Ribosomal protein L5

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Ribosomal protein L5
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols RPL5 ; DBA6; L5; PPP1R135
External IDs OMIM603634 MGI102854 HomoloGene110649 GeneCards: RPL5 Gene
RNA expression pattern
PBB GE RPL5 200937 s at tn.png
PBB GE RPL5 210035 s at tn.png
PBB GE RPL5 213080 x at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 6125 100503670
Ensembl ENSG00000122406 ENSMUSG00000058558
UniProt P46777 P47962
RefSeq (mRNA) NM_000969 NM_016980
RefSeq (protein) NP_000960 NP_058676
Location (UCSC) Chr 1:
93.3 – 93.31 Mb
Chr 5:
107.9 – 107.91 Mb
PubMed search [1] [2]

60S ribosomal protein L5 is a protein that in humans is encoded by the RPL5 gene.[1][2]

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 II. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.[3]

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.[3]

Interactions[edit]

Ribosomal protein L5 has been shown to interact with EIF5A,[4] PDCD4,[5] CSNK2B[6][7][8][9] and Mdm2.[10][11][12]

References[edit]

  1. ^ 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 331892. PMID 7937132. 
  2. ^ 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. 
  3. ^ a b "Entrez Gene: RPL5 ribosomal protein L5". 
  4. ^ 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. (UNITED STATES) 95 (4): 1607–12. doi:10.1073/pnas.95.4.1607. ISSN 0027-8424. PMC 19115. PMID 9465063. 
  5. ^ Kang, Min-Ji; Ahn Hye-Sung; Lee Ji-Young; Matsuhashi Sachiko; Park Woong-Yang (April 2002). "Up-regulation of PDCD4 in senescent human diploid fibroblasts". Biochem. Biophys. Res. Commun. (United States) 293 (1): 617–21. doi:10.1016/S0006-291X(02)00264-4. ISSN 0006-291X. PMID 12054647. 
  6. ^ Lehner, Ben; Semple Jennifer I; Brown Stephanie E; Counsell Damian; Campbell R Duncan; Sanderson Christopher M (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 (United States) 83 (1): 153–67. doi:10.1016/S0888-7543(03)00235-0. ISSN 0888-7543. PMID 14667819. 
  7. ^ Boldyreff, B; Issinger O G (February 1997). "A-Raf kinase is a new interacting partner of protein kinase CK2 beta subunit". FEBS Lett. (NETHERLANDS) 403 (2): 197–9. doi:10.1016/S0014-5793(97)00010-0. ISSN 0014-5793. PMID 9042965. 
  8. ^ Kim, J M; Cha J Y; Marshak D R; Bae Y S (September 1996). "Interaction of the beta subunit of casein kinase II with the ribosomal protein L5". Biochem. Biophys. Res. Commun. (UNITED STATES) 226 (1): 180–6. doi:10.1006/bbrc.1996.1330. ISSN 0006-291X. PMID 8806611. 
  9. ^ Ahn, B H; Kim T H; Bae Y S (October 2001). "Mapping of the interaction domain of the protein kinase CKII beta subunit with target proteins". Mol. Cells (Korea (South)) 12 (2): 158–63. ISSN 1016-8478. PMID 11710515. 
  10. ^ Zhang, Yanping; Wolf Gabrielle White; Bhat Krishna; Jin Aiwen; Allio Theresa; Burkhart William A; Xiong Yue (Dec 2003). "Ribosomal protein L11 negatively regulates oncoprotein MDM2 and mediates a p53-dependent ribosomal-stress checkpoint pathway". Mol. Cell. Biol. (United States) 23 (23): 8902–12. doi:10.1128/MCB.23.23.8902-8912.2003. ISSN 0270-7306. PMC 262682. PMID 14612427. 
  11. ^ Marechal, V; Elenbaas B; Piette J; Nicolas J C; Levine A J (November 1994). "The ribosomal L5 protein is associated with mdm-2 and mdm-2-p53 complexes". Mol. Cell. Biol. (UNITED STATES) 14 (11): 7414–20. ISSN 0270-7306. PMC 359276. PMID 7935455. 
  12. ^ Dai, Mu-Shui; Sun Xiao-Xin; Lu Hua (July 2008). "Aberrant expression of nucleostemin activates p53 and induces cell cycle arrest via inhibition of MDM2". Mol. Cell. Biol. (United States) 28 (13): 4365–76. doi:10.1128/MCB.01662-07. PMC 2447154. PMID 18426907. 

Further reading[edit]

External links[edit]