ID RS15_HUMAN Reviewed; 145 AA. AC P62841; A5D8V9; P11174; Q3KRA1; Q9UDC2; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 188. DE RecName: Full=Small ribosomal subunit protein uS19 {ECO:0000303|PubMed:24524803}; DE AltName: Full=40S ribosomal protein S15; DE AltName: Full=RIG protein; GN Name=RPS15; Synonyms=RIG; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2821540; DOI=10.1073/pnas.84.19.6659; RA Inoue C., Shiga K., Takasawa S., Kitagawa M., Yamamoto H., Okamoto H.; RT "Evolutionary conservation of the insulinoma gene rig and its possible RT function."; RL Proc. Natl. Acad. Sci. U.S.A. 84:6659-6662(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2159154; DOI=10.1073/pnas.87.9.3594; RA Shiga K., Yamamoto H., Okamoto H.; RT "Isolation and characterization of the human homologue of rig and its RT pseudogenes: the functional gene has features characteristic of RT housekeeping genes."; RL Proc. Natl. Acad. Sci. U.S.A. 87:3594-3598(1990). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Yu L., Zhao S.Y.; RT "Cloning and characterization of human insulinoma protein."; RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pancreas; 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-145. RC TISSUE=Brain; RX PubMed=1466847; DOI=10.1097/00002030-199210000-00014; RA Rosenblatt J.D., Tomkins P., Rosenthal M., Kacena A., Chan G., RA Valderama R., Harrington W. Jr., Saxton E., Diagne A., Zhao J.-Q., RA Mitsuyasu R.T., Weisbart R.H.; RT "Progressive spastic myelopathy in a patient co-infected with HIV-1 and RT HTLV-II: autoantibodies to the human homologue of rig in blood and RT cerebrospinal fluid."; RL AIDS 6:1151-1158(1992). RN [6] RP PROTEIN SEQUENCE OF 101-116. RC TISSUE=Placenta; RX PubMed=8706699; DOI=10.1111/j.1432-1033.1996.0144u.x; RA Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A., RA Thiede B., Wittmann-Liebold B., Otto A.; RT "Characterization of the human small-ribosomal-subunit proteins by N- RT terminal and internal sequencing, and mass spectrometry."; RL Eur. J. Biochem. 239:144-149(1996). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [11] RP NOMENCLATURE. RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002; RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R., RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A., RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V., RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J., RA Williamson J.R., Wilson D., Yonath A., Yusupov M.; RT "A new system for naming ribosomal proteins."; RL Curr. Opin. Struct. Biol. 24:165-169(2014). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [14] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-108, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [15] RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF RIBOSOME, FUNCTION, RP SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=23636399; DOI=10.1038/nature12104; RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M., RA Wilson D.N., Beckmann R.; RT "Structures of the human and Drosophila 80S ribosome."; RL Nature 497:80-85(2013). CC -!- FUNCTION: Component of the small ribosomal subunit (PubMed:23636399). CC The ribosome is a large ribonucleoprotein complex responsible for the CC synthesis of proteins in the cell (PubMed:23636399). CC {ECO:0000269|PubMed:23636399}. CC -!- SUBUNIT: Component of the small ribosomal subunit. CC {ECO:0000269|PubMed:23636399}. CC -!- INTERACTION: CC P62841; Q7L622: G2E3; NbExp=3; IntAct=EBI-372635, EBI-751757; CC P62841; Q5S007: LRRK2; NbExp=9; IntAct=EBI-372635, EBI-5323863; CC P62841; P62937: PPIA; NbExp=3; IntAct=EBI-372635, EBI-437708; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS19 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J02984; AAA36036.1; -; mRNA. DR EMBL; M32405; AAA36568.1; -; Genomic_DNA. DR EMBL; AF145025; AAP97277.1; -; mRNA. DR EMBL; BC064908; AAH64908.1; -; mRNA. DR EMBL; BC105810; AAI05811.1; -; mRNA. DR EMBL; BC141832; AAI41833.1; -; mRNA. DR CCDS; CCDS12067.1; -. DR PIR; A35908; R3HU15. DR RefSeq; NP_001009.1; NM_001018.4. DR PDB; 4UG0; EM; -; SP=1-145. DR PDB; 4V6X; EM; 5.00 A; AP=1-145. DR PDB; 5A2Q; EM; 3.90 A; P=1-145. DR PDB; 5AJ0; EM; 3.50 A; BP=1-145. DR PDB; 5FLX; EM; 3.90 A; P=1-145. DR PDB; 5LKS; EM; 3.60 A; SP=1-145. DR PDB; 5OA3; EM; 4.30 A; P=1-145. DR PDB; 5T2C; EM; 3.60 A; Ax=1-145. DR PDB; 5VYC; X-ray; 6.00 A; P1/P2/P3/P4/P5/P6=1-145. DR PDB; 6FEC; EM; 6.30 A; n=4-130. DR PDB; 6G18; EM; 3.60 A; P=1-145. DR PDB; 6G4S; EM; 4.00 A; P=1-145. DR PDB; 6G4W; EM; 4.50 A; P=1-145. DR PDB; 6G51; EM; 4.10 A; P=1-145. DR PDB; 6G53; EM; 4.50 A; P=1-145. DR PDB; 6G5H; EM; 3.60 A; P=1-145. DR PDB; 6G5I; EM; 3.50 A; P=1-145. DR PDB; 6IP5; EM; 3.90 A; 2w=1-145. DR PDB; 6IP6; EM; 4.50 A; 2w=1-145. DR PDB; 6IP8; EM; 3.90 A; 2w=1-145. DR PDB; 6OLE; EM; 3.10 A; SP=10-136. DR PDB; 6OLF; EM; 3.90 A; SP=10-136. DR PDB; 6OLG; EM; 3.40 A; BP=12-131. DR PDB; 6OLI; EM; 3.50 A; SP=10-136. DR PDB; 6OLZ; EM; 3.90 A; BP=12-131. DR PDB; 6OM0; EM; 3.10 A; SP=10-136. DR PDB; 6OM7; EM; 3.70 A; SP=10-136. DR PDB; 6QZP; EM; 2.90 A; SP=10-136. DR PDB; 6XA1; EM; 2.80 A; SP=13-143. DR PDB; 6Y0G; EM; 3.20 A; SP=1-145. DR PDB; 6Y2L; EM; 3.00 A; SP=1-145. DR PDB; 6Y57; EM; 3.50 A; SP=1-145. DR PDB; 6YBS; EM; 3.10 A; b=1-145. DR PDB; 6Z6L; EM; 3.00 A; SP=1-145. DR PDB; 6Z6M; EM; 3.10 A; SP=1-145. DR PDB; 6Z6N; EM; 2.90 A; SP=1-145. DR PDB; 6ZLW; EM; 2.60 A; Q=1-145. DR PDB; 6ZM7; EM; 2.70 A; SP=1-145. DR PDB; 6ZME; EM; 3.00 A; SP=1-145. DR PDB; 6ZMI; EM; 2.60 A; SP=1-145. DR PDB; 6ZMO; EM; 3.10 A; SP=1-145. DR PDB; 6ZMT; EM; 3.00 A; Q=1-145. DR PDB; 6ZMW; EM; 3.70 A; b=1-145. DR PDB; 6ZN5; EM; 3.20 A; Q=15-134. DR PDB; 6ZOJ; EM; 2.80 A; P=1-145. DR PDB; 6ZOL; EM; 2.80 A; P=1-145. DR PDB; 6ZON; EM; 3.00 A; o=1-145. DR PDB; 6ZP4; EM; 2.90 A; o=1-145. DR PDB; 6ZUO; EM; 3.10 A; P=1-145. DR PDB; 6ZV6; EM; 2.90 A; P=1-145. DR PDB; 6ZVH; EM; 2.90 A; P=10-138. DR PDB; 6ZVJ; EM; 3.80 A; o=15-133. DR PDB; 6ZXD; EM; 3.20 A; P=1-145. DR PDB; 6ZXE; EM; 3.00 A; P=1-145. DR PDB; 6ZXF; EM; 3.70 A; P=1-145. DR PDB; 6ZXG; EM; 2.60 A; P=1-145. DR PDB; 6ZXH; EM; 2.70 A; P=1-145. DR PDB; 7A09; EM; 3.50 A; o=1-145. DR PDB; 7K5I; EM; 2.90 A; P=1-145. DR PDB; 7QP6; EM; 4.70 A; b=1-145. DR PDB; 7QP7; EM; 3.70 A; b=1-145. DR PDB; 7R4X; EM; 2.15 A; P=1-145. DR PDB; 7TQL; EM; 3.40 A; Q=15-129. DR PDB; 7WTT; EM; 3.10 A; P=1-145. DR PDB; 7WTU; EM; 3.00 A; P=1-145. DR PDB; 7WTV; EM; 3.50 A; P=1-145. DR PDB; 7WTW; EM; 3.20 A; P=1-145. DR PDB; 7WTX; EM; 3.10 A; P=1-145. DR PDB; 7WTZ; EM; 3.00 A; P=1-145. DR PDB; 7WU0; EM; 3.30 A; P=1-145. DR PDB; 7XNX; EM; 2.70 A; SP=1-145. DR PDB; 7XNY; EM; 2.50 A; SP=1-145. DR PDB; 8G5Y; EM; 2.29 A; SP=1-145. DR PDB; 8G60; EM; 2.54 A; SP=1-145. DR PDB; 8G61; EM; 2.94 A; SP=1-145. DR PDB; 8G6J; EM; 2.80 A; SP=1-145. DR PDB; 8GLP; EM; 1.67 A; SP=1-145. DR PDB; 8JDJ; EM; 2.50 A; AB=1-145. DR PDB; 8JDK; EM; 2.26 A; AB=1-145. DR PDB; 8JDL; EM; 2.42 A; AB=1-145. DR PDB; 8JDM; EM; 2.67 A; AB=1-145. DR PDB; 8PPK; EM; 2.98 A; P=1-145. DR PDB; 8PPL; EM; 2.65 A; AP=1-145. DR PDB; 8T4S; EM; 2.60 A; P=1-145. DR PDBsum; 4UG0; -. DR PDBsum; 4V6X; -. DR PDBsum; 5A2Q; -. DR PDBsum; 5AJ0; -. DR PDBsum; 5FLX; -. DR PDBsum; 5LKS; -. DR PDBsum; 5OA3; -. DR PDBsum; 5T2C; -. DR PDBsum; 5VYC; -. DR PDBsum; 6FEC; -. DR PDBsum; 6G18; -. DR PDBsum; 6G4S; -. DR PDBsum; 6G4W; -. DR PDBsum; 6G51; -. DR PDBsum; 6G53; -. DR PDBsum; 6G5H; -. DR PDBsum; 6G5I; -. DR PDBsum; 6IP5; -. DR PDBsum; 6IP6; -. DR PDBsum; 6IP8; -. DR PDBsum; 6OLE; -. DR PDBsum; 6OLF; -. DR PDBsum; 6OLG; -. DR PDBsum; 6OLI; -. DR PDBsum; 6OLZ; -. DR PDBsum; 6OM0; -. DR PDBsum; 6OM7; -. DR PDBsum; 6QZP; -. DR PDBsum; 6XA1; -. DR PDBsum; 6Y0G; -. DR PDBsum; 6Y2L; -. DR PDBsum; 6Y57; -. DR PDBsum; 6YBS; -. DR PDBsum; 6Z6L; -. DR PDBsum; 6Z6M; -. DR PDBsum; 6Z6N; -. DR PDBsum; 6ZLW; -. DR PDBsum; 6ZM7; -. DR PDBsum; 6ZME; -. DR PDBsum; 6ZMI; -. DR PDBsum; 6ZMO; -. DR PDBsum; 6ZMT; -. DR PDBsum; 6ZMW; -. DR PDBsum; 6ZN5; -. DR PDBsum; 6ZOJ; -. DR PDBsum; 6ZOL; -. DR PDBsum; 6ZON; -. DR PDBsum; 6ZP4; -. DR PDBsum; 6ZUO; -. DR PDBsum; 6ZV6; -. DR PDBsum; 6ZVH; -. DR PDBsum; 6ZVJ; -. DR PDBsum; 6ZXD; -. DR PDBsum; 6ZXE; -. DR PDBsum; 6ZXF; -. DR PDBsum; 6ZXG; -. DR PDBsum; 6ZXH; -. DR PDBsum; 7A09; -. DR PDBsum; 7K5I; -. DR PDBsum; 7QP6; -. DR PDBsum; 7QP7; -. DR PDBsum; 7R4X; -. DR PDBsum; 7TQL; -. DR PDBsum; 7WTT; -. DR PDBsum; 7WTU; -. DR PDBsum; 7WTV; -. DR PDBsum; 7WTW; -. DR PDBsum; 7WTX; -. DR PDBsum; 7WTZ; -. DR PDBsum; 7WU0; -. DR PDBsum; 7XNX; -. DR PDBsum; 7XNY; -. DR PDBsum; 8G5Y; -. DR PDBsum; 8G60; -. DR PDBsum; 8G61; -. DR PDBsum; 8G6J; -. DR PDBsum; 8GLP; -. DR PDBsum; 8JDJ; -. DR PDBsum; 8JDK; -. DR PDBsum; 8JDL; -. DR PDBsum; 8JDM; -. DR PDBsum; 8PPK; -. DR PDBsum; 8PPL; -. DR PDBsum; 8T4S; -. DR AlphaFoldDB; P62841; -. DR EMDB; EMD-10668; -. DR EMDB; EMD-10674; -. DR EMDB; EMD-10690; -. DR EMDB; EMD-10772; -. DR EMDB; EMD-11098; -. DR EMDB; EMD-11099; -. DR EMDB; EMD-11100; -. DR EMDB; EMD-11276; -. DR EMDB; EMD-11288; -. DR EMDB; EMD-11289; -. DR EMDB; EMD-11292; -. DR EMDB; EMD-11299; -. DR EMDB; EMD-11301; -. DR EMDB; EMD-11302; -. DR EMDB; EMD-11310; -. DR EMDB; EMD-11320; -. DR EMDB; EMD-11322; -. DR EMDB; EMD-11325; -. DR EMDB; EMD-11335; -. DR EMDB; EMD-11440; -. DR EMDB; EMD-11441; -. DR EMDB; EMD-11456; -. DR EMDB; EMD-11458; -. DR EMDB; EMD-11517; -. DR EMDB; EMD-11518; -. DR EMDB; EMD-11519; -. DR EMDB; EMD-11520; -. DR EMDB; EMD-11521; -. DR EMDB; EMD-11602; -. DR EMDB; EMD-14113; -. DR EMDB; EMD-14114; -. DR EMDB; EMD-14317; -. DR EMDB; EMD-17804; -. DR EMDB; EMD-17805; -. DR EMDB; EMD-22681; -. DR EMDB; EMD-26067; -. DR EMDB; EMD-29757; -. DR EMDB; EMD-29758; -. DR EMDB; EMD-29759; -. DR EMDB; EMD-29760; -. DR EMDB; EMD-29771; -. DR EMDB; EMD-32800; -. DR EMDB; EMD-32801; -. DR EMDB; EMD-32802; -. DR EMDB; EMD-32803; -. DR EMDB; EMD-32804; -. DR EMDB; EMD-32806; -. DR EMDB; EMD-32807; -. DR EMDB; EMD-33329; -. DR EMDB; EMD-33330; -. DR EMDB; EMD-3770; -. DR EMDB; EMD-3883; -. DR EMDB; EMD-40205; -. DR EMDB; EMD-4070; -. DR EMDB; EMD-41039; -. DR EMDB; EMD-4242; -. DR EMDB; EMD-4337; -. DR EMDB; EMD-4348; -. DR EMDB; EMD-4349; -. DR EMDB; EMD-4350; -. DR EMDB; EMD-4351; -. DR EMDB; EMD-4352; -. DR EMDB; EMD-4353; -. DR EMDB; EMD-9701; -. DR EMDB; EMD-9702; -. DR EMDB; EMD-9703; -. DR SMR; P62841; -. DR BioGRID; 112123; 384. DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit. DR CORUM; P62841; -. DR IntAct; P62841; 91. DR MINT; P62841; -. DR STRING; 9606.ENSP00000466010; -. DR GlyGen; P62841; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P62841; -. DR MetOSite; P62841; -. DR PhosphoSitePlus; P62841; -. DR SwissPalm; P62841; -. DR BioMuta; RPS15; -. DR DMDM; 51338641; -. DR EPD; P62841; -. DR jPOST; P62841; -. DR MassIVE; P62841; -. DR MaxQB; P62841; -. DR PaxDb; 9606-ENSP00000467466; -. DR PeptideAtlas; P62841; -. DR ProteomicsDB; 57433; -. DR Pumba; P62841; -. DR TopDownProteomics; P62841; -. DR Antibodypedia; 22700; 240 antibodies from 28 providers. DR DNASU; 6209; -. DR Ensembl; ENST00000592588.7; ENSP00000467466.3; ENSG00000115268.10. DR GeneID; 6209; -. DR KEGG; hsa:6209; -. DR MANE-Select; ENST00000592588.7; ENSP00000467466.3; NM_001018.5; NP_001009.1. DR UCSC; uc002lsp.2; human. DR AGR; HGNC:10388; -. DR CTD; 6209; -. DR DisGeNET; 6209; -. DR GeneCards; RPS15; -. DR HGNC; HGNC:10388; RPS15. DR HPA; ENSG00000115268; Low tissue specificity. DR MalaCards; RPS15; -. DR MIM; 180535; gene. DR neXtProt; NX_P62841; -. DR OpenTargets; ENSG00000115268; -. DR Orphanet; 67038; B-cell chronic lymphocytic leukemia. DR PharmGKB; PA34787; -. DR VEuPathDB; HostDB:ENSG00000115268; -. DR eggNOG; KOG0898; Eukaryota. DR GeneTree; ENSGT00390000000475; -. DR InParanoid; P62841; -. DR OMA; IKTHVRD; -. DR OrthoDB; 8624at2759; -. DR PhylomeDB; P62841; -. DR PathwayCommons; P62841; -. DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression. DR Reactome; R-HSA-156902; Peptide chain elongation. DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane. DR Reactome; R-HSA-192823; Viral mRNA Translation. DR Reactome; R-HSA-2408557; Selenocysteine synthesis. DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol. DR Reactome; R-HSA-72649; Translation initiation complex formation. DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits. DR Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex. DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition. DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit. DR Reactome; R-HSA-72764; Eukaryotic Translation Termination. DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs. DR Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency. DR Reactome; R-HSA-9735869; SARS-CoV-1 modulates host translation machinery. DR Reactome; R-HSA-9754678; SARS-CoV-2 modulates host translation machinery. DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC). DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC). DR SignaLink; P62841; -. DR SIGNOR; P62841; -. DR BioGRID-ORCS; 6209; 807 hits in 1093 CRISPR screens. DR ChiTaRS; RPS15; human. DR EvolutionaryTrace; P62841; -. DR GeneWiki; RPS15; -. DR GenomeRNAi; 6209; -. DR Pharos; P62841; Tbio. DR PRO; PR:P62841; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P62841; Protein. DR Bgee; ENSG00000115268; Expressed in pituitary gland and 101 other cell types or tissues. DR ExpressionAtlas; P62841; baseline and differential. DR GO; GO:0005737; C:cytoplasm; NAS:ComplexPortal. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; NAS:UniProtKB. DR GO; GO:0045202; C:synapse; IEA:Ensembl. DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB. DR GO; GO:0097371; F:MDM2/MDM4 family protein binding; IPI:FlyBase. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase. DR GO; GO:1990948; F:ubiquitin ligase inhibitor activity; IDA:FlyBase. DR GO; GO:0002181; P:cytoplasmic translation; NAS:ComplexPortal. DR GO; GO:0097421; P:liver regeneration; IEA:Ensembl. DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB. DR GO; GO:1901798; P:positive regulation of signal transduction by p53 class mediator; IDA:FlyBase. DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central. DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:UniProtKB. DR GO; GO:0000056; P:ribosomal small subunit export from nucleus; IMP:UniProtKB. DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB. DR GO; GO:0006412; P:translation; IC:UniProtKB. DR HAMAP; MF_00531; Ribosomal_uS19; 1. DR InterPro; IPR002222; Ribosomal_uS19. DR InterPro; IPR020934; Ribosomal_uS19_CS. DR InterPro; IPR005713; Ribosomal_uS19_euk/arc. DR InterPro; IPR023575; Ribosomal_uS19_SF. DR NCBIfam; TIGR01025; uS19_arch; 1. DR PANTHER; PTHR11880:SF2; 40S RIBOSOMAL PROTEIN S15; 1. DR PANTHER; PTHR11880; RIBOSOMAL PROTEIN S19P FAMILY MEMBER; 1. DR Pfam; PF00203; Ribosomal_S19; 1. DR PIRSF; PIRSF002144; Ribosomal_S19; 1. DR PRINTS; PR00975; RIBOSOMALS19. DR SUPFAM; SSF54570; Ribosomal protein S19; 1. DR PROSITE; PS00323; RIBOSOMAL_S19; 1. DR Genevisible; P62841; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; KW Isopeptide bond; Reference proteome; Ribonucleoprotein; Ribosomal protein; KW Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..145 FT /note="Small ribosomal subunit protein uS19" FT /id="PRO_0000130027" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22814378" FT CROSSLNK 108 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT STRAND 16..19 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 22..27 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 30..36 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 39..46 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 51..65 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 69..71 FT /evidence="ECO:0007829|PDB:6ZV6" FT STRAND 76..78 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 87..89 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 93..97 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 99..106 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 109..111 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 112..115 FT /evidence="ECO:0007829|PDB:6ZV6" FT HELIX 116..119 FT /evidence="ECO:0007829|PDB:7R4X" FT TURN 133..136 FT /evidence="ECO:0007829|PDB:8T4S" FT HELIX 139..141 FT /evidence="ECO:0007829|PDB:6ZXG" SQ SEQUENCE 145 AA; 17040 MW; CA2C682302C7B387 CRC64; MAEVEQKKKR TFRKFTYRGV DLDQLLDMSY EQLMQLYSAR QRRRLNRGLR RKQHSLLKRL RKAKKEAPPM EKPEVVKTHL RDMIILPEMV GSMVGVYNGK TFNQVEIKPE MIGHYLGEFS ITYKPVKHGR PGIGATHSSR FIPLK //