RL11A_YEAST
ID RL11A_YEAST Reviewed; 174 AA.
AC P0C0W9; D6W4A0; P06380;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=60S ribosomal protein L11-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=L16;
DE AltName: Full=Large ribosomal subunit protein uL5-A {ECO:0000303|PubMed:24524803};
DE AltName: Full=RP39;
DE AltName: Full=YL22;
GN Name=RPL11A {ECO:0000303|PubMed:9559554}; Synonyms=RP39A, RPL16A;
GN OrderedLocusNames=YPR102C; ORFNames=P8283.14;
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=6090215; DOI=10.1016/0014-5793(84)80771-1;
RA Leer R.J., van Raamsdonk-Duin M.M.C., Mager W.H., Planta R.J.;
RT "The primary structure of the gene encoding yeast ribosomal protein L16.";
RL FEBS Lett. 175:371-376(1984).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP PROTEIN SEQUENCE OF 2-17, AND ACETYLATION AT SER-2 BY NATA.
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 [6]
RP SUBUNIT.
RX PubMed=7510288; DOI=10.1016/s0021-9258(17)37326-x;
RA Tsay Y.-F., Shankweiler G., Lake J., Woolford J.L. Jr.;
RT "Localization of Saccharomyces cerevisiae ribosomal protein L16 on the
RT surface of 60 S ribosomal subunits by immunoelectron microscopy.";
RL J. Biol. Chem. 269:7579-7586(1994).
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 CLEAVAGE OF INITIATOR METHIONINE, AND ACETYLATION AT SER-2 BY NATA.
RX PubMed=10601260; DOI=10.1074/jbc.274.52.37035;
RA Arnold R.J., Polevoda B., Reilly J.P., Sherman F.;
RT "The action of N-terminal acetyltransferases on yeast ribosomal proteins.";
RL J. Biol. Chem. 274:37035-37040(1999).
RN [9]
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 [10]
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [12]
RP METHYLATION AT LYS-75.
RX PubMed=22522802; DOI=10.1002/pmic.201100570;
RA Couttas T.A., Raftery M.J., Padula M.P., Herbert B.R., Wilkins M.R.;
RT "Methylation of translation-associated proteins in Saccharomyces
RT cerevisiae: Identification of methylated lysines and their
RT methyltransferases.";
RL Proteomics 12:960-972(2012).
RN [13]
RP INTERACTION WITH RPL5 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 [14]
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 [15]
RP 3D-STRUCTURE MODELING OF 7-171, 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 [16]
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 [17]
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 [18]
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). uL5
CC forms a heterotrimeric complex with uL18/RPL5 and SYO1. Interaction of
CC this complex with KAP104 allows the nuclear import of the heterotrimer
CC (PubMed:23118189). {ECO:0000269|PubMed:22096102,
CC ECO:0000269|PubMed:23118189, ECO:0000305|PubMed:9559554}.
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 -!- PTM: N-terminally acetylated by acetyltransferase NatA.
CC {ECO:0000269|PubMed:10601260, ECO:0000269|PubMed:1544921}.
CC -!- MISCELLANEOUS: Present with 39000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for uL5 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL5 family.
CC {ECO:0000305}.
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DR EMBL; X01029; CAA25515.1; -; Genomic_DNA.
DR EMBL; U32445; AAB68072.1; -; Genomic_DNA.
DR EMBL; AY693151; AAT93170.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11516.1; -; Genomic_DNA.
DR PIR; S59767; S59767.
DR RefSeq; NP_015427.1; NM_001184199.1.
DR PDB; 3J6X; EM; 6.10 A; 51=1-174.
DR PDB; 3J6Y; EM; 6.10 A; 51=1-174.
DR PDB; 3J77; EM; 6.20 A; 61=1-174.
DR PDB; 3J78; EM; 6.30 A; 61=1-174.
DR PDB; 3JCT; EM; 3.08 A; J=1-174.
DR PDB; 4V4B; EM; 11.70 A; BJ=2-174.
DR PDB; 4V6I; EM; 8.80 A; BE=1-174.
DR PDB; 4V7F; EM; 8.70 A; E=1-174.
DR PDB; 4V7R; X-ray; 4.00 A; BK/DK=1-174.
DR PDB; 4V88; X-ray; 3.00 A; BJ/DJ=1-174.
DR PDB; 4V8Y; EM; 4.30 A; BJ=2-174.
DR PDB; 4V8Z; EM; 6.60 A; BJ=2-174.
DR PDB; 4V91; EM; 3.70 A; J=1-174.
DR PDB; 5APN; EM; 3.91 A; J=1-174.
DR PDB; 5APO; EM; 3.41 A; J=1-174.
DR PDB; 5DGE; X-ray; 3.45 A; M1/m1=2-174.
DR PDB; 5FCI; X-ray; 3.40 A; M1/m1=2-174.
DR PDB; 5FCJ; X-ray; 3.10 A; M1/m1=2-174.
DR PDB; 5FL8; EM; 9.50 A; J=1-174.
DR PDB; 5GAK; EM; 3.88 A; M=1-174.
DR PDB; 5H4P; EM; 3.07 A; J=1-174.
DR PDB; 5JCS; EM; 9.50 A; J=1-174.
DR PDB; 5JUO; EM; 4.00 A; O=1-174.
DR PDB; 5JUP; EM; 3.50 A; O=1-174.
DR PDB; 5JUS; EM; 4.20 A; O=1-174.
DR PDB; 5JUT; EM; 4.00 A; O=1-174.
DR PDB; 5JUU; EM; 4.00 A; O=1-174.
DR PDB; 5M1J; EM; 3.30 A; J5=6-174.
DR PDB; 5MC6; EM; 3.80 A; AG=1-174.
DR PDB; 5NDG; X-ray; 3.70 A; M1/m1=6-174.
DR PDB; 5T62; EM; 3.30 A; M=1-174.
DR PDB; 5T6R; EM; 4.50 A; M=1-174.
DR PDB; 6FT6; EM; 3.90 A; J=1-174.
DR PDB; 6HD7; EM; 3.40 A; M=1-174.
DR PDB; 6M62; EM; 3.20 A; J=1-174.
DR PDB; 6N8J; EM; 3.50 A; J=1-174.
DR PDB; 6N8K; EM; 3.60 A; J=1-174.
DR PDB; 6N8L; EM; 3.60 A; J=1-174.
DR PDB; 6N8M; EM; 3.50 A; M=1-174.
DR PDB; 6N8N; EM; 3.80 A; M=1-174.
DR PDB; 6N8O; EM; 3.50 A; M=1-174.
DR PDB; 6QIK; EM; 3.10 A; E=1-174.
DR PDB; 6QT0; EM; 3.40 A; E=1-174.
DR PDB; 6QTZ; EM; 3.50 A; E=1-174.
DR PDB; 6RI5; EM; 3.30 A; E=1-174.
DR PDB; 6RZZ; EM; 3.20 A; E=1-174.
DR PDB; 6S05; EM; 3.90 A; E=1-174.
DR PDB; 6SNT; EM; 2.80 A; q=1-174.
DR PDB; 6SV4; EM; 3.30 A; AG/XG/zG=1-174.
DR PDB; 6T7I; EM; 3.20 A; LJ=1-174.
DR PDB; 6T7T; EM; 3.10 A; LJ=1-174.
DR PDB; 6T83; EM; 4.00 A; Jy/Ma=1-174.
DR PDB; 6YLG; EM; 3.00 A; J=1-174.
DR PDB; 6YLH; EM; 3.10 A; J=1-174.
DR PDB; 6Z6J; EM; 3.40 A; LJ=1-174.
DR PDB; 6Z6K; EM; 3.40 A; LJ=1-174.
DR PDB; 7BT6; EM; 3.12 A; J=1-174.
DR PDB; 7BTB; EM; 3.22 A; J=1-174.
DR PDB; 7OH3; EM; 3.40 A; J=1-174.
DR PDB; 7OHQ; EM; 3.10 A; J=1-174.
DR PDB; 7OHT; EM; 4.70 A; J=1-174.
DR PDBsum; 3J6X; -.
DR PDBsum; 3J6Y; -.
DR PDBsum; 3J77; -.
DR PDBsum; 3J78; -.
DR PDBsum; 3JCT; -.
DR PDBsum; 4V4B; -.
DR PDBsum; 4V6I; -.
DR PDBsum; 4V7F; -.
DR PDBsum; 4V7R; -.
DR PDBsum; 4V88; -.
DR PDBsum; 4V8Y; -.
DR PDBsum; 4V8Z; -.
DR PDBsum; 4V91; -.
DR PDBsum; 5APN; -.
DR PDBsum; 5APO; -.
DR PDBsum; 5DGE; -.
DR PDBsum; 5FCI; -.
DR PDBsum; 5FCJ; -.
DR PDBsum; 5FL8; -.
DR PDBsum; 5GAK; -.
DR PDBsum; 5H4P; -.
DR PDBsum; 5JCS; -.
DR PDBsum; 5JUO; -.
DR PDBsum; 5JUP; -.
DR PDBsum; 5JUS; -.
DR PDBsum; 5JUT; -.
DR PDBsum; 5JUU; -.
DR PDBsum; 5M1J; -.
DR PDBsum; 5MC6; -.
DR PDBsum; 5NDG; -.
DR PDBsum; 5T62; -.
DR PDBsum; 5T6R; -.
DR PDBsum; 6FT6; -.
DR PDBsum; 6HD7; -.
DR PDBsum; 6M62; -.
DR PDBsum; 6N8J; -.
DR PDBsum; 6N8K; -.
DR PDBsum; 6N8L; -.
DR PDBsum; 6N8M; -.
DR PDBsum; 6N8N; -.
DR PDBsum; 6N8O; -.
DR PDBsum; 6QIK; -.
DR PDBsum; 6QT0; -.
DR PDBsum; 6QTZ; -.
DR PDBsum; 6RI5; -.
DR PDBsum; 6RZZ; -.
DR PDBsum; 6S05; -.
DR PDBsum; 6SNT; -.
DR PDBsum; 6SV4; -.
DR PDBsum; 6T7I; -.
DR PDBsum; 6T7T; -.
DR PDBsum; 6T83; -.
DR PDBsum; 6YLG; -.
DR PDBsum; 6YLH; -.
DR PDBsum; 6Z6J; -.
DR PDBsum; 6Z6K; -.
DR PDBsum; 7BT6; -.
DR PDBsum; 7BTB; -.
DR PDBsum; 7OH3; -.
DR PDBsum; 7OHQ; -.
DR PDBsum; 7OHT; -.
DR AlphaFoldDB; P0C0W9; -.
DR SMR; P0C0W9; -.
DR BioGRID; 36268; 199.
DR DIP; DIP-4764N; -.
DR IntAct; P0C0W9; 29.
DR MINT; P0C0W9; -.
DR STRING; 4932.YPR102C; -.
DR iPTMnet; P0C0W9; -.
DR MaxQB; P0C0W9; -.
DR PaxDb; P0C0W9; -.
DR PRIDE; P0C0W9; -.
DR EnsemblFungi; YPR102C_mRNA; YPR102C; YPR102C.
DR GeneID; 856217; -.
DR KEGG; sce:YPR102C; -.
DR SGD; S000006306; RPL11A.
DR VEuPathDB; FungiDB:YPR102C; -.
DR eggNOG; KOG0397; Eukaryota.
DR GeneTree; ENSGT00910000144211; -.
DR HOGENOM; CLU_061015_3_0_1; -.
DR InParanoid; P0C0W9; -.
DR OMA; QTETIKW; -.
DR BioCyc; YEAST:G3O-34242-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; RPL16A; yeast.
DR EvolutionaryTrace; P0C0W9; -.
DR PRO; PR:P0C0W9; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P0C0W9; protein.
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:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
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 Gene3D; 3.30.1440.10; -; 1.
DR InterPro; IPR002132; Ribosomal_L5.
DR InterPro; IPR031309; Ribosomal_L5_C.
DR InterPro; IPR020929; Ribosomal_L5_CS.
DR InterPro; IPR022803; Ribosomal_L5_dom_sf.
DR InterPro; IPR031310; Ribosomal_L5_N.
DR PANTHER; PTHR11994; PTHR11994; 1.
DR Pfam; PF00281; Ribosomal_L5; 1.
DR Pfam; PF00673; Ribosomal_L5_C; 1.
DR PIRSF; PIRSF002161; Ribosomal_L5; 1.
DR SUPFAM; SSF55282; SSF55282; 1.
DR PROSITE; PS00358; RIBOSOMAL_L5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Methylation; Nucleus; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260,
FT ECO:0000269|PubMed:1544921, ECO:0007744|PubMed:22814378"
FT CHAIN 2..174
FT /note="60S ribosomal protein L11-A"
FT /id="PRO_0000125104"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:10601260,
FT ECO:0000269|PubMed:1544921, ECO:0007744|PubMed:22814378"
FT MOD_RES 75
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:22522802"
FT CONFLICT 12
FT /note="L -> D (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="E -> Q (in Ref. 1; CAA25515)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 174 AA; 19720 MW; 1E5C7D83541C6854 CRC64;
MSAKAQNPMR DLKIEKLVLN ISVGESGDRL TRASKVLEQL SGQTPVQSKA RYTVRTFGIR
RNEKIAVHVT VRGPKAEEIL ERGLKVKEYQ LRDRNFSATG NFGFGIDEHI DLGIKYDPSI
GIFGMDFYVV MNRPGARVTR RKRCKGTVGN SHKTTKEDTV SWFKQKYDAD VLDK
