60S ribosomal protein L26

RPL26
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesRPL26, DBA11, L26, ribosomal protein L26
External IDsMGI: 106022 HomoloGene: 113207 GeneCards: RPL26
Gene location (Human)
Chr.Chromosome 17 (human)[1]
Band17p13.1Start8,377,516 bp[1]
End8,383,250 bp[1]
Orthologs
SpeciesHumanMouse
Entrez

6154

19941

Ensembl

ENSG00000161970

ENSMUSG00000060938

UniProt

P61254

P61255

RefSeq (mRNA)

NM_000987
NM_001315530
NM_001315531

NM_009080

RefSeq (protein)

NP_000978
NP_001302459
NP_001302460

NP_033106

Location (UCSC)Chr 17: 8.38 – 8.38 MbChr 11: 68.9 – 68.91 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

60S ribosomal protein L26 is a protein that in humans is encoded by the RPL26 gene.[5][6]

Function

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 L24P family of ribosomal proteins. It is located in the cytoplasm. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.[6]

Interactions

RPL26 has been shown to interact with Mdm2.[7]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000161970 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000060938 - Ensembl, May 2017
  3. "Human PubMed Reference:".
  4. "Mouse PubMed Reference:".
  5. Zaman GJ (May 1993). "Sequence of a cDNA encoding human ribosomal protein L26 and of a cDNA probably encoding human ribosomal protein L6". Nucleic Acids Res. 21 (7): 1673. doi:10.1093/nar/21.7.1673. PMC 309386. PMID 8479925.
  6. 1 2 "Entrez Gene: RPL26 ribosomal protein L26".
  7. Ofir-Rosenfeld Y, Boggs K, Michael D, Kastan MB, Oren M (Oct 2008). "Mdm2 regulates p53 mRNA translation through inhibitory interactions with ribosomal protein L26". Mol. Cell. 32 (2): 180–9. doi:10.1016/j.molcel.2008.08.031. PMC 2587494. PMID 18951086.

Further reading

  • Wool IG, Chan YL, Glück A (1996). "Structure and evolution of mammalian ribosomal proteins". Biochem. Cell Biol. 73 (11–12): 933–47. doi:10.1139/o95-101. PMID 8722009.
  • Kenmochi N, Kawaguchi T, Rozen S, Davis E, Goodman N, Hudson TJ, Tanaka T, Page DC (1998). "A map of 75 human ribosomal protein genes". Genome Res. 8 (5): 509–23. doi:10.1101/gr.8.5.509. PMID 9582194.
  • Uechi T, Tanaka T, Kenmochi N (2001). "A complete map of the human ribosomal protein genes: assignment of 80 genes to the cytogenetic map and implications for human disorders". Genomics. 72 (3): 223–30. doi:10.1006/geno.2000.6470. PMID 11401437.
  • Andersen JS, Lyon CE, Fox AH, Leung AK, Lam YW, Steen H, Mann M, Lamond AI (2002). "Directed proteomic analysis of the human nucleolus". Curr. Biol. 12 (1): 1–11. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298.
  • Yoshihama M, Uechi T, Asakawa S, Kawasaki K, Kato S, Higa S, Maeda N, Minoshima S, Tanaka T, Shimizu N, Kenmochi N (2002). "The Human Ribosomal Protein Genes: Sequencing and Comparative Analysis of 73 Genes". Genome Res. 12 (3): 379–90. doi:10.1101/gr.214202. PMC 155282. PMID 11875025.
  • Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
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