RPL5

From Wikipedia, the free encyclopedia

Ribosomal protein L5

Identifiers

RPL5; MGC117339; MSTP030

External IDs

OMIM: 603634 MGI: 102854 HomoloGene: 90823

Gene ontology
Molecular Function:	• structural constituent of ribosome • protein binding • 5S rRNA binding • rRNA binding
Cellular Component:	• intracellular • nucleus • ribosome • cytosolic large ribosomal subunit (sensu Eukaryota)
Biological Process:	• translation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_000969 (mRNA)
NP_000960 (protein)

NM_016980 (mRNA)
NP_058676 (protein)

Location

Chr 1: 93.07 - 93.08 Mb

Chr 7: 114.5 - 114.5 Mb

Pubmed search

[1]

[2]

Ribosomal protein L5, also known as RPL5, is a human gene.

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 L18P family of ribosomal proteins. It is located in the cytoplasm. The protein binds 5S rRNA to form a stable complex called the 5S ribonucleoprotein particle (RNP), which is necessary for the transport of nonribosome-associated cytoplasmic 5S rRNA to the nucleolus for assembly into ribosomes. The protein interacts specifically with the beta subunit of casein kinase II. Variable expression of this gene in colorectal cancers compared to adjacent normal tissues has been observed, although no correlation between the level of expression and the severity of the disease has been found. This gene is co-transcribed with the small nucleolar RNA gene U21, which is located in its fifth intron. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.^[1]

[edit] References

^ Entrez Gene: RPL5 ribosomal protein L5.

[edit] 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.
Pogue-Geile K, Geiser JR, Shu M, et al. (1991). "Ribosomal protein genes are overexpressed in colorectal cancer: isolation of a cDNA clone encoding the human S3 ribosomal protein.". Mol. Cell. Biol. 11 (8): 3842–9. PMID 1712897.
Steitz JA, Berg C, Hendrick JP, et al. (1988). "A 5S rRNA/L5 complex is a precursor to ribosome assembly in mammalian cells.". J. Cell Biol. 106 (3): 545–56. PMID 3279045.
Hirano K, Ito M, Hartshorne DJ (1995). "Interaction of the ribosomal protein, L5, with protein phosphatase type 1.". J. Biol. Chem. 270 (34): 19786–90. PMID 7649987.
Frigerio JM, Dagorn JC, Iovanna JL (1995). "Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9, S10 and S29 human ribosomal protein mRNAs.". Biochim. Biophys. Acta 1262 (1): 64–8. PMID 7772601.
Marechal V, Elenbaas B, Piette J, et al. (1994). "The ribosomal L5 protein is associated with mdm-2 and mdm-2-p53 complexes.". Mol. Cell. Biol. 14 (11): 7414–20. PMID 7935455.
Qu LH, Nicoloso M, Michot B, et al. (1994). "U21, a novel small nucleolar RNA with a 13 nt. complementarity to 28S rRNA, is encoded in an intron of ribosomal protein L5 gene in chicken and mammals.". Nucleic Acids Res. 22 (20): 4073–81. PMID 7937132.
Ogata K, Kurahashi A, Nishiyama C, Terao K (1994). "Presence of role of the 5SrRNA-L5 protein complex (5SRNP) in the threonyl- and histidyl-tRNA synthetase complex in rat liver cytosol.". Biochim. Biophys. Acta 1218 (3): 388–400. PMID 8049265.
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. PMID 8125298.
Michael WM, Dreyfuss G (1996). "Distinct domains in ribosomal protein L5 mediate 5 S rRNA binding and nucleolar localization.". J. Biol. Chem. 271 (19): 11571–4. PMID 8626719.
Kim JM, Cha JY, Marshak DR, Bae YS (1996). "Interaction of the beta subunit of casein kinase II with the ribosomal protein L5.". Biochem. Biophys. Res. Commun. 226 (1): 180–6. doi:10.1006/bbrc.1996.1330. PMID 8806611.
Boldyreff B, Issinger OG (1997). "A-Raf kinase is a new interacting partner of protein kinase CK2 beta subunit.". FEBS Lett. 403 (2): 197–9. PMID 9042965.
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. PMID 9373149.
Schatz O, Oft M, Dascher C, et al. (1998). "Interaction of the HIV-1 rev cofactor eukaryotic initiation factor 5A with ribosomal protein L5.". Proc. Natl. Acad. Sci. U.S.A. 95 (4): 1607–12. PMID 9465063.
Kenmochi N, Kawaguchi T, Rozen S, et al. (1998). "A map of 75 human ribosomal protein genes.". Genome Res. 8 (5): 509–23. PMID 9582194.
Jäkel S, Görlich D (1998). "Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear import of ribosomal proteins in mammalian cells.". EMBO J. 17 (15): 4491–502. doi:10.1093/emboj/17.15.4491. PMID 9687515.
Guerra B, Issinger OG (1998). "p53 and the ribosomal protein L5 participate in high molecular mass complex formation with protein kinase CK2 in murine teratocarcinoma cell line F9 after serum stimulation and cisplatin treatment.". FEBS Lett. 434 (1-2): 115–20. PMID 9738462.
Park JW, Bae YS (1999). "Phosphorylation of ribosomal protein L5 by protein kinase CKII decreases its 5S rRNA binding activity.". Biochem. Biophys. Res. Commun. 263 (2): 475–81. doi:10.1006/bbrc.1999.1345. PMID 10491318.
Rosorius O, Fries B, Stauber RH, et al. (2000). "Human ribosomal protein L5 contains defined nuclear localization and export signals.". J. Biol. Chem. 275 (16): 12061–8. PMID 10766838.