40S ribosomal protein S3

RPS3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1WH9, 4UG0, 4V6X, 5A2Q, 5AJ0, 3J7P, 4UJE, 4D5L, 3J7R, 4UJD, 4V5Z, 5FLX, 4D61, 4UJC
Identifiers
Aliases	RPS3 , S3, ribosomal protein S3
External IDs	OMIM: 600454; MGI: 1350917; HomoloGene: 779; GeneCards: RPS3; OMA:RPS3 - orthologs
Gene location (Human) Chr. Chromosome 11 (human) [1] Band 11q13.4 Start 75,399,515 bp [1] End 75,422,280 bp [1]
Gene location (Mouse) Chr. Chromosome 7 (mouse) [2] Band 7 E1|7 54.07 cM Start 99,127,103 bp [2] End 99,132,945 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in left ovary right ovary right uterine tube ventricular zone ganglionic eminence canal of the cervix epithelium of colon stromal cell of endometrium granulocyte body of uterus Top expressed in otic vesicle epidermis tracheobronchial tree autopod region mesenteric lymph nodes hand ovary trachea ventricular zone lactiferous gland More reference expression data BioGPS More reference expression data
Gene ontology Molecular function tubulin binding DNA N-glycosylase activity small ribosomal subunit rRNA binding iron-sulfur cluster binding transcription factor binding oxidized purine DNA binding Hsp70 protein binding lyase activity enzyme binding mRNA binding structural constituent of ribosome damaged DNA binding ubiquitin-like protein conjugating enzyme binding protein binding DNA-(apurinic or apyrimidinic site) endonuclease activity oxidized pyrimidine DNA binding endodeoxyribonuclease activity protein kinase binding supercoiled DNA binding DNA binding Hsp90 protein binding microtubule binding protein kinase A binding RNA binding kinase binding RNA polymerase II transcription regulatory region sequence-specific DNA binding protein-containing complex binding class I DNA-(apurinic or apyrimidinic site) endonuclease activity class III/IV DNA-(apurinic or apyrimidinic site) endonuclease activity oxidized purine nucleobase lesion DNA N-glycosylase activity Cellular component cytoplasm cytosol polysome membrane focal adhesion ruffle membrane mitochondrion cytoskeleton nucleus ribosome nucleolus extracellular exosome plasma membrane spindle mitochondrial matrix small ribosomal subunit mitotic spindle mitochondrial inner membrane cytosolic small ribosomal subunit nucleoplasm extracellular matrix endoplasmic reticulum NF-kappaB complex postsynaptic density ribonucleoprotein complex synapse Biological process chromosome segregation positive regulation of endodeoxyribonuclease activity cellular response to DNA damage stimulus positive regulation of microtubule polymerization cell cycle apoptotic process negative regulation of translation regulation of transcription, DNA-templated viral transcription response to TNF agonist positive regulation of apoptotic signaling pathway response to oxidative stress transcription, DNA-templated SRP-dependent cotranslational protein targeting to membrane positive regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage positive regulation of DNA N-glycosylase activity positive regulation of JUN kinase activity nuclear-transcribed mRNA catabolic process, nonsense-mediated decay negative regulation of DNA repair positive regulation of DNA repair positive regulation of NIK/NF-kappaB signaling cell division spindle assembly negative regulation of protein ubiquitination positive regulation of gene expression translational initiation regulation of translation cellular response to hydrogen peroxide protein biosynthesis positive regulation of base-excision repair DNA repair regulation of apoptotic process rRNA processing cytoplasmic translation positive regulation of protein-containing complex assembly positive regulation of interleukin-2 production positive regulation of activated T cell proliferation positive regulation of T cell receptor signaling pathway positive regulation of NF-kappaB transcription factor activity cellular response to tumor necrosis factor Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6188 27050 Ensembl ENSG00000149273 ENSMUSG00000030744 UniProt P23396 P62908 RefSeq (mRNA) NM_001260507 NM_001005 NM_001256802 NM_001260506 NM_012052 RefSeq (protein) NP_000996 NP_001243731 NP_001247435 NP_001247436 NP_036182 Location (UCSC) Chr 11: 75.4 – 75.42 Mb Chr 7: 99.13 – 99.13 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

40S ribosomal protein S3 is a protein that in humans is encoded by the RPS3 gene. ^{[5] [6] [7]}

Function

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. ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000149273 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000030744 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Pogue-Geile K, Geiser JR, Shu M, Miller C, Wool IG, Meisler AI, Pipas JM (Aug 1991). "Ribosomal protein genes are overexpressed in colorectal cancer: isolation of a cDNA clone encoding the human S3 ribosomal protein". Mol. Cell. Biol. 11 (8): 3842–9. doi:10.1128/MCB.11.8.3842. PMC   361167 . PMID   1712897.
6. Polakiewicz RD, Munroe DJ, Sait SN, Tycowski KT, Nowak NJ, Shows TB, Housman DE, Page DC (Jul 1995). "Mapping of ribosomal protein S3 and internally nested snoRNA U15A gene to human chromosome 11q13.3-q13.5". Genomics. 25 (2): 577–80. doi: 10.1016/0888-7543(95)80063-R . PMID   7789996.
7. "Entrez Gene: RPS3 ribosomal protein S3".

Further reading

• Bommer UA, Lutsch G, Stahl J, Bielka H (1992). "Eukaryotic initiation factors eIF-2 and eIF-3: interactions, structure and localization in ribosomal initiation complexes". Biochimie. 73 (7–8): 1007–19. doi:10.1016/0300-9084(91)90142-N. PMID   1742346.
• Wool IG, Chan YL, Glück A (1996). "Structure and evolution of mammalian ribosomal proteins". Biochem. Cell Biol. 73 (11–12): 933–47. doi:10.1139/o95-101. PMID   8722009.
• Zhang XT, Tan YM, Tan YH (1990). "Isolation of a cDNA encoding human 40S ribosomal protein s3". Nucleic Acids Res. 18 (22): 6689. doi:10.1093/nar/18.22.6689. PMC   332635 . PMID   2129557.
• Kim J, Chubatsu LS, Admon A, Stahl J, Fellous R, Linn S (1995). "Implication of mammalian ribosomal protein S3 in the processing of DNA damage". J. Biol. Chem. 270 (23): 13620–9. doi: 10.1074/jbc.270.23.13620 . PMID   7775413.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID   8125298.
• Tycowski KT, Shu MD, Steitz JA (1993). "A small nucleolar RNA is processed from an intron of the human gene encoding ribosomal protein S3". Genes Dev. 7 (7A): 1176–90. doi: 10.1101/gad.7.7a.1176 . PMID   8319909.
• Vladimirov SN, Ivanov AV, Karpova GG, Musolyamov AK, Egorov TA, Thiede B, Wittmann-Liebold B, Otto A (1996). "Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry". Eur. J. Biochem. 239 (1): 144–9. doi: 10.1111/j.1432-1033.1996.0144u.x . PMID   8706699.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID   9373149.
• Kenmochi N, Kawaguchi T, Rozen S, Davis E, Goodman N, Hudson TJ, Tanaka T, Page DC (1998). "A map of 75 human ribosomal protein genes". Genome Res. 8 (5): 509–23. doi: 10.1101/gr.8.5.509 . PMID   9582194.
• Yoshihama M, Uechi T, Asakawa S, Kawasaki K, Kato S, Higa S, Maeda N, Minoshima S, Tanaka T, Shimizu N, Kenmochi N (2002). "The human ribosomal protein genes: sequencing and comparative analysis of 73 genes". Genome Res. 12 (3): 379–90. doi:10.1101/gr.214202. PMC   155282 . PMID   11875025.
• Lee CH, Kim SH, Choi JI, Choi JY, Lee CE, Kim J (2002). "Electron paramagnetic resonance study reveals a putative iron-sulfur cluster in human rpS3 protein". Mol. Cells. 13 (1): 154–6. doi: 10.1016/S1016-8478(23)15018-7 . PMID   11911468.
• Lim Y, Lee SM, Kim M, Lee JY, Moon EP, Lee BJ, Kim J (2002). "Complete genomic structure of human rpS3: identification of functional U15b snoRNA in the fifth intron". Gene. 286 (2): 291–7. doi:10.1016/S0378-1119(02)00502-4. PMID   11943484.
• Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, Cruciat C, Eberhard D, Gagneur J, Ghidelli S, Hopf C, Huhse B, Mangano R, Michon AM, Schirle M, Schlegl J, Schwab M, Stein MA, Bauer A, Casari G, Drewes G, Gavin AC, Jackson DB, Joberty G, Neubauer G, Rick J, Kuster B, Superti-Furga G (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID   14743216. S2CID   11683986.
• Jang CY, Lee JY, Kim J (2004). "RpS3, a DNA repair endonuclease and ribosomal protein, is involved in apoptosis". FEBS Lett. 560 (1–3): 81–5. Bibcode:2004FEBSL.560...81J. doi: 10.1016/S0014-5793(04)00074-2 . PMID   14988002. S2CID   27640563.
• Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi: 10.1073/pnas.0404720101 . PMC   514446 . PMID   15302935.