Atlas of Genetics and Cytogenetics in Oncology and Haematology


Home   Genes   Leukemias   Solid Tumours   Cancer-Prone   Deep Insight   Case Reports   Journals  Portal   Teaching   

X Y 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 NA

RPS27 (ribosomal protein S27)

Identity

Other namesMPS-1
MPS1
S27
HGNC (Hugo) RPS27
LocusID (NCBI) 6232
Location 1q21.3
Location_base_pair Starts at 153963239 and ends at 153964631 bp from pter ( according to hg19-Feb_2009)  [Mapping]
Local_order Human RPS27 is found on chromosome 1: 153963235 - 153964626 bp from pter. Information about the local order for RPS27 can be found at ensembl.org. Four transcripts have been identified, but only the first will be discussed below.

DNA/RNA

Description The RPS27 gene is comprised of 1.39 kb and consists of 4 exons. This gene is a member of the Human CCDS set: CCDS1059.
Transcription The transcript is 350 base pairs long.
Pseudogene Multiple RPS27 pseudogenes are dispersed throughout the genome. The RPS27L pseudogene, located at 15q22.2, is known to encode a protein that shares 96% of its amino acid sequence with RPS27 (Balasubramanian et al., 2009).

Protein

Description RPS27 is a 9461 Da protein composed of 84 amino acids. The protein contains a C4 zinc finger domain, similar to steroid and thyroid hormones, which enables DNA binding. RPS27 is found in both the cytoplasm and the nucleus.
Expression Ubiquitous expression. Expressed at high levels in actively dividing cells and in cancers of ectodermal origin, as well as in melanoma (Fernandez-Pol et al., 1993). When overexpressed, it is secreted into serum (Lee et al., 2004).
Function 1. Component of the 40S ribosomal subunit in the cytoplasm: ribosomes carry out translation of proteins. The eukaryotic ribosome is made up of a small 40S and a large 60S subunit. Together these subunits are comprised of 4 different rRNA species and almost 80 different RP's (ribosomal proteins). As a component of the 40S subunit, RPS27 is found near RPS18 and covalently bound to translation initiation factor eIF3.
2. A mediator of cellular proliferation and survival: expression is induced by a variety of growth factors and other signaling molecules, including TGF-beta and cAMP; RPS27 can bind to cAMP response elements of DNA (Fernandez-Pol et al., 1993).
3. Oncogenesis (see below).
Homology Member of the ribosomal protein S27e family.

Mutations

Note Single nucleotide polymorphisms have been identified, but have not been linked to disease.

Implicated in

Entity Various carcinomas and melanoma
Note RPS27 overexpression has been reported in many cancers including prostate cancer (Fernandez-Pol et al., 1997), colorectal cancer (Ganger et al., 1997), liver cancer (Ganger et al., 2001), breast cancer (Atsuta et al., 2002), head and neck squamous cell cancer (HNSCC) (Stack et al., 1999; Stack et al., 2004; Lee et al., 2004), gastric cancer (Wang, et al., 2006), as well as, melanoma (Santa Cruz et al., 1997).
Since high serum levels of RPS27 have been found in cancer patients, especially in head and neck squamous cell carcinoma (HNSCC), the protein can be used as a tumor marker (Fernandez-Pol et al., 1996; Lee et al., 2004; Stack et al. 2004).
Prognosis It was reported that RPS27 levels correlate with tumor stage in patients with gastric cancer, thus high levels serve as a poor prognostic indicator (Wang et al., 2006).
Oncogenesis The mechanism behind RPS27 overexpression is currently under investigation. One explanation recently offered arises from the relationship between RPS27, MDM2 and p53: RPS27 is a p53 repressible protein (He and Sun, 2007; Li et al., 2007). A 2011 study found that it competes with p53 for a central acidic binding domain on MDM2. Once bound, MDM2 is stimulated to ubiquinate and degrade the RPS27 or p53, whichever it is bound to. When RPS27 levels are elevated, it can out-compete p53 for MDM2 binding and subsequent degradation, thus stabilizing p53 levels. This would be an appropriate cellular response to genotoxic stress. The same study also found that mutant p53 cannot suppress RPS27, only the wild-type can. Since mutated p53 is found in almost 50% of all human cancers, RPS27 overexpression logically follows. Furthermore, stabilization of mutant p53 levels associated with RPS27 abundance could provide malignant cells with a growth advantage (Xiong et al., 2011).
RPS27 knockdown was found to enhance spontaneous apoptosis of tumor cells via caspase-3 activation (Wang et al., 2006; Yang et al., 2011).
HNSCC: some have questioned if RPS27 overexpression is the cause or result of cancer. A 2010 study overexpressed RPS27 in a line of HNSCC cells to study the impact on tumor behavior. They found that RPS27 overexpression resulted in reduced cancer cell growth, proliferation rate and angiogenesis. RPS27 overexpression was also found to reduce the mRNA of Paxillin, a focal adhesion protein up regulated in HNSCC and many other cancer cells. RPS27 induced Paxillin repression offers a possible explanation for the decreased HNSCC growth (Dai et al., 2010).
  

External links

Nomenclature
HGNC (Hugo)RPS27   10416
Cards
AtlasRPS27ID45550ch1q21
Entrez_Gene (NCBI)RPS27  6232  ribosomal protein S27
GeneCards (Weizmann)RPS27
Ensembl (Hinxton)ENSG00000177954 [Gene_View]  chr1:153963239-153964631 [Contig_View]  RPS27 [Vega]
ICGC DataPortalENSG00000177954
cBioPortalRPS27
AceView (NCBI)RPS27
Genatlas (Paris)RPS27
WikiGenes6232
SOURCE (Princeton)NM_001030
Genomic and cartography
GoldenPath (UCSC)RPS27  -  1q21.3   chr1:153963239-153964631 +  1q21   [Description]    (hg19-Feb_2009)
EnsemblRPS27 - 1q21 [CytoView]
Mapping of homologs : NCBIRPS27 [Mapview]
OMIM603702   
Gene and transcription
Genbank (Entrez)AK312070 AV763942 BC002658 BC070219 CD177656
RefSeq transcript (Entrez)NM_001030
RefSeq genomic (Entrez)AC_000133 NC_000001 NC_018912 NT_004487 NW_001838529 NW_004929293
Consensus coding sequences : CCDS (NCBI)RPS27
Cluster EST : UnigeneHs.654475 [ NCBI ]
CGAP (NCI)Hs.654475
Alternative Splicing : Fast-db (Paris)GSHG0001001
Alternative Splicing GalleryENSG00000177954
Gene ExpressionRPS27 [ NCBI-GEO ]     RPS27 [ SEEK ]   RPS27 [ MEM ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP42677 (Uniprot)
NextProtP42677  [Medical]
With graphics : InterProP42677
Splice isoforms : SwissVarP42677 (Swissvar)
Domaine pattern : Prosite (Expaxy)RIBOSOMAL_S27E (PS01168)   
Domains : Interpro (EBI)Ribosomal_S27e [organisation]   Ribosomal_S27e_Zn-bd_dom [organisation]   Ribosomal_zn-bd [organisation]  
Related proteins : CluSTrP42677
Domain families : Pfam (Sanger)Ribosomal_S27e (PF01667)   
Domain families : Pfam (NCBI)pfam01667   
Domain structure : Prodom (Prabi Lyon)Ribosomal_S27e (PD004466)   
DMDM Disease mutations6232
Blocks (Seattle)P42677
PDB (SRS)3J3A   
PDB (PDBSum)3J3A   
PDB (IMB)3J3A   
PDB (RSDB)3J3A   
Human Protein AtlasENSG00000177954 [gene] [tissue] [antibody] [cell] [cancer]
Peptide AtlasP42677
HPRD04744
IPIIPI00795224   
Protein Interaction databases
DIP (DOE-UCLA)P42677
IntAct (EBI)P42677
FunCoupENSG00000177954
BioGRIDRPS27
InParanoidP42677
Interologous Interaction database P42677
IntegromeDBRPS27
STRING (EMBL)RPS27
Ontologies - Pathways
Ontology : AmiGOnuclear-transcribed mRNA catabolic process, nonsense-mediated decay  mitotic cell cycle  DNA binding  structural constituent of ribosome  protein binding  nucleus  cytosol  ribosome  translation  translation  translation  translational initiation  translational elongation  translational termination  SRP-dependent cotranslational protein targeting to membrane  zinc ion binding  cell proliferation  gene expression  viral process  RNA metabolic process  mRNA metabolic process  viral life cycle  viral transcription  cytosolic small ribosomal subunit  cellular protein metabolic process  poly(A) RNA binding  
Ontology : EGO-EBInuclear-transcribed mRNA catabolic process, nonsense-mediated decay  mitotic cell cycle  DNA binding  structural constituent of ribosome  protein binding  nucleus  cytosol  ribosome  translation  translation  translation  translational initiation  translational elongation  translational termination  SRP-dependent cotranslational protein targeting to membrane  zinc ion binding  cell proliferation  gene expression  viral process  RNA metabolic process  mRNA metabolic process  viral life cycle  viral transcription  cytosolic small ribosomal subunit  cellular protein metabolic process  poly(A) RNA binding  
Pathways : KEGGRibosome   
Protein Interaction DatabaseRPS27
Wikipedia pathwaysRPS27
Gene fusion - rearrangments
Polymorphisms : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)RPS27
snp3D : Map Gene to Disease6232
SNP (GeneSNP Utah)RPS27
SNP : HGBaseRPS27
Genetic variants : HAPMAPRPS27
Exome VariantRPS27
1000_GenomesRPS27 
ICGC programENSG00000177954 
Somatic Mutations in Cancer : COSMICRPS27 
CONAN: Copy Number AnalysisRPS27 
Mutations and Diseases : HGMDRPS27
Genomic VariantsRPS27  RPS27 [DGVbeta]
dbVarRPS27
ClinVarRPS27
Pred. of missensesPolyPhen-2  SIFT(SG)  SIFT(JCVI)  Align-GVGD  MutAssessor  Mutanalyser  
Pred. splicesGeneSplicer  Human Splicing Finder  MaxEntScan  
Diseases
OMIM603702   
MedgenRPS27
GENETestsRPS27
Disease Genetic AssociationRPS27
Huge Navigator RPS27 [HugePedia]  RPS27 [HugeCancerGEM]
General knowledge
Homologs : HomoloGeneRPS27
Homology/Alignments : Family Browser (UCSC)RPS27
Phylogenetic Trees/Animal Genes : TreeFamRPS27
Chemical/Protein Interactions : CTD6232
Chemical/Pharm GKB GenePA34820
Clinical trialRPS27
Cancer Resource (Charite)ENSG00000177954
Other databases
Probes
Litterature
PubMed51 Pubmed reference(s) in Entrez
CoreMineRPS27
iHOPRPS27
OncoSearchRPS27

Bibliography

A growth factor-inducible gene encodes a novel nuclear protein with zinc finger structure.
Fernandez-Pol JA, Klos DJ, Hamilton PD.
J Biol Chem. 1993 Oct 5;268(28):21198-204.
PMID 8407955
 
Expression of metallopanstimulin and oncogenesis in human prostatic carcinoma.
Fernandez-Pol JA, Fletcher JW, Hamilton PD, Klos DJ.
Anticancer Res. 1997 May-Jun;17(3A):1519-30.
PMID 9179190
 
Metallopanstimulin is overexpressed in a patient with colonic carcinoma.
Ganger DR, Hamilton PD, Fletcher JW, Fernandez-Pol JA.
Anticancer Res. 1997 May-Jun;17(3C):1993-9.
PMID 9216656
 
Differential expression of metallopanstimulin/S27 ribosomal protein in melanocytic lesions of the skin.
Santa Cruz DJ, Hamilton PD, Klos DJ, Fernandez-Pol JA.
J Cutan Pathol. 1997 Oct;24(9):533-42. (REVIEW)
PMID 9404850
 
Overexpression of MPS antigens by squamous cell carcinomas of the head and neck: immunohistochemical and serological correlation with FDG positron emission tomography.
Stack BC Jr, Dalsaso TA, Lee C Jr, Lowe VJ, Hamilton PD, Fletcher JW, Fernandez-Pol JA.
Anticancer Res. 1999 Nov-Dec;19(6C):5503-10.
PMID 10697607
 
Differential expression of metallopanstimulin/S27 ribosomal protein in hepatic regeneration and neoplasia.
Ganger DR, Hamilton PD, Klos DJ, Jakate S, McChesney L, Fernandez-Pol JA.
Cancer Detect Prev. 2001;25(3):231-6.
PMID 11425264
 
Identification of metallopanstimulin-1 as a member of a tumor associated antigen in patients with breast cancer.
Atsuta Y, Aoki N, Sato K, Oikawa K, Nochi H, Miyokawa N, Hirata S, Kimura S, Sasajima T, Katagiri M.
Cancer Lett. 2002 Aug 8;182(1):101-7.
PMID 12175529
 
A new assay to screen for head and neck squamous cell carcinoma using the tumor marker metallopanstimulin.
Lee WJ, Keefer K, Hollenbeak CS, Stack BC Jr.
Otolaryngol Head Neck Surg. 2004 Oct;131(4):466-71.
PMID 15467619
 
Metallopanstimulin as a marker for head and neck cancer.
Stack BC Jr, Hollenbeak CS, Lee CM, Dunphy FR, Lowe VJ, Hamilton PD.
World J Surg Oncol. 2004 Dec 14;2:45.
PMID 15598348
 
MDMX regulation of p53 response to ribosomal stress.
Gilkes DM, Chen L, Chen J.
EMBO J. 2006 Nov 29;25(23):5614-25. Epub 2006 Nov 16.
PMID 17110929
 
In vitro and in vivo evidence of metallopanstimulin-1 in gastric cancer progression and tumorigenicity.
Wang YW, Qu Y, Li JF, Chen XH, Liu BY, Gu QL, Zhu ZG.
Clin Cancer Res. 2006 Aug 15;12(16):4965-73.
PMID 16914586
 
Ribosomal protein S27L is a direct p53 target that regulates apoptosis.
He H, Sun Y.
Oncogene. 2007 Apr 26;26(19):2707-16. Epub 2006 Oct 23.
PMID 17057733
 
Ribosomal protein S27-like, a p53-inducible modulator of cell fate in response to genotoxic stress.
Li J, Tan J, Zhuang L, Banerjee B, Yang X, Chau JF, Lee PL, Hande MP, Li B, Yu Q.
Cancer Res. 2007 Dec 1;67(23):11317-26.
PMID 18056458
 
Comparative analysis of processed ribosomal protein pseudogenes in four mammalian genomes.
Balasubramanian S, Zheng D, Liu YJ, Fang G, Frankish A, Carriero N, Robilotto R, Cayting P, Gerstein M.
Genome Biol. 2009;10(1):R2. Epub 2009 Jan 5.
PMID 19123937
 
Extraribosomal function of metallopanstimulin-1: reducing paxillin in head and neck squamous cell carcinoma and inhibiting tumor growth.
Dai Y, Pierson SE, Dudney WC, Stack BC Jr.
Int J Cancer. 2010 Feb 1;126(3):611-9.
PMID 19642098
 
Ribosomal protein S27-like and S27 interplay with p53-MDM2 axis as a target, a substrate and a regulator.
Xiong X, Zhao Y, He H, Sun Y.
Oncogene. 2011 Apr 14;30(15):1798-811. Epub 2010 Dec 20.
PMID 21170087
 
Knockdown of metallopanstimulin-1 inhibits NF-?B signaling at different levels: The role of apoptosis induction of gastric cancer cells.
Yang ZY, Qu Y, Zhang Q, Wei M, Liu CX, Chen XH, Yan M, Zhu ZG, Liu BY, Chen GQ, Wu YL, Gu QL.
Int J Cancer. 2011 Jul 27. doi: 10.1002/ijc.26331. [Epub ahead of print]
PMID 21796632
 
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

Search in all EBI   NCBI

Contributor(s)

Written08-2011Tiffany Pierson, Brendan C Stack Jr
Department of Otolaryngology-Head and Neck Surgery, University of Arkansas for Medical Sciences, AR 72205, USA

Citation

This paper should be referenced as such :
Pierson, T ; Stack, BCJr
RPS27 (ribosomal protein S27)
Atlas Genet Cytogenet Oncol Haematol. 2012;16(2):103-105.
Free online version   Free pdf version   [Bibliographic record ]
URL : http://AtlasGeneticsOncology.org/Genes/RPS27ID45550ch1q21.html

© Atlas of Genetics and Cytogenetics in Oncology and Haematology
indexed on : Sat Jul 26 15:02:02 CEST 2014

Home   Genes   Leukemias   Solid Tumours   Cancer-Prone   Deep Insight   Case Reports   Journals  Portal   Teaching   

For comments and suggestions or contributions, please contact us

jlhuret@AtlasGeneticsOncology.org.