ID   RS9B_YEAST              Reviewed;         195 AA.
AC   P05755; D6VQI4;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   27-MAR-2024, entry version 208.
DE   RecName: Full=Small ribosomal subunit protein uS4B {ECO:0000303|PubMed:24524803};
DE   AltName: Full=40S ribosomal protein S9-B {ECO:0000303|PubMed:9559554};
DE   AltName: Full=RP21;
DE   AltName: Full=S13;
DE   AltName: Full=YP28;
DE   AltName: Full=YS11;
GN   Name=RPS9B {ECO:0000303|PubMed:9559554}; Synonyms=RPS13B, SUP46;
GN   OrderedLocusNames=YBR189W; ORFNames=YBR1317;
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=1427034; DOI=10.1093/genetics/132.2.375;
RA   Vincent A., Liebman S.W.;
RT   "The yeast omnipotent suppressor SUP46 encodes a ribosomal protein which is
RT   a functional and structural homolog of the Escherichia coli S4 ram
RT   protein.";
RL   Genetics 132:375-386(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7871891; DOI=10.1002/yea.320101116;
RA   Demolis N., Jacquet M., Mallet L.;
RT   "A 12.5 kb fragment of the yeast chromosome II contains two adjacent genes
RT   encoding ribosomal proteins and six putative new genes, one of which
RT   encodes a putative transcriptional factor.";
RL   Yeast 10:1511-1525(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
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   PROTEIN SEQUENCE OF 2-24.
RX   PubMed=6814480; DOI=10.1021/bi00262a005;
RA   Otaka E., Higo K., Osawa S.;
RT   "Isolation of seventeen proteins and amino-terminal amino acid sequences of
RT   eight proteins from cytoplasmic ribosomes of yeast.";
RL   Biochemistry 21:4545-4550(1982).
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   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   [8]
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   [9]
RP   FUNCTION, INTERACTION WITH MPP10 AND SNORNA U3, IDENTIFICATION IN SSU
RP   PROCESSOME, AND SUBCELLULAR LOCATION.
RX   PubMed=15590835; DOI=10.1128/ec.3.6.1619-1626.2004;
RA   Bernstein K.A., Gallagher J.E.G., Mitchell B.M., Granneman S.,
RA   Baserga S.J.;
RT   "The small-subunit processome is a ribosome assembly intermediate.";
RL   Eukaryot. Cell 3:1619-1626(2004).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND IDENTIFICATION BY
RP   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-184, AND IDENTIFICATION BY
RP   MASS 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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
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   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-180, AND IDENTIFICATION BY
RP   MASS 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   [15]
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). uS4 is involved in nucleolar processing of
CC       pre-18S ribosomal RNA and ribosome assembly (PubMed:15590835).
CC       {ECO:0000269|PubMed:15590835, 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       Interacts with snoRNA U3. uS11 interacts with MPP10. Component of the
CC       ribosomal small subunit (SSU) processome composed of at least 40
CC       protein subunits and snoRNA U3 (PubMed:15590835).
CC       {ECO:0000269|PubMed:15590835, ECO:0000269|PubMed:22096102,
CC       ECO:0000305|PubMed:9559554}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}. Nucleus,
CC       nucleolus {ECO:0000269|PubMed:15590835}.
CC   -!- MISCELLANEOUS: Present with 63300 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- MISCELLANEOUS: There are 2 genes for uS4 in yeast. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M88650; AAB59327.1; -; Genomic_DNA.
DR   EMBL; U02073; AAB60283.1; -; Genomic_DNA.
DR   EMBL; Z36058; CAA85151.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07304.1; -; Genomic_DNA.
DR   PIR; S31287; S31287.
DR   RefSeq; NP_009748.3; NM_001178537.3.
DR   PDB; 6WOO; EM; 2.90 A; JJ=2-183.
DR   PDBsum; 6WOO; -.
DR   AlphaFoldDB; P05755; -.
DR   EMDB; EMD-21859; -.
DR   SMR; P05755; -.
DR   BioGRID; 32887; 231.
DR   IntAct; P05755; 31.
DR   MINT; P05755; -.
DR   STRING; 4932.YBR189W; -.
DR   iPTMnet; P05755; -.
DR   MaxQB; P05755; -.
DR   PaxDb; 4932-YBR189W; -.
DR   PeptideAtlas; P05755; -.
DR   TopDownProteomics; P05755; -.
DR   EnsemblFungi; YBR189W_mRNA; YBR189W; YBR189W.
DR   GeneID; 852487; -.
DR   KEGG; sce:YBR189W; -.
DR   AGR; SGD:S000000393; -.
DR   SGD; S000000393; RPS9B.
DR   VEuPathDB; FungiDB:YBR189W; -.
DR   eggNOG; KOG3301; Eukaryota.
DR   GeneTree; ENSGT00550000074829; -.
DR   HOGENOM; CLU_089738_0_0_1; -.
DR   InParanoid; P05755; -.
DR   OMA; HIRLITM; -.
DR   OrthoDB; 1086372at2759; -.
DR   BioCyc; YEAST:G3O-29132-MONOMER; -.
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-72649; Translation initiation complex formation.
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   BioGRID-ORCS; 852487; 5 hits in 10 CRISPR screens.
DR   PRO; PR:P05755; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P05755; Protein.
DR   GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:SGD.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR   GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR   GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IGI:SGD.
DR   GO; GO:0045903; P:positive regulation of translational fidelity; IMP:SGD.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   CDD; cd00165; S4; 1.
DR   Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
DR   InterPro; IPR022801; Ribosomal_uS4.
DR   InterPro; IPR018079; Ribosomal_uS4_CS.
DR   InterPro; IPR005710; Ribosomal_uS4_euk/arc.
DR   InterPro; IPR001912; Ribosomal_uS4_N.
DR   InterPro; IPR002942; S4_RNA-bd.
DR   InterPro; IPR036986; S4_RNA-bd_sf.
DR   NCBIfam; TIGR01018; uS4_arch; 1.
DR   PANTHER; PTHR11831; 30S 40S RIBOSOMAL PROTEIN; 1.
DR   PANTHER; PTHR11831:SF5; 40S RIBOSOMAL PROTEIN S9; 1.
DR   Pfam; PF00163; Ribosomal_S4; 1.
DR   Pfam; PF01479; S4; 1.
DR   SMART; SM01390; Ribosomal_S4; 1.
DR   SMART; SM00363; S4; 1.
DR   SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1.
DR   PROSITE; PS00632; RIBOSOMAL_S4; 1.
DR   PROSITE; PS50889; S4; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW   Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; Ribosome biogenesis; RNA-binding; rRNA processing;
KW   rRNA-binding; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:6814480"
FT   CHAIN           2..195
FT                   /note="Small ribosomal subunit protein uS4B"
FT                   /id="PRO_0000132704"
FT   DOMAIN          107..181
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00182"
FT   REGION          161..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         184
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   CROSSLNK        180
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CONFLICT        20..22
FT                   /note="ESS -> QSB (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   195 AA;  22299 MW;  F5BDCEA167003813 CRC64;
     MPRAPRTYSK TYSTPKRPYE SSRLDAELKL AGEFGLKNKR EIYRISFQLS KIRRAARDLL
     TRDEKDPKRL FEGNALIRRL VRVGVLSEDK KKLDYVLALK VEDFLERRLQ TQVYKLGLAK
     SVHHARVLIT QRHIAVGKQI VNIPSFMVRL DSEKHIDFAP TSPFGGARPG RVARRNAARK
     AEASGEAAEE AEDEE
//