From Wikipedia, the free encyclopedia
Jump to: navigation, search
For the programming language RPL-11, see Filetab.
Ribosomal protein L11
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols RPL11 ; DBA7; GIG34; L11
External IDs OMIM604175 MGI1914275 HomoloGene37376 GeneCards: RPL11 Gene
RNA expression pattern
PBB GE RPL11 200010 at tn.png
More reference expression data
Species Human Mouse
Entrez 6135 67025
Ensembl ENSG00000142676 ENSMUSG00000059291
UniProt P62913 Q9CXW4
RefSeq (mRNA) NM_000975 NM_025919
RefSeq (protein) NP_000966 NP_080195
Location (UCSC) Chr 1:
24.02 – 24.02 Mb
Chr 4:
136.03 – 136.05 Mb
PubMed search [1] [2]

60S ribosomal protein L11 is a protein that in humans is encoded by the RPL11 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 L5P family of ribosomal proteins. It is located in the cytoplasm. The protein probably associates with the 5S rRNA. Alternative splice variants encoding different isoforms may exist, but they have not been fully characterized. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.[3]


RPL11 has been shown to interact with:


  1. ^ Kenmochi N, Kawaguchi T, Rozen S, Davis E, Goodman N, Hudson TJ et al. (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. 
  2. ^ Graphodatsky AS, Vorobieva NV, Filipenko ML, Voronina EV, Frengen E, Prydz H (Jun 1999). "Assignment of the L11 ribosomal protein gene (RPL11) to human chromosome 1p36.1→p35 by in situ hybridization". Cytogenet Cell Genet 84 (1–2): 97–98. doi:10.1159/000015228. PMID 10343117. 
  3. ^ a b "Entrez Gene: RPL11 ribosomal protein L11". 
  4. ^ Koldamova RP, Lefterov IM, DiSabella MT, Almonte C, Watkins SC, Lazo JS (Jun 1999). "Human bleomycin hydrolase binds ribosomal proteins". Biochemistry 38 (22): 7111–7. doi:10.1021/bi990135l. PMID 10353821. 
  5. ^ a b c Zhang Y, Wolf GW, Bhat K, Jin A, Allio T, Burkhart WA et al. (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 262682. PMID 14612427. 
  6. ^ Dai MS, Sun XX, Lu H (Jul 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 2447154. PMID 18426907. 
  7. ^ Bernardi R, Scaglioni PP, Bergmann S, Horn HF, Vousden KH, Pandolfi PP (Jul 2004). "PML regulates p53 stability by sequestering Mdm2 to the nucleolus". Nat. Cell Biol. 6 (7): 665–72. doi:10.1038/ncb1147. PMID 15195100. 

Further reading[edit]

External links[edit]