RPL8

Ribosomal protein L8
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 4CCM​, 4CCN​, 4CCO​, 4V6X​, 5AJ0​
Identifiers
Symbols	RPL8 ; L8
External IDs	OMIM: 604177 MGI: 1350927 HomoloGene: 32141 GeneCards: RPL8 Gene
Gene ontology Molecular function • RNA binding • structural constituent of ribosome • rRNA binding • poly(A) RNA binding Cellular component • nucleolus • cytoplasm • cytosol • focal adhesion • membrane • cytosolic large ribosomal subunit Biological process • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay • cytoplasmic translation • 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	6132	26961
Ensembl	ENSG00000161016	ENSMUSG00000003970
UniProt	P62917	P62918
RefSeq (mRNA)	NM_000973	NM_012053
RefSeq (protein)	NP_000964	NP_036183
Location (UCSC)	Chr 8: 144.79 – 144.79 Mb	Chr 15: 76.9 – 76.91 Mb
PubMed search

60S ribosomal protein L8 is a protein that in humans is encoded by the RPL8 gene.^[1][2][3]

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 60S subunit. The protein belongs to the L2P family of ribosomal proteins. It is located in the cytoplasm. In rat, the protein associates with the 5.8S rRNA, very likely participates in the binding of aminoacyl-tRNA, and is a constituent of the elongation factor 2-binding site at the ribosomal subunit interface. Alternatively spliced transcript variants encoding the same protein exist. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.^[3]

References

1. Hanes J, Klaudiny J, von der Kammer H, Scheit KH (Feb 1994). "Characterization by cDNA cloning of the mRNA of human ribosomal protein L8". Biochem Biophys Res Commun 197 (3): 1223–8. doi:10.1006/bbrc.1993.2607. PMID 7506540.
2. 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.
3. "Entrez Gene: RPL8 ribosomal protein L8".

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.
• Uhlein M, Weglöhner W, Urlaub H, Wittmann-Liebold B (1998). "Functional implications of ribosomal protein L2 in protein biosynthesis as shown by in vivo replacement studies". Biochem. J. 331 (2): 423–30. PMC 1219371. PMID 9531480.
• 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.
• 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. PMC 155282. PMID 11875025.
• Brezillon S, Lannoy V, Franssen JD, et al. (2003). "Identification of natural ligands for the orphan G protein-coupled receptors GPR7 and GPR8". J. Biol. Chem. 278 (2): 776–83. doi:10.1074/jbc.M206396200. PMID 12401809.
• 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.
• Odintsova TI, Müller EC, Ivanov AV, et al. (2004). "Characterization and analysis of posttranslational modifications of the human large cytoplasmic ribosomal subunit proteins by mass spectrometry and Edman sequencing". J. Protein Chem. 22 (3): 249–58. doi:10.1023/A:1025068419698. PMID 12962325.
• 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.
• 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.
• Rush J, Moritz A, Lee KA, et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455.
• Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics". Nature 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
• 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.