RS19_MOUSE
ID RS19_MOUSE Reviewed; 145 AA.
AC Q9CZX8; Q5M9J4;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=40S ribosomal protein S19;
GN Name=Rps19;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RA Willig T.-N.D., Peters L.L., Parra M.K., Tchernia G., Mohandas N.;
RT "RPS19 gene in Mus musculus and Drosophila melanogaster, and conserved
RT features among 40 different species.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hippocampus, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH RPS19BP1.
RX PubMed=16289379; DOI=10.1016/j.bbrc.2005.10.184;
RA Maeda N., Toku S., Kenmochi N., Tanaka T.;
RT "A novel nucleolar protein interacts with ribosomal protein S19.";
RL Biochem. Biophys. Res. Commun. 339:41-46(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-115, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-143, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Required for pre-rRNA processing and maturation of 40S
CC ribosomal subunits. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RPS19BP1. {ECO:0000269|PubMed:16289379}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS19 family.
CC {ECO:0000305}.
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DR EMBL; AF216207; AAF65683.1; -; Genomic_DNA.
DR EMBL; AK013524; BAB28898.1; -; mRNA.
DR EMBL; AK018725; BAB31370.1; -; mRNA.
DR EMBL; AK028244; BAC25836.1; -; mRNA.
DR EMBL; BC034506; AAH34506.1; -; mRNA.
DR EMBL; BC086938; AAH86938.1; -; mRNA.
DR CCDS; CCDS20966.1; -.
DR RefSeq; NP_075622.1; NM_023133.1.
DR RefSeq; XP_006539743.1; XM_006539680.2.
DR RefSeq; XP_006539744.1; XM_006539681.2.
DR PDB; 7CPU; EM; 2.82 A; ST=1-145.
DR PDB; 7CPV; EM; 3.03 A; ST=1-145.
DR PDB; 7LS1; EM; 3.30 A; B3=1-145.
DR PDB; 7LS2; EM; 3.10 A; B3=1-145.
DR PDBsum; 7CPU; -.
DR PDBsum; 7CPV; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; Q9CZX8; -.
DR SMR; Q9CZX8; -.
DR BioGRID; 203007; 83.
DR ComplexPortal; CPX-5261; 40S cytosolic small ribosomal subunit.
DR IntAct; Q9CZX8; 5.
DR MINT; Q9CZX8; -.
DR STRING; 10090.ENSMUSP00000104067; -.
DR iPTMnet; Q9CZX8; -.
DR PhosphoSitePlus; Q9CZX8; -.
DR SwissPalm; Q9CZX8; -.
DR EPD; Q9CZX8; -.
DR jPOST; Q9CZX8; -.
DR MaxQB; Q9CZX8; -.
DR PaxDb; Q9CZX8; -.
DR PeptideAtlas; Q9CZX8; -.
DR PRIDE; Q9CZX8; -.
DR ProteomicsDB; 299817; -.
DR TopDownProteomics; Q9CZX8; -.
DR Antibodypedia; 30832; 339 antibodies from 35 providers.
DR DNASU; 20085; -.
DR Ensembl; ENSMUST00000108429; ENSMUSP00000104067; ENSMUSG00000040952.
DR Ensembl; ENSMUST00000108430; ENSMUSP00000104068; ENSMUSG00000040952.
DR GeneID; 20085; -.
DR KEGG; mmu:20085; -.
DR UCSC; uc009fqq.1; mouse.
DR CTD; 6223; -.
DR MGI; MGI:1333780; Rps19.
DR VEuPathDB; HostDB:ENSMUSG00000040952; -.
DR eggNOG; KOG3411; Eukaryota.
DR GeneTree; ENSGT00390000013102; -.
DR InParanoid; Q9CZX8; -.
DR OMA; MTAPRNK; -.
DR OrthoDB; 1434984at2759; -.
DR PhylomeDB; Q9CZX8; -.
DR TreeFam; TF315008; -.
DR Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-MMU-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-MMU-72649; Translation initiation complex formation.
DR Reactome; R-MMU-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-MMU-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-MMU-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-MMU-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-MMU-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR BioGRID-ORCS; 20085; 26 hits in 77 CRISPR screens.
DR ChiTaRS; Rps19; mouse.
DR PRO; PR:Q9CZX8; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9CZX8; protein.
DR Bgee; ENSMUSG00000040952; Expressed in blastocyst and 64 other tissues.
DR ExpressionAtlas; Q9CZX8; baseline and differential.
DR Genevisible; Q9CZX8; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:MGI.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; ISS:HGNC-UCL.
DR GO; GO:0005730; C:nucleolus; ISS:HGNC-UCL.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0005840; C:ribosome; ISO:MGI.
DR GO; GO:0015935; C:small ribosomal subunit; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0017134; F:fibroblast growth factor binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:0031369; F:translation initiation factor binding; ISO:MGI.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISO:MGI.
DR GO; GO:0030218; P:erythrocyte differentiation; ISS:HGNC-UCL.
DR GO; GO:0031640; P:killing of cells of another organism; ISO:MGI.
DR GO; GO:0030490; P:maturation of SSU-rRNA; ISO:MGI.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISO:MGI.
DR GO; GO:0002548; P:monocyte chemotaxis; ISO:MGI.
DR GO; GO:0060266; P:negative regulation of respiratory burst involved in inflammatory response; ISO:MGI.
DR GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
DR GO; GO:0007000; P:nucleolus organization; ISO:MGI.
DR GO; GO:0060265; P:positive regulation of respiratory burst involved in inflammatory response; ISO:MGI.
DR GO; GO:0000028; P:ribosomal small subunit assembly; ISO:MGI.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; ISO:MGI.
DR GO; GO:0006364; P:rRNA processing; ISO:MGI.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR001266; Ribosomal_S19e.
DR InterPro; IPR018277; Ribosomal_S19e_CS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11710; PTHR11710; 1.
DR Pfam; PF01090; Ribosomal_S19e; 1.
DR SMART; SM01413; Ribosomal_S19e; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00628; RIBOSOMAL_S19E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Methylation; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..145
FT /note="40S ribosomal protein S19"
FT /id="PRO_0000153811"
FT MOD_RES 23
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P39019"
FT MOD_RES 67
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P39019"
FT MOD_RES 111
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P39019"
FT MOD_RES 115
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 143
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 145 AA; 16085 MW; 180032B887FA6E41 CRC64;
MPGVTVKDVN QQEFVRALAA FLKKSGKLKV PEWVDTVKLA KHKELAPYDE NWFYTRAAST
ARHLYLRGGA GVGSMTKIYG GRQRNGVRPS HFSRGSKSVA RRVLQALEGL KMVEKDQDGG
RKLTPQGQRD LDRIAGQVAA ANKKH
