RS9B_YEAST
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 03-AUG-2022, entry version 199.
DE RecName: Full=40S ribosomal protein S9-B {ECO:0000303|PubMed:9559554};
DE AltName: Full=RP21;
DE AltName: Full=S13;
DE AltName: Full=Small ribosomal subunit protein uS4-B {ECO:0000303|PubMed:24524803};
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}.
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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 SMR; P05755; -.
DR BioGRID; 32887; 138.
DR IntAct; P05755; 31.
DR MINT; P05755; -.
DR STRING; 4932.YBR189W; -.
DR iPTMnet; P05755; -.
DR MaxQB; P05755; -.
DR PaxDb; P05755; -.
DR PRIDE; P05755; -.
DR TopDownProteomics; P05755; -.
DR EnsemblFungi; YBR189W_mRNA; YBR189W; YBR189W.
DR GeneID; 852487; -.
DR KEGG; sce:YBR189W; -.
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; IVHLDSQ; -.
DR BioCyc; YEAST:G3O-29132-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: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:0015935; C:small ribosomal subunit; IBA:GO_Central.
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:0006412; P:translation; IEA:InterPro.
DR CDD; cd00165; S4; 1.
DR Gene3D; 3.10.290.10; -; 1.
DR InterPro; IPR022801; Ribosomal_S4/S9.
DR InterPro; IPR005710; Ribosomal_S4/S9_euk/arc.
DR InterPro; IPR001912; Ribosomal_S4/S9_N.
DR InterPro; IPR018079; Ribosomal_S4_CS.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR PANTHER; PTHR11831; PTHR11831; 1.
DR Pfam; PF01479; S4; 1.
DR SMART; SM01390; Ribosomal_S4; 1.
DR SMART; SM00363; S4; 1.
DR TIGRFAMs; TIGR01018; uS4_arch; 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="40S ribosomal protein S9-B"
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
