Search Results
Overview
| Uniprot ID | P62913 |
|---|---|
| Protein Name | Large ribosomal subunit protein uL5 |
| Gene Name | RPL11 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 144 | PGFSIADKKRRTGCI |
| 145 | GFSIADKKRRTGCIG |
| 159 | GAKHRISKEEAMRWF |
| 38 | DRLTRAAKVLEQLTG |
| 52 | GQTPVFSKARYTVRS |
| 67 | FGIRRNEKIAVHCTV |
| 78 | HCTVRGAKAEEILEK |
| 85 | KAEEILEKGLKVREY |
Function
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:19191325, PubMed:32669547). The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules (PubMed:19191325, PubMed:32669547). The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain (PubMed:19191325, PubMed:32669547). The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:19191325, PubMed:32669547). As part of the 5S RNP/5S ribonucleoprotein particle it is an essential component of the LSU, required for its formation and the maturation of rRNAs (PubMed:12962325, PubMed:19061985, PubMed:24120868). It also couples ribosome biogenesis to p53/TP53 activation. As part of the 5S RNP it accumulates in the nucleoplasm and inhibits MDM2, when ribosome biogenesis is perturbed, mediating the stabilization and the activation of TP53 (PubMed:24120868). Promotes nucleolar location of PML (By similarity)
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 |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0032991 | protein-containing complex |
| Molecular Function | GO:0008097 | 5S rRNA binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0003735 | structural constituent of ribosome |
| Molecular Function | GO:1990948 | ubiquitin ligase inhibitor activity |
| Molecular Function | GO:0031625 | ubiquitin protein ligase binding |
| Biological Process | GO:0002181 | cytoplasmic translation |
| Biological Process | GO:1901740 | negative regulation of myoblast fusion |
| Biological Process | GO:0032435 | negative regulation of proteasomal ubiquitin-dependent protein catabolic process |
| Biological Process | GO:2000059 | negative regulation of ubiquitin-dependent protein catabolic process |
| Biological Process | GO:1901798 | positive regulation of signal transduction by p53 class mediator |
| Biological Process | GO:0034504 | protein localization to nucleus |
| Biological Process | GO:0006605 | protein targeting |
| Biological Process | GO:1901796 | regulation of signal transduction by p53 class mediator |
| Biological Process | GO:0000027 | ribosomal large subunit assembly |
| Biological Process | GO:0042273 | ribosomal large subunit biogenesis |
| Biological Process | GO:0006364 | rRNA processing |
| Biological Process | GO:0007283 | spermatogenesis |
| Biological Process | GO:0006941 | striated muscle contraction |
| 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 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.
[5] 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.
[6] 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.
[7] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.
[8] 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.