RPLP2

Ribosomal protein, large, P2
Rendering of RPLP2 from PDB 1S4J​
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1S4J​, 2JDL​, 2LBF​, 2W1O​, 4BEH​, 4V6X​
Identifiers
Symbols	RPLP2 ; D11S2243E; LP2; P2; RPP2
External IDs	OMIM: 180530 HomoloGene: 133574 GeneCards: RPLP2 Gene
Gene ontology Molecular function • RNA binding • structural constituent of ribosome Cellular component • cytosol • focal adhesion • membrane • cytosolic large ribosomal subunit • extracellular exosome Biological process • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay • translation • translational initiation • translational elongation • translational termination • SRP-dependent cotranslational protein targeting to membrane • gene expression • viral process • viral life cycle • viral transcription • cellular protein metabolic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	6181	67186
Ensembl	ENSG00000177600	ENSMUSG00000025508
UniProt	P05387	P99027
RefSeq (mRNA)	NM_001004	NM_026020
RefSeq (protein)	NP_000995	NP_080296
Location (UCSC)	Chr 11: 0.81 – 0.81 Mb	Chr 7: 141.45 – 141.45 Mb
PubMed search

60S acidic ribosomal protein P2 is a protein that in humans is encoded by the RPLP2 gene.^[1][2]

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 P1. The P2 protein can interact with P0 and P1 to form a pentameric complex consisting of P1 and P2 dimers, and a P0 monomer. The protein is located in the cytoplasm. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.^[2]

Interactions

RPLP2 has been shown to interact with RPLP1.^[3]

References

1. Rich BE, Steitz JA (March 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. PMC 368077. PMID 3323886.
2. "Entrez Gene: RPLP2 ribosomal protein, large, P2".
3. Tchórzewski, M; Boldyreff B; Issinger O G; Grankowski N (July 2000). "Analysis of the protein-protein interactions between the human acidic ribosomal P-proteins: evaluation by the two hybrid system". Int. J. Biochem. Cell Biol. (England) 32 (7): 737–746. doi:10.1016/S1357-2725(00)00017-0. PMID 10856704.

Further reading

• Wool IG, Chan YL, Gl?ck A (1996). "Structure and evolution of mammalian ribosomal proteins". Biochem. Cell Biol. 73 (11–12): 933–947. doi:10.1139/o95-101. PMID 8722009.
• Hochstrasser DF, Frutiger S, Paquet N, et al. (1993). "Human liver protein map: a reference database established by microsequencing and gel comparison". Electrophoresis 13 (12): 992–1001. doi:10.1002/elps.11501301201. PMID 1286669.
• Sharp MG, Adams SM, Elvin P, et al. (1990). "A sequence previously identified as metastasis-related encodes an acidic ribosomal phosphoprotein, P2". Br. J. Cancer 61 (1): 83–8. doi:10.1038/bjc.1990.19. PMC 1971331. PMID 2153399.
• Kato S, Sekine S, Oh SW, et al. (1995). "Construction of a human full-length cDNA bank". Gene 150 (2): 243–250. doi:10.1016/0378-1119(94)90433-2. PMID 7821789.
• Matoba R, Okubo K, Hori N, et al. (1994). "The addition of 5'-coding information to a 3'-directed cDNA library improves analysis of gene expression". Gene 146 (2): 199–207. doi:10.1016/0378-1119(94)90293-3. PMID 8076819.
• Scanlan MJ, Gordan JD, Williamson B, et al. (1999). "Antigens recognized by autologous antibody in patients with renal-cell carcinoma". Int. J. Cancer 83 (4): 456–464. doi:10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5. PMID 10508479. replacement character in |last8= at position 2 (help); replacement character in |last9= at position 2 (help)
• Tch?rzewski M, Boldyreff B, Issinger O, Grankowski N (2000). "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): 737–746. doi:10.1016/S1357-2725(00)00017-0. PMID 10856704.
• 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): 223–230. 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): 379–390. doi:10.1101/gr.214202. PMC 155282. PMID 11875025.
• Freeman JL, Gonzalo P, Pitcher JA, et al. (2002). "Beta 2-adrenergic receptor stimulated, G protein-coupled receptor kinase 2 mediated, phosphorylation of ribosomal protein P2". Biochemistry 41 (42): 12850–12857. doi:10.1021/bi020145d. PMID 12379128.
• 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): 16899–16903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Tch?rzewski 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): 203–211. doi:10.1016/S1357-2725(02)00133-4. 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): 279–286. doi:10.1074/mcp.D300003-MCP200. PMID 14729942.
• Gardner-Thorpe J, Ito H, Ashley SW, Whang EE (2004). "Ribosomal protein P2: a potential molecular target for antisense therapy of human malignancies". Anticancer Res. 23 (6C): 4549–60. PMID 14981896.
• Giorgianni F, Beranova-Giorgianni S, Desiderio DM (2004). "Identification and characterization of phosphorylated proteins in the human pituitary". Proteomics 4 (3): 587–598. doi:10.1002/pmic.200300584. PMID 14997482.
• Brandenberger R, Wei H, Zhang S, et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–716. doi:10.1038/nbt971. PMID 15146197.
• 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): 2121–2127. 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. doi:10.1038/nature03207. PMID 15635413.