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40S ribosomal protein S27

From Wikipedia, the free encyclopedia
(Redirected from RPS27)
RPS27
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesRPS27, MPS-1, MPS1, S27, ribosomal protein S27, DBA17
External IDsOMIM: 603702; MGI: 1915191; HomoloGene: 803; GeneCards: RPS27; OMA:RPS27 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001030
NM_001349946
NM_001349947

NM_026467
NM_001311101
NM_001361106

RefSeq (protein)

NP_001021
NP_001336875
NP_001336876

NP_001298030
NP_080743
NP_001348035

Location (UCSC)Chr 1: 153.99 – 153.99 MbChr 9: 66.85 – 66.86 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

40S ribosomal protein S27, also known as metallopan-stimulin 1 or MPS-1, is a protein that in humans is encoded by the RPS27 gene.[5][6][7] Metallopanstimulin is a zinc finger protein proposed to be involved DNA repair as well as oncogenesis.[8]

Function

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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 40S subunit. The protein belongs to the S27E family of ribosomal proteins. It contains a C4-type zinc finger domain that can bind to zinc. The encoded protein has been shown to be able to bind to nucleic acid. It is located in the cytoplasm as a ribosomal component, but it has also been detected in the nucleus. Studies in rat indicate that ribosomal protein S27 is located near ribosomal protein S18 in the 40S subunit and is covalently linked to translation initiation factor eIF3. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.[7]

Clinical significance

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Its expression is increased in several types of malignancy and MPS levels have been reported to drop with treatment of some cancers. It has also been used as a target for some chemotherapies, which aim to chelate out the zinc from the zinc finger motif of the MPS, thus yielding it inactive. These therapies have shown promise for the treatment of cancer in laboratory experiments and some limited clinical trials. Head and neck cancer transfected to overexpress this protein have demonstrated suppressed growth.[8]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000177954Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000036781Ensembl, 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. ^ Tsui SK, Lee SM, Fung KP, Waye MM, Lee CY (Oct 1996). "Primary structures and sequence analysis of human ribosomal proteins L39 and S27". Biochemistry and Molecular Biology International. 40 (3): 611–6. doi:10.1080/15216549600201203. PMID 8908372. S2CID 7909023.
  6. ^ Fernandez-Pol JA, Klos DJ, Hamilton PD (Oct 1993). "A growth factor-inducible gene encodes a novel nuclear protein with zinc finger structure". The Journal of Biological Chemistry. 268 (28): 21198–204. doi:10.1016/S0021-9258(19)36910-8. PMID 8407955.
  7. ^ a b "Entrez Gene: RPS27 ribosomal protein S27 (metallopanstimulin 1)".
  8. ^ a b Fernandez-Pol JA (1996). "Metallopanstimulin as a novel tumor marker in sera of patients with various types of common cancers: implications for prevention and therapy". Anticancer Research. 16 (4B): 2177–85. PMID 8694540.

Further reading

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