Ribosomal protein S6

RPS6
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	4UG0, 4V6X, 5A2Q, 5AJ0, 4D5L, 4UJE, 5FLX, 4UJC, 3J7P, 4KZZ, 4UJD, 4KZY, 4D61, 3J7R, 4KZX
Identifiers
Aliases	RPS6, S6, ribosomal protein S6
External IDs	OMIM: 180460; MGI: 98159; HomoloGene: 85949; GeneCards: RPS6; OMA:RPS6 - orthologs
Gene location (Human)
Chr.	Chromosome 9 (human)
End	19,380,236 bp
Gene location (Mouse)
Chr.	Chromosome 4 (mouse)
End	86,775,649 bp
RNA expression pattern
	Top expressed in
	skin of hip; ; skin of thigh; ; lactiferous duct; ; gonad; ; pylorus; ; pancreatic ductal cell; ; left ovary; ; vulva; ; germinal epithelium; ; caput epididymis;
	Top expressed in
	uterus; ; thymus; ; ovary; ; embryo; ; lens; ; urinary bladder; ; spleen; ; ventricular zone; ; embryo; ; epiblast;
	More reference expression data
	n/a
Gene ontology
Molecular function	structural constituent of ribosome; protein binding; protein kinase binding; RNA binding;
Cellular component	cell body; cytosol; ribosome; membrane; intracellular anatomical structure; nucleolus; small ribosomal subunit; cytoplasmic ribonucleoprotein granule; nucleus; nucleoplasm; cytoplasm; polysome; cytosolic small ribosomal subunit; dendrite; perinuclear region of cytoplasm; endoplasmic reticulum; ribonucleoprotein complex;
Biological process	viral transcription; SRP-dependent cotranslational protein targeting to membrane; TOR signaling; positive regulation of apoptotic process; translational initiation; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; protein biosynthesis; G1 phase; mitotic cell cycle; placenta development; T cell proliferation involved in immune response; rRNA processing; activation-induced cell death of T cells; mitotic cell cycle checkpoint signaling; gastrulation; mammalian oogenesis stage; T cell differentiation in thymus; ribosomal small subunit biogenesis; glucose homeostasis; negative regulation of apoptotic process; erythrocyte development; G1/S transition of mitotic cell cycle;
	Sources:Amigo / QuickGO
Orthologs
	6194
	20104
	ENSG00000137154
	ENSMUSG00000028495
	P62753
	P62754
	NM_001010
	NM_009096
	NP_001001
	NP_033122
	Wikidata
View/Edit Human	View/Edit Mouse

Ribosomal protein S6 (rpS6 or eS6) is a component of the 40S ribosomal subunit and is therefore involved in translation. Mouse model studies have shown that phosphorylation of eS6 is involved in the regulation of cell size, cell proliferation, and glucose homeostasis.^[5]^[6]^[7]

Studies show that the p70 ribosomal protein S6 kinases (S6K1 and S6K2) and p90 ribosomal protein S6 kinases (RSK) both phosphorylate eS6 and that S6K1 and S6K2 predominate this function.

Pathways leading to the induction of human eS6 phosphorylation have been found to enhance IL-8 protein synthesis. This mechanism is dependent on A/U-rich proximal sequences (APS) found in the 3'UTR of IL-8 immediately after the stop codon.^[8]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000137154 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000028495 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Ruvinsky I, Sharon N, Lerer T, Cohen H, Stolovich-Rain M, Nir T, et al. (September 2005). "Ribosomal protein S6 phosphorylation is a determinant of cell size and glucose homeostasis". Genes & Development. 19 (18): 2199–211. doi:10.1101/gad.351605. PMC 1221890. PMID 16166381.
^ Ruvinsky I, Meyuhas O (June 2006). "Ribosomal protein S6 phosphorylation: from protein synthesis to cell size". Trends in Biochemical Sciences. 31 (6): 342–8. doi:10.1016/j.tibs.2006.04.003. PMID 16679021.
^ Ruvinsky I, Katz M, Dreazen A, Gielchinsky Y, Saada A, Freedman N, et al. (May 2009). "Mice deficient in ribosomal protein S6 phosphorylation suffer from muscle weakness that reflects a growth defect and energy deficit". PLOS ONE. 4 (5): e5618. Bibcode:2009PLoSO...4.5618R. doi:10.1371/journal.pone.0005618. PMC 2682700. PMID 19479038.
^ Ang Z, Abdi Gunawan Koen R, Er JZ, Lee LT, Tam Kit Chung J, Guo H, Ding JL (2019). "Novel AU-rich proximal UTR sequences (APS) enhance CXCL8 synthesis upon the induction of rpS6 phosphorylation". PLOS Genet. 15 (4): e1008077. doi:10.1371/journal.pgen.1008077. PMC 6476525. PMID 30969964.

External links

Ribosomal+Protein+S6 at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
Overview of all the structural information available in the PDB for UniProt: P62753 (Human 40S ribosomal protein S6) at the PDBe-KB.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000137154 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000028495 – 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.

[pmid16166381-5] Ruvinsky I, Sharon N, Lerer T, Cohen H, Stolovich-Rain M, Nir T, et al. (September 2005). "Ribosomal protein S6 phosphorylation is a determinant of cell size and glucose homeostasis". Genes & Development. 19 (18): 2199–211. doi:10.1101/gad.351605. PMC 1221890. PMID 16166381.

[6] Ruvinsky I, Meyuhas O (June 2006). "Ribosomal protein S6 phosphorylation: from protein synthesis to cell size". Trends in Biochemical Sciences. 31 (6): 342–8. doi:10.1016/j.tibs.2006.04.003. PMID 16679021.

[7] Ruvinsky I, Katz M, Dreazen A, Gielchinsky Y, Saada A, Freedman N, et al. (May 2009). "Mice deficient in ribosomal protein S6 phosphorylation suffer from muscle weakness that reflects a growth defect and energy deficit". PLOS ONE. 4 (5): e5618. Bibcode:2009PLoSO...4.5618R. doi:10.1371/journal.pone.0005618. PMC 2682700. PMID 19479038.

[pmid25633224-8] Ang Z, Abdi Gunawan Koen R, Er JZ, Lee LT, Tam Kit Chung J, Guo H, Ding JL (2019). "Novel AU-rich proximal UTR sequences (APS) enhance CXCL8 synthesis upon the induction of rpS6 phosphorylation". PLOS Genet. 15 (4): e1008077. doi:10.1371/journal.pgen.1008077. PMC 6476525. PMID 30969964.

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