RS21B_YEAST
ID RS21B_YEAST Reviewed; 87 AA.
AC Q3E754; D6VW49; P05760;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=40S ribosomal protein S21-B {ECO:0000303|PubMed:9559554};
DE AltName: Full=S26;
DE AltName: Full=Small ribosomal subunit protein eS21-B {ECO:0000303|PubMed:24524803};
DE AltName: Full=YS25;
GN Name=RPS21B {ECO:0000303|PubMed:9559554}; Synonyms=RPS25B, RPS26B;
GN OrderedLocusNames=YJL136C; ORFNames=J0664;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8813765;
RX DOI=10.1002/(sici)1097-0061(19960630)12:8<787::aid-yea954>3.0.co;2-4;
RA Katsoulou C., Tzermia M., Tavernarakis N., Alexandraki D.;
RT "Sequence analysis of a 40.7 kb segment from the left arm of yeast
RT chromosome X reveals 14 known genes and 13 new open reading frames
RT including homologues of genes clustered on the right arm of chromosome
RT XI.";
RL Yeast 12:787-797(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
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 [5]
RP ACETYLATION AT MET-1 BY NATB.
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 proteins.";
RL J. Biol. Chem. 274:37035-37040(1999).
RN [6]
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 [7]
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=14627813; DOI=10.1093/nar/gkg899;
RA Tabb-Massey A., Caffrey J.M., Logsden P., Taylor S., Trent J.O.,
RA Ellis S.R.;
RT "Ribosomal proteins Rps0 and Rps21 of Saccharomyces cerevisiae have
RT overlapping functions in the maturation of the 3' end of 18S rRNA.";
RL Nucleic Acids Res. 31:6798-6805(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., Yusupova G.,
RA Yusupov M.;
RT "The structure of the eukaryotic ribosome at 3.0 A resolution.";
RL Science 334:1524-1529(2011).
RN [10]
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 (PubMed:22096102). eS21 is required for the processing of the
CC 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation
CC of 40S ribosomal subunits. Has a physiological role leading to 18S rRNA
CC stability (PubMed:14627813). {ECO:0000269|PubMed:14627813,
CC ECO:0000305|PubMed:22096102}.
CC -!- SUBUNIT: Component of the small ribosomal subunit (SSU). 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:14627813, ECO:0000269|PubMed:22096102}.
CC -!- PTM: N-terminally acetylated by acetyltransferase NatB.
CC {ECO:0000269|PubMed:10601260}.
CC -!- DISRUPTION PHENOTYPE: Reduction in growth rate, a decrease in free 40S
CC subunits, an increase in the amount of free 60S subunits and a decrease
CC in polysome size. {ECO:0000269|PubMed:14627813}.
CC -!- MISCELLANEOUS: Present with 15300 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for eS21 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS21 family.
CC {ECO:0000305}.
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DR EMBL; X87371; CAA60819.1; -; Genomic_DNA.
DR EMBL; Z49411; CAA89431.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08665.1; -; Genomic_DNA.
DR PIR; S56918; S56918.
DR RefSeq; NP_012399.1; NM_001181569.1.
DR AlphaFoldDB; Q3E754; -.
DR SMR; Q3E754; -.
DR BioGRID; 33621; 376.
DR IntAct; Q3E754; 3.
DR MINT; Q3E754; -.
DR STRING; 4932.YJL136C; -.
DR iPTMnet; Q3E754; -.
DR MaxQB; Q3E754; -.
DR PaxDb; Q3E754; -.
DR PRIDE; Q3E754; -.
DR TopDownProteomics; Q3E754; -.
DR EnsemblFungi; YJL136C_mRNA; YJL136C; YJL136C.
DR GeneID; 853305; -.
DR KEGG; sce:YJL136C; -.
DR SGD; S000003672; RPS21B.
DR VEuPathDB; FungiDB:YJL136C; -.
DR eggNOG; KOG3486; Eukaryota.
DR GeneTree; ENSGT00390000017515; -.
DR HOGENOM; CLU_167122_2_0_1; -.
DR InParanoid; Q3E754; -.
DR OMA; ALCGYIR; -.
DR BioCyc; YEAST:G3O-31583-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-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-SCE-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-SCE-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition.
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:Q3E754; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; Q3E754; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000461; P:endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR Gene3D; 3.30.1230.20; -; 1.
DR InterPro; IPR001931; Ribosomal_S21e.
DR InterPro; IPR018279; Ribosomal_S21e_CS.
DR InterPro; IPR038579; Ribosomal_S21e_sf.
DR PANTHER; PTHR10442; PTHR10442; 1.
DR Pfam; PF01249; Ribosomal_S21e; 1.
DR PIRSF; PIRSF002148; Ribosomal_S21e; 1.
DR PROSITE; PS00996; RIBOSOMAL_S21E; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; rRNA processing.
FT CHAIN 1..87
FT /note="40S ribosomal protein S21-B"
FT /id="PRO_0000194762"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:10601260"
SQ SEQUENCE 87 AA; 9760 MW; 52E1C247575A7410 CRC64;
MENDKGQLVE LYVPRKCSAT NRIIKADDHA SVQINVAKVD EEGRAIPGEY ITYALSGYVR
SRGESDDSLN RLAQNDGLLK NVWSYSR
