ID   RSSA2_YEAST             Reviewed;         252 AA.
AC   P46654; D6VY50;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 190.
DE   RecName: Full=Small ribosomal subunit protein uS2B {ECO:0000303|PubMed:24524803};
DE   AltName: Full=40S ribosomal protein S0-B {ECO:0000255|HAMAP-Rule:MF_03015, ECO:0000303|PubMed:9559554};
DE   AltName: Full=Nucleic acid-binding protein NAB1B;
GN   Name=RPS0B {ECO:0000255|HAMAP-Rule:MF_03015,
GN   ECO:0000303|PubMed:9559554}; Synonyms=NAB1B, NAB4, YST2;
GN   OrderedLocusNames=YLR048W; ORFNames=L2118;
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=8626693; DOI=10.1074/jbc.271.19.11383;
RA   Demianova M.A., Formosa T.G., Ellis S.R.;
RT   "Yeast proteins related to the p40/laminin receptor precursor are essential
RT   components of the 40 S ribosomal subunit.";
RL   J. Biol. Chem. 271:11383-11391(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
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   PROTEIN SEQUENCE OF 2-27; 63-79 AND 89-134, CLEAVAGE OF INITIATOR
RP   METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA   Bienvenut W.V., Peters C.;
RL   Submitted (MAY-2005) to UniProtKB.
RN   [5]
RP   PROTEIN SEQUENCE OF 53-56; 102-111 AND 135-146.
RC   STRAIN=ATCC 44827 / SKQ2N;
RX   PubMed=9038161; DOI=10.1074/jbc.272.9.5544;
RA   Norbeck J., Blomberg A.;
RT   "Metabolic and regulatory changes associated with growth of Saccharomyces
RT   cerevisiae in 1.4 M NaCl. Evidence for osmotic induction of glycerol
RT   dissimilation via the dihydroxyacetone pathway.";
RL   J. Biol. Chem. 272:5544-5554(1997).
RN   [6]
RP   GENE EVOLUTION.
RX   PubMed=9718729; DOI=10.1093/oxfordjournals.molbev.a026000;
RA   Ardini E., Pesole G., Tagliabue E., Magnifico A., Castronovo V.,
RA   Sobel M.E., Colnaghi M.I., Menard S.;
RT   "The 67-kDa laminin receptor originated from a ribosomal protein that
RT   acquired a dual function during evolution.";
RL   Mol. Biol. Evol. 15:1017-1025(1998).
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   FUNCTION, AND SUBUNIT.
RX   PubMed=9973221;
RA   Ford C.L., Randal-Whitis L., Ellis S.R.;
RT   "Yeast proteins related to the p40/laminin receptor precursor are required
RT   for 20S ribosomal RNA processing and the maturation of 40S ribosomal
RT   subunits.";
RL   Cancer Res. 59:704-710(1999).
RN   [9]
RP   CLEAVAGE OF INITIATOR METHIONINE, AND ACETYLATION AT SER-2 BY NATA.
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   [10]
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   [11]
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   [12]
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   [13]
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   [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 (PubMed:22096102). uS2 is required for the assembly and/or
CC       stability of the 40S ribosomal subunit. Required for the processing of
CC       the 20S rRNA-precursor to mature 18S rRNA in a late step of the
CC       maturation of 40S ribosomal subunits (PubMed:9973221, PubMed:14627813).
CC       {ECO:0000269|PubMed:14627813, ECO:0000269|PubMed:9973221,
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:0000255|HAMAP-Rule:MF_03015,
CC       ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14627813,
CC       ECO:0000269|PubMed:22096102}.
CC   -!- PTM: N-terminally acetylated by acetyltransferase NatA.
CC       {ECO:0000269|PubMed:10601260, ECO:0000269|Ref.4}.
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 60900 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- MISCELLANEOUS: There are 2 genes for uS2 in yeast. {ECO:0000305}.
CC   -!- MISCELLANEOUS: This protein appears to have acquired a second function
CC       as a laminin receptor specifically in the vertebrate lineage. This
CC       protein does not bind laminin. {ECO:0000305|PubMed:9718729}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_03015}.
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DR   EMBL; U33756; AAC49276.1; -; Genomic_DNA.
DR   EMBL; X94607; CAA64295.1; -; Genomic_DNA.
DR   EMBL; Z73220; CAA97578.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09366.1; -; Genomic_DNA.
DR   PIR; S59364; S59364.
DR   RefSeq; NP_013149.1; NM_001181935.1.
DR   PDB; 6WOO; EM; 2.90 A; AA=2-207.
DR   PDBsum; 6WOO; -.
DR   AlphaFoldDB; P46654; -.
DR   EMDB; EMD-21859; -.
DR   SMR; P46654; -.
DR   BioGRID; 31323; 432.
DR   IntAct; P46654; 91.
DR   MINT; P46654; -.
DR   STRING; 4932.YLR048W; -.
DR   iPTMnet; P46654; -.
DR   MaxQB; P46654; -.
DR   PaxDb; 4932-YLR048W; -.
DR   PeptideAtlas; P46654; -.
DR   EnsemblFungi; YLR048W_mRNA; YLR048W; YLR048W.
DR   GeneID; 850737; -.
DR   KEGG; sce:YLR048W; -.
DR   AGR; SGD:S000004038; -.
DR   SGD; S000004038; RPS0B.
DR   VEuPathDB; FungiDB:YLR048W; -.
DR   eggNOG; KOG0830; Eukaryota.
DR   GeneTree; ENSGT00950000183099; -.
DR   HOGENOM; CLU_058171_2_0_1; -.
DR   InParanoid; P46654; -.
DR   OMA; QQKTKDM; -.
DR   OrthoDB; 5480124at2759; -.
DR   BioCyc; YEAST:G3O-32204-MONOMER; -.
DR   BioGRID-ORCS; 850737; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P46654; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P46654; 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; IMP: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   GO; GO:0000028; P:ribosomal small subunit assembly; IMP:SGD.
DR   GO; GO:0006407; P:rRNA export from nucleus; IGI:SGD.
DR   CDD; cd01425; RPS2; 1.
DR   HAMAP; MF_03015; Ribosomal_S2_euk; 1.
DR   InterPro; IPR001865; Ribosomal_uS2.
DR   InterPro; IPR018130; Ribosomal_uS2_CS.
DR   InterPro; IPR027498; Ribosomal_uS2_euk.
DR   InterPro; IPR005707; Ribosomal_uS2_euk/arc.
DR   InterPro; IPR023591; Ribosomal_uS2_flav_dom_sf.
DR   NCBIfam; TIGR01012; uS2_euk_arch; 1.
DR   PANTHER; PTHR11489; 40S RIBOSOMAL PROTEIN SA; 1.
DR   PANTHER; PTHR11489:SF9; 40S RIBOSOMAL PROTEIN SA; 1.
DR   Pfam; PF00318; Ribosomal_S2; 2.
DR   PRINTS; PR00395; RIBOSOMALS2.
DR   SUPFAM; SSF52313; Ribosomal protein S2; 1.
DR   PROSITE; PS00962; RIBOSOMAL_S2_1; 1.
DR   PROSITE; PS00963; RIBOSOMAL_S2_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   Ribosome biogenesis; rRNA processing.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03015,
FT                   ECO:0000269|PubMed:10601260, ECO:0000269|Ref.4"
FT   CHAIN           2..252
FT                   /note="Small ribosomal subunit protein uS2B"
FT                   /id="PRO_0000134371"
FT   REGION          213..252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        214..232
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03015,
FT                   ECO:0000269|PubMed:10601260, ECO:0000269|Ref.4"
SQ   SEQUENCE   252 AA;  27962 MW;  B9B7CDFB335EFAC3 CRC64;
     MSLPATFDLT PEDAQLLLAA NTHLGARNVQ VHQEPYVFNA RPDGVHVINV GKTWEKLVLA
     ARIIAAIPNP EDVVAISSRT YGQRAVLKFA AHTGATPIAG RFTPGSFTNY ITRSFKEPRL
     VIVTDPRLDA QAIKEASYVN IPVIALTDLD SPSEFVDVAI PCNNRGKHSI GLIWYLLARE
     VLRLRGALVD RTQPWSIMPD LYFYRNPEEV EQVAEEAAAA EEGEEEEVKE EVTEGQAEAT
     EWAEENADNV EW
//