- RPS3
Ribosomal protein S3, also known as RPS3, is a human
gene .cite web | title = Entrez Gene: RPS3 ribosomal protein S3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6188| accessdate = ]PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: RPS3 ribosomal protein S3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6188| accessdate = ]References
Further reading
PBB_Further_reading
citations =
*cite journal | author=Bommer UA, Lutsch G, Stahl J, Bielka H |title=Eukaryotic initiation factors eIF-2 and eIF-3: interactions, structure and localization in ribosomal initiation complexes. |journal=Biochimie |volume=73 |issue= 7-8 |pages= 1007–19 |year= 1992 |pmid= 1742346 |doi=
*cite journal | author=Wool IG, Chan YL, Glück A |title=Structure and evolution of mammalian ribosomal proteins. |journal=Biochem. Cell Biol. |volume=73 |issue= 11-12 |pages= 933–47 |year= 1996 |pmid= 8722009 |doi=
*cite journal | author=Pogue-Geile K, Geiser JR, Shu M, "et al." |title=Ribosomal protein genes are overexpressed in colorectal cancer: isolation of a cDNA clone encoding the human S3 ribosomal protein. |journal=Mol. Cell. Biol. |volume=11 |issue= 8 |pages= 3842–9 |year= 1991 |pmid= 1712897 |doi=
*cite journal | author=Zhang XT, Tan YM, Tan YH |title=Isolation of a cDNA encoding human 40S ribosomal protein s3. |journal=Nucleic Acids Res. |volume=18 |issue= 22 |pages= 6689 |year= 1991 |pmid= 2129557 |doi=
*cite journal | author=Kim J, Chubatsu LS, Admon A, "et al." |title=Implication of mammalian ribosomal protein S3 in the processing of DNA damage. |journal=J. Biol. Chem. |volume=270 |issue= 23 |pages= 13620–9 |year= 1995 |pmid= 7775413 |doi=
*cite journal | author=Polakiewicz RD, Munroe DJ, Sait SN, "et al." |title=Mapping of ribosomal protein S3 and internally nested snoRNA U15A gene to human chromosome 11q13.3-q13.5. |journal=Genomics |volume=25 |issue= 2 |pages= 577–80 |year= 1995 |pmid= 7789996 |doi=
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=
*cite journal | author=Tycowski KT, Shu MD, Steitz JA |title=A small nucleolar RNA is processed from an intron of the human gene encoding ribosomal protein S3. |journal=Genes Dev. |volume=7 |issue= 7A |pages= 1176–90 |year= 1993 |pmid= 8319909 |doi=
*cite journal | author=Vladimirov SN, Ivanov AV, Karpova GG, "et al." |title=Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry. |journal=Eur. J. Biochem. |volume=239 |issue= 1 |pages= 144–9 |year= 1996 |pmid= 8706699 |doi=
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=
*cite journal | author=Kenmochi N, Kawaguchi T, Rozen S, "et al." |title=A map of 75 human ribosomal protein genes. |journal=Genome Res. |volume=8 |issue= 5 |pages= 509–23 |year= 1998 |pmid= 9582194 |doi=
*cite journal | author=Yoshihama M, Uechi T, Asakawa S, "et al." |title=The human ribosomal protein genes: sequencing and comparative analysis of 73 genes. |journal=Genome Res. |volume=12 |issue= 3 |pages= 379–90 |year= 2002 |pmid= 11875025 |doi= 10.1101/gr.214202
*cite journal | author=Lee CH, Kim SH, Choi JI, "et al." |title=Electron paramagnetic resonance study reveals a putative iron-sulfur cluster in human rpS3 protein. |journal=Mol. Cells |volume=13 |issue= 1 |pages= 154–6 |year= 2002 |pmid= 11911468 |doi=
*cite journal | author=Lim Y, Lee SM, Kim M, "et al." |title=Complete genomic structure of human rpS3: identification of functional U15b snoRNA in the fifth intron. |journal=Gene |volume=286 |issue= 2 |pages= 291–7 |year= 2002 |pmid= 11943484 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Bouwmeester T, Bauch A, Ruffner H, "et al." |title=A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway. |journal=Nat. Cell Biol. |volume=6 |issue= 2 |pages= 97–105 |year= 2004 |pmid= 14743216 |doi= 10.1038/ncb1086
*cite journal | author=Jang CY, Lee JY, Kim J |title=RpS3, a DNA repair endonuclease and ribosomal protein, is involved in apoptosis. |journal=FEBS Lett. |volume=560 |issue= 1-3 |pages= 81–5 |year= 2004 |pmid= 14988002 |doi= 10.1016/S0014-5793(04)00074-2
*cite journal | author=Beausoleil SA, Jedrychowski M, Schwartz D, "et al." |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130–5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101PBB_Controls
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