RPS2

RPS2

Ribosomal protein S2, also known as RPS2, is a human gene.cite web | title = Entrez Gene: RPS2 ribosomal protein S2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6187| 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. The protein belongs to the S5P family of ribosomal proteins. It is located in the cytoplasm. This gene shares sequence similarity with mouse LLRep3. It is co-transcribed with the small nucleolar RNA gene U64, which is located in its third intron. 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: RPS2 ribosomal protein S2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6187| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*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=Slynn G, Jenner D, Potts W, "et al." |title=Human cDNA sequence homologous to the mouse LLRep3 gene family. |journal=Nucleic Acids Res. |volume=18 |issue= 3 |pages= 681 |year= 1990 |pmid= 2308862 |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=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=Bortoluzzi S, d'Alessi F, Romualdi C, Danieli GA |title=Differential expression of genes coding for ribosomal proteins in different human tissues. |journal=Bioinformatics |volume=17 |issue= 12 |pages= 1152–7 |year= 2002 |pmid= 11751223 |doi=
*cite journal | author=Kowalczyk P, Woszczyński M, Ostrowski J |title=Increased expression of ribosomal protein S2 in liver tumors, posthepactomized livers, and proliferating hepatocytes in vitro. |journal=Acta Biochim. Pol. |volume=49 |issue= 3 |pages= 615–24 |year= 2003 |pmid= 12422231 |doi= 024903615
*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=Koga M, Shichijo S, Yamada A, "et al." |title=Identification of ribosomal proteins S2 and L10a as tumor antigens recognized by HLA-A26-restricted CTL. |journal=Tissue Antigens |volume=61 |issue= 2 |pages= 136–45 |year= 2004 |pmid= 12694581 |doi=
*cite journal | author=Jin J, Smith FD, Stark C, "et al." |title=Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization. |journal=Curr. Biol. |volume=14 |issue= 16 |pages= 1436–50 |year= 2004 |pmid= 15324660 |doi= 10.1016/j.cub.2004.07.051
*cite journal | author=Swiercz R, Person MD, Bedford MT |title=Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3). |journal=Biochem. J. |volume=386 |issue= Pt 1 |pages= 85–91 |year= 2005 |pmid= 15473865 |doi= 10.1042/BJ20041466
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Andersen JS, Lam YW, Leung AK, "et al." |title=Nucleolar proteome dynamics. |journal=Nature |volume=433 |issue= 7021 |pages= 77–83 |year= 2005 |pmid= 15635413 |doi= 10.1038/nature03207
*cite journal | author=Yu Y, Ji H, Doudna JA, Leary JA |title=Mass spectrometric analysis of the human 40S ribosomal subunit: native and HCV IRES-bound complexes. |journal=Protein Sci. |volume=14 |issue= 6 |pages= 1438–46 |year= 2005 |pmid= 15883184 |doi= 10.1110/ps.041293005
*cite journal | author=Antoine M, Reimers K, Wirz W, "et al." |title=Identification of an unconventional nuclear localization signal in human ribosomal protein S2. |journal=Biochem. Biophys. Res. Commun. |volume=335 |issue= 1 |pages= 146–53 |year= 2005 |pmid= 16061210 |doi= 10.1016/j.bbrc.2005.07.069
*cite journal | author=Antoine M, Reimers K, Wirz W, "et al." |title=Fibroblast growth factor 3, a protein with a dual subcellular fate, is interacting with human ribosomal protein S2. |journal=Biochem. Biophys. Res. Commun. |volume=338 |issue= 2 |pages= 1248–55 |year= 2006 |pmid= 16263090 |doi= 10.1016/j.bbrc.2005.10.079
*cite journal | author=Beausoleil SA, Villén J, Gerber SA, "et al." |title=A probability-based approach for high-throughput protein phosphorylation analysis and site localization. |journal=Nat. Biotechnol. |volume=24 |issue= 10 |pages= 1285–92 |year= 2006 |pmid= 16964243 |doi= 10.1038/nbt1240
*cite journal | author=Olsen JV, Blagoev B, Gnad F, "et al." |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. |journal=Cell |volume=127 |issue= 3 |pages= 635–48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026

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