RPS3 Gene

HGNC Family	S ribosomal proteins (RPS)
Name	ribosomal protein S3
Description	Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 40S subunit, where it forms part of the domain where translation is initiated. The protein belongs to the S3P family of ribosomal proteins. Studies of the mouse and rat proteins have demonstrated that the protein has an extraribosomal role as an endonuclease involved in the repair of UV-induced DNA damage. The protein appears to be located in both the cytoplasm and nucleus but not in the nucleolus. Higher levels of expression of this gene in colon adenocarcinomas and adenomatous polyps compared to adjacent normal colonic mucosa have been observed. This gene is co-transcribed with the small nucleolar RNA genes U15A and U15B, which are located in its first and fifth introns, respectively. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, May 2012]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nRPS3 is a multifunctional protein that, beyond its canonical role as a component of the 40S ribosomal subunit, serves as an essential regulatory factor in NF‐κB signaling. It directly interacts with NF‐κB subunits (such as p65) to enhance DNA binding and achieve selective transcription of key target genes involved in immune and stress responses. In response to lymphocytic and inflammatory stimuli, RPS3 translocates to the nucleus to form NF‐κB complexes, a process that is finely tuned by phosphorylation events and can be subverted by pathogenic virulence factors to modulate host immunity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "8"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to modulating transcription, RPS3 plays a critical role in maintaining genomic integrity. It exhibits intrinsic DNA repair endonuclease (AP lyase) activity and shows a high binding affinity for oxidatively modified bases, such as 7,8‑dihydro‑8‑oxoguanine and apurinic/apyrimidinic sites. RPS3 acts as an accessory factor in base excision repair by interacting with repair enzymes like OGG1, APE/Ref‑1, and uracil‑DNA glycosylase, thereby facilitating lesion processing. Furthermore, RPS3 can function as a pro‑apoptotic factor by engaging with proteins such as TRADD and caspase‑dependent pathways to sensitize cells to genotoxic stress."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "9", "end_ref": "16"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nWithin the translational machinery, RPS3 is indispensable for efficient protein synthesis. It contributes to the formation and function of the 40S ribosomal subunit by interacting with mRNA near the entry channel, thereby facilitating the scanning and accurate selection of the initiation codon. Its role in translation is further regulated by post‑translational modifications—such as arginine methylation, phosphorylation, and sumoylation—which determine whether RPS3 remains engaged in the ribosome or functions extraribosomally. Moreover, RPS3 can exert autoregulation by binding to its own mRNA, thereby controlling its translation and ensuring appropriate ribosomal composition."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "17", "end_ref": "22"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in transcription, DNA repair, and translation, RPS3 contributes to diverse cellular processes linked to cell proliferation, mitosis, and oncogenesis. It is implicated in the regulation of mitotic spindle dynamics, and its phosphorylation by kinases such as PKCδ and Lyn shifts its functional balance toward DNA repair or the modulation of drug‐resistance pathways. Aberrant expression, post‑translational modifications, or mislocalization of RPS3 have been correlated with enhanced tumor cell survival, radioresistance, and metastatic potential in cancers including colon, osteosarcoma, melanoma, and glioblastoma. In cancer cells, extracellular secretion (often governed by glycosylation and fucosylation processes) and exploitation by viral proteins (such as HIV‑1 Tat and SARS‑CoV‑2 NSP1) further underscore its emerging role in pathogenesis and host–pathogen interactions."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "23", "end_ref": "38"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Fengyi Wan, D Eric Anderson, Robert A Barnitz, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Ribosomal protein S3: a KH domain subunit in NF-kappaB complexes that mediates selective gene regulation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.cell.2007.10.009"}], "href": "https://doi.org/10.1016/j.cell.2007.10.009"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18045535"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18045535"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Sridevi Yadavilli, Lindsey D Mayo, Maureen Higgins, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Ribosomal protein S3: A multi-functional protein that interacts with both p53 and MDM2 through its KH domain."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "DNA Repair (Amst) (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.dnarep.2009.07.003"}], "href": "https://doi.org/10.1016/j.dnarep.2009.07.003"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19656744"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19656744"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Eun Hee Ahn, Dae Won Kim, Hye Won Kang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Transduced PEP-1-ribosomal protein S3 (rpS3) ameliorates 12-O-tetradecanoylphorbol-13-acetate-induced inflammation in mice."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Toxicology (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.tox.2010.08.004"}], "href": "https://doi.org/10.1016/j.tox.2010.08.004"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20709134"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20709134"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Fengyi Wan, Amanda Weaver, Xiaofei Gao, et al. "}, {"type": "b", "children": [{"type": "t", "text": "IKKβ phosphorylation regulates RPS3 nuclear translocation and NF-κB function during infection with Escherichia coli strain O157:H7."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Immunol (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ni.2007"}], "href": "https://doi.org/10.1038/ni.2007"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21399639"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21399639"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Eric M Wier, Jordan Neighoff, Xin Sun, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Identification of an N-terminal truncation of the NF-κB p65 subunit that specifically modulates ribosomal protein S3-dependent NF-κB gene expression."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M112.388694"}], "href": "https://doi.org/10.1074/jbc.M112.388694"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23115242"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23115242"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Eric M Wier, Kai Fu, Andrea Hodgson, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Caspase-3 cleaved p65 fragment dampens NF-κB-mediated anti-apoptotic transcription by interfering with the p65/RPS3 interaction."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FEBS Lett (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.febslet.2015.10.019"}], "href": "https://doi.org/10.1016/j.febslet.2015.10.019"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26526615"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26526615"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Xiang He, He-Wei Jiang, Hong Chen, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Systematic Identification of "}, {"type": "a", "children": [{"type": "t", "text": "i"}], "href": "i"}, {"type": "t", "text": "Mycobacterium tuberculosis"}, {"type": "a", "children": [{"type": "t", "text": "/i"}], "href": "/i"}, {"type": "t", "text": " Effectors Reveals that BfrB Suppresses Innate Immunity."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Proteomics (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/mcp.RA117.000296"}], "href": "https://doi.org/10.1074/mcp.RA117.000296"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29018126"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29018126"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Hisako Ono, Yosuke Iizumi, Wakana Goi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Ribosomal protein S3 regulates XIAP expression independently of the NF-κB pathway in breast cancer cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncol Rep (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.3892/or.2017.6008"}], "href": "https://doi.org/10.3892/or.2017.6008"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29048653"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29048653"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Chang Hoon Lee, Sang Hwa Kim, Jun Il Choi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Electron paramagnetic resonance study reveals a putative iron-sulfur cluster in human rpS3 protein."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cells (2002)"}]}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11911468"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11911468"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Chang-Young Jang, Jae Yung Lee, Joon Kim "}, {"type": "b", "children": [{"type": "t", "text": "RpS3, a DNA repair endonuclease and ribosomal protein, is involved in apoptosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FEBS Lett (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/S0014-5793(04)00074-2"}], "href": "https://doi.org/10.1016/S0014-5793(04"}, {"type": "t", "text": "00074-2) PMID: "}, {"type": "a", "children": [{"type": "t", "text": "14988002"}], "href": "https://pubmed.ncbi.nlm.nih.gov/14988002"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Vijay Hegde, Mu Wang, Walter A Deutsch "}, {"type": "b", "children": [{"type": "t", "text": "Human ribosomal protein S3 interacts with DNA base excision repair proteins hAPE/Ref-1 and hOGG1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochemistry (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1021/bi049234b"}], "href": "https://doi.org/10.1021/bi049234b"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15518571"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15518571"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Vijay Hegde, Mu Wang, I Saira Mian, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The high binding affinity of human ribosomal protein S3 to 7,8-dihydro-8-oxoguanine is abrogated by a single amino acid change."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "DNA Repair (Amst) (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.dnarep.2006.04.001"}], "href": "https://doi.org/10.1016/j.dnarep.2006.04.001"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16737853"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16737853"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Soo Hyun Choi, So Young Kim, Jae Jin An, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Human PEP-1-ribosomal protein S3 protects against UV-induced skin cell death."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FEBS Lett (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.febslet.2006.11.038"}], "href": "https://doi.org/10.1016/j.febslet.2006.11.038"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17140567"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17140567"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Sung Il Ko, Jong-Hwa Park, Min Ju Park, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Human ribosomal protein S3 (hRpS3) interacts with uracil-DNA glycosylase (hUNG) and stimulates its glycosylase activity."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mutat Res (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.mrfmmm.2008.09.013"}], "href": "https://doi.org/10.1016/j.mrfmmm.2008.09.013"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18973764"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18973764"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Chang-Young Jang, Hag Dong Kim, Joon Kim "}, {"type": "b", "children": [{"type": "t", "text": "Ribosomal protein S3 interacts with TRADD to induce apoptosis through caspase dependent JNK activation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbrc.2012.04.020"}], "href": "https://doi.org/10.1016/j.bbrc.2012.04.020"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22510408"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22510408"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "YongJoong Kim, Hag Dong Kim, Joon Kim "}, {"type": "b", "children": [{"type": "t", "text": "Cytoplasmic ribosomal protein S3 (rpS3) plays a pivotal role in mitochondrial DNA damage surveillance."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochim Biophys Acta (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbamcr.2013.07.015"}], "href": "https://doi.org/10.1016/j.bbamcr.2013.07.015"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23911537"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23911537"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Hyun-Seock Shin, Chang-Young Jang, Hag Dong Kim, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Arginine methylation of ribosomal protein S3 affects ribosome assembly."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbrc.2009.05.055"}], "href": "https://doi.org/10.1016/j.bbrc.2009.05.055"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19460357"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19460357"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Hag Dong Kim, Tae-Sung Kim, Yoo Jin Joo, et al. "}, {"type": "b", "children": [{"type": "t", "text": "RpS3 translation is repressed by interaction with its own mRNA."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Biochem (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/jcb.22537"}], "href": "https://doi.org/10.1002/jcb.22537"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20217897"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20217897"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Dmitri Graifer, Alexey Malygin, Dmitry O Zharkov, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Eukaryotic ribosomal protein S3: A constituent of translational machinery and an extraribosomal player in various cellular processes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochimie (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.biochi.2013.11.001"}], "href": "https://doi.org/10.1016/j.biochi.2013.11.001"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24239944"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24239944"}]}, {"type": "r", "ref": 20, "children": [{"type": "t", "text": "Ora Haimov, Hadar Sinvani, Franck Martin, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Efficient and Accurate Translation Initiation Directed by TISU Involves RPS3 and RPS10e Binding and Differential Eukaryotic Initiation Factor 1A Regulation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biol (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/MCB.00150-17"}], "href": "https://doi.org/10.1128/MCB.00150-17"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28584194"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28584194"}]}, {"type": "r", "ref": 21, "children": [{"type": "t", "text": "Elena Babaylova, Alexey Malygin, Alexander Gopanenko, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Tetrapeptide 60-63 of human ribosomal protein uS3 is crucial for translation initiation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochim Biophys Acta Gene Regul Mech (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbagrm.2019.194411"}], "href": "https://doi.org/10.1016/j.bbagrm.2019.194411"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31356988"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31356988"}]}, {"type": "r", "ref": 22, "children": [{"type": "t", "text": "Iu S Khaĭrulina, M V Molotkov, K N Bulygin, et al. "}, {"type": "b", "children": [{"type": "t", "text": "[Protein S3 fragments neighboring mRNA during elongation and translation termination on the human ribosome]."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Bioorg Khim (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1134/s1068162008060071"}], "href": "https://doi.org/10.1134/s1068162008060071"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19088750"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19088750"}]}, {"type": "r", "ref": 23, "children": [{"type": "t", "text": "Tae-Sung Kim, Hag Dong Kim, Joon Kim "}, {"type": "b", "children": [{"type": "t", "text": "PKCdelta-dependent functional switch of rpS3 between translation and DNA repair."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochim Biophys Acta (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbamcr.2008.10.017"}], "href": "https://doi.org/10.1016/j.bbamcr.2008.10.017"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19059439"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19059439"}]}, {"type": "r", "ref": 24, "children": [{"type": "t", "text": "Chang-Young Jang, Hag Dong Kim, Xianghua Zhang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Ribosomal protein S3 localizes on the mitotic spindle and functions as a microtubule associated protein in mitosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbrc.2012.10.093"}], "href": "https://doi.org/10.1016/j.bbrc.2012.10.093"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23131551"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23131551"}]}, {"type": "r", "ref": 25, "children": [{"type": "t", "text": "Hee Jung Yang, HyeSook Youn, Ki Moon Seong, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Phosphorylation of ribosomal protein S3 and antiapoptotic TRAF2 protein mediates radioresistance in non-small cell lung cancer cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M112.385989"}], "href": "https://doi.org/10.1074/jbc.M112.385989"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23188828"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23188828"}]}, {"type": "r", "ref": 26, "children": [{"type": "t", "text": "YongJoong Kim, Hag Dong Kim, Buhyun Youn, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Ribosomal protein S3 is secreted as a homodimer in cancer cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbrc.2013.10.132"}], "href": "https://doi.org/10.1016/j.bbrc.2013.10.132"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24211576"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24211576"}]}, {"type": "r", "ref": 27, "children": [{"type": "t", "text": "Yun Tian, Lijun Qin, Huijuan Qiu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "RPS3 regulates melanoma cell growth and apoptosis by targeting Cyto C/Ca2+/MICU1 dependent mitochondrial signaling."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncotarget (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.18632/oncotarget.4868"}], "href": "https://doi.org/10.18632/oncotarget.4868"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26336993"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26336993"}]}, {"type": "r", "ref": 28, "children": [{"type": "t", "text": "YongJoong Kim, Min Seon Lee, Hag Dong Kim, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Ribosomal protein S3 (rpS3) secreted from various cancer cells is N-linked glycosylated."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncotarget (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.18632/oncotarget.10180"}], "href": "https://doi.org/10.18632/oncotarget.10180"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27384988"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27384988"}]}, {"type": "r", "ref": 29, "children": [{"type": "t", "text": "Wanyeon Kim, HyeSook Youn, Sungmin Lee, et al. "}, {"type": "b", "children": [{"type": "t", "text": "RNF138-mediated ubiquitination of rpS3 is required for resistance of glioblastoma cells to radiation-induced apoptosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Exp Mol Med (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/emm.2017.247"}], "href": "https://doi.org/10.1038/emm.2017.247"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29371697"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29371697"}]}, {"type": "r", "ref": 30, "children": [{"type": "t", "text": "Jiyoung Kim, Yeon-Soo Kim "}, {"type": "b", "children": [{"type": "t", "text": "Effect of HIV-1 Tat on the formation of the mitotic spindle by interaction with ribosomal protein S3."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Sci Rep (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41598-018-27008-w"}], "href": "https://doi.org/10.1038/s41598-018-27008-w"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29875444"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29875444"}]}, {"type": "r", "ref": 31, "children": [{"type": "t", "text": "Anastasia S Ochkasova, Maria I Meschaninova, Aliya G Venyaminova, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The human ribosome can interact with the abasic site in mRNA via a specific peptide of the uS3 protein located near the mRNA entry channel."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochimie (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.biochi.2018.12.015"}], "href": "https://doi.org/10.1016/j.biochi.2018.12.015"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30594661"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30594661"}]}, {"type": "r", "ref": 32, "children": [{"type": "t", "text": "Elie Alam, Lama Maaliki, Zeina Nasr "}, {"type": "b", "children": [{"type": "t", "text": "Ribosomal protein S3 selectively affects colon cancer growth by modulating the levels of p53 and lactate dehydrogenase."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Biol Rep (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s11033-020-05683-1"}], "href": "https://doi.org/10.1007/s11033-020-05683-1"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32748020"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32748020"}]}, {"type": "r", "ref": 33, "children": [{"type": "t", "text": "Hee Woong Yang, Youjin Jung, Hag Dong Kim, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Ribosomal protein S3-derived repair domain peptides regulate UV-induced matrix metalloproteinase-1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbrc.2020.06.094"}], "href": "https://doi.org/10.1016/j.bbrc.2020.06.094"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32828277"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32828277"}]}, {"type": "r", "ref": 34, "children": [{"type": "t", "text": "Gregory Watson, Daniel Lester, Hui Ren, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Fucosylated Proteome Profiling Identifies a Fucosylated, Non-Ribosomal, Stress-Responsive Species of Ribosomal Protein S3."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cells (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.3390/cells10061310"}], "href": "https://doi.org/10.3390/cells10061310"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "34070332"}], "href": "https://pubmed.ncbi.nlm.nih.gov/34070332"}]}, {"type": "r", "ref": 35, "children": [{"type": "t", "text": "Niphat Jirapongwattana, Suyanee Thongchot, Wannasiri Chiraphapphaiboon, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Mesothelin‑specific T cell cytotoxicity against triple negative breast cancer is enhanced by 40s ribosomal protein subunit 3‑treated self‑differentiated dendritic cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncol Rep (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.3892/or.2022.8338"}], "href": "https://doi.org/10.3892/or.2022.8338"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "35616135"}], "href": "https://pubmed.ncbi.nlm.nih.gov/35616135"}]}, {"type": "r", "ref": 36, "children": [{"type": "t", "text": "J Shi, T Zhang, Z-G Yang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "RPS3 predicts poor overall survival in HBV-related hepatocellular carcinoma patients: a data-mining with LASSO-regression algorithm."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Eur Rev Med Pharmacol Sci (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.26355/eurrev_202209_29773"}], "href": "https://doi.org/10.26355/eurrev_202209_29773"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "36196722"}], "href": "https://pubmed.ncbi.nlm.nih.gov/36196722"}]}, {"type": "r", "ref": 37, "children": [{"type": "t", "text": "Woo Sung Ahn, Hag Dong Kim, Tae Sung Kim, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Phosphorylation of rpS3 by Lyn increases translation of Multi-Drug Resistance (MDR1) gene."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "BMB Rep (2023)"}]}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "36724904"}], "href": "https://pubmed.ncbi.nlm.nih.gov/36724904"}]}, {"type": "r", "ref": 38, "children": [{"type": "t", "text": "Tal Havkin-Solomon, Elad Itzhaki, Nir Joffe, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Selective translational control of cellular and viral mRNAs by RPS3 mRNA binding."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nucleic Acids Res (2023)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/nar/gkad269"}], "href": "https://doi.org/10.1093/nar/gkad269"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "37070189"}], "href": "https://pubmed.ncbi.nlm.nih.gov/37070189"}]}]}]}
Synonyms	S3
Proteins	RS3_HUMAN
NCBI Gene ID	6188
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

RPS3 has 24,227 functional associations with biological entities spanning 9 categories (molecular profile, organism, chemical, functional term, phrase or reference, disease, phenotype or trait, structural feature, cell line, cell type or tissue, gene, protein or microRNA, sequence feature) extracted from 120 datasets.

Click the + buttons to view associations for RPS3 from the datasets below.

If available, associations are ranked by standardized value

Harmonizome 3.0

RPS3 Gene

Functional Associations

Please acknowledge the Harmonizome in your publications by citing the following reference(s):

	Dataset	Summary
	Achilles Cell Line Gene Essentiality Profiles	cell lines with fitness changed by RPS3 gene knockdown relative to other cell lines from the Achilles Cell Line Gene Essentiality Profiles dataset.
	Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles	tissues with high or low expression of RPS3 gene relative to other tissues from the Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles dataset.
	Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles	tissues with high or low expression of RPS3 gene relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.
	Allen Brain Atlas Aging Dementia and Traumatic Brain Injury Tissue Sample Gene Expression Profiles	tissue samples with high or low expression of RPS3 gene relative to other tissue samples from the Allen Brain Atlas Aging Dementia and Traumatic Brain Injury Tissue Sample Gene Expression Profiles dataset.
	Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by RNA-seq	tissue samples with high or low expression of RPS3 gene relative to other tissue samples from the Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by RNA-seq dataset.
	Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles	tissues with high or low expression of RPS3 gene relative to other tissues from the Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles dataset.
	BioGPS Cell Line Gene Expression Profiles	cell lines with high or low expression of RPS3 gene relative to other cell lines from the BioGPS Cell Line Gene Expression Profiles dataset.
	BioGPS Human Cell Type and Tissue Gene Expression Profiles	cell types and tissues with high or low expression of RPS3 gene relative to other cell types and tissues from the BioGPS Human Cell Type and Tissue Gene Expression Profiles dataset.
	BioGPS Mouse Cell Type and Tissue Gene Expression Profiles	cell types and tissues with high or low expression of RPS3 gene relative to other cell types and tissues from the BioGPS Mouse Cell Type and Tissue Gene Expression Profiles dataset.
	Carcinogenome Chemical Perturbation Carcinogenicity Signatures	small molecule perturbations changing expression of RPS3 gene from the Carcinogenome Chemical Perturbation Carcinogenicity Signatures dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of RPS3 gene relative to other cell lines from the CCLE Cell Line Gene CNV Profiles dataset.
	CCLE Cell Line Gene Expression Profiles	cell lines with high or low expression of RPS3 gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with RPS3 protein from the CCLE Cell Line Proteomics dataset.
	CellMarker Gene-Cell Type Associations	cell types associated with RPS3 gene from the CellMarker Gene-Cell Type Associations dataset.
	ChEA Transcription Factor Binding Site Profiles	transcription factor binding site profiles with transcription factor binding evidence at the promoter of RPS3 gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of RPS3 gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets dataset.
	ChEA Transcription Factor Targets 2022	transcription factors binding the promoter of RPS3 gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets 2022 dataset.
	CMAP Signatures of Differentially Expressed Genes for Small Molecules	small molecule perturbations changing expression of RPS3 gene from the CMAP Signatures of Differentially Expressed Genes for Small Molecules dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing RPS3 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing RPS3 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores	cellular components co-occuring with RPS3 protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025	cellular components co-occuring with RPS3 protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.
	CORUM Protein Complexes	protein complexs containing RPS3 protein from the CORUM Protein Complexes dataset.
	COSMIC Cell Line Gene CNV Profiles	cell lines with high or low copy number of RPS3 gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset.
	COSMIC Cell Line Gene Mutation Profiles	cell lines with RPS3 gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Chemical Interactions	chemicals interacting with RPS3 gene/protein from the curated CTD Gene-Chemical Interactions dataset.
	CTD Gene-Disease Associations	diseases associated with RPS3 gene/protein from the curated CTD Gene-Disease Associations dataset.
	DeepCoverMOA Drug Mechanisms of Action	small molecule perturbations with high or low expression of RPS3 protein relative to other small molecule perturbations from the DeepCoverMOA Drug Mechanisms of Action dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores	diseases co-occuring with RPS3 gene in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores 2025	diseases co-occuring with RPS3 gene in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.
	DisGeNET Gene-Disease Associations	diseases associated with RPS3 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.
	DisGeNET Gene-Phenotype Associations	phenotypes associated with RPS3 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Phenoptype Associations dataset.
	ENCODE Histone Modification Site Profiles	histone modification site profiles with high histone modification abundance at RPS3 gene from the ENCODE Histone Modification Site Profiles dataset.
	ENCODE Transcription Factor Binding Site Profiles	transcription factor binding site profiles with transcription factor binding evidence at the promoter of RPS3 gene from the ENCODE Transcription Factor Binding Site Profiles dataset.
	ENCODE Transcription Factor Targets	transcription factors binding the promoter of RPS3 gene in ChIP-seq datasets from the ENCODE Transcription Factor Targets dataset.
	ESCAPE Omics Signatures of Genes and Proteins for Stem Cells	PubMedIDs of publications reporting gene signatures containing RPS3 from the ESCAPE Omics Signatures of Genes and Proteins for Stem Cells dataset.
	GDSC Cell Line Gene Expression Profiles	cell lines with high or low expression of RPS3 gene relative to other cell lines from the GDSC Cell Line Gene Expression Profiles dataset.
	GeneRIF Biological Term Annotations	biological terms co-occuring with RPS3 gene in literature-supported statements describing functions of genes from the GeneRIF Biological Term Annotations dataset.
	GeneSigDB Published Gene Signatures	PubMedIDs of publications reporting gene signatures containing RPS3 from the GeneSigDB Published Gene Signatures dataset.
	GEO Signatures of Differentially Expressed Genes for Diseases	disease perturbations changing expression of RPS3 gene from the GEO Signatures of Differentially Expressed Genes for Diseases dataset.