ID RL11B_YEAST Reviewed; 174 AA. AC Q3E757; D6VUL7; P06380; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 31-JUL-2019, entry version 132. DE RecName: Full=60S ribosomal protein L11-B {ECO:0000303|PubMed:9559554}; DE AltName: Full=L16; DE AltName: Full=Large ribosomal subunit protein uL5-B {ECO:0000303|PubMed:24524803}; DE AltName: Full=RP39; DE AltName: Full=YL22; GN Name=RPL11B {ECO:0000303|PubMed:9559554}; Synonyms=RP39B, RPL16B; GN OrderedLocusNames=YGR085C; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6390341; DOI=10.1093/nar/12.22.8295; RA Teem J.L., Abovich N., Kaufer N.F., Schwindinger W.F., Warner J.R., RA Levy A., Woolford J.L. Jr., Leer R.J., van Raamsdonk-Duin M.M.C., RA Mager W.H., Planta R.J., Schultz L., Friesen J.D., Fried H.M., RA Rosbash M.; RT "A comparison of yeast ribosomal protein gene DNA sequences."; RL Nucleic Acids Res. 12:8295-8312(1984). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169869; RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., RA Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., RA Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., RA Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E., RA Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., RA Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., RA Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., RA Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., RA Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., RA Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., RA Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., RA Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., RA Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., RA Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., RA Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., RA Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., RA Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., RA Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., RA Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., RA van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., RA Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., RA Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., RA Zollner A., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."; RL Nature 387:81-84(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., RA Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and RT now."; RL G3 (Bethesda) 4:389-398(2014). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11. RX PubMed=3023862; DOI=10.1128/MCB.6.2.674; RA Rotenberg M.O., Woolford J.L. Jr.; RT "Tripartite upstream promoter element essential for expression of RT Saccharomyces cerevisiae ribosomal protein genes."; RL Mol. Cell. Biol. 6:674-687(1986). RN [5] 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 RT cerevisiae."; RL Yeast 14:471-477(1998). RN [6] 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 RT proteins."; RL J. Biol. Chem. 274:37035-37040(1999). 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., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [9] RP SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=22096102; DOI=10.1126/science.1212642; RA Ben-Shem A., Garreau de Loubresse N., Melnikov S., Jenner L., RA Yusupova G., Yusupov M.; RT "The structure of the eukaryotic ribosome at 3.0 A resolution."; RL Science 334:1524-1529(2011). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP 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., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [11] 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 [12] 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., RA Pratte D., Amlacher S., Strauss D., Yoneda Y., Katahira J., RA Sinning I., Hurt E.; RT "Synchronizing nuclear import of ribosomal proteins with ribosome RT assembly."; RL Science 338:666-671(2012). RN [13] 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 [14] RP STRUCTURE BY ELECTRON MICROSCOPY (7.3 ANGSTROMS) OF 7-171. RX PubMed=17115051; DOI=10.1038/nsmb1177; RA Schueler M., Connell S.R., Lescoute A., Giesebrecht J., Dabrowski M., RA Schroeer B., Mielke T., Penczek P.A., Westhof E., Spahn C.M.T.; RT "Structure of the ribosome-bound cricket paralysis virus IRES RNA."; RL Nat. Struct. Mol. Biol. 13:1092-1096(2006). CC -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein CC complex responsible for the synthesis of proteins in the cell. The CC small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and CC translates the encoded message by selecting cognate aminoacyl- CC transfer RNA (tRNA) molecules. The large subunit (LSU) contains CC the ribosomal catalytic site termed the peptidyl transferase CC center (PTC), which catalyzes the formation of peptide bonds, CC thereby polymerizing the amino acids delivered by tRNAs into a CC polypeptide chain. The nascent polypeptides leave the ribosome CC through a tunnel in the LSU and interact with protein factors that CC function in enzymatic processing, targeting, and the membrane CC insertion of nascent chains at the exit of the ribosomal tunnel. CC {ECO:0000305|PubMed:22096102}. CC -!- SUBUNIT: Component of the large ribosomal subunit (LSU). Mature CC yeast ribosomes consist of a small (40S) and a large (60S) CC subunit. The 40S small subunit contains 1 molecule of ribosomal CC RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). CC The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S CC rRNA) and 46 different proteins (encoded by 81 genes) CC (PubMed:9559554, PubMed:22096102). uL5 forms a heterotrimeric CC complex with uL18/RPL5 and SYO1. Interaction of this complex with CC 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}. CC Nucleus {ECO:0000269|PubMed:23118189}. Note=The SYO1-uL5-uL18 CC complex is transported into the nucleus by KAP104. CC {ECO:0000269|PubMed:23118189}. CC -!- PTM: N-terminally acetylated by acetyltransferase NatA. CC {ECO:0000269|PubMed:10601260}. CC -!- MISCELLANEOUS: Present with 21200 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z72870; CAA97087.1; -; Genomic_DNA. DR EMBL; M12933; AAA34990.1; -; Genomic_DNA. DR EMBL; BK006941; DAA08178.1; -; Genomic_DNA. DR PIR; A02764; R5BY16. DR RefSeq; NP_011599.1; NM_001181214.1. DR PDB; 2NOQ; EM; 7.30 A; H=7-171. DR PDB; 3J0Q; EM; 10.60 A; k=7-171. DR PDB; 4U3M; X-ray; 3.00 A; M1/m1=2-174. DR PDB; 4U3N; X-ray; 3.20 A; M1/m1=2-174. DR PDB; 4U3U; X-ray; 2.90 A; M1/m1=2-174. DR PDB; 4U4N; X-ray; 3.10 A; M1/m1=2-174. DR PDB; 4U4O; X-ray; 3.60 A; M1/m1=2-174. DR PDB; 4U4Q; X-ray; 3.00 A; M1/m1=2-174. DR PDB; 4U4R; X-ray; 2.80 A; M1/m1=2-174. DR PDB; 4U4U; X-ray; 3.00 A; M1/m1=2-174. DR PDB; 4U4Y; X-ray; 3.20 A; M1/m1=2-174. DR PDB; 4U4Z; X-ray; 3.10 A; M1/m1=2-174. DR PDB; 4U50; X-ray; 3.20 A; M1/m1=2-174. DR PDB; 4U51; X-ray; 3.20 A; M1/m1=2-174. DR PDB; 4U52; X-ray; 3.00 A; M1/m1=2-174. DR PDB; 4U53; X-ray; 3.30 A; M1/m1=2-174. DR PDB; 4U55; X-ray; 3.20 A; M1/m1=2-174. DR PDB; 4U56; X-ray; 3.45 A; M1/m1=2-174. DR PDB; 4U6F; X-ray; 3.10 A; M1/m1=2-174. DR PDB; 4V8T; EM; 8.10 A; J=1-174. DR PDB; 5DAT; X-ray; 3.15 A; M1/m1=2-174. DR PDB; 5DC3; X-ray; 3.25 A; M1/m1=2-174. DR PDB; 5DGF; X-ray; 3.30 A; M1/m1=2-174. DR PDB; 5DGV; X-ray; 3.10 A; M1/m1=2-174. DR PDB; 5I4L; X-ray; 3.10 A; M1/m1=6-174. DR PDB; 5LYB; X-ray; 3.25 A; M1/m1=6-174. DR PDB; 5MEI; X-ray; 3.50 A; CM/s=6-174. DR PDB; 5NDV; X-ray; 3.30 A; M1/m1=6-174. DR PDB; 5NDW; X-ray; 3.70 A; M1/m1=6-174. DR PDB; 5OBM; X-ray; 3.40 A; M1/m1=6-174. DR PDB; 5ON6; X-ray; 3.10 A; CM/s=6-174. DR PDB; 5TBW; X-ray; 3.00 A; CM/s=6-174. DR PDB; 5TGA; X-ray; 3.30 A; M1/m1=6-174. DR PDB; 5TGM; X-ray; 3.50 A; M1/m1=6-174. DR PDB; 6GQ1; EM; 4.40 A; J=6-174. DR PDB; 6GQB; EM; 3.90 A; J=6-174. DR PDB; 6GQV; EM; 4.00 A; J=6-174. DR PDB; 6HHQ; X-ray; 3.10 A; CM/s=1-174. DR PDB; 6I7O; EM; 5.30 A; AG/XG=6-174. DR PDB; 6Q8Y; EM; 3.10 A; AG=6-174. DR PDBsum; 2NOQ; -. DR PDBsum; 3J0Q; -. 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; 4V8T; -. DR PDBsum; 5DAT; -. DR PDBsum; 5DC3; -. DR PDBsum; 5DGF; -. DR PDBsum; 5DGV; -. DR PDBsum; 5I4L; -. DR PDBsum; 5LYB; -. DR PDBsum; 5MEI; -. DR PDBsum; 5NDV; -. DR PDBsum; 5NDW; -. DR PDBsum; 5OBM; -. DR PDBsum; 5ON6; -. DR PDBsum; 5TBW; -. DR PDBsum; 5TGA; -. DR PDBsum; 5TGM; -. DR PDBsum; 6GQ1; -. DR PDBsum; 6GQB; -. DR PDBsum; 6GQV; -. DR PDBsum; 6HHQ; -. DR PDBsum; 6I7O; -. DR PDBsum; 6Q8Y; -. DR SMR; Q3E757; -. DR BioGrid; 33327; 300. DR DIP; DIP-29386N; -. DR IntAct; Q3E757; 20. DR MINT; Q3E757; -. DR STRING; 4932.YGR085C; -. DR iPTMnet; Q3E757; -. DR MaxQB; Q3E757; -. DR PaxDb; Q3E757; -. DR PRIDE; Q3E757; -. DR EnsemblFungi; YGR085C_mRNA; YGR085C_mRNA; YGR085C. DR GeneID; 852976; -. DR KEGG; sce:YGR085C; -. DR EuPathDB; FungiDB:YGR085C; -. DR SGD; S000003317; RPL11B. DR GeneTree; ENSGT00910000144211; -. DR HOGENOM; HOG000231312; -. DR InParanoid; Q3E757; -. DR KO; K02868; -. DR OMA; AMCWFQQ; -. DR BioCyc; YEAST:G3O-30797-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 EvolutionaryTrace; Q3E757; -. DR PRO; PR:Q3E757; -. DR Proteomes; UP000002311; Chromosome VII. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 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; Complete proteome; Cytoplasm; Methylation; KW Nucleus; Reference proteome; Ribonucleoprotein; Ribosomal protein; KW RNA-binding; rRNA-binding. FT INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378, FT ECO:0000269|PubMed:10601260}. FT CHAIN 2 174 60S ribosomal protein L11-B. FT /FTId=PRO_0000125105. FT MOD_RES 2 2 N-acetylserine. FT {ECO:0000244|PubMed:22814378, FT ECO:0000269|PubMed:10601260}. FT MOD_RES 75 75 N6,N6,N6-trimethyllysine. FT {ECO:0000269|PubMed:22522802}. FT CONFLICT 138 138 V -> A (in Ref. 1). {ECO:0000305}. FT STRAND 14 21 {ECO:0000244|PDB:4U4R}. FT STRAND 25 27 {ECO:0000244|PDB:4U4U}. FT HELIX 28 41 {ECO:0000244|PDB:4U4R}. FT STRAND 46 48 {ECO:0000244|PDB:4U4R}. FT STRAND 55 57 {ECO:0000244|PDB:4U4R}. FT STRAND 66 71 {ECO:0000244|PDB:4U4R}. FT HELIX 74 86 {ECO:0000244|PDB:4U4R}. FT TURN 87 89 {ECO:0000244|PDB:4U4R}. FT STRAND 90 92 {ECO:0000244|PDB:4U4R}. FT STRAND 93 96 {ECO:0000244|PDB:4U4R}. FT STRAND 102 107 {ECO:0000244|PDB:4U4R}. FT HELIX 109 111 {ECO:0000244|PDB:4U4R}. FT TURN 118 120 {ECO:0000244|PDB:4U4R}. FT STRAND 125 131 {ECO:0000244|PDB:4U4R}. FT TURN 134 136 {ECO:0000244|PDB:4U4R}. FT HELIX 137 140 {ECO:0000244|PDB:4U4R}. FT STRAND 141 144 {ECO:0000244|PDB:4U4Q}. FT HELIX 150 152 {ECO:0000244|PDB:4U4R}. FT HELIX 156 164 {ECO:0000244|PDB:4U4R}. FT TURN 165 167 {ECO:0000244|PDB:4U4R}. FT STRAND 170 172 {ECO:0000244|PDB:4U4R}. SQ SEQUENCE 174 AA; 19750 MW; 04F6CD88FEBD63E4 CRC64; MSTKAQNPMR DLKIEKLVLN ISVGESGDRL TRASKVLEQL SGQTPVQSKA RYTVRTFGIR RNEKIAVHVT VRGPKAEEIL ERGLKVKEYQ LRDRNFSATG NFGFGIDEHI DLGIKYDPSI GIFGMDFYVV MNRPGARVTR RKRCKGTVGN SHKTTKEDTV SWFKQKYDAD VLDK //