ID   RL24B_YEAST             Reviewed;         155 AA.
AC   P24000; A2TBN3; D6VUS9;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   27-MAR-2024, entry version 192.
DE   RecName: Full=Large ribosomal subunit protein eL24B {ECO:0000303|PubMed:24524803};
DE   AltName: Full=60S ribosomal protein L24-B {ECO:0000303|PubMed:9559554};
DE   AltName: Full=L30;
DE   AltName: Full=RP29;
DE   AltName: Full=YL21;
GN   Name=RPL24B {ECO:0000303|PubMed:9559554}; Synonyms=RPL30B;
GN   OrderedLocusNames=YGR148C; ORFNames=G6635;
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=2204809; DOI=10.1128/mcb.10.10.5235-5243.1990;
RA   Baronas-Lowell D.M., Warner J.R.;
RT   "Ribosomal protein L30 is dispensable in the yeast Saccharomyces
RT   cerevisiae.";
RL   Mol. Cell. Biol. 10:5235-5243(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8585325; DOI=10.1002/yea.320111410;
RA   Skala J., Nawrocki A., Goffeau A.;
RT   "The sequence of a 27 kb segment on the right arm of chromosome VII from
RT   Saccharomyces cerevisiae reveals MOL1, NAT2, RPL30B, RSR1, CYS4, PEM1/CHO2,
RT   NSR1 genes and ten new open reading frames.";
RL   Yeast 11:1421-1427(1995).
RN   [3]
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., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [4]
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   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-86.
RC   STRAIN=ATCC 201390 / BY4743;
RX   PubMed=17244705; DOI=10.1073/pnas.0610354104;
RA   Juneau K., Palm C., Miranda M., Davis R.W.;
RT   "High-density yeast-tiling array reveals previously undiscovered introns
RT   and extensive regulation of meiotic splicing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1522-1527(2007).
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   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   [10]
RP   IDENTIFICATION BY 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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [12]
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   [13]
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   [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).
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:14562095,
CC       ECO:0000269|PubMed:22096102}.
CC   -!- MISCELLANEOUS: Present with 36900 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- MISCELLANEOUS: There are 2 genes for eL24 in yeast. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL24 family.
CC       {ECO:0000305}.
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DR   EMBL; M34387; AAA34736.1; -; Genomic_DNA.
DR   EMBL; X85807; CAA59806.1; -; Genomic_DNA.
DR   EMBL; Z72933; CAA97162.1; -; Genomic_DNA.
DR   EMBL; AY557819; AAS56145.1; -; Genomic_DNA.
DR   EMBL; EF123136; ABM97480.1; -; mRNA.
DR   EMBL; BK006941; DAA08240.1; -; Genomic_DNA.
DR   PIR; A35925; R6BYY0.
DR   RefSeq; NP_011664.3; NM_001181277.3.
DR   PDB; 6T7I; EM; 3.20 A; LW=1-155.
DR   PDBsum; 6T7I; -.
DR   AlphaFoldDB; P24000; -.
DR   EMDB; EMD-10396; -.
DR   SMR; P24000; -.
DR   BioGRID; 33396; 222.
DR   DIP; DIP-4722N; -.
DR   IntAct; P24000; 7.
DR   MINT; P24000; -.
DR   STRING; 4932.YGR148C; -.
DR   iPTMnet; P24000; -.
DR   MaxQB; P24000; -.
DR   PaxDb; 4932-YGR148C; -.
DR   PeptideAtlas; P24000; -.
DR   EnsemblFungi; YGR148C_mRNA; YGR148C; YGR148C.
DR   GeneID; 853051; -.
DR   KEGG; sce:YGR148C; -.
DR   AGR; SGD:S000003380; -.
DR   SGD; S000003380; RPL24B.
DR   VEuPathDB; FungiDB:YGR148C; -.
DR   eggNOG; KOG1722; Eukaryota.
DR   GeneTree; ENSGT00950000183105; -.
DR   HOGENOM; CLU_106411_0_0_1; -.
DR   InParanoid; P24000; -.
DR   OMA; TILYRRQ; -.
DR   OrthoDB; 178748at2759; -.
DR   BioCyc; YEAST:G3O-30851-MONOMER; -.
DR   BioGRID-ORCS; 853051; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P24000; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P24000; Protein.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IDA:SGD.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR   CDD; cd00472; Ribosomal_L24e_L24; 1.
DR   Gene3D; 6.10.250.1270; -; 1.
DR   Gene3D; 2.30.170.20; Ribosomal protein L24e; 1.
DR   InterPro; IPR038630; L24e/L24_sf.
DR   InterPro; IPR000988; Ribosomal_eL24-rel.
DR   InterPro; IPR023442; Ribosomal_eL24_CS.
DR   PANTHER; PTHR10792; 60S RIBOSOMAL PROTEIN L24; 1.
DR   PANTHER; PTHR10792:SF1; TRASH DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01246; Ribosomal_L24e; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   PROSITE; PS01073; RIBOSOMAL_L24E; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Phosphoprotein; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein.
FT   CHAIN           1..155
FT                   /note="Large ribosomal subunit protein eL24B"
FT                   /id="PRO_0000136895"
FT   REGION          66..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..127
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..155
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         7
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
SQ   SEQUENCE   155 AA;  17548 MW;  7EE89CE40D7A657F CRC64;
     MKVEVDSFSG AKIYPGRGTL FVRGDSKIFR FQNSKSASLF KQRKNPRRIA WTVLFRKHHK
     KGITEEVAKK RSRKTVKAQR PITGASLDLI KERRSLKPEV RKANREEKLK ANKEKKRAEK
     AARKAEKAKS AGVQGSKVSK QQAKGAFQKV AATSR
//