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40S ribosomal protein S25

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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

6230

75617

Ensembl

ENSG00000118181

ENSMUSG00000009927

UniProt

P62851

P62852

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: ENSG00000118181 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000009927 – Ensembl, 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 1748303.329-33&rft.date=1991-11&rft_id=info:doi/10.1016/0378-1119(91)90335-9&rft_id=info:pmid/1748303&rft.aulast=Li&rft.aufirst=ML&rft.au=Latoud, C&rft.au=Center, MS&rfr_id=info:sid/en.wikipedia.org:40S ribosomal protein S25" class="Z3988">
  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 22777350.2782-91&rft.date=2013-05&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6714567#id-name=PMC&rft_id=info:pmid/22777350&rft_id=info:doi/10.1038/onc.2012.289&rft.aulast=Zhang&rft.aufirst=X&rft.au=Wang, W&rft.au=Wang, H&rft.au=Wang, MH&rft.au=Xu, W&rft.au=Zhang, R&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6714567&rfr_id=info:sid/en.wikipedia.org:40S ribosomal protein S25" class="Z3988">
  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 11101529.6569-81&rft.date=2000-12&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC305846#id-name=PMC&rft_id=info:pmid/11101529&rft_id=info:doi/10.1093/emboj/19.23.6569&rft.aulast=Ajuh&rft.aufirst=P&rft.au=Kuster, B&rft.au=Panov, K&rft.au=Zomerdijk, JC&rft.au=Mann, M&rft.au=Lamond, AI&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC305846&rfr_id=info:sid/en.wikipedia.org:40S ribosomal protein S25" class="Z3988">
  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 22377630.107-18&rft.date=2012-05&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3338253#id-name=PMC&rft_id=info:pmid/22377630&rft_id=info:doi/10.1534/genetics.111.136549&rft.aulast=Steffen&rft.aufirst=KK&rft.au=McCormick, MA&rft.au=Pham, KM&rft.au=MacKay, VL&rft.au=Delaney, JR&rft.au=Murakami, CJ&rft.au=Kaeberlein, M&rft.au=Kennedy, BK&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3338253&rfr_id=info:sid/en.wikipedia.org:40S ribosomal protein S25" class="Z3988">
  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 25516984.319-25&rft.date=2015-01&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4299178#id-name=PMC&rft_id=info:pmid/25516984&rft_id=info:doi/10.1073/pnas.1421328111&rft_id=info:bibcode/2015PNAS..112..319F&rft.aulast=Fuchs&rft.aufirst=G&rft.au=Petrov, AN&rft.au=Marceau, CD&rft.au=Popov, LM&rft.au=Chen, J&rft.au=O'Leary, SE&rft.au=Wang, R&rft.au=Carette, JE&rft.au=Sarnow, P&rft.au=Puglisi, JD&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4299178&rfr_id=info:sid/en.wikipedia.org:40S ribosomal protein S25" class="Z3988">
  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 19952110.2753-64&rft.date=2009-12&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2788332#id-name=PMC&rft_id=info:pmid/19952110&rft_id=info:doi/10.1101/gad.1832209&rft.aulast=Landry&rft.aufirst=DM&rft.au=Hertz, MI&rft.au=Thompson, SR&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2788332&rfr_id=info:sid/en.wikipedia.org:40S ribosomal protein S25" class="Z3988">
  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 23275440.1016-26&rft.date=2013-03&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3623076#id-name=PMC&rft_id=info:pmid/23275440&rft_id=info:doi/10.1128/MCB.00879-12&rft.aulast=Hertz&rft.aufirst=MI&rft.au=Landry, DM&rft.au=Willis, AE&rft.au=Luo, G&rft.au=Thompson, SR&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3623076&rfr_id=info:sid/en.wikipedia.org:40S ribosomal protein S25" class="Z3988">

Further reading

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  • Wool IG, Chan YL, Glück A (1996). "Structure and evolution of mammalian ribosomal proteins". Biochemistry and Cell Biology. 73 (11–12): 933–47. doi:10.1139/o95-101. PMID 8722009.11–12&rft.pages=933-47&rft.date=1996&rft_id=info:doi/10.1139/o95-101&rft_id=info:pmid/8722009&rft.aulast=Wool&rft.aufirst=IG&rft.au=Chan, YL&rft.au=Glück, A&rfr_id=info:sid/en.wikipedia.org:40S ribosomal protein S25" class="Z3988">
  • Li M, Center MS (February 1992). "Regulation of ribosomal protein S25 in HL60 cells isolated for resistance to adriamycin". FEBS Letters. 298 (2–3): 142–4. Bibcode:1992FEBSL.298..142L. doi:10.1016/0014-5793(92)80041-E. PMID 1544436. S2CID 9001148.2–3&rft.pages=142-4&rft.date=1992-02&rft_id=info:doi/10.1016/0014-5793(92)80041-E&rft_id=https://api.semanticscholar.org/CorpusID:9001148#id-name=S2CID&rft_id=info:pmid/1544436&rft_id=info:bibcode/1992FEBSL.298..142L&rft.aulast=Li&rft.aufirst=M&rft.au=Center, MS&rft_id=https://doi.org/10.1016%2F0014-5793%2892%2980041-E&rfr_id=info:sid/en.wikipedia.org:40S ribosomal protein S25" class="Z3988">
  • Marion MJ, Marion C (May 1988). "Ribosomal proteins S2, S6, S10, S14, S15 and S25 are localized on the surface of mammalian 40 S subunits and stabilize their conformation. A study with immobilized trypsin". FEBS Letters. 232 (2): 281–5. Bibcode:1988FEBSL.232..281M. doi:10.1016/0014-5793(88)80753-1. PMID 3378620. S2CID 44333810.281-5&rft.date=1988-05&rft_id=info:doi/10.1016/0014-5793(88)80753-1&rft_id=https://api.semanticscholar.org/CorpusID:44333810#id-name=S2CID&rft_id=info:pmid/3378620&rft_id=info:bibcode/1988FEBSL.232..281M&rft.aulast=Marion&rft.aufirst=MJ&rft.au=Marion, C&rft_id=https://doi.org/10.1016%2F0014-5793%2888%2980753-1&rfr_id=info:sid/en.wikipedia.org:40S ribosomal protein S25" class="Z3988">
  • Kato S, Sekine S, Oh SW, Kim NS, Umezawa Y, Abe N, et al. (December 1994). "Construction of a human full-length cDNA bank". Gene. 150 (2): 243–50. doi:10.1016/0378-1119(94)90433-2. PMID 7821789.243-50&rft.date=1994-12&rft_id=info:doi/10.1016/0378-1119(94)90433-2&rft_id=info:pmid/7821789&rft.aulast=Kato&rft.aufirst=S&rft.au=Sekine, S&rft.au=Oh, SW&rft.au=Kim, NS&rft.au=Umezawa, Y&rft.au=Abe, N&rft.au=Yokoyama-Kobayashi, M&rft.au=Aoki, T&rfr_id=info:sid/en.wikipedia.org:40S ribosomal protein S25" class="Z3988">
  • Imai T, Sudo K, Miwa T (March 1994). "Assignment of the human ribosomal protein S25 gene (RPS25) to chromosome 11q23.3 by sequence analysis of the marker D11S456". Genomics. 20 (1): 142–3. doi:10.1006/geno.1994.1145. PMID 8020948.142-3&rft.date=1994-03&rft_id=info:doi/10.1006/geno.1994.1145&rft_id=info:pmid/8020948&rft.aulast=Imai&rft.aufirst=T&rft.au=Sudo, K&rft.au=Miwa, T&rfr_id=info:sid/en.wikipedia.org:40S ribosomal protein S25" class="Z3988">
  • Miwa T, Sudo K, Nakamura Y, Imai T (July 1993). "Fifty sequenced-tagged sites on human chromosome 11". Genomics. 17 (1): 211–4. doi:10.1006/geno.1993.1304. PMID 8406452.211-4&rft.date=1993-07&rft_id=info:doi/10.1006/geno.1993.1304&rft_id=info:pmid/8406452&rft.aulast=Miwa&rft.aufirst=T&rft.au=Sudo, K&rft.au=Nakamura, Y&rft.au=Imai, T&rfr_id=info:sid/en.wikipedia.org:40S ribosomal protein S25" class="Z3988">
  • Vladimirov SN, Ivanov AV, Karpova GG, Musolyamov AK, Egorov TA, Thiede B, et al. (July 1996). "Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry". European Journal of Biochemistry. 239 (1): 144–9. doi:10.1111/j.1432-1033.1996.0144u.x. PMID 8706699.144-9&rft.date=1996-07&rft_id=info:doi/10.1111/j.1432-1033.1996.0144u.x&rft_id=info:pmid/8706699&rft.aulast=Vladimirov&rft.aufirst=SN&rft.au=Ivanov, AV&rft.au=Karpova, GG&rft.au=Musolyamov, AK&rft.au=Egorov, TA&rft.au=Thiede, B&rft.au=Wittmann-Liebold, B&rft.au=Otto, A&rft_id=https://doi.org/10.1111%2Fj.1432-1033.1996.0144u.x&rfr_id=info:sid/en.wikipedia.org:40S ribosomal protein S25" class="Z3988">
  • Kenmochi N, Kawaguchi T, Rozen S, Davis E, Goodman N, Hudson TJ, et al. (May 1998). "A map of 75 human ribosomal protein genes". Genome Research. 8 (5): 509–23. doi:10.1101/gr.8.5.509. PMID 9582194.509-23&rft.date=1998-05&rft_id=info:doi/10.1101/gr.8.5.509&rft_id=info:pmid/9582194&rft.aulast=Kenmochi&rft.aufirst=N&rft.au=Kawaguchi, T&rft.au=Rozen, S&rft.au=Davis, E&rft.au=Goodman, N&rft.au=Hudson, TJ&rft.au=Tanaka, T&rft.au=Page, DC&rft_id=https://doi.org/10.1101%2Fgr.8.5.509&rfr_id=info:sid/en.wikipedia.org:40S ribosomal protein S25" class="Z3988">
  • Kubota S, Copeland TD, Pomerantz RJ (February 1999). "Nuclear and nucleolar targeting of human ribosomal protein S25: common features shared with HIV-1 regulatory proteins". Oncogene. 18 (7): 1503–14. doi:10.1038/sj.onc.1202429. PMID 10050887. S2CID 25682899.1503-14&rft.date=1999-02&rft_id=https://api.semanticscholar.org/CorpusID:25682899#id-name=S2CID&rft_id=info:pmid/10050887&rft_id=info:doi/10.1038/sj.onc.1202429&rft.aulast=Kubota&rft.aufirst=S&rft.au=Copeland, TD&rft.au=Pomerantz, RJ&rfr_id=info:sid/en.wikipedia.org:40S ribosomal protein S25" class="Z3988">
  • 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 11101529.6569-81&rft.date=2000-12&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC305846#id-name=PMC&rft_id=info:pmid/11101529&rft_id=info:doi/10.1093/emboj/19.23.6569&rft.aulast=Ajuh&rft.aufirst=P&rft.au=Kuster, B&rft.au=Panov, K&rft.au=Zomerdijk, JC&rft.au=Mann, M&rft.au=Lamond, AI&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC305846&rfr_id=info:sid/en.wikipedia.org:40S ribosomal protein S25" class="Z3988">
  • Yoshihama M, Uechi T, Asakawa S, Kawasaki K, Kato S, Higa S, et al. (March 2002). "The human ribosomal protein genes: sequencing and comparative analysis of 73 genes". Genome Research. 12 (3): 379–90. doi:10.1101/gr.214202. PMC 155282. PMID 11875025.379-90&rft.date=2002-03&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC155282#id-name=PMC&rft_id=info:pmid/11875025&rft_id=info:doi/10.1101/gr.214202&rft.aulast=Yoshihama&rft.aufirst=M&rft.au=Uechi, T&rft.au=Asakawa, S&rft.au=Kawasaki, K&rft.au=Kato, S&rft.au=Higa, S&rft.au=Maeda, N&rft.au=Minoshima, S&rft.au=Tanaka, T&rft.au=Shimizu, N&rft.au=Kenmochi, N&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC155282&rfr_id=info:sid/en.wikipedia.org:40S ribosomal protein S25" class="Z3988">
  • Lehner B, Sanderson CM (July 2004). "A protein interaction framework for human mRNA degradation". Genome Research. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747.1315-23&rft.date=2004-07&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC442147#id-name=PMC&rft_id=info:pmid/15231747&rft_id=info:doi/10.1101/gr.2122004&rft.aulast=Lehner&rft.aufirst=B&rft.au=Sanderson, CM&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC442147&rfr_id=info:sid/en.wikipedia.org:40S ribosomal protein S25" class="Z3988">
  • Yu Y, Ji H, Doudna JA, Leary JA (June 2005). "Mass spectrometric analysis of the human 40S ribosomal subunit: native and HCV IRES-bound complexes". Protein Science. 14 (6): 1438–46. doi:10.1110/ps.041293005. PMC 2253395. PMID 15883184.1438-46&rft.date=2005-06&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2253395#id-name=PMC&rft_id=info:pmid/15883184&rft_id=info:doi/10.1110/ps.041293005&rft.aulast=Yu&rft.aufirst=Y&rft.au=Ji, H&rft.au=Doudna, JA&rft.au=Leary, JA&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2253395&rfr_id=info:sid/en.wikipedia.org:40S ribosomal protein S25" class="Z3988">
  • Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, et al. (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.957-68&rft.date=2005-09&rft_id=info:hdl/11858/00-001M-0000-0010-8592-0&rft_id=https://api.semanticscholar.org/CorpusID:8235923#id-name=S2CID&rft_id=info:pmid/16169070&rft_id=info:doi/10.1016/j.cell.2005.08.029&rft.aulast=Stelzl&rft.aufirst=U&rft.au=Worm, U&rft.au=Lalowski, M&rft.au=Haenig, C&rft.au=Brembeck, FH&rft.au=Goehler, H&rft.au=Stroedicke, M&rft.au=Zenkner, M&rft.au=Schoenherr, A&rft.au=Koeppen, S&rft.au=Timm, J&rft.au=Mintzlaff, S&rft.au=Abraham, C&rft.au=Bock, N&rft.au=Kietzmann, S&rft.au=Goedde, A&rft.au=Toksöz, E&rft.au=Droege, A&rft.au=Krobitsch, S&rft.au=Korn, B&rft.au=Birchmeier, W&rft.au=Lehrach, H&rft.au=Wanker, EE&rfr_id=info:sid/en.wikipedia.org:40S ribosomal protein S25" class="Z3988">
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