RL23B_YEAST
ID RL23B_YEAST Reviewed; 137 AA.
AC P0CX42; D3DM23; P04451;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=60S ribosomal protein L23-B {ECO:0000303|PubMed:9559554};
DE AltName: Full=L17a;
DE AltName: Full=Large ribosomal subunit protein uL14-B {ECO:0000303|PubMed:24524803};
DE AltName: Full=YL32;
GN Name=RPL23B {ECO:0000303|PubMed:9559554}; Synonyms=RPL17AB, RPL17B;
GN OrderedLocusNames=YER117W;
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=7668045; DOI=10.1002/yea.320110807;
RA Berroteran R.W., Hampsey M.;
RT "Sequence, map position and genome organization of the RPL17B gene,
RT encoding ribosomal protein L17b in Saccharomyces cerevisiae.";
RL Yeast 11:761-766(1995).
RN [2]
RP ERRATUM OF PUBMED:7668045.
RA Berroteran R.W., Hampsey M.;
RL Yeast 12:91-91(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (RPL23A).
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7502586; DOI=10.1002/yea.320111112;
RA Obermaier B., Gassenhuber J., Piravandi E., Domdey H.;
RT "Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces
RT cerevisiae chromosome II.";
RL Yeast 11:1103-1112(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 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 [7]
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 [8]
RP ACETYLATION AT SER-2, AND METHYLATION.
RX PubMed=16096273; DOI=10.1074/jbc.m507672200;
RA Porras-Yakushi T.R., Whitelegge J.P., Miranda T.B., Clarke S.;
RT "A novel SET domain methyltransferase modifies ribosomal protein Rpl23ab in
RT yeast.";
RL J. Biol. Chem. 280:34590-34598(2005).
RN [9]
RP METHYLATION AT LYS-106 AND LYS-110.
RX PubMed=17327221; DOI=10.1074/jbc.m611896200;
RA Porras-Yakushi T.R., Whitelegge J.P., Clarke S.;
RT "Yeast ribosomal/cytochrome c SET domain methyltransferase subfamily:
RT identification of Rpl23ab methylation sites and recognition motifs.";
RL J. Biol. Chem. 282:12368-12376(2007).
RN [10]
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., Yusupova G.,
RA Yusupov M.;
RT "The structure of the eukaryotic ribosome at 3.0 A resolution.";
RL Science 334:1524-1529(2011).
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 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).
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).
CC {ECO:0000269|PubMed:22096102, ECO:0000305|PubMed:9559554}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}.
CC -!- PTM: Methylated by RKM1 at 2 different sites, but it is unclear which
CC are the 2 methylated residues among Lys-40, Lys-106 and/or Lys-110.
CC {ECO:0000269|PubMed:16096273}.
CC -!- MASS SPECTROMETRY: Mass=14430.702; Method=Electrospray;
CC Note=Monoisotopic mass with either 7 methylation modifications or 1
CC acetylation and 4 methylation modifications.;
CC Evidence={ECO:0000269|PubMed:11983894};
CC -!- MISCELLANEOUS: There are 2 genes for uL14 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL14 family.
CC {ECO:0000305}.
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DR EMBL; U15653; AAA61906.1; -; Genomic_DNA.
DR EMBL; U18916; AAC03215.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07777.1; -; Genomic_DNA.
DR PIR; A02792; R5BY17.
DR RefSeq; NP_009466.1; NM_001178327.1.
DR RefSeq; NP_011042.3; NM_001179007.3.
DR AlphaFoldDB; P0CX42; -.
DR SMR; P0CX42; -.
DR BioGRID; 32617; 260.
DR BioGRID; 36862; 164.
DR IntAct; P0CX42; 2.
DR MINT; P0CX42; -.
DR iPTMnet; P0CX42; -.
DR PRIDE; P0CX42; -.
DR EnsemblFungi; YBL087C_mRNA; YBL087C; YBL087C.
DR EnsemblFungi; YER117W_mRNA; YER117W; YER117W.
DR GeneID; 852191; -.
DR GeneID; 856853; -.
DR KEGG; sce:YBL087C; -.
DR KEGG; sce:YER117W; -.
DR SGD; S000000919; RPL23B.
DR VEuPathDB; FungiDB:YBL087C; -.
DR VEuPathDB; FungiDB:YER117W; -.
DR GeneTree; ENSGT00390000004690; -.
DR HOGENOM; CLU_095071_3_0_1; -.
DR InParanoid; P0CX42; -.
DR BioCyc; YEAST:G3O-30281-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 PRO; PR:P0CX42; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P0CX42; protein.
DR ExpressionAtlas; P0CX42; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0070180; F:large ribosomal subunit rRNA 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 Gene3D; 2.40.150.20; -; 1.
DR HAMAP; MF_01367; Ribosomal_L14; 1.
DR InterPro; IPR036853; Ribosomal_L14_sf.
DR InterPro; IPR000218; Ribosomal_L14P.
DR InterPro; IPR019972; Ribosomal_L14P_CS.
DR PANTHER; PTHR11761; PTHR11761; 1.
DR Pfam; PF00238; Ribosomal_L14; 1.
DR SMART; SM01374; Ribosomal_L14; 1.
DR SUPFAM; SSF50193; SSF50193; 1.
DR PROSITE; PS00049; RIBOSOMAL_L14; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Methylation; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16096273,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..137
FT /note="60S ribosomal protein L23-B"
FT /id="PRO_0000409767"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:16096273,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 106
FT /note="N6,N6-dimethyllysine; by RKM1"
FT /evidence="ECO:0000269|PubMed:17327221"
FT MOD_RES 110
FT /note="N6,N6-dimethyllysine; by RKM1"
FT /evidence="ECO:0000269|PubMed:17327221"
SQ SEQUENCE 137 AA; 14473 MW; DEB983B3CB1DFAB1 CRC64;
MSGNGAQGTK FRISLGLPVG AIMNCADNSG ARNLYIIAVK GSGSRLNRLP AASLGDMVMA
TVKKGKPELR KKVMPAIVVR QAKSWRRRDG VFLYFEDNAG VIANPKGEMK GSAITGPVGK
ECADLWPRVA SNSGVVV
