RS19A_YEAST
ID RS19A_YEAST Reviewed; 144 AA.
AC P07280; D6W1U7;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=40S ribosomal protein S19-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=RP55A;
DE AltName: Full=S16a;
DE AltName: Full=Small ribosomal subunit protein eS19-A {ECO:0000303|PubMed:24524803};
DE AltName: Full=YP45;
DE AltName: Full=YS16A;
GN Name=RPS19A {ECO:0000303|PubMed:9559554}; Synonyms=RP55A, RPS16AA;
GN OrderedLocusNames=YOL121C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6387623; DOI=10.1093/nar/12.19.7345;
RA Molenaar C.M.T., Woudt L.P., Jansen A.E.M., Mager W.H., Planta R.J.,
RA Donovan D.M., Pearson N.J.;
RT "Structure and organization of two linked ribosomal protein genes in
RT yeast.";
RL Nucleic Acids Res. 12:7345-7358(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8896268;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1041::aid-yea989>3.0.co;2-i;
RA Lafuente M.J., Gamo F.-J., Gancedo C.;
RT "DNA sequence analysis of a 10 624 bp fragment of the left arm of
RT chromosome XV from Saccharomyces cerevisiae reveals a RNA binding protein,
RT a mitochondrial protein, two ribosomal proteins and two new open reading
RT frames.";
RL Yeast 12:1041-1045(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP PROTEIN SEQUENCE OF 2-50.
RX PubMed=6814480; DOI=10.1021/bi00262a005;
RA Otaka E., Higo K., Osawa S.;
RT "Isolation of seventeen proteins and amino-terminal amino acid sequences of
RT eight proteins from cytoplasmic ribosomes of yeast.";
RL Biochemistry 21:4545-4550(1982).
RN [6]
RP NOMENCLATURE, AND SUBUNIT.
RX PubMed=9559554;
RX DOI=10.1002/(sici)1097-0061(19980330)14:5<471::aid-yea241>3.0.co;2-u;
RA Planta R.J., Mager W.H.;
RT "The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae.";
RL Yeast 14:471-477(1998).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP FUNCTION IN RIBOSOME SYNTHESIS, MUTAGENESIS OF ILE-65, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16159874; DOI=10.1074/jbc.m506916200;
RA Leger-Silvestre I., Caffrey J.M., Dawaliby R., Alvarez-Arias D.A., Gas N.,
RA Bertolone S.J., Gleizes P.E., Ellis S.R.;
RT "Specific role for yeast homologs of the Diamond Blackfan anemia-associated
RT Rps19 protein in ribosome synthesis.";
RL J. Biol. Chem. 280:38177-38185(2005).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ILE-15; ARG-57; ARG-63;
RP ILE-65; ARG-102 AND ARG-122.
RX PubMed=17726054; DOI=10.1093/nar/gkm626;
RA Gregory L.A., Aguissa-Toure A.H., Pinaud N., Legrand P., Gleizes P.E.,
RA Fribourg S.;
RT "Molecular basis of Diamond-Blackfan anemia: structure and function
RT analysis of RPS19.";
RL Nucleic Acids Res. 35:5913-5921(2007).
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 X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS) OF 80S RIBOSOME.
RX PubMed=21109664; DOI=10.1126/science.1194294;
RA Ben-Shem A., Jenner L., Yusupova G., Yusupov M.;
RT "Crystal structure of the eukaryotic ribosome.";
RL Science 330:1203-1209(2010).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 80S RIBOSOME, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=22096102; DOI=10.1126/science.1212642;
RA Ben-Shem A., Garreau de Loubresse N., Melnikov S., Jenner L., Yusupova G.,
RA Yusupov M.;
RT "The structure of the eukaryotic ribosome at 3.0 A resolution.";
RL Science 334:1524-1529(2011).
CC -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell. The small
CC ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC molecules. The large subunit (LSU) contains the ribosomal catalytic
CC site termed the peptidyl transferase center (PTC), which catalyzes the
CC formation of peptide bonds, thereby polymerizing the amino acids
CC delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC leave the ribosome through a tunnel in the LSU and interact with
CC protein factors that function in enzymatic processing, targeting, and
CC the membrane insertion of nascent chains at the exit of the ribosomal
CC tunnel (PubMed:22096102). eS19 is required for proper maturation of the
CC small (40S) ribosomal subunit. Binds to 40S pre-ribosomal particles,
CC probably required after association of NOC4 but before association of
CC ENP1, TSR1 and RIO2 with 20/21S pre-rRNA (PubMed:16159874,
CC PubMed:17726054). {ECO:0000269|PubMed:16159874,
CC ECO:0000269|PubMed:17726054, ECO:0000305|PubMed:22096102}.
CC -!- SUBUNIT: Component of the small ribosomal subunit (SSU). Mature yeast
CC ribosomes consist of a small (40S) and a large (60S) subunit. The 40S
CC small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33
CC different proteins (encoded by 57 genes). The large 60S subunit
CC contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different
CC proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).
CC {ECO:0000269|PubMed:22096102, ECO:0000305|PubMed:9559554}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:22096102}.
CC -!- DISRUPTION PHENOTYPE: Disruption of a single RPS19 gene reduces cell
CC growth; a double disruption is lethal. Depletion experiments show the
CC proteins are required for correct maturation of precursor rRNA to
CC generate the 18S small rRNA. A specific site between the 18S and 5.8S
CC precursors (site A2 in ETS1) is not cleaved in disruption mutants.
CC Partially assembled ribosomes are retained in the nucleolus rather than
CC being exported to the cytoplasm. All effects are exacerbated in the
CC double disruption. Increases association of NOC4 with 20S/21S pre-rRNA,
CC decreases association of ENP1, TSR1 and RIO2 with 20S/21S pre-rRNA.
CC {ECO:0000269|PubMed:16159874, ECO:0000269|PubMed:17726054}.
CC -!- MISCELLANEOUS: Present with 29000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for eS19 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS19 family.
CC {ECO:0000305}.
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DR EMBL; X02635; CAA26482.1; -; Genomic_DNA.
DR EMBL; X95258; CAA64549.1; -; Genomic_DNA.
DR EMBL; Z74863; CAA99140.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10663.1; -; Genomic_DNA.
DR PIR; S05868; R3BY9E.
DR RefSeq; NP_014520.1; NM_001183375.1.
DR PDB; 3J6X; EM; 6.10 A; 19=1-144.
DR PDB; 3J6Y; EM; 6.10 A; 19=1-144.
DR PDB; 3J77; EM; 6.20 A; 19=1-144.
DR PDB; 3J78; EM; 6.30 A; 19=1-144.
DR PDB; 4U3M; X-ray; 3.00 A; C9/c9=2-144.
DR PDB; 4U3N; X-ray; 3.20 A; C9/c9=2-144.
DR PDB; 4U3U; X-ray; 2.90 A; C9/c9=2-144.
DR PDB; 4U4N; X-ray; 3.10 A; C9/c9=2-144.
DR PDB; 4U4O; X-ray; 3.60 A; C9/c9=2-144.
DR PDB; 4U4Q; X-ray; 3.00 A; C9/c9=2-144.
DR PDB; 4U4R; X-ray; 2.80 A; C9/c9=2-144.
DR PDB; 4U4U; X-ray; 3.00 A; C9/c9=2-144.
DR PDB; 4U4Y; X-ray; 3.20 A; C9/c9=2-144.
DR PDB; 4U4Z; X-ray; 3.10 A; C9/c9=2-144.
DR PDB; 4U50; X-ray; 3.20 A; C9/c9=2-144.
DR PDB; 4U51; X-ray; 3.20 A; C9/c9=2-144.
DR PDB; 4U52; X-ray; 3.00 A; C9/c9=2-144.
DR PDB; 4U53; X-ray; 3.30 A; C9/c9=2-144.
DR PDB; 4U55; X-ray; 3.20 A; C9/c9=2-144.
DR PDB; 4U56; X-ray; 3.45 A; C9/c9=2-144.
DR PDB; 4U6F; X-ray; 3.10 A; C9/c9=2-144.
DR PDB; 4V6I; EM; 8.80 A; AS=1-144.
DR PDB; 4V7R; X-ray; 4.00 A; AM/CM=1-144.
DR PDB; 4V88; X-ray; 3.00 A; AT/CT=1-144.
DR PDB; 4V8Y; EM; 4.30 A; AT=1-144.
DR PDB; 4V8Z; EM; 6.60 A; AT=1-144.
DR PDB; 4V92; EM; 3.70 A; T=3-144.
DR PDB; 5DAT; X-ray; 3.15 A; C9/c9=2-144.
DR PDB; 5DC3; X-ray; 3.25 A; C9/c9=2-144.
DR PDB; 5DGE; X-ray; 3.45 A; C9/c9=2-144.
DR PDB; 5DGF; X-ray; 3.30 A; C9/c9=2-144.
DR PDB; 5DGV; X-ray; 3.10 A; C9/c9=2-144.
DR PDB; 5FCI; X-ray; 3.40 A; C9/c9=2-144.
DR PDB; 5FCJ; X-ray; 3.10 A; C9/c9=2-144.
DR PDB; 5I4L; X-ray; 3.10 A; C9/c9=2-144.
DR PDB; 5JUO; EM; 4.00 A; QB=1-144.
DR PDB; 5JUP; EM; 3.50 A; QB=1-144.
DR PDB; 5JUS; EM; 4.20 A; QB=1-144.
DR PDB; 5JUT; EM; 4.00 A; QB=1-144.
DR PDB; 5JUU; EM; 4.00 A; QB=1-144.
DR PDB; 5LYB; X-ray; 3.25 A; C9/c9=2-144.
DR PDB; 5M1J; EM; 3.30 A; T2=2-144.
DR PDB; 5MC6; EM; 3.80 A; I=1-144.
DR PDB; 5MEI; X-ray; 3.50 A; U/c9=2-144.
DR PDB; 5NDG; X-ray; 3.70 A; C9/c9=2-144.
DR PDB; 5NDV; X-ray; 3.30 A; C9/c9=2-144.
DR PDB; 5NDW; X-ray; 3.70 A; C9/c9=2-144.
DR PDB; 5OBM; X-ray; 3.40 A; C9/c9=2-144.
DR PDB; 5ON6; X-ray; 3.10 A; U/c9=2-144.
DR PDB; 5TBW; X-ray; 3.00 A; U/c9=2-144.
DR PDB; 5TGA; X-ray; 3.30 A; C9/c9=2-144.
DR PDB; 5TGM; X-ray; 3.50 A; C9/c9=2-144.
DR PDB; 6EML; EM; 3.60 A; I=1-144.
DR PDB; 6FAI; EM; 3.40 A; T=1-144.
DR PDB; 6GQ1; EM; 4.40 A; AJ=2-144.
DR PDB; 6GQB; EM; 3.90 A; AJ=2-144.
DR PDB; 6GQV; EM; 4.00 A; AJ=2-144.
DR PDB; 6HHQ; X-ray; 3.10 A; U/c9=1-144.
DR PDB; 6I7O; EM; 5.30 A; I/Ib=2-144.
DR PDB; 6Q8Y; EM; 3.10 A; I=2-144.
DR PDB; 6RBD; EM; 3.47 A; T=1-144.
DR PDB; 6RBE; EM; 3.80 A; T=1-144.
DR PDB; 6S47; EM; 3.28 A; BU=2-144.
DR PDB; 6SNT; EM; 2.80 A; T=1-144.
DR PDB; 6SV4; EM; 3.30 A; I/Ib/Ic=1-144.
DR PDB; 6T4Q; EM; 2.60 A; ST=2-144.
DR PDB; 6T7I; EM; 3.20 A; ST=1-144.
DR PDB; 6T7T; EM; 3.10 A; ST=1-144.
DR PDB; 6T83; EM; 4.00 A; Tb/u=1-144.
DR PDB; 6TB3; EM; 2.80 A; I=2-144.
DR PDB; 6TNU; EM; 3.10 A; I=2-144.
DR PDB; 6WDR; EM; 3.70 A; T=2-144.
DR PDB; 6WOO; EM; 2.90 A; TT=2-144.
DR PDB; 6XIQ; EM; 4.20 A; AJ=1-144.
DR PDB; 6XIR; EM; 3.20 A; AJ=1-144.
DR PDB; 6Y7C; EM; 3.80 A; T=1-144.
DR PDB; 6Z6J; EM; 3.40 A; ST=1-144.
DR PDB; 6Z6K; EM; 3.40 A; ST=1-144.
DR PDB; 6ZCE; EM; 5.30 A; U=1-144.
DR PDB; 6ZQD; EM; 3.80 A; DT=1-144.
DR PDB; 6ZQE; EM; 7.10 A; DT=1-144.
DR PDB; 6ZQF; EM; 4.90 A; DT=1-144.
DR PDB; 6ZQG; EM; 3.50 A; DT=1-144.
DR PDB; 6ZU9; EM; 6.20 A; K=1-144.
DR PDB; 6ZVI; EM; 3.00 A; B=2-144.
DR PDB; 7A1G; EM; 3.00 A; J=2-144.
DR PDB; 7AJU; EM; 3.80 A; DT=1-144.
DR PDB; 7B7D; EM; 3.30 A; I=2-144.
DR PDB; 7D4I; EM; 4.00 A; SU=1-144.
DR PDB; 7D63; EM; 12.30 A; SU=1-144.
DR PDB; 7NRC; EM; 3.90 A; SI=2-144.
DR PDB; 7NRD; EM; 4.36 A; SI=2-144.
DR PDBsum; 3J6X; -.
DR PDBsum; 3J6Y; -.
DR PDBsum; 3J77; -.
DR PDBsum; 3J78; -.
DR PDBsum; 4U3M; -.
DR PDBsum; 4U3N; -.
DR PDBsum; 4U3U; -.
DR PDBsum; 4U4N; -.
DR PDBsum; 4U4O; -.
DR PDBsum; 4U4Q; -.
DR PDBsum; 4U4R; -.
DR PDBsum; 4U4U; -.
DR PDBsum; 4U4Y; -.
DR PDBsum; 4U4Z; -.
DR PDBsum; 4U50; -.
DR PDBsum; 4U51; -.
DR PDBsum; 4U52; -.
DR PDBsum; 4U53; -.
DR PDBsum; 4U55; -.
DR PDBsum; 4U56; -.
DR PDBsum; 4U6F; -.
DR PDBsum; 4V6I; -.
DR PDBsum; 4V7R; -.
DR PDBsum; 4V88; -.
DR PDBsum; 4V8Y; -.
DR PDBsum; 4V8Z; -.
DR PDBsum; 4V92; -.
DR PDBsum; 5DAT; -.
DR PDBsum; 5DC3; -.
DR PDBsum; 5DGE; -.
DR PDBsum; 5DGF; -.
DR PDBsum; 5DGV; -.
DR PDBsum; 5FCI; -.
DR PDBsum; 5FCJ; -.
DR PDBsum; 5I4L; -.
DR PDBsum; 5JUO; -.
DR PDBsum; 5JUP; -.
DR PDBsum; 5JUS; -.
DR PDBsum; 5JUT; -.
DR PDBsum; 5JUU; -.
DR PDBsum; 5LYB; -.
DR PDBsum; 5M1J; -.
DR PDBsum; 5MC6; -.
DR PDBsum; 5MEI; -.
DR PDBsum; 5NDG; -.
DR PDBsum; 5NDV; -.
DR PDBsum; 5NDW; -.
DR PDBsum; 5OBM; -.
DR PDBsum; 5ON6; -.
DR PDBsum; 5TBW; -.
DR PDBsum; 5TGA; -.
DR PDBsum; 5TGM; -.
DR PDBsum; 6EML; -.
DR PDBsum; 6FAI; -.
DR PDBsum; 6GQ1; -.
DR PDBsum; 6GQB; -.
DR PDBsum; 6GQV; -.
DR PDBsum; 6HHQ; -.
DR PDBsum; 6I7O; -.
DR PDBsum; 6Q8Y; -.
DR PDBsum; 6RBD; -.
DR PDBsum; 6RBE; -.
DR PDBsum; 6S47; -.
DR PDBsum; 6SNT; -.
DR PDBsum; 6SV4; -.
DR PDBsum; 6T4Q; -.
DR PDBsum; 6T7I; -.
DR PDBsum; 6T7T; -.
DR PDBsum; 6T83; -.
DR PDBsum; 6TB3; -.
DR PDBsum; 6TNU; -.
DR PDBsum; 6WDR; -.
DR PDBsum; 6WOO; -.
DR PDBsum; 6XIQ; -.
DR PDBsum; 6XIR; -.
DR PDBsum; 6Y7C; -.
DR PDBsum; 6Z6J; -.
DR PDBsum; 6Z6K; -.
DR PDBsum; 6ZCE; -.
DR PDBsum; 6ZQD; -.
DR PDBsum; 6ZQE; -.
DR PDBsum; 6ZQF; -.
DR PDBsum; 6ZQG; -.
DR PDBsum; 6ZU9; -.
DR PDBsum; 6ZVI; -.
DR PDBsum; 7A1G; -.
DR PDBsum; 7AJU; -.
DR PDBsum; 7B7D; -.
DR PDBsum; 7D4I; -.
DR PDBsum; 7D63; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR AlphaFoldDB; P07280; -.
DR SMR; P07280; -.
DR BioGRID; 34280; 736.
DR IntAct; P07280; 36.
DR MINT; P07280; -.
DR STRING; 4932.YOL121C; -.
DR iPTMnet; P07280; -.
DR MaxQB; P07280; -.
DR PaxDb; P07280; -.
DR PRIDE; P07280; -.
DR TopDownProteomics; P07280; -.
DR EnsemblFungi; YOL121C_mRNA; YOL121C; YOL121C.
DR GeneID; 854028; -.
DR KEGG; sce:YOL121C; -.
DR SGD; S000005481; RPS19A.
DR VEuPathDB; FungiDB:YOL121C; -.
DR eggNOG; KOG3411; Eukaryota.
DR GeneTree; ENSGT00940000176238; -.
DR HOGENOM; CLU_108559_3_0_1; -.
DR InParanoid; P07280; -.
DR OMA; YIDGPVG; -.
DR BioCyc; YEAST:G3O-33517-MON; -.
DR Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SCE-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-SCE-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-SCE-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-SCE-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-SCE-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:P07280; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P07280; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:SGD.
DR GO; GO:0006407; P:rRNA export from nucleus; IMP:SGD.
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; Cytoplasm; Direct protein sequencing; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Ribosome biogenesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6814480"
FT CHAIN 2..144
FT /note="40S ribosomal protein S19-A"
FT /id="PRO_0000153835"
FT MUTAGEN 15
FT /note="I->F: Partial loss of function; decreased 18S rRNA,
FT decreases binding to 20S pre-rRNA complex, slow growth in
FT double RPS19A/RPS19B mutant."
FT /evidence="ECO:0000269|PubMed:17726054"
FT MUTAGEN 57
FT /note="R->E,Q: Loss of mature 18S rRNA, protein doesn't
FT bind 20S pre-RNA complex. Lethal in double RPS19A/RPS19B
FT mutant."
FT /evidence="ECO:0000269|PubMed:17726054"
FT MUTAGEN 63
FT /note="R->E: Loss of mature 18S rRNA, protein binds 20S
FT pre-RNA complex poorly. Lethal in double RPS19A/RPS19B
FT mutant."
FT /evidence="ECO:0000269|PubMed:17726054"
FT MUTAGEN 65
FT /note="I->P: Lethal in double RPS19A/RPS19B mutant,
FT considerable decrease in 18S rRNA production."
FT /evidence="ECO:0000269|PubMed:16159874,
FT ECO:0000269|PubMed:17726054"
FT MUTAGEN 102
FT /note="R->E: Decreases mature 18S rRNA, protein binds 20S
FT pre-RNA complex poorly. Lethal in double RPS19A/RPS19B
FT mutant."
FT /evidence="ECO:0000269|PubMed:17726054"
FT MUTAGEN 122
FT /note="R->E: Decreases mature 18S rRNA, protein binds 20S
FT pre-RNA complex poorly. Lethal in double RPS19A/RPS19B
FT mutant."
FT /evidence="ECO:0000269|PubMed:17726054"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 11..25
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 32..36
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 53..67
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 98..110
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 126..140
FT /evidence="ECO:0007829|PDB:6ZVI"
SQ SEQUENCE 144 AA; 15917 MW; FE06D94B993B11B2 CRC64;
MPGVSVRDVA AQDFINAYAS FLQRQGKLEV PGYVDIVKTS SGNEMPPQDA EGWFYKRAAS
VARHIYMRKQ VGVGKLNKLY GGAKSRGVRP YKHIDASGSI NRKVLQALEK IGIVEISPKG
GRRISENGQR DLDRIAAQTL EEDE
