40S ribosomal protein S2
The RPS2 gene is the gene which, in humans, encodes the 40S ribosomal protein S2.[5][6]
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.[6]
Interactions
[edit]RPS2 has been shown to interact with PRMT3.[7]
References
[edit]- ^ a b c GRCh38: Ensembl release 89: ENSG00000140988 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000044533 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Kenmochi N, Kawaguchi T, Rozen S, Davis E, Goodman N, Hudson TJ, Tanaka T, Page DC (Aug 1998). "A map of 75 human ribosomal protein genes". Genome Res. 8 (5): 509–23. doi:10.1101/gr.8.5.509. PMID 9582194.
- ^ a b "Entrez Gene: RPS2 ribosomal protein S2".
- ^ Choi, Seeyoung; Jung Cho-Rok; Kim Jin-Young; Im Dong-Soo (Sep 2008). "PRMT3 inhibits ubiquitination of ribosomal protein S2 and together forms an active enzyme complex". Biochim. Biophys. Acta. 1780 (9): 1062–9. doi:10.1016/j.bbagen.2008.05.010. ISSN 0006-3002. PMID 18573314.
Further reading
[edit]- 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.
- 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. doi:10.1093/nar/18.3.681. PMC 333503. PMID 2308862.
- 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. doi:10.1111/j.1432-1033.1996.0144u.x. PMID 8706699.
- 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. doi:10.1093/bioinformatics/17.12.1152. PMID 11751223.
- 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:10.18388/abp.2002_3770. PMID 12422231.
- 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- 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. doi:10.1046/j.0001-2815.2002.00009.x. PMID 12694581.
- 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. Bibcode:2004CBio...14.1436J. doi:10.1016/j.cub.2004.07.051. PMID 15324660. S2CID 2371325.
- 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. PMC 1134769. PMID 15473865.
- 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. PMC 528928. PMID 15489334.
- Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID 15635413. S2CID 4344740.
- 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. PMC 2253395. PMID 15883184.
- 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.
- 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.
- 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. S2CID 14294292.
- 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. S2CID 7827573.
External links
[edit]- Overview of all the structural information available in the PDB for UniProt: P15880 (40S ribosomal protein S2) at the PDBe-KB.
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