ID   RL19A_YEAST             Reviewed;         189 AA.
AC   P0CX82; D6VPX3; P05735;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=Large ribosomal subunit protein eL19A {ECO:0000303|PubMed:24524803};
DE   AltName: Full=60S ribosomal protein L19-A {ECO:0000303|PubMed:9559554};
DE   AltName: Full=L23;
DE   AltName: Full=RP15L;
DE   AltName: Full=RP33;
DE   AltName: Full=YL14;
GN   Name=RPL19A {ECO:0000303|PubMed:9559554}; Synonyms=RPL23A, YL14A;
GN   OrderedLocusNames=YBR084C-A; ORFNames=YBR084BC;
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].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7785339; DOI=10.1002/yea.320110411;
RA   Song J.M., Cheung E., Rabinowitz J.C.;
RT   "Nucleotide sequence and characterization of the Saccharomyces cerevisiae
RT   RPL19A gene encoding a homolog of the mammalian ribosomal protein L19.";
RL   Yeast 11:383-389(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC 204508 / S288c;
RA   Suzuki K., Tomiyoshi A., Otaka E.;
RL   Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
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 2-31.
RX   PubMed=6355773; DOI=10.1007/bf00425772;
RA   Otaka E., Higo K., Itoh T.;
RT   "Yeast ribosomal proteins: VII. Cytoplasmic ribosomal proteins from
RT   Schizosaccharomyces pombe.";
RL   Mol. Gen. Genet. 191:519-524(1983).
RN   [6]
RP   PROTEIN SEQUENCE OF 2-21.
RX   PubMed=1544921; DOI=10.1016/s0021-9258(18)42785-8;
RA   Takakura H., Tsunasawa S., Miyagi M., Warner J.R.;
RT   "NH2-terminal acetylation of ribosomal proteins of Saccharomyces
RT   cerevisiae.";
RL   J. Biol. Chem. 267:5442-5445(1992).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-189.
RX   PubMed=2836393; DOI=10.1016/s0021-9258(18)68558-8;
RA   Shannon K.W., Rabinowitz J.C.;
RT   "Isolation and characterization of the Saccharomyces cerevisiae MIS1 gene
RT   encoding mitochondrial C1-tetrahydrofolate synthase.";
RL   J. Biol. Chem. 263:7717-7725(1988).
RN   [8]
RP   IDENTIFICATION.
RX   PubMed=8485583; DOI=10.1038/ng0393-266;
RA   Gish W., States D.J.;
RT   "Identification of protein coding regions by database similarity search.";
RL   Nat. Genet. 3:266-272(1993).
RN   [9]
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   [10]
RP   MASS SPECTROMETRY.
RX   PubMed=11983894; DOI=10.1073/pnas.082119899;
RA   Lee S.-W., Berger S.J., Martinovic S., Pasa-Tolic L., Anderson G.A.,
RA   Shen Y., Zhao R., Smith R.D.;
RT   "Direct mass spectrometric analysis of intact proteins of the yeast large
RT   ribosomal subunit using capillary LC/FTICR.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:5942-5947(2002).
RN   [11]
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   [12]
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   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-37 AND SER-91, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [16]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-21; LYS-53; LYS-60; LYS-146
RP   AND LYS-186, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=22106047; DOI=10.1002/pmic.201100166;
RA   Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT   "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL   Proteomics 12:236-240(2012).
RN   [17]
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   [18]
RP   3D-STRUCTURE MODELING OF 3-143, AND ELECTRON MICROSCOPY.
RX   PubMed=11701127; DOI=10.1016/s0092-8674(01)00539-6;
RA   Spahn C.M.T., Beckmann R., Eswar N., Penczek P.A., Sali A., Blobel G.,
RA   Frank J.;
RT   "Structure of the 80S ribosome from Saccharomyces cerevisiae -- tRNA-
RT   ribosome and subunit-subunit interactions.";
RL   Cell 107:373-386(2001).
RN   [19]
RP   3D-STRUCTURE MODELING, AND ELECTRON MICROSCOPY.
RX   PubMed=14976550; DOI=10.1038/sj.emboj.7600102;
RA   Spahn C.M.T., Gomez-Lorenzo M.G., Grassucci R.A., Joergensen R.,
RA   Andersen G.R., Beckmann R., Penczek P.A., Ballesta J.P.G., Frank J.;
RT   "Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome
RT   facilitate tRNA translocation.";
RL   EMBO J. 23:1008-1019(2004).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (4.0 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   [21]
RP   X-RAY CRYSTALLOGRAPHY (3.0 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. eL19 may play a role in the last stages of translation
CC       initiation, in particular subunit joining and shedding/releasing
CC       factors. {ECO:0000305|PubMed:22096102}.
CC   -!- SUBUNIT: Component of the large ribosomal subunit (LSU). 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). eL19 lies in close proximity to the
CC       binding site for eukaryotic initiation factor eIF4G (PubMed:9559554,
CC       PubMed:22096102). {ECO:0000269|PubMed:22096102,
CC       ECO:0000305|PubMed:9559554}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:22096102}.
CC   -!- MASS SPECTROMETRY: Mass=21573.158; Method=Electrospray; Note=Average
CC       mass.; Evidence={ECO:0000269|PubMed:11983894};
CC   -!- MISCELLANEOUS: Present with 97700 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- MISCELLANEOUS: There are 2 genes for eL19 in yeast. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL19 family.
CC       {ECO:0000305}.
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DR   EMBL; Z36751; CAA85322.1; -; Genomic_DNA.
DR   EMBL; D17337; BAA04155.1; -; mRNA.
DR   EMBL; Z35953; CAA85030.1; -; Genomic_DNA.
DR   EMBL; Z35954; CAA85032.1; -; Genomic_DNA.
DR   EMBL; J03724; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BK006936; DAA07204.1; -; Genomic_DNA.
DR   PIR; S44597; S44597.
DR   RefSeq; NP_009526.1; NM_001178267.1.
DR   RefSeq; NP_009641.1; NM_001180057.1.
DR   PDB; 2WW9; EM; 8.60 A; J=1-189.
DR   PDB; 2WWA; EM; 8.90 A; J=1-189.
DR   PDB; 3J6X; EM; 6.10 A; 59=1-189.
DR   PDB; 3J6Y; EM; 6.10 A; 59=1-189.
DR   PDB; 3J77; EM; 6.20 A; 69=1-189.
DR   PDB; 3J78; EM; 6.30 A; 69=1-189.
DR   PDB; 3JCT; EM; 3.08 A; R=1-189.
DR   PDB; 4U3M; X-ray; 3.00 A; M9/m9=2-189.
DR   PDB; 4U3N; X-ray; 3.20 A; M9/m9=2-189.
DR   PDB; 4U3U; X-ray; 2.90 A; M9/m9=2-189.
DR   PDB; 4U4N; X-ray; 3.10 A; M9/m9=2-189.
DR   PDB; 4U4O; X-ray; 3.60 A; M9/m9=2-189.
DR   PDB; 4U4Q; X-ray; 3.00 A; M9/m9=2-189.
DR   PDB; 4U4R; X-ray; 2.80 A; M9/m9=2-189.
DR   PDB; 4U4U; X-ray; 3.00 A; M9/m9=2-189.
DR   PDB; 4U4Y; X-ray; 3.20 A; M9/m9=2-189.
DR   PDB; 4U4Z; X-ray; 3.10 A; M9/m9=2-189.
DR   PDB; 4U50; X-ray; 3.20 A; M9/m9=2-189.
DR   PDB; 4U51; X-ray; 3.20 A; M9/m9=2-189.
DR   PDB; 4U52; X-ray; 3.00 A; M9/m9=2-189.
DR   PDB; 4U53; X-ray; 3.30 A; M9/m9=2-189.
DR   PDB; 4U55; X-ray; 3.20 A; M9/m9=2-189.
DR   PDB; 4U56; X-ray; 3.45 A; M9/m9=2-189.
DR   PDB; 4U6F; X-ray; 3.10 A; M9/m9=2-189.
DR   PDB; 4V4B; EM; 11.70 A; BP=2-143.
DR   PDB; 4V6I; EM; 8.80 A; BT=1-189.
DR   PDB; 4V7F; EM; 8.70 A; R=1-189.
DR   PDB; 4V7R; X-ray; 4.00 A; BS/DS=1-189.
DR   PDB; 4V88; X-ray; 3.00 A; BR/DR=1-189.
DR   PDB; 4V91; EM; 3.70 A; R=1-189.
DR   PDB; 5APN; EM; 3.91 A; R=1-189.
DR   PDB; 5APO; EM; 3.41 A; R=1-189.
DR   PDB; 5DAT; X-ray; 3.15 A; M9/m9=2-189.
DR   PDB; 5DC3; X-ray; 3.25 A; M9/m9=2-189.
DR   PDB; 5DGE; X-ray; 3.45 A; M9/m9=2-189.
DR   PDB; 5DGF; X-ray; 3.30 A; M9/m9=2-189.
DR   PDB; 5DGV; X-ray; 3.10 A; M9/m9=2-189.
DR   PDB; 5FCI; X-ray; 3.40 A; M9/m9=2-189.
DR   PDB; 5FCJ; X-ray; 3.10 A; M9/m9=2-189.
DR   PDB; 5GAK; EM; 3.88 A; T=1-189.
DR   PDB; 5H4P; EM; 3.07 A; R=1-189.
DR   PDB; 5I4L; X-ray; 3.10 A; M9/m9=2-189.
DR   PDB; 5JCS; EM; 9.50 A; R=1-189.
DR   PDB; 5JUO; EM; 4.00 A; W=1-189.
DR   PDB; 5JUP; EM; 3.50 A; W=1-189.
DR   PDB; 5JUS; EM; 4.20 A; W=1-189.
DR   PDB; 5JUT; EM; 4.00 A; W=1-189.
DR   PDB; 5JUU; EM; 4.00 A; W=1-189.
DR   PDB; 5LYB; X-ray; 3.25 A; M9/m9=2-189.
DR   PDB; 5M1J; EM; 3.30 A; R5=2-189.
DR   PDB; 5MC6; EM; 3.80 A; BF=1-189.
DR   PDB; 5MEI; X-ray; 3.50 A; CT/z=2-189.
DR   PDB; 5NDG; X-ray; 3.70 A; M9/m9=2-189.
DR   PDB; 5NDV; X-ray; 3.30 A; M9/m9=2-189.
DR   PDB; 5NDW; X-ray; 3.70 A; M9/m9=2-189.
DR   PDB; 5OBM; X-ray; 3.40 A; M9/m9=2-189.
DR   PDB; 5ON6; X-ray; 3.10 A; CT/z=2-189.
DR   PDB; 5T62; EM; 3.30 A; e=1-189.
DR   PDB; 5T6R; EM; 4.50 A; e=1-189.
DR   PDB; 5TBW; X-ray; 3.00 A; CT/z=2-189.
DR   PDB; 5TGA; X-ray; 3.30 A; M9/m9=2-189.
DR   PDB; 5TGM; X-ray; 3.50 A; M9/m9=2-189.
DR   PDB; 6ELZ; EM; 3.30 A; R=1-189.
DR   PDB; 6EM5; EM; 4.30 A; R=1-189.
DR   PDB; 6FT6; EM; 3.90 A; R=1-189.
DR   PDB; 6GQ1; EM; 4.40 A; R=2-189.
DR   PDB; 6GQB; EM; 3.90 A; R=2-189.
DR   PDB; 6GQV; EM; 4.00 A; R=2-189.
DR   PDB; 6HD7; EM; 3.40 A; T=1-189.
DR   PDB; 6HHQ; X-ray; 3.10 A; CT/z=1-189.
DR   PDB; 6I7O; EM; 5.30 A; BF/YF=2-189.
DR   PDB; 6M62; EM; 3.20 A; R=1-189.
DR   PDB; 6N8J; EM; 3.50 A; R=1-189.
DR   PDB; 6N8K; EM; 3.60 A; R=1-189.
DR   PDB; 6N8L; EM; 3.60 A; R=1-189.
DR   PDB; 6N8M; EM; 3.50 A; e=1-189.
DR   PDB; 6N8N; EM; 3.80 A; e=1-189.
DR   PDB; 6N8O; EM; 3.50 A; e=1-189.
DR   PDB; 6OIG; EM; 3.80 A; R=2-189.
DR   PDB; 6Q8Y; EM; 3.10 A; BF=2-189.
DR   PDB; 6QIK; EM; 3.10 A; R=1-189.
DR   PDB; 6QT0; EM; 3.40 A; R=1-189.
DR   PDB; 6QTZ; EM; 3.50 A; R=1-189.
DR   PDB; 6R84; EM; 3.60 A; T=2-153.
DR   PDB; 6R86; EM; 3.40 A; T=2-153.
DR   PDB; 6R87; EM; 3.40 A; T=2-153.
DR   PDB; 6RI5; EM; 3.30 A; R=1-189.
DR   PDB; 6RZZ; EM; 3.20 A; R=1-189.
DR   PDB; 6S05; EM; 3.90 A; R=1-189.
DR   PDB; 6S47; EM; 3.28 A; AT=2-189.
DR   PDB; 6SNT; EM; 2.80 A; x=1-189.
DR   PDB; 6SV4; EM; 3.30 A; BF/YF/ZF=1-189.
DR   PDB; 6T4Q; EM; 2.60 A; LR=2-189.
DR   PDB; 6T7I; EM; 3.20 A; LR=1-189.
DR   PDB; 6T7T; EM; 3.10 A; LR=1-189.
DR   PDB; 6T83; EM; 4.00 A; C/Ry=1-189.
DR   PDB; 6TB3; EM; 2.80 A; BF=2-189.
DR   PDB; 6TNU; EM; 3.10 A; BF=2-189.
DR   PDB; 6WOO; EM; 2.90 A; R=2-189.
DR   PDB; 6XIQ; EM; 4.20 A; R=1-189.
DR   PDB; 6XIR; EM; 3.20 A; R=1-189.
DR   PDB; 6YLG; EM; 3.00 A; R=1-189.
DR   PDB; 6YLH; EM; 3.10 A; R=1-189.
DR   PDB; 6YLX; EM; 3.90 A; R=1-189.
DR   PDB; 6YLY; EM; 3.80 A; R=1-189.
DR   PDB; 6Z6J; EM; 3.40 A; LR=1-189.
DR   PDB; 6Z6K; EM; 3.40 A; LR=1-189.
DR   PDB; 7AZY; EM; 2.88 A; H=1-189.
DR   PDB; 7B7D; EM; 3.30 A; Ln=2-189.
DR   PDB; 7BT6; EM; 3.12 A; R=1-189.
DR   PDB; 7BTB; EM; 3.22 A; R=1-189.
DR   PDB; 7MPI; EM; 3.05 A; AR=2-189.
DR   PDB; 7MPJ; EM; 2.70 A; AR=2-189.
DR   PDB; 7N8B; EM; 3.05 A; AR=2-189.
DR   PDB; 7NAC; EM; 3.04 A; R=1-189.
DR   PDB; 7NAD; EM; 3.04 A; R=1-189.
DR   PDB; 7NAF; EM; 3.13 A; R=88-145.
DR   PDB; 7NRC; EM; 3.90 A; LT=2-189.
DR   PDB; 7NRD; EM; 4.36 A; LT=2-189.
DR   PDB; 7OF1; EM; 3.10 A; R=1-189.
DR   PDB; 7OH3; EM; 3.40 A; R=1-189.
DR   PDB; 7OHQ; EM; 3.10 A; R=1-189.
DR   PDB; 7OHR; EM; 4.72 A; R=1-189.
DR   PDB; 7OHV; EM; 3.90 A; R=1-189.
DR   PDB; 7OSA; X-ray; 3.00 A; eL19=1-189.
DR   PDB; 7OSM; X-ray; 3.00 A; eL19=1-189.
DR   PDB; 7R72; EM; 3.07 A; R=1-189.
DR   PDB; 7R7A; EM; 3.04 A; R=1-189.
DR   PDB; 7RR5; EM; 3.23 A; LR=1-189.
DR   PDB; 7TOO; EM; 2.70 A; AL19=1-189.
DR   PDB; 7TOP; EM; 2.40 A; AL19=1-189.
DR   PDB; 7U0H; EM; 2.76 A; R=1-189.
DR   PDB; 7UG6; EM; 2.90 A; R=1-189.
DR   PDB; 7UOO; EM; 2.34 A; R=1-189.
DR   PDB; 7UQB; EM; 2.43 A; R=1-189.
DR   PDB; 7UQZ; EM; 2.44 A; R=1-189.
DR   PDB; 7V08; EM; 2.36 A; R=1-189.
DR   PDB; 7Z34; EM; 3.80 A; R=1-189.
DR   PDB; 7ZPQ; EM; 3.47 A; BQ=2-189.
DR   PDB; 7ZRS; EM; 4.80 A; BQ=2-189.
DR   PDB; 7ZS5; EM; 3.20 A; BS=2-161.
DR   PDB; 7ZUW; EM; 4.30 A; BQ=2-189.
DR   PDB; 7ZUX; EM; 2.50 A; EQ=2-189.
DR   PDB; 7ZW0; EM; 2.40 A; LU=1-189.
DR   PDB; 8AAF; EM; 2.50 A; E=1-189.
DR   PDB; 8AGT; EM; 2.60 A; E=1-189.
DR   PDB; 8AGU; EM; 2.70 A; E=1-189.
DR   PDB; 8AGV; EM; 2.60 A; E=1-189.
DR   PDB; 8AGW; EM; 2.60 A; E=1-189.
DR   PDB; 8AGX; EM; 2.40 A; E=1-189.
DR   PDB; 8AGZ; EM; 2.60 A; E=1-189.
DR   PDB; 8BIP; EM; 3.10 A; LR=2-189.
DR   PDB; 8BJQ; EM; 3.80 A; LR=2-189.
DR   PDB; 8BQD; EM; 3.90 A; BF=2-189.
DR   PDB; 8BQX; EM; 3.80 A; BF=2-189.
DR   PDB; 8CCS; EM; 1.97 A; D=1-189.
DR   PDB; 8CDL; EM; 2.72 A; D=1-189.
DR   PDB; 8CDR; EM; 2.04 A; D=1-189.
DR   PDB; 8CEH; EM; 2.05 A; D=1-189.
DR   PDB; 8CF5; EM; 2.71 A; D=1-189.
DR   PDB; 8CG8; EM; 2.57 A; D=1-189.
DR   PDB; 8CGN; EM; 2.28 A; D=1-189.
DR   PDB; 8CIV; EM; 2.47 A; D=1-189.
DR   PDB; 8CKU; EM; 3.11 A; D=1-189.
DR   PDB; 8CMJ; EM; 3.79 A; D=1-189.
DR   PDB; 8EUB; EM; 2.52 A; AR=1-189.
DR   PDB; 8EVP; EM; 2.38 A; AR=1-189.
DR   PDB; 8EVQ; EM; 2.72 A; AR=1-189.
DR   PDB; 8EVR; EM; 2.87 A; AR=1-189.
DR   PDB; 8EVS; EM; 2.62 A; AR=1-189.
DR   PDB; 8EVT; EM; 2.20 A; AR=1-189.
DR   PDB; 8EWB; EM; 2.87 A; AR=1-189.
DR   PDB; 8EWC; EM; 2.45 A; AR=1-189.
DR   PDB; 8HFR; EM; 2.64 A; RP=1-189.
DR   PDBsum; 2WW9; -.
DR   PDBsum; 2WWA; -.
DR   PDBsum; 3J6X; -.
DR   PDBsum; 3J6Y; -.
DR   PDBsum; 3J77; -.
DR   PDBsum; 3J78; -.
DR   PDBsum; 3JCT; -.
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; 4V4B; -.
DR   PDBsum; 4V6I; -.
DR   PDBsum; 4V7F; -.
DR   PDBsum; 4V7R; -.
DR   PDBsum; 4V88; -.
DR   PDBsum; 4V91; -.
DR   PDBsum; 5APN; -.
DR   PDBsum; 5APO; -.
DR   PDBsum; 5DAT; -.
DR   PDBsum; 5DC3; -.
DR   PDBsum; 5DGE; -.
DR   PDBsum; 5DGF; -.
DR   PDBsum; 5DGV; -.
DR   PDBsum; 5FCI; -.
DR   PDBsum; 5FCJ; -.
DR   PDBsum; 5GAK; -.
DR   PDBsum; 5H4P; -.
DR   PDBsum; 5I4L; -.
DR   PDBsum; 5JCS; -.
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; 5T62; -.
DR   PDBsum; 5T6R; -.
DR   PDBsum; 5TBW; -.
DR   PDBsum; 5TGA; -.
DR   PDBsum; 5TGM; -.
DR   PDBsum; 6ELZ; -.
DR   PDBsum; 6EM5; -.
DR   PDBsum; 6FT6; -.
DR   PDBsum; 6GQ1; -.
DR   PDBsum; 6GQB; -.
DR   PDBsum; 6GQV; -.
DR   PDBsum; 6HD7; -.
DR   PDBsum; 6HHQ; -.
DR   PDBsum; 6I7O; -.
DR   PDBsum; 6M62; -.
DR   PDBsum; 6N8J; -.
DR   PDBsum; 6N8K; -.
DR   PDBsum; 6N8L; -.
DR   PDBsum; 6N8M; -.
DR   PDBsum; 6N8N; -.
DR   PDBsum; 6N8O; -.
DR   PDBsum; 6OIG; -.
DR   PDBsum; 6Q8Y; -.
DR   PDBsum; 6QIK; -.
DR   PDBsum; 6QT0; -.
DR   PDBsum; 6QTZ; -.
DR   PDBsum; 6R84; -.
DR   PDBsum; 6R86; -.
DR   PDBsum; 6R87; -.
DR   PDBsum; 6RI5; -.
DR   PDBsum; 6RZZ; -.
DR   PDBsum; 6S05; -.
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; 6WOO; -.
DR   PDBsum; 6XIQ; -.
DR   PDBsum; 6XIR; -.
DR   PDBsum; 6YLG; -.
DR   PDBsum; 6YLH; -.
DR   PDBsum; 6YLX; -.
DR   PDBsum; 6YLY; -.
DR   PDBsum; 6Z6J; -.
DR   PDBsum; 6Z6K; -.
DR   PDBsum; 7AZY; -.
DR   PDBsum; 7B7D; -.
DR   PDBsum; 7BT6; -.
DR   PDBsum; 7BTB; -.
DR   PDBsum; 7MPI; -.
DR   PDBsum; 7MPJ; -.
DR   PDBsum; 7N8B; -.
DR   PDBsum; 7NAC; -.
DR   PDBsum; 7NAD; -.
DR   PDBsum; 7NAF; -.
DR   PDBsum; 7NRC; -.
DR   PDBsum; 7NRD; -.
DR   PDBsum; 7OF1; -.
DR   PDBsum; 7OH3; -.
DR   PDBsum; 7OHQ; -.
DR   PDBsum; 7OHR; -.
DR   PDBsum; 7OHV; -.
DR   PDBsum; 7OSA; -.
DR   PDBsum; 7OSM; -.
DR   PDBsum; 7R72; -.
DR   PDBsum; 7R7A; -.
DR   PDBsum; 7RR5; -.
DR   PDBsum; 7TOO; -.
DR   PDBsum; 7TOP; -.
DR   PDBsum; 7U0H; -.
DR   PDBsum; 7UG6; -.
DR   PDBsum; 7UOO; -.
DR   PDBsum; 7UQB; -.
DR   PDBsum; 7UQZ; -.
DR   PDBsum; 7V08; -.
DR   PDBsum; 7Z34; -.
DR   PDBsum; 7ZPQ; -.
DR   PDBsum; 7ZRS; -.
DR   PDBsum; 7ZS5; -.
DR   PDBsum; 7ZUW; -.
DR   PDBsum; 7ZUX; -.
DR   PDBsum; 7ZW0; -.
DR   PDBsum; 8AAF; -.
DR   PDBsum; 8AGT; -.
DR   PDBsum; 8AGU; -.
DR   PDBsum; 8AGV; -.
DR   PDBsum; 8AGW; -.
DR   PDBsum; 8AGX; -.
DR   PDBsum; 8AGZ; -.
DR   PDBsum; 8BIP; -.
DR   PDBsum; 8BJQ; -.
DR   PDBsum; 8BQD; -.
DR   PDBsum; 8BQX; -.
DR   PDBsum; 8CCS; -.
DR   PDBsum; 8CDL; -.
DR   PDBsum; 8CDR; -.
DR   PDBsum; 8CEH; -.
DR   PDBsum; 8CF5; -.
DR   PDBsum; 8CG8; -.
DR   PDBsum; 8CGN; -.
DR   PDBsum; 8CIV; -.
DR   PDBsum; 8CKU; -.
DR   PDBsum; 8CMJ; -.
DR   PDBsum; 8EUB; -.
DR   PDBsum; 8EVP; -.
DR   PDBsum; 8EVQ; -.
DR   PDBsum; 8EVR; -.
DR   PDBsum; 8EVS; -.
DR   PDBsum; 8EVT; -.
DR   PDBsum; 8EWB; -.
DR   PDBsum; 8EWC; -.
DR   PDBsum; 8HFR; -.
DR   AlphaFoldDB; P0CX82; -.
DR   EMDB; EMD-0047; -.
DR   EMDB; EMD-0048; -.
DR   EMDB; EMD-0049; -.
DR   EMDB; EMD-0202; -.
DR   EMDB; EMD-0369; -.
DR   EMDB; EMD-0370; -.
DR   EMDB; EMD-0371; -.
DR   EMDB; EMD-0372; -.
DR   EMDB; EMD-0373; -.
DR   EMDB; EMD-0374; -.
DR   EMDB; EMD-10068; -.
DR   EMDB; EMD-10071; -.
DR   EMDB; EMD-10098; -.
DR   EMDB; EMD-10262; -.
DR   EMDB; EMD-10315; -.
DR   EMDB; EMD-10377; -.
DR   EMDB; EMD-10396; -.
DR   EMDB; EMD-10397; -.
DR   EMDB; EMD-10398; -.
DR   EMDB; EMD-10431; -.
DR   EMDB; EMD-10537; -.
DR   EMDB; EMD-10838; -.
DR   EMDB; EMD-10839; -.
DR   EMDB; EMD-10841; -.
DR   EMDB; EMD-10842; -.
DR   EMDB; EMD-11096; -.
DR   EMDB; EMD-11097; -.
DR   EMDB; EMD-11951; -.
DR   EMDB; EMD-12081; -.
DR   EMDB; EMD-12534; -.
DR   EMDB; EMD-12535; -.
DR   EMDB; EMD-12866; -.
DR   EMDB; EMD-12892; -.
DR   EMDB; EMD-12905; -.
DR   EMDB; EMD-12906; -.
DR   EMDB; EMD-12910; -.
DR   EMDB; EMD-14471; -.
DR   EMDB; EMD-14990; -.
DR   EMDB; EMD-16563; -.
DR   EMDB; EMD-16591; -.
DR   EMDB; EMD-16594; -.
DR   EMDB; EMD-16609; -.
DR   EMDB; EMD-16616; -.
DR   EMDB; EMD-16634; -.
DR   EMDB; EMD-16648; -.
DR   EMDB; EMD-16684; -.
DR   EMDB; EMD-16702; -.
DR   EMDB; EMD-16729; -.
DR   EMDB; EMD-20077; -.
DR   EMDB; EMD-21859; -.
DR   EMDB; EMD-22196; -.
DR   EMDB; EMD-22198; -.
DR   EMDB; EMD-23934; -.
DR   EMDB; EMD-23935; -.
DR   EMDB; EMD-24235; -.
DR   EMDB; EMD-24269; -.
DR   EMDB; EMD-24270; -.
DR   EMDB; EMD-24290; -.
DR   EMDB; EMD-24296; -.
DR   EMDB; EMD-24652; -.
DR   EMDB; EMD-26033; -.
DR   EMDB; EMD-26034; -.
DR   EMDB; EMD-28610; -.
DR   EMDB; EMD-28632; -.
DR   EMDB; EMD-28633; -.
DR   EMDB; EMD-28634; -.
DR   EMDB; EMD-28635; -.
DR   EMDB; EMD-28636; -.
DR   EMDB; EMD-28642; -.
DR   EMDB; EMD-28643; -.
DR   EMDB; EMD-30108; -.
DR   EMDB; EMD-30170; -.
DR   EMDB; EMD-30174; -.
DR   EMDB; EMD-3461; -.
DR   EMDB; EMD-4140; -.
DR   EMDB; EMD-4302; -.
DR   EMDB; EMD-4427; -.
DR   EMDB; EMD-4474; -.
DR   EMDB; EMD-4560; -.
DR   EMDB; EMD-4630; -.
DR   EMDB; EMD-4636; -.
DR   EMDB; EMD-4751; -.
DR   EMDB; EMD-4752; -.
DR   EMDB; EMD-4753; -.
DR   EMDB; EMD-4884; -.
DR   EMDB; EMD-8362; -.
DR   EMDB; EMD-8368; -.
DR   SMR; P0CX82; -.
DR   BioGRID; 32671; 393.
DR   BioGRID; 32789; 251.
DR   IntAct; P0CX82; 6.
DR   MINT; P0CX82; -.
DR   STRING; 4932.YBL027W; -.
DR   BindingDB; P0CX82; -.
DR   ChEMBL; CHEMBL1741172; -.
DR   CarbonylDB; P0CX82; -.
DR   iPTMnet; P0CX82; -.
DR   MaxQB; P0CX82; -.
DR   PaxDb; 4932-YBL027W; -.
DR   PeptideAtlas; P0CX82; -.
DR   TopDownProteomics; P0CX82; -.
DR   EnsemblFungi; YBL027W_mRNA; YBL027W; YBL027W.
DR   EnsemblFungi; YBR084C-A_mRNA; YBR084C-A; YBR084C-A.
DR   GeneID; 852254; -.
DR   GeneID; 852379; -.
DR   KEGG; sce:YBL027W; -.
DR   KEGG; sce:YBR084C-A; -.
DR   AGR; SGD:S000002156; -.
DR   SGD; S000002156; RPL19A.
DR   VEuPathDB; FungiDB:YBL027W; -.
DR   VEuPathDB; FungiDB:YBR084C-A; -.
DR   eggNOG; KOG1696; Eukaryota.
DR   HOGENOM; CLU_083919_0_0_1; -.
DR   InParanoid; P0CX82; -.
DR   OMA; NRVWIDP; -.
DR   OrthoDB; 5483247at2759; -.
DR   BioCyc; YEAST:G3O-29228-MONOMER; -.
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-72689; Formation of a pool of free 40S subunits.
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   BioGRID-ORCS; 852254; 5 hits in 10 CRISPR screens.
DR   BioGRID-ORCS; 852379; 9 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P0CX82; -.
DR   PRO; PR:P0CX82; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P0CX82; Protein.
DR   ExpressionAtlas; P0CX82; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
DR   CDD; cd01417; Ribosomal_L19e_E; 1.
DR   Gene3D; 1.10.1200.240; -; 1.
DR   Gene3D; 1.10.1650.10; -; 1.
DR   HAMAP; MF_01475; Ribosomal_eL19; 1.
DR   InterPro; IPR035970; 60S_ribosomal_eL19_sf.
DR   InterPro; IPR039547; Ribosomal_eL19.
DR   InterPro; IPR023638; Ribosomal_eL19_CS.
DR   InterPro; IPR000196; Ribosomal_eL19_dom.
DR   InterPro; IPR015972; Ribosomal_eL19_dom1.
DR   InterPro; IPR033935; Ribosomal_eL19_euk.
DR   PANTHER; PTHR10722; 60S RIBOSOMAL PROTEIN L19; 1.
DR   PANTHER; PTHR10722:SF0; 60S RIBOSOMAL PROTEIN L19; 1.
DR   Pfam; PF01280; Ribosomal_L19e; 1.
DR   SMART; SM01416; Ribosomal_L19e; 1.
DR   SUPFAM; SSF48140; Ribosomal protein L19 (L19e); 1.
DR   PROSITE; PS00526; RIBOSOMAL_L19E; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW   Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1544921,
FT                   ECO:0000269|PubMed:6355773"
FT   CHAIN           2..189
FT                   /note="Large ribosomal subunit protein eL19A"
FT                   /id="PRO_0000131184"
FT   REGION          58..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..85
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         30
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         37
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         91
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CROSSLNK        21
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CROSSLNK        53
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CROSSLNK        60
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CROSSLNK        146
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CROSSLNK        186
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CONFLICT        54
FT                   /note="A -> S (in Ref. 7; J03724)"
FT                   /evidence="ECO:0000305"
FT   HELIX           5..15
FT                   /evidence="ECO:0007829|PDB:7NAD"
FT   STRAND          21..24
FT                   /evidence="ECO:0007829|PDB:7NAD"
FT   HELIX           29..33
FT                   /evidence="ECO:0007829|PDB:7NAD"
FT   HELIX           38..46
FT                   /evidence="ECO:0007829|PDB:7NAD"
FT   STRAND          49..52
FT                   /evidence="ECO:0007829|PDB:7NAD"
FT   HELIX           91..111
FT                   /evidence="ECO:0007829|PDB:7NAD"
FT   HELIX           117..128
FT                   /evidence="ECO:0007829|PDB:7NAD"
FT   HELIX           135..161
FT                   /evidence="ECO:0007829|PDB:7NAD"
SQ   SEQUENCE   189 AA;  21704 MW;  776C3AB3D348EE99 CRC64;
     MANLRTQKRL AASVVGVGKR KVWLDPNETS EIAQANSRNA IRKLVKNGTI VKKAVTVHSK
     SRTRAHAQSK REGRHSGYGK RKGTREARLP SQVVWIRRLR VLRRLLAKYR DAGKIDKHLY
     HVLYKESKGN AFKHKRALVE HIIQAKADAQ REKALNEEAE ARRLKNRAAR DRRAQRVAEK
     RDALLKEDA
//