40S ribosomal protein S2

RPS2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4UG0, 4V6X, 5A2Q, 5AJ0, 5FLX, 4D61, 4D5L, 4UJD, 4UJE, 4UJC
Identifiers
Aliases	RPS2 , LLREP3, S2, ribosomal protein S2
External IDs	OMIM: 603624 MGI: 105110 HomoloGene: 37714 GeneCards: RPS2
Gene location (Human) Chr. Chromosome 16 (human) [1] Band 16p13.3 Start 1,962,058 bp [1] End 1,964,841 bp [1]
Gene location (Mouse) Chr. Chromosome 17 (mouse) [2] Band 17|17 A3.3 Start 24,937,090 bp [2] End 24,940,903 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in stromal cell of endometrium right uterine tube body of pancreas ganglionic eminence zone of skin skin of abdomen spleen lymph node canal of the cervix anterior pituitary Top expressed in lip esophagus ovary zone of skin lens ganglionic eminence ileum quadriceps femoris muscle uterus urinary bladder More reference expression data BioGPS n/a
Gene ontology Molecular function structural constituent of ribosome protein binding enzyme binding fibroblast growth factor binding mRNA binding RNA binding cadherin binding Cellular component cytosol ribosome membrane focal adhesion cytosolic small ribosomal subunit nucleolus small ribosomal subunit extracellular exosome nucleus nucleoplasm synapse Biological process viral transcription SRP-dependent cotranslational protein targeting to membrane translational initiation positive regulation of transferase activity nuclear-transcribed mRNA catabolic process, nonsense-mediated decay protein biosynthesis rRNA processing protein methylation positive regulation of ubiquitin-protein transferase activity cellular response to interleukin-4 Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6187 16898 Ensembl ENSG00000140988 ENSMUSG00000044533 UniProt P15880 P25444 RefSeq (mRNA) NM_002952 NM_008503 RefSeq (protein) NP_002943 NP_032529 Location (UCSC) Chr 16: 1.96 – 1.96 Mb Chr 17: 24.94 – 24.94 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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

RPS2 has been shown to interact with PRMT3. ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000140988 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000044533 – 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. 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.
6. "Entrez Gene: RPS2 ribosomal protein S2".
7. 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

• 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

• Overview of all the structural information available in the PDB for UniProt : P15880 (40S ribosomal protein S2) at the PDBe-KB .