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RS18B_YEAST
ID   RS18B_YEAST             Reviewed;         146 AA.
AC   P0CX56; D6VT75; P35271;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=40S ribosomal protein S18-B {ECO:0000303|PubMed:9559554};
DE   AltName: Full=Small ribosomal subunit protein uS13-B {ECO:0000303|PubMed:24524803};
GN   Name=RPS18B {ECO:0000303|PubMed:9559554}; OrderedLocusNames=YML026C;
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=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(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   PROTEIN SEQUENCE OF 2-36; 58-68 AND 81-88, 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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-146.
RX   PubMed=8096171; DOI=10.1007/bf00387732;
RA   Kaufmann E.;
RT   "In vitro binding to the leucine tRNA gene identifies a novel yeast
RT   homeobox gene.";
RL   Chromosoma 102:174-179(1993).
RN   [5]
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   [6]
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   [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   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   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [11]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-36; LYS-49; LYS-80 AND LYS-96,
RP   AND IDENTIFICATION BY 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   [12]
RP   METHYLATION AT LYS-48 BY RKM1.
RX   PubMed=22522802; DOI=10.1002/pmic.201100570;
RA   Couttas T.A., Raftery M.J., Padula M.P., Herbert B.R., Wilkins M.R.;
RT   "Methylation of translation-associated proteins in Saccharomyces
RT   cerevisiae: Identification of methylated lysines and their
RT   methyltransferases.";
RL   Proteomics 12:960-972(2012).
RN   [13]
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 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:22096102}.
CC   -!- PTM: N-terminally acetylated by acetyltransferase NatA.
CC       {ECO:0000269|PubMed:10601260, ECO:0000269|Ref.3}.
CC   -!- MISCELLANEOUS: Present with 112000 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- MISCELLANEOUS: There are 2 genes for uS13 in yeast. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS13 family.
CC       {ECO:0000305}.
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DR   EMBL; Z46659; CAA86629.1; -; Genomic_DNA.
DR   EMBL; X62392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BK006946; DAA09872.1; -; Genomic_DNA.
DR   PIR; S50886; S50886.
DR   RefSeq; NP_010738.1; NM_001180758.1.
DR   RefSeq; NP_013686.1; NM_001182384.1.
DR   AlphaFoldDB; P0CX56; -.
DR   SMR; P0CX56; -.
DR   BioGRID; 32505; 660.
DR   BioGRID; 35143; 217.
DR   IntAct; P0CX56; 3.
DR   MINT; P0CX56; -.
DR   iPTMnet; P0CX56; -.
DR   PRIDE; P0CX56; -.
DR   EnsemblFungi; YDR450W_mRNA; YDR450W; YDR450W.
DR   EnsemblFungi; YML026C_mRNA; YML026C; YML026C.
DR   GeneID; 852061; -.
DR   GeneID; 854982; -.
DR   KEGG; sce:YDR450W; -.
DR   KEGG; sce:YML026C; -.
DR   SGD; S000004488; RPS18B.
DR   VEuPathDB; FungiDB:YDR450W; -.
DR   VEuPathDB; FungiDB:YML026C; -.
DR   GeneTree; ENSGT00390000012691; -.
DR   HOGENOM; CLU_103849_0_1_1; -.
DR   InParanoid; P0CX56; -.
DR   BioCyc; YEAST:G3O-32628-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:P0CX56; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P0CX56; protein.
DR   ExpressionAtlas; P0CX56; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; NAS:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0015935; C:small ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; NAS:SGD.
DR   GO; GO:0002181; P:cytoplasmic translation; NAS: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:0006407; P:rRNA export from nucleus; IGI:SGD.
DR   Gene3D; 4.10.910.10; -; 1.
DR   HAMAP; MF_01315; Ribosomal_S13_S18; 1.
DR   InterPro; IPR027437; 30s_Rbsml_prot_S13_C.
DR   InterPro; IPR001892; Ribosomal_S13.
DR   InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR   InterPro; IPR018269; Ribosomal_S13_CS.
DR   Pfam; PF00416; Ribosomal_S13; 1.
DR   PIRSF; PIRSF002134; Ribosomal_S13; 1.
DR   SUPFAM; SSF46946; SSF46946; 1.
DR   PROSITE; PS00646; RIBOSOMAL_S13_1; 1.
DR   PROSITE; PS50159; RIBOSOMAL_S13_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW   Methylation; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:10601260, ECO:0000269|Ref.3,
FT                   ECO:0007744|PubMed:22814378"
FT   CHAIN           2..146
FT                   /note="40S ribosomal protein S18-B"
FT                   /id="PRO_0000409774"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:10601260, ECO:0000269|Ref.3,
FT                   ECO:0007744|PubMed:22814378"
FT   MOD_RES         48
FT                   /note="N6-methyllysine; by RKM1"
FT                   /evidence="ECO:0000269|PubMed:22522802"
FT   CROSSLNK        36
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CROSSLNK        49
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CROSSLNK        80
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CROSSLNK        96
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CONFLICT        27..29
FT                   /note="KIV -> EFG (in Ref. 4; X62392)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   146 AA;  17038 MW;  1F50BF9ADD20CA19 CRC64;
     MSLVVQEQGS FQHILRLLNT NVDGNIKIVY ALTTIKGVGR RYSNLVCKKA DVDLHKRAGE
     LTQEELERIV QIMQNPTHYK IPAWFLNRQN DITDGKDYHT LANNVESKLR DDLERLKKIR
     AHRGIRHFWG LRVRGQHTKT TGRRRA
 
 
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