69 | YKGQQIGKVVQVYRK |
| 77 | VVQVYRKKYVIYIER |
Function
Component of the large ribosomal subunit (PubMed:23636399, PubMed:26100019, PubMed:32669547). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399, PubMed:26100019, PubMed:32669547)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0022625 | cytosolic large ribosomal subunit |
| Cellular Component | GO:0022626 | cytosolic ribosome |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005730 | nucleolus |
| Biological Process | GO:0045727 | positive regulation of translation |
| Biological Process | GO:1904803 | regulation of translation involved in cellular response to UV |
| Biological Process | GO:0042273 | ribosomal large subunit biogenesis |
| Biological Process | GO:0006364 | rRNA processing |
| Biological Process | GO:0006412 | translation |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:1990904 | ribonucleoprotein complex |
| Molecular Function | GO:0048027 | mRNA 5'-UTR binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0003735 | structural constituent of ribosome |
| Biological Process | GO:0071480 | cellular response to gamma radiation |
| Biological Process | GO:0034644 | cellular response to UV |
| Biological Process | GO:0002181 | cytoplasmic translation |
| Biological Process | GO:0030330 | DNA damage response, signal transduction by p53 class mediator |
| Biological Process | GO:0043517 | positive regulation of DNA damage response, signal transduction by p53 class mediator |
| Biological Process | GO:1902167 | positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator |
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] 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.
[4] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.
[5] 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.
[6] 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.