RS7B_YEAST
ID RS7B_YEAST Reviewed; 190 AA.
AC P48164; D6W184;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=40S ribosomal protein S7-B {ECO:0000303|PubMed:9559554};
DE AltName: Full=Small ribosomal subunit protein eS7-B {ECO:0000303|PubMed:24524803};
GN Name=RPS7B {ECO:0000303|PubMed:9559554}; OrderedLocusNames=YNL096C;
GN ORFNames=N2212;
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=ATCC 96604 / S288c / FY1679;
RX PubMed=8771715;
RX DOI=10.1002/(sici)1097-0061(199605)12:6<599::aid-yea938>3.0.co;2-9;
RA Garcia-Cantalejo J.M., Boskovic J., Jimenez A.;
RT "Sequence analysis of a 14.2 kb fragment of Saccharomyces cerevisiae
RT chromosome XIV that includes the ypt53, tRNALeu and gsr m2 genes and four
RT new open reading frames.";
RL Yeast 12:599-608(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(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 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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND SER-31, AND
RP IDENTIFICATION BY 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 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). eS7 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 -!- PTM: N-terminally acetylated by acetyltransferase NatA.
CC {ECO:0000269|PubMed:10601260}.
CC -!- MISCELLANEOUS: Present with 43500 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for eS7 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS7 family.
CC {ECO:0000305}.
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DR EMBL; X85811; CAA59821.1; -; Genomic_DNA.
DR EMBL; Z71372; CAA95972.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10450.1; -; Genomic_DNA.
DR PIR; S52729; S52729.
DR RefSeq; NP_014303.3; NM_001182934.3.
DR AlphaFoldDB; P48164; -.
DR SMR; P48164; -.
DR BioGRID; 35728; 201.
DR DIP; DIP-3841N; -.
DR IntAct; P48164; 12.
DR MINT; P48164; -.
DR STRING; 4932.YNL096C; -.
DR iPTMnet; P48164; -.
DR MaxQB; P48164; -.
DR PaxDb; P48164; -.
DR PRIDE; P48164; -.
DR EnsemblFungi; YNL096C_mRNA; YNL096C; YNL096C.
DR GeneID; 855628; -.
DR KEGG; sce:YNL096C; -.
DR SGD; S000005040; RPS7B.
DR VEuPathDB; FungiDB:YNL096C; -.
DR eggNOG; KOG3320; Eukaryota.
DR GeneTree; ENSGT00390000014122; -.
DR HOGENOM; CLU_088621_1_2_1; -.
DR InParanoid; P48164; -.
DR OMA; HVLFLAK; -.
DR BioCyc; YEAST:G3O-33124-MON; -.
DR PRO; PR:P48164; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P48164; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; NAS:SGD.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IBA:GO_Central.
DR GO; GO:0042254; P:ribosome biogenesis; IGI:SGD.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR InterPro; IPR000554; Ribosomal_S7e.
DR PANTHER; PTHR11278; PTHR11278; 1.
DR Pfam; PF01251; Ribosomal_S7e; 1.
DR PROSITE; PS00948; RIBOSOMAL_S7E; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Ribosome biogenesis; rRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260"
FT CHAIN 2..190
FT /note="40S ribosomal protein S7-B"
FT /id="PRO_0000174213"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:10601260"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 190 AA; 21634 MW; 46553FB74A5FAF4B CRC64;
MSSVQSKILS QAPSELELQV AKTFIDLESS SPELKADLRP LQIKSIREID VTGGKKALVL
FVPVPALSAY HKVQTKLTRE LEKKFPDRHV IFLAERRILP KPSRTSRQVQ KRPRSRTLTA
VHDKVLEDMV FPTEIVGKRV RYLVGGNKIQ KVLLDSKDVQ QIDYKLESFQ AVYNKLTGKQ
IVFEIPSQTN
