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 16-NOV-2011, entry version 64. DE RecName: Full=60S ribosomal protein L11-B; DE AltName: Full=L16; DE AltName: Full=RP39; DE AltName: Full=YL22; GN Name=RPL11B; Synonyms=RP39B, RPL16B; 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 MEDLINE=85062814; 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 96604 / S288c / FY1679; RX MEDLINE=97313265; 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; RG Saccharomyces Genome Database; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11. RX MEDLINE=87064353; PubMed=3023862; 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 MEDLINE=20069684; 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 MEDLINE=22923954; 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 MEDLINE=22923965; 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31; THR-53 AND THR-56, RP AND MASS SPECTROMETRY. 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 RT spectrometry."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). RN [10] 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: Binds to 5S ribosomal RNA. CC -!- SUBUNIT: Component of the large ribosomal subunit. Mature CC ribosomes consist of a small (40S) and a large (60S) subunit. The CC 40S subunit contains 32 different proteins (encoded by 56 genes) CC and 1 molecule of RNA (18S). The 60S subunit contains 46 different CC proteins (encoded by 81 genes) and 3 molecules of RNA (25S, 5.8S CC and 5S). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- PTM: N-terminally acetylated by acetyltransferase NatA. CC -!- MISCELLANEOUS: Present with 21200 molecules/cell in log phase SD CC medium. CC -!- MISCELLANEOUS: There are 2 genes for L11 in yeast. CC -!- SIMILARITY: Belongs to the ribosomal protein L5P family. 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 PDBsum; 2NOQ; -. DR ProteinModelPortal; Q3E757; -. DR SMR; Q3E757; 7-171. DR DIP; DIP-29386N; -. DR IntAct; Q3E757; 15. DR MINT; MINT-564941; -. DR STRING; Q3E757; -. DR EnsemblFungi; YGR085C; YGR085C; YGR085C. DR GeneID; 852976; -. DR KEGG; sce:YGR085C; -. DR NMPDR; fig|4932.3.peg.2716; -. DR SGD; S000003317; RPL11B. DR eggNOG; fuNOG04041; -. DR GeneTree; EFGT00050000005601; -. DR HOGENOM; HBG592167; -. DR OMA; KPKTKKN; -. DR OrthoDB; EOG4M0JB6; -. DR PhylomeDB; Q3E757; -. DR NextBio; 972774; -. DR ArrayExpress; Q3E757; -. DR Genevestigator; Q3E757; -. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; TAS:SGD. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; TAS:SGD. DR GO; GO:0002181; P:cytoplasmic translation; TAS:SGD. DR GO; GO:0000027; P:ribosomal large subunit assembly; IMP:SGD. DR InterPro; IPR002132; Ribosomal_L5. DR InterPro; IPR020929; Ribosomal_L5_CS. DR InterPro; IPR022803; Ribosomal_L5_domain. DR Gene3D; G3DSA:3.30.1440.10; Ribosomal_L5; 1. DR KO; K02868; -. DR PANTHER; PTHR11994; Ribosomal_L5; 1. DR Pfam; PF00281; Ribosomal_L5; 1. DR Pfam; PF00673; Ribosomal_L5_C; 1. DR PIRSF; PIRSF002161; Ribosomal_L5; 1. DR SUPFAM; SSF55282; Ribosomal_L5; 1. DR PROSITE; PS00358; RIBOSOMAL_L5; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Complete proteome; Cytoplasm; KW Phosphoprotein; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT INIT_MET 1 1 Removed. FT CHAIN 2 174 60S ribosomal protein L11-B. FT /FTId=PRO_0000125105. FT MOD_RES 2 2 N-acetylserine. FT MOD_RES 31 31 Phosphothreonine. FT MOD_RES 53 53 Phosphothreonine. FT MOD_RES 56 56 Phosphothreonine. FT CONFLICT 138 138 V -> A (in Ref. 1). 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 //