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40S ribosomal protein S25

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(Redirected from RPS25 (gene))

RPS25
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesRPS25, S25, ribosomal protein S25
External IDsOMIM: 180465; MGI: 1922867; HomoloGene: 133893; GeneCards: RPS25; OMA:RPS25 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001028

NM_024266

RefSeq (protein)

NP_001019

NP_077228

Location (UCSC)Chr 11: 119.02 – 119.02 MbChr 9: 44.32 – 44.32 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

40S ribosomal protein S25 (eS25) is a protein that in humans is encoded by the RPS25 gene.[5][6]

Ribosomes are cellular macromolecules that catalyze protein synthesis across all kingdoms of life. The eukaryotic ribosome consists of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 distinct proteins. The RPS25 gene encodes the eukaryote-specific ribosomal protein eS25 that is a component of the 40S subunit. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.[6]

Interactions

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Besides the interactions that position eS25 at its location in the E site region of the 40S ribosomal subunit, eS25 has been suggested to interact with other cellular proteins. One study has found that eS25 interacts with MDM2 as part of a regulatory feedback loop that stabilizes p53.[7] Additionally, eS25 has been shown to interact with CDC5L.[8]

Function

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As a ribosomal protein, eS25 likely plays a role in general protein synthesis; however, the RPS25 gene is non-essential for cellular viability in budding yeast and in select mammalian cell lines, implying that it is not essential for eukaryotic protein synthesis.[9][10] Studies have implicated eS25 in the control of several specialized forms of translation, including that mediated by viral IRESs.[11][12]

See also

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References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000118181Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000009927Ensembl, 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. ^ Li ML, Latoud C, Center MS (November 1991). "Cloning and sequencing a cDNA encoding human ribosomal protein S25". Gene. 107 (2): 329–33. doi:10.1016/0378-1119(91)90335-9. PMID 1748303.
  6. ^ a b "Entrez Gene: RPS25 ribosomal protein S25".
  7. ^ Zhang X, Wang W, Wang H, Wang MH, Xu W, Zhang R (May 2013). "Identification of ribosomal protein S25 (RPS25)-MDM2-p53 regulatory feedback loop". Oncogene. 32 (22): 2782–91. doi:10.1038/onc.2012.289. PMC 6714567. PMID 22777350.
  8. ^ Ajuh P, Kuster B, Panov K, Zomerdijk JC, Mann M, Lamond AI (December 2000). "Functional analysis of the human CDC5L complex and identification of its components by mass spectrometry". The EMBO Journal. 19 (23): 6569–81. doi:10.1093/emboj/19.23.6569. PMC 305846. PMID 11101529.
  9. ^ Steffen KK, McCormick MA, Pham KM, MacKay VL, Delaney JR, Murakami CJ, et al. (May 2012). "Ribosome deficiency protects against ER stress in Saccharomyces cerevisiae". Genetics. 191 (1): 107–18. doi:10.1534/genetics.111.136549. PMC 3338253. PMID 22377630.
  10. ^ Fuchs G, Petrov AN, Marceau CD, Popov LM, Chen J, O'Leary SE, et al. (January 2015). "Kinetic pathway of 40S ribosomal subunit recruitment to hepatitis C virus internal ribosome entry site". Proceedings of the National Academy of Sciences of the United States of America. 112 (2): 319–25. Bibcode:2015PNAS..112..319F. doi:10.1073/pnas.1421328111. PMC 4299178. PMID 25516984.
  11. ^ Landry DM, Hertz MI, Thompson SR (December 2009). "RPS25 is essential for translation initiation by the Dicistroviridae and hepatitis C viral IRESs". Genes & Development. 23 (23): 2753–64. doi:10.1101/gad.1832209. PMC 2788332. PMID 19952110.
  12. ^ Hertz MI, Landry DM, Willis AE, Luo G, Thompson SR (March 2013). "Ribosomal protein S25 dependency reveals a common mechanism for diverse internal ribosome entry sites and ribosome shunting". Molecular and Cellular Biology. 33 (5): 1016–26. doi:10.1128/MCB.00879-12. PMC 3623076. PMID 23275440.

Further reading

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