Jump to content

60S ribosomal protein L11

From Wikipedia, the free encyclopedia
RPL11
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesRPL11, DBA7, GIG34, L11, ribosomal protein L11, uL5
External IDsOMIM: 604175; MGI: 1914275; HomoloGene: 37376; GeneCards: RPL11; OMA:RPL11 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001199802
NM_000975

NM_025919

RefSeq (protein)

NP_000966
NP_001186731
NP_000966.2

NP_080195

Location (UCSC)Chr 1: 23.69 – 23.7 MbChr 4: 135.76 – 135.78 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

60S ribosomal protein L11 is a protein that in humans is encoded by the RPL11 gene.[5][6]

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 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.[citation needed]

Interactions

[edit]

RPL11 has been shown to interact with:

References

[edit]
  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000142676Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000059291Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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.
  6. ^ 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. S2CID 26672114.
  7. ^ 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.
  8. ^ a b c 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 262682. PMID 14612427.
  9. ^ 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.
  10. ^ Uchi R, Kogo R, Kawahara K, Sudo T, Yokobori T, Eguchi H, et al. (October 2013). "PICT1 regulates TP53 via RPL11 and is involved in gastric cancer progression". British Journal of Cancer. 109 (8): 2199–206. doi:10.1038/bjc.2013.561. PMC 3798961. PMID 24045667.
  11. ^ 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. S2CID 26281860.

Further reading

[edit]
[edit]