Search Results
Overview
| Uniprot ID | P26373 |
|---|---|
| Protein Name | Large ribosomal subunit protein eL13 |
| Gene Name | RPL13 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 105 | VDPRRRNKSTESLQA |
| 123 | RLKEYRSKLILFPRK |
| 174 | RVITEEEKNFKAFAS |
| 177 | TEEEKNFKAFASLRM |
| 200 | GIRAKRAKEAAEQDV |
| 209 | AAEQDVEKKK***** |
| 210 | AEQDVEKKK****** |
Function
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399, PubMed:31630789, PubMed:32669547). The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules (Probable). 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 (Probable). 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 (Probable). As part of the LSU, it is probably required for its formation and the maturation of rRNAs (PubMed:31630789). Plays a role in bone development (PubMed:31630789)
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:0005783 | endoplasmic reticulum |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005730 | nucleolus |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0045202 | synapse |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0003735 | structural constituent of ribosome |
| Biological Process | GO:0060348 | bone development |
| Biological Process | GO:0002181 | cytoplasmic translation |
| Biological Process | GO:1901740 | negative regulation of myoblast fusion |
| 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] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.
[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.