RPS2

Ribosomal protein S2
Identifiers
Symbols	RPS2 ; LLREP3; MGC102851; MGC117344; MGC117345
External IDs	Template:OMIM5 Template:MGI HomoloGene: 37714
Gene ontology Molecular function Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Ribosomal protein S2, also known as RPS2, is a human gene.

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.

Further reading

• Wool IG, Chan YL, Glück A (1996). "Structure and evolution of mammalian ribosomal proteins". Biochem. Cell Biol. 73 (11–12): 933–47. PMID 8722009.CS1 maint: Multiple names: authors list (link)
• Slynn G, Jenner D, Potts W; et al. (1990). "Human cDNA sequence homologous to the mouse LLRep3 gene family". Nucleic Acids Res. 18 (3): 681. PMID 2308862.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Vladimirov SN, Ivanov AV, Karpova GG; et al. (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. PMID 8706699.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Kenmochi N, Kawaguchi T, Rozen S; et al. (1998). "A map of 75 human ribosomal protein genes". Genome Res. 8 (5): 509–23. PMID 9582194.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Bortoluzzi S, d'Alessi F, Romualdi C, Danieli GA (2002). "Differential expression of genes coding for ribosomal proteins in different human tissues". Bioinformatics. 17 (12): 1152–7. PMID 11751223.CS1 maint: Multiple names: authors list (link)
• Kowalczyk P, Woszczyński M, Ostrowski J (2003). "Increased expression of ribosomal protein S2 in liver tumors, posthepactomized livers, and proliferating hepatocytes in vitro". Acta Biochim. Pol. 49 (3): 615–24. doi:024903615 . PMID 12422231.CS1 maint: Multiple names: authors list (link)
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Koga M, Shichijo S, Yamada A; et al. (2004). "Identification of ribosomal proteins S2 and L10a as tumor antigens recognized by HLA-A26-restricted CTL". Tissue Antigens. 61 (2): 136–45. PMID 12694581.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Jin J, Smith FD, Stark C; et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Swiercz R, Person MD, Bedford MT (2005). "Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3)". Biochem. J. 386 (Pt 1): 85–91. doi:10.1042/BJ20041466. PMID 15473865.CS1 maint: Multiple names: authors list (link)
• Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Andersen JS, Lam YW, Leung AK; et al. (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Yu Y, Ji H, Doudna JA, Leary JA (2005). "Mass spectrometric analysis of the human 40S ribosomal subunit: native and HCV IRES-bound complexes". Protein Sci. 14 (6): 1438–46. doi:10.1110/ps.041293005. PMID 15883184.CS1 maint: Multiple names: authors list (link)
• Antoine M, Reimers K, Wirz W; et al. (2005). "Identification of an unconventional nuclear localization signal in human ribosomal protein S2". Biochem. Biophys. Res. Commun. 335 (1): 146–53. doi:10.1016/j.bbrc.2005.07.069. PMID 16061210.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Antoine M, Reimers K, Wirz W; et al. (2006). "Fibroblast growth factor 3, a protein with a dual subcellular fate, is interacting with human ribosomal protein S2". Biochem. Biophys. Res. Commun. 338 (2): 1248–55. doi:10.1016/j.bbrc.2005.10.079. PMID 16263090.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Beausoleil SA, Villén J, Gerber SA; et al. (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nat. Biotechnol. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Olsen JV, Blagoev B, Gnad F; et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)