ID   RS3A2_YEAST             Reviewed;         255 AA.
AC   P23248; D6VZB0;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 194.
DE   RecName: Full=Small ribosomal subunit protein eS1B {ECO:0000255|HAMAP-Rule:MF_03122, ECO:0000303|PubMed:24524803};
DE   AltName: Full=40S ribosomal protein S1-B {ECO:0000303|PubMed:9559554};
DE   AltName: Full=RP10B;
GN   Name=RPS1B {ECO:0000255|HAMAP-Rule:MF_03122,
GN   ECO:0000303|PubMed:9559554}; Synonyms=PLC2, RPS10B;
GN   OrderedLocusNames=YML063W;
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=SEY2102;
RX   PubMed=2017143; DOI=10.1007/bf00261691;
RA   Garrett J.M., Singh K.K., Vonder Haar R.A., Emr S.D.;
RT   "Mitochondrial protein import: isolation and characterization of the
RT   Saccharomyces cerevisiae MFT1 gene.";
RL   Mol. Gen. Genet. 225:483-491(1991).
RN   [2]
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   [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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-21.
RX   PubMed=1544921; DOI=10.1016/s0021-9258(18)42785-8;
RA   Takakura H., Tsunasawa S., Miyagi M., Warner J.R.;
RT   "NH2-terminal acetylation of ribosomal proteins of Saccharomyces
RT   cerevisiae.";
RL   J. Biol. Chem. 267:5442-5445(1992).
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245 AND THR-254, AND
RP   IDENTIFICATION BY 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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245 AND THR-254, AND
RP   IDENTIFICATION BY 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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, 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   [12]
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   [13]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-248, 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   [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. {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). eS1 interacts directly with uS11 and
CC       eS26, which form part of the mRNA exit tunnel (PubMed:9559554,
CC       PubMed:22096102). {ECO:0000269|PubMed:22096102,
CC       ECO:0000305|PubMed:9559554}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03122,
CC       ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
CC   -!- PTM: N-terminally acetylated by acetyltransferase NatA. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Present with 107000 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- MISCELLANEOUS: There are 2 genes for eS1 in yeast. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_03122}.
CC   -!- CAUTION: Was originally thought to be MFT1, the mitochondrial fusion
CC       target protein. {ECO:0000305|PubMed:2017143}.
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DR   EMBL; X55360; CAA39044.1; -; Genomic_DNA.
DR   EMBL; Z38114; CAA86258.1; -; Genomic_DNA.
DR   EMBL; AY557981; AAS56307.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09834.1; -; Genomic_DNA.
DR   PIR; S14051; S14051.
DR   RefSeq; NP_013648.1; NM_001182422.1.
DR   PDB; 6WOO; EM; 2.90 A; BB=20-233.
DR   PDBsum; 6WOO; -.
DR   AlphaFoldDB; P23248; -.
DR   EMDB; EMD-21859; -.
DR   SMR; P23248; -.
DR   BioGRID; 35103; 329.
DR   IntAct; P23248; 75.
DR   MINT; P23248; -.
DR   STRING; 4932.YML063W; -.
DR   iPTMnet; P23248; -.
DR   MaxQB; P23248; -.
DR   PaxDb; 4932-YML063W; -.
DR   PeptideAtlas; P23248; -.
DR   TopDownProteomics; P23248; -.
DR   EnsemblFungi; YML063W_mRNA; YML063W; YML063W.
DR   GeneID; 854939; -.
DR   KEGG; sce:YML063W; -.
DR   AGR; SGD:S000004528; -.
DR   SGD; S000004528; RPS1B.
DR   VEuPathDB; FungiDB:YML063W; -.
DR   eggNOG; KOG1628; Eukaryota.
DR   GeneTree; ENSGT00940000165721; -.
DR   HOGENOM; CLU_062507_0_0_1; -.
DR   InParanoid; P23248; -.
DR   OMA; KRTQDPF; -.
DR   OrthoDB; 5475993at2759; -.
DR   BioCyc; YEAST:G3O-32658-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; 854939; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P23248; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P23248; Protein.
DR   GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; NAS:SGD.
DR   GO; GO:0003735; F:structural constituent of ribosome; NAS:SGD.
DR   GO; GO:0002181; P:cytoplasmic translation; NAS:SGD.
DR   GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IGI:SGD.
DR   HAMAP; MF_03122; Ribosomal_eS1_euk; 1.
DR   InterPro; IPR001593; Ribosomal_eS1.
DR   InterPro; IPR018281; Ribosomal_eS1_CS.
DR   InterPro; IPR027500; Ribosomal_eS1_euk.
DR   PANTHER; PTHR11830; 40S RIBOSOMAL PROTEIN S3A; 1.
DR   PANTHER; PTHR11830:SF0; 40S RIBOSOMAL PROTEIN S3A; 1.
DR   Pfam; PF01015; Ribosomal_S3Ae; 1.
DR   SMART; SM01397; Ribosomal_S3Ae; 1.
DR   PROSITE; PS01191; RIBOSOMAL_S3AE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW   Isopeptide bond; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03122,
FT                   ECO:0000269|PubMed:1544921"
FT   CHAIN           2..255
FT                   /note="Small ribosomal subunit protein eS1B"
FT                   /id="PRO_0000153542"
FT   MOD_RES         2
FT                   /note="N-acetylalanine; partial"
FT                   /evidence="ECO:0000250|UniProtKB:P33442, ECO:0000255|HAMAP-
FT                   Rule:MF_03122"
FT   MOD_RES         245
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         254
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956"
FT   CROSSLNK        248
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
SQ   SEQUENCE   255 AA;  28812 MW;  192A913E3AD5C7DE CRC64;
     MAVGKNKRLS RGKKGLKKKV VDPFTRKEWF DIKAPSTFEN RNVGKTLVNK STGLKNASDA
     LKGRVVEVCL ADLQGSEDHS FRKVKLRVDE VQGKNLLTNF HGMDFTTDKL RSMVRKWQTL
     IEANVTVKTS DDYVLRIFAI AFTRKQANQV KRHSYAQSSH IRAIRKVISE ILTREVQNST
     LAQLTSKLIP EVINKEIENA TKDIFPLQNI HVRKVKLLKQ PKFDVGALMA LHGEGSGEEK
     GKKVSGFKDE VLETV
//