Search Results
Overview
| Uniprot ID | P62829 |
|---|---|
| Protein Name | Large ribosomal subunit protein uL14 |
| Gene Name | RPL23 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 113 | VNNKGEMKGSAITGP |
| 66 | DMVMATVKKGKPELR |
| 75 | GKPELRKKVHPAVVI |
Function
Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005730 | nucleolus |
| 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:0005925 | focal adhesion |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0032991 | protein-containing complex |
| Cellular Component | GO:0005840 | ribosome |
| Cellular Component | GO:0045202 | synapse |
| Molecular Function | GO:0070180 | large ribosomal subunit rRNA binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0003735 | structural constituent of ribosome |
| Molecular Function | GO:0001223 | transcription coactivator binding |
| 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:0070314 | G1 to G0 transition |
| Biological Process | GO:1901740 | negative regulation of myoblast fusion |
| Biological Process | GO:0000122 | negative regulation of transcription by RNA polymerase II |
| Biological Process | GO:2000059 | negative regulation of ubiquitin-dependent protein catabolic process |
| Biological Process | GO:0008284 | positive regulation of cell population proliferation |
| Biological Process | GO:1901798 | positive regulation of signal transduction by p53 class mediator |
| Biological Process | GO:0050821 | protein stabilization |
| Biological Process | GO:0032986 | protein-DNA complex disassembly |
| Biological Process | GO:1903450 | regulation of G1 to G0 transition |
| Biological Process | GO:0006610 | ribosomal protein import into nucleus |
| 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] 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.
[4] 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.