RS19_HUMAN
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 03-AUG-2022, entry version 211.
DE RecName: Full=40S ribosomal protein S19;
DE AltName: Full=Small ribosomal subunit protein eS19 {ECO:0000303|PubMed:24524803};
GN Name=RPS19;
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=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 80S RIBOSOME.
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]
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 [22]
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 [23]
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 [24]
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 [25]
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 [26]
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: Required for pre-rRNA processing and maturation of 40S
CC ribosomal subunits. {ECO:0000269|PubMed:16990592}.
CC -!- SUBUNIT: Interacts with RPS19BP1. {ECO:0000250}.
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: Nucleus {ECO:0000269|PubMed:12586610,
CC ECO:0000269|PubMed:17517689}. Note=Located more specifically in the
CC nucleoli.
CC -!- TISSUE SPECIFICITY: Higher level expression is seen in the colon
CC carcinoma tissue than normal colon tissue.
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.26}. 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}.
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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 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 AlphaFoldDB; P39019; -.
DR SMR; P39019; -.
DR BioGRID; 112137; 515.
DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR CORUM; P39019; -.
DR IntAct; P39019; 75.
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; P39019; -.
DR PeptideAtlas; P39019; -.
DR PRIDE; P39019; -.
DR ProteomicsDB; 55308; -.
DR TopDownProteomics; P39019; -.
DR Antibodypedia; 30832; 339 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 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; Blackfan-Diamond 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; 1434984at2759; -.
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-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; 812 hits in 1053 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 209 other tissues.
DR ExpressionAtlas; P39019; baseline and differential.
DR Genevisible; P39019; HS.
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: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; IC:FlyBase.
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; IMP:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
DR GO; GO:0006412; P:translation; IC:UniProtKB.
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; 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="40S ribosomal protein S19"
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.26"
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:6ZLW"
FT HELIX 11..24
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:6YBS"
FT TURN 32..36
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:6ZOJ"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:6ZV6"
FT HELIX 52..66
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 72..78
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 97..106
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 107..111
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 125..139
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:6ZXE"
SQ SEQUENCE 145 AA; 16060 MW; 181F2DB898E56E41 CRC64;
MPGVTVKDVN QQEFVRALAA FLKKSGKLKV PEWVDTVKLA KHKELAPYDE NWFYTRAAST
ARHLYLRGGA GVGSMTKIYG GRQRNGVMPS HFSRGSKSVA RRVLQALEGL KMVEKDQDGG
RKLTPQGQRD LDRIAGQVAA ANKKH
