RL21B_YEAST
ID RL21B_YEAST Reviewed; 160 AA.
AC Q12672; D6W3T7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=60S ribosomal protein L21-B {ECO:0000303|PubMed:9559554};
DE AltName: Full=Large ribosomal subunit protein eL21-B {ECO:0000303|PubMed:24524803};
GN Name=RPL21B {ECO:0000303|PubMed:9559554}; OrderedLocusNames=YPL079W;
GN ORFNames=LPF6W;
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 [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 [2]
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 [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-32, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [8]
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 66400 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106, ECO:0000269|PubMed:22096102}.
CC -!- MISCELLANEOUS: There are 2 genes for eL21 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL21 family.
CC {ECO:0000305}.
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DR EMBL; U41849; AAB68259.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11353.1; -; Genomic_DNA.
DR PIR; S61108; S61108.
DR RefSeq; NP_015246.1; NM_001183893.1.
DR AlphaFoldDB; Q12672; -.
DR SMR; Q12672; -.
DR BioGRID; 36101; 336.
DR IntAct; Q12672; 2.
DR STRING; 4932.YPL079W; -.
DR iPTMnet; Q12672; -.
DR MaxQB; Q12672; -.
DR PaxDb; Q12672; -.
DR PRIDE; Q12672; -.
DR EnsemblFungi; YPL079W_mRNA; YPL079W; YPL079W.
DR GeneID; 856026; -.
DR KEGG; sce:YPL079W; -.
DR SGD; S000006000; RPL21B.
DR VEuPathDB; FungiDB:YPL079W; -.
DR eggNOG; KOG1732; Eukaryota.
DR GeneTree; ENSGT00950000182922; -.
DR HOGENOM; CLU_103610_0_1_1; -.
DR InParanoid; Q12672; -.
DR OMA; VAYDTHI; -.
DR BioCyc; YEAST:G3O-33986-MON; -.
DR PRO; PR:Q12672; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12672; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
DR Gene3D; 2.30.30.70; -; 1.
DR InterPro; IPR036948; Ribosomal_L21_sf.
DR InterPro; IPR001147; Ribosomal_L21e.
DR InterPro; IPR018259; Ribosomal_L21e_CS.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR20981; PTHR20981; 1.
DR Pfam; PF01157; Ribosomal_L21e; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR PROSITE; PS01171; RIBOSOMAL_L21E; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Isopeptide bond; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Ubl conjugation.
FT CHAIN 1..160
FT /note="60S ribosomal protein L21-B"
FT /id="PRO_0000149683"
FT CROSSLNK 32
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 160 AA; 18274 MW; 733AF5208D555F7E CRC64;
MGKSHGYRSR TRYMFQRDFR KHGAVHMSTY LKIYKVGDIV DIKANGSIQK GMPHKFYQGK
TGVVYNVTKS SVGVIINKMV GNRYLEKRLN LRVEHIKHSK CRQEFLERVK ANAAKRAEAK
AQGVAVQLKR QPAQPRESRI VSTEGNVPQT LAPVPYETFI
