RPLP0

RPLP0
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4V6X, 5AJ0, 3J92, 4V5Z,%%s4V5Z, 5AJ0, 4V6X, 3J92
Identifiers
Aliases	RPLP0 , L10E, LP0, P0, PRLP0, RPP0, ribosomal protein lateral stalk subunit P0
External IDs	OMIM: 180510 MGI: 1927636 HomoloGene: 6517 GeneCards: RPLP0
Gene location (Human) Chr. Chromosome 12 (human) [1] Band 12q24.23 Start 120,196,699 bp [1] End 120,201,235 bp [1]
Gene location (Mouse) Chr. Chromosome 5 (mouse) [2] Band 5|5 F Start 115,559,467 bp [2] End 115,563,727 bp [2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0001948 protein binding • structural constituent of ribosome • RNA binding • large ribosomal subunit rRNA binding • peptide binding Cellular component • ribosome • focal adhesion • intracellular anatomical structure • cytoplasmic ribonucleoprotein granule • cytosolic large ribosomal subunit • extracellular exosome • cytoplasm • nucleus • endoplasmic reticulum • cytosol • membrane • GO:0097483, GO:0097481 postsynaptic density • postsynapse • ribonucleoprotein complex • dendrite • synapse Biological process • ribosome biogenesis • viral transcription • SRP-dependent cotranslational protein targeting to membrane • translational initiation • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay • protein biosynthesis • rRNA processing • GO:0022415 viral process • interleukin-12-mediated signaling pathway • ribosomal large subunit assembly • cytoplasmic translation • lactation • response to selenium ion • cellular response to cAMP • cellular response to interleukin-4 • cellular response to Thyroid stimulating hormone • cellular response to phorbol 13-acetate 12-myristate Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	6175	11837
Ensembl	ENSG00000089157	ENSMUSG00000067274
UniProt	P05388	P14869
RefSeq (mRNA)	NM_053275 NM_001002	NM_007475
RefSeq (protein)	NP_000993 NP_444505 NP_000993.1 NP_444505.1	NP_031501
Location (UCSC)	Chr 12: 120.2 – 120.2 Mb	Chr 5: 115.56 – 115.56 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

60S acidic ribosomal protein P0 is a protein that in humans is encoded by the RPLP0 gene. ^{[5] [6]}

Ribosomes catalyze protein synthesis and 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 60S subunit. The protein, which is the functional equivalent of the E. coli L10 ribosomal protein, belongs to the L10P family of ribosomal proteins. It is a neutral phosphoprotein with a C-terminal end that is nearly identical to the C-terminal ends of the acidic ribosomal phosphoproteins P1 and P2. The P0 protein can interact with P1 and P2 to form a pentameric complex consisting of P1 and P2 dimers, and a P0 monomer. The protein is located in the cytoplasm. Transcript variants derived from alternative splicing exist; they encode the same protein. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome. ^[6]

References

1. GRCh38: Ensembl release 89: ENSG00000089157 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000067274 - 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: RPLP0 ribosomal protein, large, P0".

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.
• Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID   1602151.
• 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. doi:10.1128/mcb.7.11.4065. PMC   368077 . PMID   3323886.
• Towbin H, Ramjoué HP, Kuster H, et al. (1982). "Monoclonal antibodies against eucaryotic ribosomes. Use to characterize a ribosomal protein not previously identified and antigenically related to the acidic phosphoproteins P1/P2". J. Biol. Chem. 257 (21): 12709–15. doi: 10.1016/S0021-9258(18)33569-5 . PMID   6182142.
• Kato S, Sekine S, Oh SW, et al. (1995). "Construction of a human full-length cDNA bank". Gene. 150 (2): 243–50. doi:10.1016/0378-1119(94)90433-2. PMID   7821789.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID   8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID   9373149.
• <Please add first missing authors to populate metadata.> (1999). "Toward a complete human genome sequence". Genome Res. 8 (11): 1097–108. doi: 10.1101/gr.8.11.1097 . PMID   9847074.
• Tchórzewski 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): 737–46. doi:10.1016/S1357-2725(00)00017-0. 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. doi: 10.1046/j.1432-1327.2001.02091.x . 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.
• Andersen JS, Lyon CE, Fox AH, et al. (2002). "Directed proteomic analysis of the human nucleolus". Curr. Biol. 12 (1): 1–11. doi: 10.1016/S0960-9822(01)00650-9 . PMID   11790298. S2CID   14132033.
• 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 . PMC   139241 . 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. doi:10.1016/S1357-2725(02)00133-4. PMID   12479870.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi: 10.1038/ng1285 . PMID   14702039.
• 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.
• Bouwmeester T, Bauch A, Ruffner H, et al. (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID   14743216. S2CID   11683986.
• Villacé P, Marión RM, Ortín J (2004). "The composition of Staufen-containing RNA granules from human cells indicates their role in the regulated transport and translation of messenger RNAs". Nucleic Acids Res. 32 (8): 2411–20. doi:10.1093/nar/gkh552. PMC   419443 . PMID   15121898.