ID RS19_HUMAN Reviewed; 145 AA. AC P39019; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 220. DE RecName: Full=Small ribosomal subunit protein eS19 {ECO:0000303|PubMed:24524803}; DE AltName: Full=40S ribosomal protein S19; GN Name=RPS19 {ECO:0000312|HGNC:HGNC:10402}; 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], AND TISSUE SPECIFICITY. RX PubMed=1339304; RA Kondoh N., Schweinfest C.W., Henderson K.W., Papas T.S.; RT "Differential expression of S19 ribosomal protein, laminin-binding protein, RT and human lymphocyte antigen class I messenger RNAs associated with colon RT carcinoma progression and differentiation."; RL Cancer Res. 52:791-796(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS DBA1 ARG-52 AND TRP-62. RX PubMed=9988267; DOI=10.1038/5951; RA Draptchinskaia N., Gustavsson P., Andersson B., Pettersson M., RA Willig T.-N.D., Dianzani I., Ball S., Tchernia G., Klar J., Matsson H., RA Tentler D., Mohandas N., Carlsson B., Dahl N.; RT "The gene encoding ribosomal protein S19 is mutated in Diamond-Blackfan RT anaemia."; RL Nat. Genet. 21:169-175(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon, Eye, and Placenta; 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 PROTEIN SEQUENCE OF 2-11. 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 [5] RP PROTEIN SEQUENCE OF 2-24; 30-38; 83-94; 102-111 AND 134-145, CLEAVAGE OF RP INITIATOR METHIONINE, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma, and Mammary carcinoma; RA Bienvenut W.V., Calvo F., Kolch W., Lourenco F., Olson M.F.; RL Submitted (DEC-2009) to UniProtKB. RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 120-137. RX PubMed=9582194; DOI=10.1101/gr.8.5.509; RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J., RA Tanaka T., Page D.C.; RT "A map of 75 human ribosomal protein genes."; RL Genome Res. 8:509-523(1998). 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 REVIEW ON DBA1 VARIANTS. RX PubMed=15075082; RA Campagnoli M.F., Garelli E., Quarello P., Carando A., Varotto S., RA Nobili B., Longoni D., Pecile V., Zecca M., Dufour C., Ramenghi U., RA Dianzan I.; RT "Molecular basis of Diamond-Blackfan anemia: new findings from the Italian RT registry and a review of the literature."; RL Haematologica 89:480-489(2004). RN [9] RP FUNCTION. RX PubMed=16990592; DOI=10.1182/blood-2006-07-038232; RA Flygare J., Aspesi A., Bailey J.C., Miyake K., Caffrey J.M., Karlsson S., RA Ellis S.R.; RT "Human RPS19, the gene mutated in Diamond-Blackfan anemia, encodes a RT ribosomal protein required for the maturation of 40S ribosomal subunits."; RL Blood 109:980-986(2007). RN [10] RP SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANTS DBA1 PHE-15; PRO-18; RP LEU-47; ARG-52; GLN-56; PRO-57; GLU-61; GLN-62; TRP-62; HIS-101 AND RP ARG-120. RX PubMed=17517689; DOI=10.1093/hmg/ddm120; RA Angelini M., Cannata S., Mercaldo V., Gibello L., Santoro C., Dianzani I., RA Loreni F.; RT "Missense mutations associated with Diamond-Blackfan anemia affect the RT assembly of ribosomal protein S19 into the ribosome."; RL Hum. Mol. Genet. 16:1720-1727(2007). RN [11] RP REVIEW ON VARIANTS DBA1. RX PubMed=18412286; DOI=10.1002/humu.20752; RA Campagnoli M.F., Ramenghi U., Armiraglio M., Quarello P., Garelli E., RA Carando A., Avondo F., Pavesi E., Fribourg S., Gleizes P.E., Loreni F., RA Dianzani I.; RT "RPS19 mutations in patients with Diamond-Blackfan anemia."; RL Hum. Mutat. 29:911-920(2008). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-23 AND LYS-111, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [13] RP INTERACTION WITH SIN NOMBRE HANTAVIRUS NUCLEOPROTEIN (MICROBIAL INFECTION). RX PubMed=20844026; DOI=10.1128/jvi.01388-10; RA Haque A., Mir M.A.; RT "Interaction of hantavirus nucleocapsid protein with ribosomal protein RT S19."; RL J. Virol. 84:12450-12453(2010). RN [14] 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 [15] RP IDENTIFICATION BY MASS SPECTROMETRY [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 [16] 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 [17] RP INTERACTION WITH SIN NOMBRE VIRUS NUCLEOPROTEIN (MICROBIAL INFECTION). RX PubMed=25062117; DOI=10.1042/bj20140449; RA Ganaie S.S., Haque A., Cheng E., Bonny T.S., Salim N.N., Mir M.A.; RT "Ribosomal protein S19-binding domain provides insights into hantavirus RT nucleocapsid protein-mediated translation initiation mechanism."; RL Biochem. J. 464:109-121(2014). RN [18] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-67, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [19] 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 [20] 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). RN [21] {ECO:0007744|PDB:7MQA} RP STRUCTURE BY ELECTRON MICROSCOPY (2.70 ANGSTROMS), FUNCTION, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=34516797; DOI=10.1126/science.abj5338; RA Singh S., Vanden Broeck A., Miller L., Chaker-Margot M., Klinge S.; RT "Nucleolar maturation of the human small subunit processome."; RL Science 373:eabj5338-eabj5338(2021). RN [22] RP VARIANTS DBA1 PHE-15; GLN-56; GLU-61; TRP-62; HIS-101 AND ARG-120. RX PubMed=10590074; RA Willig T.-N.D., Draptchinskaia N., Dianzani I., Ball S., Niemeyer C., RA Ramenghi U., Orfali K., Gustavsson P., Garelli E., Brusco A., Tiemann C., RA Perignon J.L., Bouchier C., Cicchiello L., Dahl N., Mohandas N., RA Tchernia G.; RT "Mutations in ribosomal protein S19 gene and Diamond Blackfan anemia: wide RT variations in phenotypic expression."; RL Blood 94:4294-4306(1999). RN [23] RP VARIANTS DBA1 PRO-18; LEU-47 AND TRP-62. RX PubMed=11112378; DOI=10.1006/bcmd.2000.0324; RA Ramenghi U., Campagnoli M.F., Garelli E., Carando A., Brusco A., RA Bagnara G.P., Strippoli P., Izzi G.C., Brandalise S., Riccardi R., RA Dianzani I.; RT "Diamond-Blackfan anemia: report of seven further mutations in the RPS19 RT gene and evidence of mutation heterogeneity in the Italian population."; RL Blood Cells Mol. Dis. 26:417-422(2000). RN [24] RP VARIANTS DBA1 PHE-15 AND MET-55, AND SUBCELLULAR LOCATION. RX PubMed=12586610; DOI=10.1182/blood-2002-12-3878; RA Da Costa L., Tchernia G., Gascard P., Lo A., Meerpohl J., Niemeyer C., RA Chasis J.-A., Fixler J., Mohandas N.; RT "Nucleolar localization of RPS19 protein in normal cells and RT mislocalization due to mutations in the nucleolar localization signals in 2 RT Diamond-Blackfan anemia patients: potential insights into RT pathophysiology."; RL Blood 101:5039-5045(2003). RN [25] RP VARIANTS DBA1 GLN-62 AND PRO-131. RX PubMed=12750732; DOI=10.1038/sj.thj.6200230; RA Proust A., Da Costa L., Rince P., Landois A., Tamary H., Zaizov R., RA Tchernia G., Delaunay J.; RT "Ten novel Diamond-Blackfan anemia mutations and three polymorphisms within RT the rps19 gene."; RL Hematol. J. 4:132-136(2003). RN [26] RP VARIANTS DBA1 ARG-18; GLN-56; 58-ALA--THR-60 DEL; PHE-59; GLN-62; HIS-101 RP AND ARG-131. RX PubMed=15384984; DOI=10.1111/j.1365-2141.2004.05152.x; RA Gazda H.T., Zhong R., Long L., Niewiadomska E., Lipton J.M., Ploszynska A., RA Zaucha J.M., Vlachos A., Atsidaftos E., Viskochil D.H., Niemeyer C.M., RA Meerpohl J.J., Rokicka-Milewska R., Pospisilova D., Wiktor-Jedrzejczak W., RA Nathan D.G., Beggs A.H., Sieff C.A.; RT "RNA and protein evidence for haplo-insufficiency in Diamond-Blackfan RT anaemia patients with RPS19 mutations."; RL Br. J. Haematol. 127:105-113(2004). RN [27] RP ERRATUM OF PUBMED:15384984, AND VARIANT DBA1 PRO-17. RA Pereira J.C., Fiskerstrand T., Ribeiro M.L.; RL Hum. Genet. 115:349-349(2004). 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). Required for pre- CC rRNA processing and maturation of 40S ribosomal subunits CC (PubMed:16990592). Part of the small subunit (SSU) processome, first CC precursor of the small eukaryotic ribosomal subunit. During the CC assembly of the SSU processome in the nucleolus, many ribosome CC biogenesis factors, an RNA chaperone and ribosomal proteins associate CC with the nascent pre-rRNA and work in concert to generate RNA folding, CC modifications, rearrangements and cleavage as well as targeted CC degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). CC {ECO:0000269|PubMed:16990592, ECO:0000269|PubMed:23636399, CC ECO:0000269|PubMed:34516797}. CC -!- SUBUNIT: Component of the small ribosomal subunit (PubMed:23636399). CC Part of the small subunit (SSU) processome, composed of more than 70 CC proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3. CC Interacts with RPS19BP1; the interaction is direct and mediates the CC integration of RPS19 in state post-A1 (PubMed:34516797). Interacts with CC RPS19BP1 (By similarity). {ECO:0000250|UniProtKB:Q9CZX8, CC ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:34516797}. CC -!- SUBUNIT: (Microbial infection) Interacts with Sin nombre virus CC nucleoprotein (via N-terminus); this interaction probably mediates the CC loading of the 40S ribosomal subunit on viral capped mRNA during N- CC mediated translation initiation. {ECO:0000269|PubMed:20844026}. CC -!- INTERACTION: CC P39019; P54253: ATXN1; NbExp=3; IntAct=EBI-354451, EBI-930964; CC P39019; P42858: HTT; NbExp=3; IntAct=EBI-354451, EBI-466029; CC P39019; P11309: PIM1; NbExp=7; IntAct=EBI-354451, EBI-696621; CC P39019; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-354451, EBI-742688; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}. Nucleus, CC nucleolus {ECO:0000269|PubMed:12586610, ECO:0000269|PubMed:17517689, CC ECO:0000269|PubMed:34516797}. CC -!- TISSUE SPECIFICITY: Higher level expression is seen in the colon CC carcinoma tissue than normal colon tissue. CC {ECO:0000269|PubMed:1339304}. CC -!- DISEASE: Diamond-Blackfan anemia 1 (DBA1) [MIM:105650]: A form of CC Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic CC anemia that usually presents early in infancy. Diamond-Blackfan anemia CC is characterized by a moderate to severe macrocytic anemia, CC erythroblastopenia, and an increased risk of developing leukemia. 30 to CC 40% of Diamond-Blackfan anemia patients present with short stature and CC congenital anomalies, the most frequent being craniofacial (Pierre- CC Robin syndrome and cleft palate), thumb and urogenital anomalies. CC {ECO:0000269|PubMed:10590074, ECO:0000269|PubMed:11112378, CC ECO:0000269|PubMed:12586610, ECO:0000269|PubMed:12750732, CC ECO:0000269|PubMed:15384984, ECO:0000269|PubMed:17517689, CC ECO:0000269|PubMed:18412286, ECO:0000269|PubMed:9988267, CC ECO:0000269|Ref.27}. Note=The disease is caused by variants affecting CC the gene represented in this entry. CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS19 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; M81757; AAA89070.1; -; mRNA. DR EMBL; AF092907; AAD13668.1; -; Genomic_DNA. DR EMBL; AF092906; AAD13668.1; JOINED; Genomic_DNA. DR EMBL; BC000023; AAH00023.1; -; mRNA. DR EMBL; BC007615; AAH07615.1; -; mRNA. DR EMBL; BC018616; AAH18616.1; -; mRNA. DR EMBL; AB007155; BAA28593.1; -; Genomic_DNA. DR CCDS; CCDS12588.1; -. DR PIR; I52692; I52692. DR RefSeq; NP_001013.1; NM_001022.3. DR RefSeq; NP_001308412.1; NM_001321483.1. DR RefSeq; NP_001308413.1; NM_001321484.1. DR PDB; 4UG0; EM; -; ST=1-145. DR PDB; 4V6X; EM; 5.00 A; AT=1-145. DR PDB; 5A2Q; EM; 3.90 A; T=1-145. DR PDB; 5AJ0; EM; 3.50 A; BT=1-145. DR PDB; 5FLX; EM; 3.90 A; T=1-145. DR PDB; 5LKS; EM; 3.60 A; ST=1-145. DR PDB; 5OA3; EM; 4.30 A; T=1-145. DR PDB; 5T2C; EM; 3.60 A; AU=1-145. DR PDB; 5VYC; X-ray; 6.00 A; T1/T2/T3/T4/T5/T6=1-145. DR PDB; 6G18; EM; 3.60 A; T=1-145. DR PDB; 6G4S; EM; 4.00 A; T=1-145. DR PDB; 6G4W; EM; 4.50 A; T=1-145. DR PDB; 6G51; EM; 4.10 A; T=1-145. DR PDB; 6G53; EM; 4.50 A; T=1-145. DR PDB; 6G5H; EM; 3.60 A; T=1-145. DR PDB; 6G5I; EM; 3.50 A; T=1-145. DR PDB; 6IP5; EM; 3.90 A; 20=1-145. DR PDB; 6IP6; EM; 4.50 A; 20=1-145. DR PDB; 6IP8; EM; 3.90 A; 20=1-145. DR PDB; 6OLE; EM; 3.10 A; ST=2-144. DR PDB; 6OLF; EM; 3.90 A; ST=2-144. DR PDB; 6OLG; EM; 3.40 A; BT=2-144. DR PDB; 6OLI; EM; 3.50 A; ST=2-144. DR PDB; 6OLZ; EM; 3.90 A; BT=2-144. DR PDB; 6OM0; EM; 3.10 A; ST=2-144. DR PDB; 6OM7; EM; 3.70 A; ST=2-144. DR PDB; 6QZP; EM; 2.90 A; ST=2-144. DR PDB; 6XA1; EM; 2.80 A; ST=2-142. DR PDB; 6Y0G; EM; 3.20 A; ST=1-145. DR PDB; 6Y2L; EM; 3.00 A; ST=1-145. DR PDB; 6Y57; EM; 3.50 A; ST=1-145. DR PDB; 6YBS; EM; 3.10 A; d=1-145. DR PDB; 6Z6L; EM; 3.00 A; ST=1-145. DR PDB; 6Z6M; EM; 3.10 A; ST=1-145. DR PDB; 6Z6N; EM; 2.90 A; ST=1-145. DR PDB; 6ZLW; EM; 2.60 A; U=1-145. DR PDB; 6ZM7; EM; 2.70 A; ST=1-145. DR PDB; 6ZME; EM; 3.00 A; ST=1-145. DR PDB; 6ZMI; EM; 2.60 A; ST=1-145. DR PDB; 6ZMO; EM; 3.10 A; ST=1-145. DR PDB; 6ZMT; EM; 3.00 A; U=1-145. DR PDB; 6ZMW; EM; 3.70 A; d=1-145. DR PDB; 6ZN5; EM; 3.20 A; U=2-145. DR PDB; 6ZOJ; EM; 2.80 A; T=1-145. DR PDB; 6ZOL; EM; 2.80 A; T=1-145. DR PDB; 6ZON; EM; 3.00 A; x=1-145. DR PDB; 6ZP4; EM; 2.90 A; x=1-145. DR PDB; 6ZUO; EM; 3.10 A; T=1-145. DR PDB; 6ZV6; EM; 2.90 A; T=1-145. DR PDB; 6ZVH; EM; 2.90 A; T=2-144. DR PDB; 6ZVJ; EM; 3.80 A; x=2-142. DR PDB; 6ZXD; EM; 3.20 A; T=1-145. DR PDB; 6ZXE; EM; 3.00 A; T=1-145. DR PDB; 6ZXF; EM; 3.70 A; T=1-145. DR PDB; 6ZXG; EM; 2.60 A; T=1-145. DR PDB; 6ZXH; EM; 2.70 A; T=1-145. DR PDB; 7A09; EM; 3.50 A; x=1-145. DR PDB; 7K5I; EM; 2.90 A; T=1-145. DR PDB; 7MQA; EM; 2.70 A; NP=1-145. DR PDB; 7QP6; EM; 4.70 A; d=1-145. DR PDB; 7QP7; EM; 3.70 A; d=1-145. DR PDB; 7R4X; EM; 2.15 A; T=1-145. DR PDB; 7TQL; EM; 3.40 A; U=4-142. DR PDB; 7WTT; EM; 3.10 A; T=1-145. DR PDB; 7WTU; EM; 3.00 A; T=1-145. DR PDB; 7WTV; EM; 3.50 A; T=1-145. DR PDB; 7WTW; EM; 3.20 A; T=1-145. DR PDB; 7WTX; EM; 3.10 A; T=1-145. DR PDB; 7WTZ; EM; 3.00 A; T=1-145. DR PDB; 7WU0; EM; 3.30 A; T=1-145. DR PDB; 7XNX; EM; 2.70 A; ST=1-145. DR PDB; 7XNY; EM; 2.50 A; ST=1-145. DR PDB; 8G5Y; EM; 2.29 A; ST=1-145. DR PDB; 8G5Z; EM; 2.64 A; ST=2-144. DR PDB; 8G60; EM; 2.54 A; ST=1-145. DR PDB; 8G61; EM; 2.94 A; ST=1-145. DR PDB; 8G6J; EM; 2.80 A; ST=1-145. DR PDB; 8GLP; EM; 1.67 A; ST=1-145. DR PDB; 8JDJ; EM; 2.50 A; AF=1-145. DR PDB; 8JDK; EM; 2.26 A; AF=1-145. DR PDB; 8JDL; EM; 2.42 A; AF=1-145. DR PDB; 8JDM; EM; 2.67 A; AF=1-145. DR PDB; 8PPK; EM; 2.98 A; T=1-145. DR PDB; 8PPL; EM; 2.65 A; AT=1-145. DR PDB; 8T4S; EM; 2.60 A; T=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; 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; 7MQA; -. 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; 8G5Z; -. 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; P39019; -. 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-23938; -. 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-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; P39019; -. DR BioGRID; 112137; 614. DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit. DR CORUM; P39019; -. DR IntAct; P39019; 80. DR MINT; P39019; -. DR STRING; 9606.ENSP00000470972; -. DR DrugBank; DB11638; Artenimol. DR GlyGen; P39019; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P39019; -. DR MetOSite; P39019; -. DR PhosphoSitePlus; P39019; -. DR SwissPalm; P39019; -. DR BioMuta; RPS19; -. DR DMDM; 730640; -. DR CPTAC; CPTAC-436; -. DR CPTAC; CPTAC-437; -. DR EPD; P39019; -. DR jPOST; P39019; -. DR MassIVE; P39019; -. DR MaxQB; P39019; -. DR PaxDb; 9606-ENSP00000470972; -. DR PeptideAtlas; P39019; -. DR ProteomicsDB; 55308; -. DR Pumba; P39019; -. DR TopDownProteomics; P39019; -. DR Antibodypedia; 30832; 371 antibodies from 35 providers. DR DNASU; 6223; -. DR Ensembl; ENST00000593863.5; ENSP00000470004.1; ENSG00000105372.8. DR Ensembl; ENST00000598742.6; ENSP00000470972.1; ENSG00000105372.8. DR Ensembl; ENST00000600467.6; ENSP00000469228.2; ENSG00000105372.8. DR GeneID; 6223; -. DR KEGG; hsa:6223; -. DR MANE-Select; ENST00000598742.6; ENSP00000470972.1; NM_001022.4; NP_001013.1. DR UCSC; uc002ort.4; human. DR AGR; HGNC:10402; -. DR CTD; 6223; -. DR DisGeNET; 6223; -. DR GeneCards; RPS19; -. DR GeneReviews; RPS19; -. DR HGNC; HGNC:10402; RPS19. DR HPA; ENSG00000105372; Low tissue specificity. DR MalaCards; RPS19; -. DR MIM; 105650; phenotype. DR MIM; 603474; gene. DR neXtProt; NX_P39019; -. DR OpenTargets; ENSG00000105372; -. DR Orphanet; 124; Diamond-Blackfan anemia. DR PharmGKB; PA34803; -. DR VEuPathDB; HostDB:ENSG00000105372; -. DR eggNOG; KOG3411; Eukaryota. DR GeneTree; ENSGT00390000013102; -. DR HOGENOM; CLU_108559_0_1_1; -. DR InParanoid; P39019; -. DR OMA; MTAPRNK; -. DR OrthoDB; 168043at2759; -. DR PhylomeDB; P39019; -. DR TreeFam; TF315008; -. DR PathwayCommons; P39019; -. 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; P39019; -. DR SIGNOR; P39019; -. DR BioGRID-ORCS; 6223; 850 hits in 1131 CRISPR screens. DR ChiTaRS; RPS19; human. DR GeneWiki; Ribosomal_protein_S19; -. DR GenomeRNAi; 6223; -. DR Pharos; P39019; Tbio. DR PRO; PR:P39019; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P39019; Protein. DR Bgee; ENSG00000105372; Expressed in upper leg skin and 211 other cell types or tissues. DR ExpressionAtlas; P39019; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO. DR GO; GO:0005840; C:ribosome; IDA:UniProtKB. DR GO; GO:0032040; C:small-subunit processome; IDA:UniProtKB. DR GO; GO:0017134; F:fibroblast growth factor binding; IPI:BHF-UCL. DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB. DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase. DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB. DR GO; GO:0002181; P:cytoplasmic translation; NAS:ComplexPortal. DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB. DR GO; GO:0030218; P:erythrocyte differentiation; IMP:HGNC-UCL. DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB. DR GO; GO:0030490; P:maturation of SSU-rRNA; IMP:UniProtKB. DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:UniProtKB. DR GO; GO:0002548; P:monocyte chemotaxis; IDA:UniProtKB. DR GO; GO:0060266; P:negative regulation of respiratory burst involved in inflammatory response; IDA:UniProtKB. DR GO; GO:0007000; P:nucleolus organization; IMP:UniProtKB. DR GO; GO:0060265; P:positive regulation of respiratory burst involved in inflammatory response; IDA:UniProtKB. DR GO; GO:0009991; P:response to extracellular stimulus; TAS:HGNC-UCL. DR GO; GO:0000028; P:ribosomal small subunit assembly; IMP:UniProtKB. DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IDA:UniProtKB. DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB. DR GO; GO:0006412; P:translation; IC:UniProtKB. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR001266; Ribosomal_eS19. DR InterPro; IPR018277; Ribosomal_eS19_CS. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR11710; 40S RIBOSOMAL PROTEIN S19; 1. DR PANTHER; PTHR11710:SF0; 40S RIBOSOMAL PROTEIN S19; 1. DR Pfam; PF01090; Ribosomal_S19e; 1. DR SMART; SM01413; Ribosomal_S19e; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS00628; RIBOSOMAL_S19E; 1. DR Genevisible; P39019; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Diamond-Blackfan anemia; KW Direct protein sequencing; Disease variant; Host-virus interaction; KW Methylation; Nucleus; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:8706699, ECO:0000269|Ref.5" FT CHAIN 2..145 FT /note="Small ribosomal subunit protein eS19" FT /id="PRO_0000153810" FT MOD_RES 23 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 67 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 111 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 115 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9CZX8" FT MOD_RES 143 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9CZX8" FT VARIANT 9..14 FT /note="Missing (in DBA1)" FT /id="VAR_055436" FT VARIANT 15 FT /note="V -> F (in DBA1; affects protein stability; does not FT localize to the nucleolus; dbSNP:rs104894717)" FT /evidence="ECO:0000269|PubMed:10590074, FT ECO:0000269|PubMed:12586610, ECO:0000269|PubMed:17517689" FT /id="VAR_018438" FT VARIANT 17 FT /note="A -> P (in DBA1; dbSNP:rs782329429)" FT /evidence="ECO:0000269|Ref.27" FT /id="VAR_046145" FT VARIANT 18..19 FT /note="LA -> E (in DBA1)" FT /id="VAR_055437" FT VARIANT 18 FT /note="L -> P (in DBA1; affects protein stability; does not FT localize to the nucleolus; affects assembly into a FT functional ribosomal subunit)" FT /evidence="ECO:0000269|PubMed:11112378, FT ECO:0000269|PubMed:17517689" FT /id="VAR_018439" FT VARIANT 18 FT /note="L -> R (in DBA1)" FT /evidence="ECO:0000269|PubMed:15384984" FT /id="VAR_046146" FT VARIANT 21 FT /note="F -> S (in DBA1)" FT /id="VAR_055438" FT VARIANT 47 FT /note="P -> L (in DBA1; affects assembly into a functional FT ribosomal subunit)" FT /evidence="ECO:0000269|PubMed:11112378, FT ECO:0000269|PubMed:17517689" FT /id="VAR_018440" FT VARIANT 52 FT /note="W -> C (in DBA1)" FT /id="VAR_055439" FT VARIANT 52 FT /note="W -> R (in DBA1; affects assembly into a functional FT ribosomal subunit)" FT /evidence="ECO:0000269|PubMed:17517689, FT ECO:0000269|PubMed:9988267" FT /id="VAR_018441" FT VARIANT 55 FT /note="T -> M (in DBA1; dbSNP:rs147508369)" FT /evidence="ECO:0000269|PubMed:12586610" FT /id="VAR_018442" FT VARIANT 56 FT /note="R -> Q (in DBA1; affects assembly into a functional FT ribosomal subunit)" FT /evidence="ECO:0000269|PubMed:10590074, FT ECO:0000269|PubMed:15384984, ECO:0000269|PubMed:17517689" FT /id="VAR_018437" FT VARIANT 57 FT /note="A -> P (in DBA1; affects protein stability; does not FT localize to the nucleolus; affects assembly into a FT functional ribosomal subunit)" FT /evidence="ECO:0000269|PubMed:17517689" FT /id="VAR_055440" FT VARIANT 58..60 FT /note="Missing (in DBA1)" FT /evidence="ECO:0000269|PubMed:15384984" FT /id="VAR_046147" FT VARIANT 59 FT /note="S -> F (in DBA1)" FT /evidence="ECO:0000269|PubMed:15384984" FT /id="VAR_046148" FT VARIANT 61 FT /note="A -> E (in DBA1; does not localize to the nucleolus; FT affects assembly into a functional ribosomal subunit)" FT /evidence="ECO:0000269|PubMed:10590074, FT ECO:0000269|PubMed:17517689" FT /id="VAR_018443" FT VARIANT 62 FT /note="R -> Q (in DBA1; affects assembly into a functional FT ribosomal subunit; dbSNP:rs1555841301)" FT /evidence="ECO:0000269|PubMed:12750732, FT ECO:0000269|PubMed:15384984, ECO:0000269|PubMed:17517689" FT /id="VAR_018444" FT VARIANT 62 FT /note="R -> W (in DBA1; increased protein degradation; FT affects assembly into a functional ribosomal subunit; FT dbSNP:rs104894711)" FT /evidence="ECO:0000269|PubMed:10590074, FT ECO:0000269|PubMed:11112378, ECO:0000269|PubMed:17517689, FT ECO:0000269|PubMed:9988267" FT /id="VAR_006924" FT VARIANT 64 FT /note="L -> P (in DBA1)" FT /id="VAR_055441" FT VARIANT 76 FT /note="T -> P (in DBA1)" FT /id="VAR_055442" FT VARIANT 78..83 FT /note="IYGGRQ -> R (in DBA1)" FT /id="VAR_055443" FT VARIANT 101 FT /note="R -> H (in DBA1; increased protein degradation; FT affects assembly into a functional ribosomal subunit)" FT /evidence="ECO:0000269|PubMed:10590074, FT ECO:0000269|PubMed:15384984, ECO:0000269|PubMed:17517689" FT /id="VAR_018445" FT VARIANT 120 FT /note="G -> R (in DBA1)" FT /evidence="ECO:0000269|PubMed:10590074, FT ECO:0000269|PubMed:17517689" FT /id="VAR_018446" FT VARIANT 127 FT /note="G -> E (in DBA1; affects protein stability; does not FT localize to the nucleolus; affects assembly into a FT functional ribosomal subunit; dbSNP:rs786200936)" FT /id="VAR_055444" FT VARIANT 131 FT /note="L -> P (in DBA1)" FT /evidence="ECO:0000269|PubMed:12750732" FT /id="VAR_018447" FT VARIANT 131 FT /note="L -> R (in DBA1)" FT /evidence="ECO:0000269|PubMed:15384984" FT /id="VAR_046149" FT VARIANT 135 FT /note="A -> T (in DBA1)" FT /id="VAR_055445" FT HELIX 6..8 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 11..25 FT /evidence="ECO:0007829|PDB:7R4X" FT TURN 32..36 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 39..42 FT /evidence="ECO:0007829|PDB:6ZOJ" FT STRAND 43..45 FT /evidence="ECO:0007829|PDB:6ZV6" FT STRAND 48..50 FT /evidence="ECO:0007829|PDB:8T4S" FT HELIX 52..66 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 72..78 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 81..85 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 88..93 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 97..109 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 112..115 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 119..123 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 125..142 FT /evidence="ECO:0007829|PDB:7R4X" SQ SEQUENCE 145 AA; 16060 MW; 181F2DB898E56E41 CRC64; MPGVTVKDVN QQEFVRALAA FLKKSGKLKV PEWVDTVKLA KHKELAPYDE NWFYTRAAST ARHLYLRGGA GVGSMTKIYG GRQRNGVMPS HFSRGSKSVA RRVLQALEGL KMVEKDQDGG RKLTPQGQRD LDRIAGQVAA ANKKH //