40S ribosomal protein S19

RPS19
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	4UG0, 4V6X, 5A2Q, 5AJ0, 5FLX, 3J7R, 4D61, 4D5L, 4UJD, 3J7P, 4UJE, 4UJC
Identifiers
Aliases	RPS19, DBA, DBA1, S19, Ribosomal protein S19, eS19, LOH19CR1
External IDs	OMIM: 603474; MGI: 1333780; HomoloGene: 37416; GeneCards: RPS19; OMA:RPS19 - orthologs
Gene location (Human)
Chr.	Chromosome 19 (human)
End	41,872,925 bp
Gene location (Mouse)
Chr.	Chromosome 7 (mouse)
End	24,889,806 bp
RNA expression pattern
	Top expressed in
	Top expressed in
	More reference expression data
	n/a
Gene ontology
Molecular function
Cellular component
Biological process
	Sources:Amigo / QuickGO
Orthologs
	6223
	20085
	ENSG00000105372
	ENSMUSG00000040952
	P39019
	Q9CZX8
	NM_001022; NM_001321483; NM_001321484; NM_001321485
	NM_023133
	NP_001013; NP_001308412; NP_001308413; NP_001308414
NP_075622; NP_001347044; NP_001347045; NP_001347047; NP_001347048;
	NP_001347054; NP_001347057
	Wikidata
View/Edit Human	View/Edit Mouse

40S ribosomal protein S19 is a protein that in humans is encoded by the RPS19 gene.^[5]^[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 S19E family of ribosomal proteins. It is located in the cytoplasm. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.^[6]

Clinical significance

Mutations in this gene cause Diamond–Blackfan anemia (DBA), a constitutional erythroblastopenia characterized by absent or decreased erythroid precursors, in a subset of patients. This suggests a possible extra-ribosomal function for this gene in erythropoietic differentiation and proliferation, in addition to its ribosomal function. Higher expression levels of this gene in some primary colon carcinomas compared to matched normal colon tissues has been observed.^[6]

Interactions

Ribosomal protein S19 has been shown to interact with basic fibroblast growth factor.^[7] RPS19 is also secreted extracellularly and its extracellular oligomers (crosslinked by the transglutaminase Coagulation factor XIII) is also known to bind and probably inhibit Macrophage migration inhibitory factor; though S19 oligomers themselves share MCIP's function as another very strong macrophage chemoattractant and bind to anaphylotoxin C5 receptor^[8]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000105372 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000040952 – 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.
^ Kenmochi N, Kawaguchi T, Rozen S, Davis E, Goodman N, Hudson TJ, Tanaka T, Page DC (August 1998). "A map of 75 human ribosomal protein genes". Genome Res. 8 (5): 509–23. doi:10.1101/gr.8.5.509. PMID 9582194.
^ ^a ^b ^c "Entrez Gene: RPS19 ribosomal protein S19".
^ Soulet F, Al Saati T, Roga S, Amalric F, Bouche G (November 2001). "Fibroblast growth factor-2 interacts with free ribosomal protein S19". Biochem. Biophys. Res. Commun. 289 (2): 591–6. doi:10.1006/bbrc.2001.5960. PMID 11716516.
^ Molecular Basis of Cell and Developmental Biology: Ana-Maria Filip, Jörg Klug, Sevil Cayli, Suada Fröhlich, Tamara Henke, Philipp Lacher, Regina Eickhoff, Patrick Bulau, Monika Linder, Christine Carlsson-Skwirut, Lin Leng, Richard Bucala, Sandra Kraemer, Jürgen Bernhagen, and Andreas Meinhardt. "Ribosomal Protein S19 Interacts with Macrophage Migration Inhibitory Factor and Attenuates Its Pro-inflammatory Function"' J. Biol. Chem. 2009 284: 7977–7985. First Published on January 20, 2009, doi:10.1074/jbc.M808620200

Wool IG, Chan YL, Glück A (1996). "Structure and evolution of mammalian ribosomal proteins". Biochem. Cell Biol. 73 (11–12): 933–47. doi:10.1139/o95-101. PMID 8722009.
Morimoto K, Lin S, Sakamoto K (2007). "The functions of RPS19 and their relationship to Diamond-Blackfan anemia: a review". Mol. Genet. Metab. 90 (4): 358–62. doi:10.1016/j.ymgme.2006.11.004. PMID 17178250.
Yamamoto T (2007). "Roles of the ribosomal protein S19 dimer and the C5a receptor in pathophysiological functions of phagocytic leukocytes". Pathol. Int. 57 (1): 1–11. doi:10.1111/j.1440-1827.2007.02049.x. PMID 17199736. S2CID 22946804.
Kondoh N, Schweinfest CW, Henderson KW, Papas TS (1992). "Differential expression of S19 ribosomal protein, laminin-binding protein, and human lymphocyte antigen class I messenger RNAs associated with colon carcinoma progression and differentiation". Cancer Res. 52 (4): 791–6. PMID 1339304.
Vladimirov SN, Ivanov AV, Karpova GG, Musolyamov AK, Egorov TA, Thiede B, Wittmann-Liebold B, Otto A (1996). "Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry". Eur. J. Biochem. 239 (1): 144–9. doi:10.1111/j.1432-1033.1996.0144u.x. PMID 8706699.
Draptchinskaia N, Gustavsson P, Andersson B, Pettersson M, Willig TN, Dianzani I, Ball S, Tchernia G, Klar J, Matsson H, Tentler D, Mohandas N, Carlsson B, Dahl N (1999). "The gene encoding ribosomal protein S19 is mutated in Diamond-Blackfan anaemia". Nat. Genet. 21 (2): 169–75. doi:10.1038/5951. PMID 9988267. S2CID 26664929.
Willig TN, Draptchinskaia N, Dianzani I, Ball S, Niemeyer C, Ramenghi U, Orfali K, Gustavsson P, Garelli E, Brusco A, Tiemann C, Pérignon JL, Bouchier C, Cicchiello L, Dahl N, Mohandas N, Tchernia G (2000). "Mutations in ribosomal protein S19 gene and diamond blackfan anemia: wide variations in phenotypic expression". Blood. 94 (12): 4294–306. PMID 10590074.
Matsson H, Klar J, Draptchinskaia N, Gustavsson P, Carlsson B, Bowers D, de Bont E, Dahl N (2000). "Truncating ribosomal protein S19 mutations and variable clinical expression in Diamond-Blackfan anemia". Hum. Genet. 105 (5): 496–500. doi:10.1007/s004390051136. PMID 10598818.
Tentler D, Gustavsson P, Elinder G, Eklöf O, Gordon L, Mandel A, Dahl N (2000). "A microdeletion in 19q13.2 associated with mental retardation, skeletal malformations, and Diamond-Blackfan anaemia suggests a novel contiguous gene syndrome". J. Med. Genet. 37 (2): 128–31. doi:10.1136/jmg.37.2.128. PMC 1734524. PMID 10662814.
Ramenghi U, Campagnoli MF, Garelli E, Carando A, Brusco A, Bagnara GP, Strippoli P, Izzi GC, Brandalise S, Riccardi R, Dianzani I (2001). "Diamond-Blackfan anemia: report of seven further mutations in the RPS19 gene and evidence of mutation heterogeneity in the Italian population". Blood Cells Mol. Dis. 26 (5): 417–22. doi:10.1006/bcmd.2000.0324. PMID 11112378.
Nishimura T, Horino K, Nishiura H, Shibuya Y, Hiraoka T, Tanase S, Yamamoto T (2001). "Apoptotic cells of an epithelial cell line, AsPC-1, release monocyte chemotactic S19 ribosomal protein dimer". J. Biochem. 129 (3): 445–54. doi:10.1093/oxfordjournals.jbchem.a002876. PMID 11226885.
Soulet F, Al Saati T, Roga S, Amalric F, Bouche G (2002). "Fibroblast growth factor-2 interacts with free ribosomal protein S19". Biochem. Biophys. Res. Commun. 289 (2): 591–6. doi:10.1006/bbrc.2001.5960. PMID 11716516.
Shibuya Y, Shiokawa M, Nishiura H, Nishimura T, Nishino N, Okabe H, Takagi K, Yamamoto T (2001). "Identification of Receptor-Binding Sites of Monocyte Chemotactic S19 Ribosomal Protein Dimer". Am. J. Pathol. 159 (6): 2293–301. doi:10.1016/S0002-9440(10)63079-9. PMC 1850605. PMID 11733378.
Li B, Sun M, He B, Yu J, Zhang YD, Zhang YL (2004). "Identification of differentially expressed genes in human uterine leiomyomas using differential display". Cell Res. 12 (1): 39–45. doi:10.1038/sj.cr.7290108. PMID 11942409.
Da Costa L, Tchernia G, Gascard P, Lo A, Meerpohl J, Niemeyer C, Chasis JA, Fixler J, Mohandas N (2004). "Nucleolar localization of RPS19 protein in normal cells and mislocalization due to mutations in the nucleolar localization signals in 2 Diamond-Blackfan anemia patients: potential insights into pathophysiology". Blood. 101 (12): 5039–45. doi:10.1182/blood-2002-12-3878. PMID 12586610.
Shrestha A, Shiokawa M, Nishimura T, Nishiura H, Tanaka Y, Nishino N, Shibuya Y, Yamamoto T (2003). "Switch Moiety in Agonist/Antagonist Dual Effect of S19 Ribosomal Protein Dimer on Leukocyte Chemotactic C5a Receptor". Am. J. Pathol. 162 (4): 1381–8. doi:10.1016/S0002-9440(10)63934-X. PMC 1851224. PMID 12651630.
Proust A, Da Costa L, Rince P, Landois A, Tamary H, Zaizov R, Tchernia G, Delaunay J (2003). "Ten novel Diamond-Blackfan anemia mutations and three polymorphisms within the rps19 gene". Hematol. J. 4 (2): 132–6. doi:10.1038/sj.thj.6200230. PMID 12750732.

External links

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000105372 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000040952 – 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.

[pmid9582194-5] Kenmochi N, Kawaguchi T, Rozen S, Davis E, Goodman N, Hudson TJ, Tanaka T, Page DC (August 1998). "A map of 75 human ribosomal protein genes". Genome Res. 8 (5): 509–23. doi:10.1101/gr.8.5.509. PMID 9582194.

[entrez-6] "Entrez Gene: RPS19 ribosomal protein S19".

[pmid11716516-7] Soulet F, Al Saati T, Roga S, Amalric F, Bouche G (November 2001). "Fibroblast growth factor-2 interacts with free ribosomal protein S19". Biochem. Biophys. Res. Commun. 289 (2): 591–6. doi:10.1006/bbrc.2001.5960. PMID 11716516.

[8] Molecular Basis of Cell and Developmental Biology: Ana-Maria Filip, Jörg Klug, Sevil Cayli, Suada Fröhlich, Tamara Henke, Philipp Lacher, Regina Eickhoff, Patrick Bulau, Monika Linder, Christine Carlsson-Skwirut, Lin Leng, Richard Bucala, Sandra Kraemer, Jürgen Bernhagen, and Andreas Meinhardt. "Ribosomal Protein S19 Interacts with Macrophage Migration Inhibitory Factor and Attenuates Its Pro-inflammatory Function"' J. Biol. Chem. 2009 284: 7977–7985. First Published on January 20, 2009, doi:10.1074/jbc.M808620200

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