RPLP1

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Ribosomal protein, large, P1
Identifiers
Symbols RPLP1 ; P1; FLJ27448; RPP1
External IDs Template:OMIM5 Template:MGI HomoloGene37388
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, large, P1, also known as RPLP1, is a human gene.[1]

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 phosphoprotein that is a component of the 60S subunit. The protein, which is a functional equivalent of the E. coli L7/L12 ribosomal protein, belongs to the L12P family of ribosomal proteins. It plays an important role in the elongation step of protein synthesis. Unlike most ribosomal proteins, which are basic, the encoded protein is acidic. Its C-terminal end is nearly identical to the C-terminal ends of the ribosomal phosphoproteins P0 and P2. The P1 protein can interact with P0 and P2 to form a pentameric complex consisting of P1 and P2 dimers, and a P0 monomer. The protein is located in the cytoplasm. Two alternatively spliced transcript variants that encode different proteins have been observed. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.[1]

References

  1. 1.0 1.1 "Entrez Gene: RPLP1 ribosomal protein, large, P1".

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.
  • Rich BE, Steitz JA (1988). "Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of cDNA clones, in vitro synthesis, and assembly". Mol. Cell. Biol. 7 (11): 4065–74. PMID 3323886.
  • Kato S, Sekine S, Oh SW; et al. (1995). "Construction of a human full-length cDNA bank". Gene. 150 (2): 243–50. PMID 7821789.
  • Tchórzewski M, Boldyreff B, Issinger O, Grankowski N. "Analysis of the protein-protein interactions between the human acidic ribosomal P-proteins: evaluation by the two hybrid system". Int. J. Biochem. Cell Biol. 32 (7): 737–46. PMID 10856704.
  • Chan SH, Hung FS, Chan DS, Shaw PC (2001). "Trichosanthin interacts with acidic ribosomal proteins P0 and P1 and mitotic checkpoint protein MAD2B". Eur. J. Biochem. 268 (7): 2107–12. PMID 11277934.
  • Uechi T, Tanaka T, Kenmochi N (2001). "A complete map of the human ribosomal protein genes: assignment of 80 genes to the cytogenetic map and implications for human disorders". Genomics. 72 (3): 223–30. doi:10.1006/geno.2000.6470. PMID 11401437.
  • Yoshihama M, Uechi T, Asakawa S; et al. (2002). "The human ribosomal protein genes: sequencing and comparative analysis of 73 genes". Genome Res. 12 (3): 379–90. doi:10.1101/gr.214202. PMID 11875025.
  • Kang MJ, Ahn HS, Lee JY; et al. (2002). "Up-regulation of PDCD4 in senescent human diploid fibroblasts". Biochem. Biophys. Res. Commun. 293 (1): 617–21. doi:10.1016/S0006-291X(02)00264-4. PMID 12054647.
  • 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.
  • Tchórzewski M, Krokowski D, Rzeski W; et al. (2003). "The subcellular distribution of the human ribosomal "stalk" components: P1, P2 and P0 proteins". Int. J. Biochem. Cell Biol. 35 (2): 203–11. PMID 12479870.
  • Shu H, Chen S, Bi Q; et al. (2004). "Identification of phosphoproteins and their phosphorylation sites in the WEHI-231 B lymphoma cell line". Mol. Cell Proteomics. 3 (3): 279–86. doi:10.1074/mcp.D300003-MCP200. PMID 14729942.
  • Giorgianni F, Beranova-Giorgianni S, Desiderio DM (2004). "Identification and characterization of phosphorylated proteins in the human pituitary". Proteomics. 4 (3): 587–98. doi:10.1002/pmic.200300584. PMID 14997482.
  • 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.
  • Tao WA, Wollscheid B, O'Brien R; et al. (2005). "Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry". Nat. Methods. 2 (8): 591–8. doi:10.1038/nmeth776. PMID 16094384.
  • Gevaert K, Staes A, Van Damme J; et al. (2006). "Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC". Proteomics. 5 (14): 3589–99. doi:10.1002/pmic.200401217. PMID 16097034.
  • Stelzl U, Worm U, Lalowski M; et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070.
  • Rual JF, Venkatesan K, Hao T; et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
  • Nousiainen M, Silljé HH, Sauer G; et al. (2006). "Phosphoproteome analysis of the human mitotic spindle". Proc. Natl. Acad. Sci. U.S.A. 103 (14): 5391–6. doi:10.1073/pnas.0507066103. PMID 16565220.
  • Beranova-Giorgianni S, Zhao Y, Desiderio DM, Giorgianni F. "Phosphoproteomic analysis of the human pituitary". Pituitary. 9 (2): 109–20. doi:10.1007/s11102-006-8916-x. PMID 16807684.

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