RL5_YEAST
ID RL5_YEAST Reviewed; 297 AA.
AC P26321; D6W3N6;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 4.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=60S ribosomal protein L5 {ECO:0000303|PubMed:9559554};
DE AltName: Full=L1;
DE AltName: Full=L1a;
DE AltName: Full=Large ribosomal subunit protein uL18 {ECO:0000303|PubMed:24524803};
DE AltName: Full=Ribosomal 5S RNA-binding protein;
DE AltName: Full=YL3;
GN Name=RPL5 {ECO:0000303|PubMed:9559554}; Synonyms=RPL1, RPL1A;
GN OrderedLocusNames=YPL131W; ORFNames=LPI14W;
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=2007570; DOI=10.1016/s0021-9258(18)38092-x;
RA Tang B., Nazar R.N.;
RT "Structure of the yeast ribosomal 5 S RNA-binding protein YL3.";
RL J. Biol. Chem. 266:6120-6123(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1325447; DOI=10.1016/s0021-9258(19)37105-4;
RA Tang B., Nazar R.N.;
RT "Unbalanced regulation of the ribosomal 5 S RNA-binding protein in
RT Saccharomyces cerevisiae expressing mutant 5 S rRNAs.";
RL J. Biol. Chem. 267:17738-17742(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8474444; DOI=10.1128/mcb.13.5.2835-2845.1993;
RA Deshmukh M.P., Tsay Y.F., Paulovich A.G., Woolford J.L. Jr.;
RT "Yeast ribosomal protein L1 is required for the stability of newly
RT synthesized 5S rRNA and the assembly of 60S ribosomal subunits.";
RL Mol. Cell. Biol. 13:2835-2845(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [5]
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 [6]
RP PROTEIN SEQUENCE OF 2-31 AND 219-253.
RX PubMed=393511; DOI=10.1111/j.1432-1033.1979.tb04274.x;
RA Nazar R.N., Yaguchi M., Willick G.E., Rollin C.F., Roy C.;
RT "The 5-S RNA binding protein from yeast (Saccharomyces cerevisiae)
RT ribosomes. Evolution of the eukaryotic 5-S RNA binding protein.";
RL Eur. J. Biochem. 102:573-582(1979).
RN [7]
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, AND IDENTIFICATION BY
RP 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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167; SER-176 AND SER-235, 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 [12]
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 [13]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-164, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [14]
RP INTERACTION WITH RPL11A; RPL11B AND SYO1, AND SUBCELLULAR LOCATION.
RX PubMed=23118189; DOI=10.1126/science.1226960;
RA Kressler D., Bange G., Ogawa Y., Stjepanovic G., Bradatsch B., Pratte D.,
RA Amlacher S., Strauss D., Yoneda Y., Katahira J., Sinning I., Hurt E.;
RT "Synchronizing nuclear import of ribosomal proteins with ribosome
RT assembly.";
RL Science 338:666-671(2012).
RN [15]
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 [16]
RP 3D-STRUCTURE MODELING OF 11-232, 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 [17]
RP 3D-STRUCTURE MODELING OF 11-232, 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 [18]
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 [19]
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. {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) (PubMed:9559554, PubMed:22096102). uL18
CC forms a heterotrimeric complex with SYO1 and uL5 (RPL11A/RPL11B).
CC Interaction of this complex with KAP104 allows the nuclear import of
CC the heterotrimer (PubMed:23118189). {ECO:0000269|PubMed:22096102,
CC ECO:0000269|PubMed:23118189, ECO:0000305|PubMed:9559554}.
CC -!- INTERACTION:
CC P26321; Q02892: NOG1; NbExp=2; IntAct=EBI-15398, EBI-12105;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}. Nucleus
CC {ECO:0000269|PubMed:23118189}. Note=The SYO1-uL5-uL18 complex is
CC transported into the nucleus by KAP104. {ECO:0000269|PubMed:23118189}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL18 family.
CC {ECO:0000305}.
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DR EMBL; M65056; AAA35234.1; -; Genomic_DNA.
DR EMBL; M94864; AAA35236.1; -; Genomic_DNA.
DR EMBL; L01796; AAA34979.1; -; Genomic_DNA.
DR EMBL; U43703; AAB68228.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11302.1; -; Genomic_DNA.
DR PIR; S42144; S42144.
DR RefSeq; NP_015194.1; NM_001183945.1.
DR PDB; 3J6X; EM; 6.10 A; L5=1-297.
DR PDB; 3J6Y; EM; 6.10 A; L5=1-297.
DR PDB; 3J77; EM; 6.20 A; L5=1-297.
DR PDB; 3J78; EM; 6.30 A; L5=1-297.
DR PDB; 3JCT; EM; 3.08 A; D=1-297.
DR PDB; 4U3M; X-ray; 3.00 A; L5/l5=2-297.
DR PDB; 4U3N; X-ray; 3.20 A; L5/l5=2-297.
DR PDB; 4U3U; X-ray; 2.90 A; L5/l5=2-297.
DR PDB; 4U4N; X-ray; 3.10 A; L5/l5=2-297.
DR PDB; 4U4O; X-ray; 3.60 A; L5/l5=2-297.
DR PDB; 4U4Q; X-ray; 3.00 A; L5/l5=2-297.
DR PDB; 4U4R; X-ray; 2.80 A; L5/l5=2-297.
DR PDB; 4U4U; X-ray; 3.00 A; L5/l5=2-297.
DR PDB; 4U4Y; X-ray; 3.20 A; L5/l5=2-297.
DR PDB; 4U4Z; X-ray; 3.10 A; L5/l5=2-297.
DR PDB; 4U50; X-ray; 3.20 A; L5/l5=2-297.
DR PDB; 4U51; X-ray; 3.20 A; L5/l5=2-297.
DR PDB; 4U52; X-ray; 3.00 A; L5/l5=2-297.
DR PDB; 4U53; X-ray; 3.30 A; L5/l5=2-297.
DR PDB; 4U55; X-ray; 3.20 A; L5/l5=2-297.
DR PDB; 4U56; X-ray; 3.45 A; L5/l5=2-297.
DR PDB; 4U6F; X-ray; 3.10 A; L5/l5=2-297.
DR PDB; 4V4B; EM; 11.70 A; BE=11-232.
DR PDB; 4V6I; EM; 8.80 A; BQ=1-297.
DR PDB; 4V7F; EM; 8.70 A; P=1-297.
DR PDB; 4V7R; X-ray; 4.00 A; BE/DE=1-297.
DR PDB; 4V88; X-ray; 3.00 A; BD/DD=1-297.
DR PDB; 4V8T; EM; 8.10 A; D=1-297.
DR PDB; 4V8Y; EM; 4.30 A; BD=2-297.
DR PDB; 4V8Z; EM; 6.60 A; BD=2-297.
DR PDB; 4V91; EM; 3.70 A; D=1-297.
DR PDB; 5APN; EM; 3.91 A; D=1-297.
DR PDB; 5APO; EM; 3.41 A; D=1-297.
DR PDB; 5DAT; X-ray; 3.15 A; L5/l5=2-297.
DR PDB; 5DC3; X-ray; 3.25 A; L5/l5=2-297.
DR PDB; 5DGE; X-ray; 3.45 A; L5/l5=2-297.
DR PDB; 5DGF; X-ray; 3.30 A; L5/l5=2-297.
DR PDB; 5DGV; X-ray; 3.10 A; L5/l5=2-297.
DR PDB; 5FCI; X-ray; 3.40 A; L5/l5=2-297.
DR PDB; 5FCJ; X-ray; 3.10 A; L5/l5=2-297.
DR PDB; 5FL8; EM; 9.50 A; D=1-297.
DR PDB; 5GAK; EM; 3.88 A; H=1-297.
DR PDB; 5H4P; EM; 3.07 A; D=1-297.
DR PDB; 5I4L; X-ray; 3.10 A; L5/l5=2-297.
DR PDB; 5JCS; EM; 9.50 A; D=1-297.
DR PDB; 5JUO; EM; 4.00 A; I=1-297.
DR PDB; 5JUP; EM; 3.50 A; I=1-297.
DR PDB; 5JUS; EM; 4.20 A; I=1-297.
DR PDB; 5JUT; EM; 4.00 A; I=1-297.
DR PDB; 5JUU; EM; 4.00 A; I=1-297.
DR PDB; 5LYB; X-ray; 3.25 A; L5/l5=2-297.
DR PDB; 5M1J; EM; 3.30 A; D5=2-297.
DR PDB; 5MC6; EM; 3.80 A; BI=1-297.
DR PDB; 5MEI; X-ray; 3.50 A; CG/m=2-297.
DR PDB; 5NDG; X-ray; 3.70 A; L5/l5=2-297.
DR PDB; 5NDV; X-ray; 3.30 A; L5/l5=2-297.
DR PDB; 5NDW; X-ray; 3.70 A; L5/l5=2-297.
DR PDB; 5OBM; X-ray; 3.40 A; L5/l5=2-297.
DR PDB; 5ON6; X-ray; 3.10 A; CG/m=2-297.
DR PDB; 5T62; EM; 3.30 A; G=1-297.
DR PDB; 5T6R; EM; 4.50 A; G=1-297.
DR PDB; 5TBW; X-ray; 3.00 A; CG/m=2-297.
DR PDB; 5TGA; X-ray; 3.30 A; L5/l5=2-297.
DR PDB; 5TGM; X-ray; 3.50 A; L5/l5=2-297.
DR PDB; 6FT6; EM; 3.90 A; D=1-297.
DR PDB; 6GQ1; EM; 4.40 A; D=2-297.
DR PDB; 6GQB; EM; 3.90 A; D=2-297.
DR PDB; 6GQV; EM; 4.00 A; D=2-297.
DR PDB; 6HD7; EM; 3.40 A; H=1-297.
DR PDB; 6HHQ; X-ray; 3.10 A; CG/m=1-297.
DR PDB; 6I7O; EM; 5.30 A; BI/YI=4-297.
DR PDB; 6M62; EM; 3.20 A; D=1-297.
DR PDB; 6N8J; EM; 3.50 A; D=1-297.
DR PDB; 6N8K; EM; 3.60 A; D=1-297.
DR PDB; 6N8L; EM; 3.60 A; D=1-297.
DR PDB; 6N8M; EM; 3.50 A; G=1-297.
DR PDB; 6N8N; EM; 3.80 A; G=1-297.
DR PDB; 6N8O; EM; 3.50 A; G=1-297.
DR PDB; 6OIG; EM; 3.80 A; D=2-297.
DR PDB; 6Q8Y; EM; 3.10 A; BI=2-297.
DR PDB; 6QIK; EM; 3.10 A; P=1-297.
DR PDB; 6QT0; EM; 3.40 A; P=1-297.
DR PDB; 6QTZ; EM; 3.50 A; P=1-297.
DR PDB; 6R84; EM; 3.60 A; H=2-297.
DR PDB; 6R86; EM; 3.40 A; H=2-297.
DR PDB; 6R87; EM; 3.40 A; H=2-297.
DR PDB; 6RI5; EM; 3.30 A; P=1-297.
DR PDB; 6RZZ; EM; 3.20 A; P=1-297.
DR PDB; 6S05; EM; 3.90 A; P=1-297.
DR PDB; 6S47; EM; 3.28 A; AG=2-297.
DR PDB; 6SNT; EM; 2.80 A; k=1-297.
DR PDB; 6SV4; EM; 3.30 A; BI/YI/ZI=1-297.
DR PDB; 6T4Q; EM; 2.60 A; LD=4-297.
DR PDB; 6T7I; EM; 3.20 A; LD=1-297.
DR PDB; 6T7T; EM; 3.10 A; LD=1-297.
DR PDB; 6T83; EM; 4.00 A; Dy/Ga=1-297.
DR PDB; 6TB3; EM; 2.80 A; BI=4-297.
DR PDB; 6TNU; EM; 3.10 A; BI=4-297.
DR PDB; 6WOO; EM; 2.90 A; D=3-297.
DR PDB; 6YLG; EM; 3.00 A; D=1-297.
DR PDB; 6YLH; EM; 3.10 A; D=1-297.
DR PDB; 6Z6J; EM; 3.40 A; LD=1-297.
DR PDB; 6Z6K; EM; 3.40 A; LD=1-297.
DR PDB; 7AZY; EM; 2.88 A; t=1-297.
DR PDB; 7B7D; EM; 3.30 A; LG=4-297.
DR PDB; 7BT6; EM; 3.12 A; D=1-297.
DR PDB; 7BTB; EM; 3.22 A; D=1-297.
DR PDB; 7NRC; EM; 3.90 A; LG=4-297.
DR PDB; 7NRD; EM; 4.36 A; LG=4-297.
DR PDB; 7OH3; EM; 3.40 A; D=1-297.
DR PDB; 7OHQ; EM; 3.10 A; D=1-297.
DR PDB; 7OHT; EM; 4.70 A; D=1-297.
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; 4V8T; -.
DR PDBsum; 4V8Y; -.
DR PDBsum; 4V8Z; -.
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; 5FL8; -.
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; 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; 6YLG; -.
DR PDBsum; 6YLH; -.
DR PDBsum; 6Z6J; -.
DR PDBsum; 6Z6K; -.
DR PDBsum; 7AZY; -.
DR PDBsum; 7B7D; -.
DR PDBsum; 7BT6; -.
DR PDBsum; 7BTB; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR PDBsum; 7OH3; -.
DR PDBsum; 7OHQ; -.
DR PDBsum; 7OHT; -.
DR AlphaFoldDB; P26321; -.
DR SMR; P26321; -.
DR BioGRID; 36050; 262.
DR ComplexPortal; CPX-1601; 60S cytosolic large ribosomal subunit.
DR DIP; DIP-1790N; -.
DR IntAct; P26321; 169.
DR MINT; P26321; -.
DR STRING; 4932.YPL131W; -.
DR CarbonylDB; P26321; -.
DR iPTMnet; P26321; -.
DR MaxQB; P26321; -.
DR PaxDb; P26321; -.
DR PRIDE; P26321; -.
DR EnsemblFungi; YPL131W_mRNA; YPL131W; YPL131W.
DR GeneID; 855972; -.
DR KEGG; sce:YPL131W; -.
DR SGD; S000006052; RPL5.
DR VEuPathDB; FungiDB:YPL131W; -.
DR eggNOG; KOG0875; Eukaryota.
DR GeneTree; ENSGT00950000183210; -.
DR HOGENOM; CLU_056222_1_0_1; -.
DR InParanoid; P26321; -.
DR OMA; KSQFQGY; -.
DR BioCyc; YEAST:G3O-34030-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-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 ChiTaRS; RPL1A; yeast.
DR EvolutionaryTrace; P26321; -.
DR PRO; PR:P26321; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P26321; protein.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008097; F:5S rRNA binding; IDA:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IMP:SGD.
DR HAMAP; MF_01337_A; Ribosomal_L18_A; 1.
DR InterPro; IPR005485; Rbsml_L5_euk/L18_arc.
DR InterPro; IPR025607; Rbsml_L5e_C.
DR PANTHER; PTHR23410; PTHR23410; 1.
DR Pfam; PF14204; Ribosomal_L18_c; 1.
DR Pfam; PF17144; Ribosomal_L5e; 1.
DR PRINTS; PR00058; RIBOSOMALL5.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:393511"
FT CHAIN 2..297
FT /note="60S ribosomal protein L5"
FT /id="PRO_0000131454"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT CROSSLNK 164
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 18
FT /note="T -> Y (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="K -> R (in Ref. 1; AAA35234 and 2; AAA35236)"
FT /evidence="ECO:0000305"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:4U3U"
FT HELIX 10..14
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 30..37
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 59..68
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 71..79
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 80..86
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:4U4U"
FT HELIX 95..112
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:4U3U"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:4U4U"
FT TURN 185..188
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 202..214
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 216..221
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 224..228
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 236..249
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 262..270
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 279..292
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 293..296
FT /evidence="ECO:0007829|PDB:4U4R"
SQ SEQUENCE 297 AA; 33715 MW; 14E3B2931C3CAE2B CRC64;
MAFQKDAKSS AYSSRFQTPF RRRREGKTDY YQRKRLVTQH KAKYNTPKYR LVVRFTNKDI
ICQIISSTIT GDVVLAAAYS HELPRYGITH GLTNWAAAYA TGLLIARRTL QKLGLDETYK
GVEEVEGEYE LTEAVEDGPR PFKVFLDIGL QRTTTGARVF GALKGASDGG LYVPHSENRF
PGWDFETEEI DPELLRSYIF GGHVSQYMEE LADDDEERFS ELFKGYLADD IDADSLEDIY
TSAHEAIRAD PAFKPTEKKF TKEQYAAESK KYRQTKLSKE ERAARVAAKI AALAGQQ
