40S ribosomal protein S27

RPS27

Available structures

Human UniProt search: PDBe RCSB

List of PDB id codes
4UG0, 4V6X, 5A2Q, 5AJ0, 4KZY, 3J7R, 4D61, 4KZX, 4D5L, 5FLX, 4UJD, 3J7P, 4KZZ, 4UJE, 4UJC

Identifiers

Aliases

RPS27, MPS-1, MPS1, S27, ribosomal protein S27, DBA17

External IDs

OMIM: 603702 HomoloGene: 803 GeneCards: RPS27

Gene location (Human)

Chr.	Chromosome 1 (human)^[1]

Band	1q21.3	Start	153,990,762 bp^[1]
Band	1q21.3	End	153,992,155 bp^[1]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

ganglionic eminence

canal of the cervix

lymph node

Achilles tendon

uterine tube

corpus callosum

gastric mucosa

right uterine tube

left uterine tube

left lobe of thyroid gland

n/a

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	DNA binding structural constituent of ribosome zinc ion binding metal ion binding protein binding RNA binding
Cellular component	cytosol ribosome intracellular anatomical structure nucleus nucleoplasm cytosolic small ribosomal subunit postsynaptic density presynapse glutamatergic synapse GABA-ergic synapse
Biological process	viral transcription SRP-dependent cotranslational protein targeting to membrane translational initiation ribosomal small subunit assembly nuclear-transcribed mRNA catabolic process, nonsense-mediated decay cell population proliferation protein biosynthesis sister chromatid cohesion rRNA processing
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


6232


n/a

Ensembl


ENSG00000177954


n/a

UniProt


P42677


n/a

RefSeq (mRNA)


NM_001030 NM_001349946 NM_001349947


n/a

RefSeq (protein)


NP_001021 NP_001336875 NP_001336876


n/a

Location (UCSC)

Chr 1: 153.99 – 153.99 Mb

n/a

PubMed search

^[2]

n/a

Wikidata

View/Edit Human

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.^[3]^[4]^[5] Metallopanstimulin is a zinc finger protein proposed to be involved DNA repair as well as oncogenesis.^[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 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.^[5]

Clinical significance

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.^[6]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000177954 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ 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.
^ ^a ^b "Entrez Gene: RPS27 ribosomal protein S27 (metallopanstimulin 1)".
^ ^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.

Scurry WC, Stack BC (Dec 2007). "Role of metalloproteins in the clinical management of head and neck squamous cell carcinoma". Head & Neck. 29 (12): 1144–55. CiteSeerX 10.1.1.610.1189. doi:10.1002/hed.20655. PMID 17657798. S2CID 11534394.
Stack BC, Hollenbeak CS, Lee CM, Dunphy FR, Lowe VJ, Hamilton PD (December 2004). "Metallopanstimulin as a marker for head and neck cancer". World Journal of Surgical Oncology. 2: 45. doi:10.1186/1477-7819-2-45. PMC 544581. PMID 15598348.
Lee WJ, Keefer K, Hollenbeak CS, Stack BC (Oct 2004). "A new assay to screen for head and neck squamous cell carcinoma using the tumor marker metallopanstimulin". Otolaryngology–Head and Neck Surgery. 131 (4): 466–71. doi:10.1016/j.otohns.2004.03.011. PMID 15467619. S2CID 22629299.
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.
Fernandez-Pol JA, Klos DJ, Hamilton PD (Aug 1994). "Metallopanstimulin gene product produced in a baculovirus expression system is a nuclear phosphoprotein that binds to DNA". Cell Growth & Differentiation. 5 (8): 811–25. PMID 7986747.
Vladimirov SN, Ivanov AV, Karpova GG, Musolyamov AK, Egorov TA, Thiede B, Wittmann-Liebold B, Otto A (Jul 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.
Kenmochi N, Kawaguchi T, Rozen S, Davis E, Goodman N, Hudson TJ, Tanaka T, Page DC (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.
Yoshihama M, Uechi T, Asakawa S, Kawasaki K, Kato S, Higa S, Maeda N, Minoshima S, Tanaka T, Shimizu N, Kenmochi N (Mar 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.
Atsuta Y, Aoki N, Sato K, Oikawa K, Nochi H, Miyokawa N, Hirata S, Kimura S, Sasajima T, Katagiri M (Aug 2002). "Identification of metallopanstimulin-1 as a member of a tumor associated antigen in patients with breast cancer". Cancer Letters. 182 (1): 101–7. doi:10.1016/S0304-3835(02)00068-X. PMID 12175529.
Martin-Lluesma S, Stucke VM, Nigg EA (Sep 2002). "Role of Hec1 in spindle checkpoint signaling and kinetochore recruitment of Mad1/Mad2". Science. 297 (5590): 2267–70. Bibcode:2002Sci...297.2267M. doi:10.1126/science.1075596. PMID 12351790. S2CID 7879023.
Liu ST, Chan GK, Hittle JC, Fujii G, Lees E, Yen TJ (Apr 2003). "Human MPS1 kinase is required for mitotic arrest induced by the loss of CENP-E from kinetochores". Molecular Biology of the Cell. 14 (4): 1638–51. doi:10.1091/mbc.02-05-0074. PMC 153128. PMID 12686615.
Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, Cruciat C, Eberhard D, Gagneur J, Ghidelli S, Hopf C, Huhse B, Mangano R, Michon AM, Schirle M, Schlegl J, Schwab M, Stein MA, Bauer A, Casari G, Drewes G, Gavin AC, Jackson DB, Joberty G, Neubauer G, Rick J, Kuster B, Superti-Furga G (Feb 2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nature Cell Biology. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216. S2CID 11683986.
Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M (Jan 2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID 15635413. S2CID 4344740.
Yu Y, Ji H, Doudna JA, Leary JA (Jun 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.
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
Bhonde MR, Hanski ML, Budczies J, Cao M, Gillissen B, Moorthy D, Simonetta F, Scherübl H, Truss M, Hagemeier C, Mewes HW, Daniel PT, Zeitz M, Hanski C (Mar 2006). "DNA damage-induced expression of p53 suppresses mitotic checkpoint kinase hMps1: the lack of this suppression in p53MUT cells contributes to apoptosis". The Journal of Biological Chemistry. 281 (13): 8675–85. doi:10.1074/jbc.M511333200. PMID 16446370.
Wang YW, Qu Y, Li JF, Chen XH, Liu BY, Gu QL, Zhu ZG (Aug 2006). "In vitro and in vivo evidence of metallopanstimulin-1 in gastric cancer progression and tumorigenicity". Clinical Cancer Research. 12 (16): 4965–73. doi:10.1158/1078-0432.CCR-05-2316. PMID 16914586.
Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (Nov 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.

Protein biosynthesis: translation (bacterial, archaeal, eukaryotic)

Proteins

Initiation factor

Bacterial

Mitochondrial

MTIF1
MTIF2
MTIF3

Archaeal

aIF1
aIF2
aIF5
aIF6

Eukaryotic

eIF1	eIF1 B SUI1 family eIF1A Y
eIF2	α kinase β γ eIF2A eIF2B 1 2 3 4 5 eIF2D
eIF3	A B C D E F G H I J K L M
eIF4	A 1 2 3 E1 2 3 G 1 2 3 B H
eIF5	EIF5 EIF5A 2 5B
eIF6	EIF6

Elongation factor

Bacterial/Mitochondrial	EF-Tu EF-Ts EF-G EF-4 EF-P TSFM GFM1 GFM2
Archaeal/Eukaryotic	a/eEF-1 A1 2 3 B P1 P2 P3 D E G a/eEF-2

Release factor

Class 1
- eRF1
Class 2/RF3
- GSPT1
- GSPT2

Ribosomal Proteins

Cytoplasmic

60S subunit	RPL3 RPL4 RPL5 RPL6 RPL7 RPL7A RPL8 RPL9 RPL10 RPL10A RPL10-like RPL11 RPL12 RPL13 RPL13A RPL14 RPL15 RPL17 RPL18 RPL18A RPL19 RPL21 RPL22 RPL23 RPL23A RPL24 RPL26 RPL27 RPL27A RPL28 RPL29 RPL30 RPL31 RPL32 RPL34 RPL35 RPL35A RPL36 RPL36A RPL37 RPL37A RPL38 RPL39 RPL40 RPL41 RPLP0 RPLP1 RPLP2 RRP15-like RSL24D1
40S subunit	RPSA RPS2 RPS3 RPS3A RPS4 (RPS4X, RPS4Y1, RPS4Y2) RPS5 RPS6 RPS7 RPS8 RPS9 RPS10 RPS11 RPS12 RPS13 RPS14 RPS15 RPS15A RPS16 RPS17 RPS18 RPS19 RPS20 RPS21 RPS23 RPS24 RPS25 RPS26 RPS27 RPS27A RPS28 RPS29 RPS30 RACK1

Mitochondrial

39S subunit	MRPL1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42
28S subunit	MRPS1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35

Other concepts

Ribosomal RNA / ribosome subunits

Archaea
(70S)

Large (50S):

Small (30S):

Bacteria
(70S)

Large (50S):

Small (30S):

Eukaryotes

Cytoplasmic (80S)	Large (60S): 5S 5.8S 28S Small (40S): 18S
Mitochondrial (55S)	Large (28S): MT-RNR2, 16S MT-tRNA^Val Small (39S): MT-RNR1, 12S
Chloroplast (70S)	Large (50S): 5S 4.5S 23S Small (30S): 16S

Ribosomal proteins

(See article table)

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Function

Clinical significance

References

Further reading