Search Results
Overview
| Uniprot ID | P46782 |
|---|---|
| Protein Name | Small ribosomal subunit protein uS7 |
| Gene Name | RPS5 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 182 | DELINAAKGSSNSYA |
| 191 | SSNSYAIKKKDELER |
| 192 | SNSYAIKKKDELERV |
| 47 | AVKEKYAKYLPHSAG |
| 63 | YAAKRFRKAQCPIVE |
Function
Component of the small ribosomal subunit (PubMed:23636399). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (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)
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:0005783 | endoplasmic reticulum |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005925 | focal adhesion |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:1990904 | ribonucleoprotein complex |
| Cellular Component | GO:0005840 | ribosome |
| Cellular Component | GO:0032040 | small-subunit processome |
| Cellular Component | GO:0045202 | synapse |
| Molecular Function | GO:0003729 | mRNA binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0019843 | rRNA binding |
| Molecular Function | GO:0003735 | structural constituent of ribosome |
| Biological Process | GO:0002181 | cytoplasmic translation |
| Biological Process | GO:0006450 | regulation of translational fidelity |
| Biological Process | GO:0042274 | ribosomal small subunit biogenesis |
| Biological Process | GO:0006412 | translation |
| Biological Process | GO:0006413 | translational initiation |
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.