Search Results
Overview
| Uniprot ID | P23396 |
|---|---|
| Protein Name | Small ribosomal subunit protein uS3 |
| Gene Name | RPS3 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 10 | VQISKKRKFVADGIF |
| 108 | QAESLRYKLLGGLAV |
| 141 | CEVVVSGKLRGQRAK |
| 202 | TGKIGPKKPLPDHVS |
| 62 | TQNVLGEKGRRIREL |
| 75 | ELTAVVQKRFGFPEG |
Function
Component of the small ribosomal subunit (PubMed:23636399, PubMed:8706699). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399, PubMed:8706699). Has endonuclease activity and plays a role in repair of damaged DNA (PubMed:7775413). Cleaves phosphodiester bonds of DNAs containing altered bases with broad specificity and cleaves supercoiled DNA more efficiently than relaxed DNA (PubMed:15707971). Displays high binding affinity for 7,8-dihydro-8-oxoguanine (8-oxoG), a common DNA lesion caused by reactive oxygen species (ROS) (PubMed:14706345). Has also been shown to bind with similar affinity to intact and damaged DNA (PubMed:18610840). Stimulates the N-glycosylase activity of the base excision protein OGG1 (PubMed:15518571). Enhances the uracil excision activity of UNG1 (PubMed:18973764). Also stimulates the cleavage of the phosphodiester backbone by APEX1 (PubMed:18973764). When located in the mitochondrion, reduces cellular ROS levels and mitochondrial DNA damage (PubMed:23911537). Has also been shown to negatively regulate DNA repair in cells exposed to hydrogen peroxide (PubMed:17049931). Plays a role in regulating transcription as part of the NF-kappa-B p65-p50 complex where it binds to the RELA/p65 subunit, enhances binding of the complex to DNA and promotes transcription of target genes (PubMed:18045535). Represses its own translation by binding to its cognate mRNA (PubMed:20217897). Binds to and protects TP53/p53 from MDM2-mediated ubiquitination (PubMed:19656744). Involved in spindle formation and chromosome movement during mitosis by regulating microtubule polymerization (PubMed:23131551). Involved in induction of apoptosis through its role in activation of CASP8 (PubMed:14988002). Induces neuronal apoptosis by interacting with the E2F1 transcription factor and acting synergistically with it to up-regulate pro-apoptotic proteins BCL2L11/BIM and HRK/Dp5 (PubMed:20605787). Interacts with TRADD following exposure to UV radiation and induces apoptosis by caspase-dependent JNK activation (PubMed:22510408)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Molecular Function | GO:0030544 | Hsp70 protein binding |
| 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:0005743 | mitochondrial inner membrane |
| Cellular Component | GO:0005759 | mitochondrial matrix |
| Cellular Component | GO:0072686 | mitotic spindle |
| Cellular Component | GO:0071159 | NF-kappaB complex |
| Cellular Component | GO:0005730 | nucleolus |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0005886 | plasma membrane |
| Cellular Component | GO:0014069 | postsynaptic density |
| Cellular Component | GO:1990904 | ribonucleoprotein complex |
| Cellular Component | GO:0005840 | ribosome |
| Cellular Component | GO:0032587 | ruffle membrane |
| Molecular Function | GO:0140078 | class I DNA-(apurinic or apyrimidinic site) endonuclease activity |
| Molecular Function | GO:0003684 | damaged DNA binding |
| Molecular Function | GO:0003677 | DNA binding |
| Molecular Function | GO:0004520 | DNA endonuclease activity |
| Molecular Function | GO:0003906 | DNA-(apurinic or apyrimidinic site) endonuclease activity |
| Molecular Function | GO:0001228 | DNA-binding transcription activator activity, RNA polymerase II-specific |
| Molecular Function | GO:0140297 | DNA-binding transcription factor binding |
| Molecular Function | GO:0019899 | enzyme binding |
| Molecular Function | GO:0051879 | Hsp90 protein binding |
| Molecular Function | GO:0051536 | iron-sulfur cluster binding |
| Molecular Function | GO:0019900 | kinase binding |
| Molecular Function | GO:0008017 | microtubule binding |
| Molecular Function | GO:0003729 | mRNA binding |
| Molecular Function | GO:0032357 | oxidized purine DNA binding |
| Molecular Function | GO:0032358 | oxidized pyrimidine DNA binding |
| Molecular Function | GO:0051018 | protein kinase A binding |
| Molecular Function | GO:0019901 | protein kinase binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0070181 | small ribosomal subunit rRNA binding |
| Molecular Function | GO:0003735 | structural constituent of ribosome |
| Molecular Function | GO:0097100 | supercoiled DNA binding |
| Molecular Function | GO:0015631 | tubulin binding |
| Molecular Function | GO:0044390 | ubiquitin-like protein conjugating enzyme binding |
| Biological Process | GO:0006915 | apoptotic process |
| Biological Process | GO:0006284 | base-excision repair |
| Biological Process | GO:0051301 | cell division |
| Biological Process | GO:0070301 | cellular response to hydrogen peroxide |
| Biological Process | GO:0034614 | cellular response to reactive oxygen species |
| Biological Process | GO:0007059 | chromosome segregation |
| Biological Process | GO:0002181 | cytoplasmic translation |
| Biological Process | GO:0002183 | cytoplasmic translational initiation |
| Biological Process | GO:0006974 | DNA damage response |
| Biological Process | GO:0006281 | DNA repair |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Biological Process | GO:0045738 | negative regulation of DNA repair |
| Biological Process | GO:0031397 | negative regulation of protein ubiquitination |
| Biological Process | GO:0017148 | negative regulation of translation |
| Biological Process | GO:2001235 | positive regulation of apoptotic signaling pathway |
| Biological Process | GO:1905053 | positive regulation of base-excision repair |
| Biological Process | GO:0045739 | positive regulation of DNA repair |
| Biological Process | GO:2000144 | positive regulation of DNA-templated transcription initiation |
| Biological Process | GO:0010628 | positive regulation of gene expression |
| Biological Process | GO:1902231 | positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage |
| Biological Process | GO:0031116 | positive regulation of microtubule polymerization |
| Biological Process | GO:1901224 | positive regulation of non-canonical NF-kappaB signal transduction |
| Biological Process | GO:0042981 | regulation of apoptotic process |
| Biological Process | GO:0061481 | response to TNF agonist |
| Biological Process | GO:0051225 | spindle assembly |
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] 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.