60S ribosomal protein L5

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RPL5
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases RPL5, DBA6, L5, PPP1R135, MSTP030, Ribosomal protein L5
External IDs MGI: 102854 HomoloGene: 110649 GeneCards: RPL5
RNA expression pattern
PBB GE RPL5 200937 s at fs.png

PBB GE RPL5 213080 x at fs.png

PBB GE RPL5 210035 s at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_000969

NM_016980

RefSeq (protein)

NP_000960

NP_058676.1
NP_058676

Location (UCSC) Chr 1: 92.83 – 92.84 Mb Chr 5: 107.9 – 107.91 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

60S ribosomal protein L5 is a protein that in humans is encoded by the RPL5 gene.[3][4]

Function[edit]

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 2.

Clinical significance[edit]

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.[5]

Interactions[edit]

Ribosomal protein L5 has been shown to interact with:

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ Qu LH, Nicoloso M, Michot B, Azum MC, Caizergues-Ferrer M, Renalier MH, Bachellerie JP (November 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. doi:10.1093/nar/22.20.4073. PMC 331892Freely accessible. PMID 7937132. 
  4. ^ Frigerio JM, Dagorn JC, Iovanna JL (July 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. doi:10.1016/0167-4781(95)00045-i. PMID 7772601. 
  5. ^ "Entrez Gene: RPL5 ribosomal protein L5". 
  6. ^ Lehner B, Semple JI, Brown SE, Counsell D, Campbell RD, Sanderson CM (January 2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region". Genomics. 83 (1): 153–67. doi:10.1016/s0888-7543(03)00235-0. PMID 14667819. 
  7. ^ Boldyreff B, Issinger OG (February 1997). "A-Raf kinase is a new interacting partner of protein kinase CK2 beta subunit". FEBS Lett. 403 (2): 197–9. doi:10.1016/s0014-5793(97)00010-0. PMID 9042965. 
  8. ^ Kim JM, Cha JY, Marshak DR, Bae YS (September 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. 
  9. ^ Ahn BH, Kim TH, Bae YS (October 2001). "Mapping of the interaction domain of the protein kinase CKII beta subunit with target proteins". Mol. Cells. 12 (2): 158–63. PMID 11710515. 
  10. ^ Schatz O, Oft M, Dascher C, Schebesta M, Rosorius O, Jaksche H, Dobrovnik M, Bevec D, Hauber J (February 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. doi:10.1073/pnas.95.4.1607. PMC 19115Freely accessible. PMID 9465063. 
  11. ^ Zhang Y, Wolf GW, Bhat K, Jin A, Allio T, Burkhart WA, Xiong Y (Dec 2003). "Ribosomal protein L11 negatively regulates oncoprotein MDM2 and mediates a p53-dependent ribosomal-stress checkpoint pathway". Mol. Cell. Biol. 23 (23): 8902–12. doi:10.1128/mcb.23.23.8902-8912.2003. PMC 262682Freely accessible. PMID 14612427. 
  12. ^ Marechal V, Elenbaas B, Piette J, Nicolas JC, Levine AJ (November 1994). "The ribosomal L5 protein is associated with mdm-2 and mdm-2-p53 complexes". Mol. Cell. Biol. 14 (11): 7414–20. doi:10.1128/mcb.14.11.7414. PMC 359276Freely accessible. PMID 7935455. 
  13. ^ Dai MS, Sun XX, Lu H (July 2008). "Aberrant expression of nucleostemin activates p53 and induces cell cycle arrest via inhibition of MDM2". Mol. Cell. Biol. 28 (13): 4365–76. doi:10.1128/MCB.01662-07. PMC 2447154Freely accessible. PMID 18426907. 
  14. ^ Kang MJ, Ahn HS, Lee JY, Matsuhashi S, Park WY (April 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. 

Further reading[edit]

External links[edit]