RS14B_YEAST
ID RS14B_YEAST Reviewed; 138 AA.
AC P39516; D6VW00;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=40S ribosomal protein S14-B {ECO:0000303|PubMed:9559554};
DE AltName: Full=RP59B;
DE AltName: Full=Small ribosomal subunit protein uS11-B {ECO:0000303|PubMed:24524803};
GN Name=RPS14B {ECO:0000303|PubMed:9559554}; Synonyms=CRY2;
GN OrderedLocusNames=YJL191W; ORFNames=J0354;
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=8293976; DOI=10.1093/genetics/135.3.719;
RA Paulovich A.G., Thompson J.R., Larkin J.C., Li Z., Woolford J.L. Jr.;
RT "Molecular genetics of cryptopleurine resistance in Saccharomyces
RT cerevisiae: expression of a ribosomal protein gene family.";
RL Genetics 135:719-730(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7754713; DOI=10.1002/yea.320100912;
RA Purnelle B., Coster F., Goffeau A.;
RT "The sequence of a 36 kb segment on the left arm of yeast chromosome X
RT identifies 24 open reading frames including NUC1, PRP21 (SPP91), CDC6,
RT CRY2, the gene for S24, a homologue to the aconitase gene ACO1 and two
RT homologues to chromosome III genes.";
RL Yeast 10:1235-1249(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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 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 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 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 IDENTIFICATION BY MASS SPECTROMETRY [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 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). uS11 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). uS11 interacts with eS1 forming part of
CC the mRNA exit tunnel (PubMed:9559554, PubMed:22096102). uS11 interacts
CC with snoRNA U3. uS11 interacts with MPP10. Component of the ribosomal
CC small subunit (SSU) processome composed of at least 40 protein subunits
CC and snoRNA U3 (PubMed:15590835). {ECO:0000269|PubMed:15590835,
CC ECO:0000269|PubMed:22096102, ECO:0000305|PubMed:9559554}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:15590835}.
CC -!- MISCELLANEOUS: Present with 3370 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for uS11 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS11 family.
CC {ECO:0000305}.
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DR EMBL; L12564; AAA17764.1; -; Genomic_DNA.
DR EMBL; X77688; CAA54769.1; -; Genomic_DNA.
DR EMBL; Z49466; CAA89486.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08616.1; -; Genomic_DNA.
DR PIR; S46643; S46643.
DR RefSeq; NP_012344.1; NM_001181624.1.
DR PDB; 5I4L; X-ray; 3.10 A; C4/c4=11-138.
DR PDB; 5MEI; X-ray; 3.50 A; P/c4=11-138.
DR PDB; 5NDV; X-ray; 3.30 A; C4/c4=11-138.
DR PDB; 5NDW; X-ray; 3.70 A; C4/c4=11-138.
DR PDB; 5OBM; X-ray; 3.40 A; C4/c4=11-138.
DR PDB; 5ON6; X-ray; 3.10 A; P/c4=11-138.
DR PDB; 5TBW; X-ray; 3.00 A; P/c4=11-138.
DR PDB; 5TGA; X-ray; 3.30 A; C4/c4=11-138.
DR PDB; 6GQ1; EM; 4.40 A; AE=12-138.
DR PDB; 6GQB; EM; 3.90 A; AE=12-138.
DR PDB; 6GQV; EM; 4.00 A; AE=12-138.
DR PDB; 6HHQ; X-ray; 3.10 A; P/c4=1-138.
DR PDB; 6I7O; EM; 5.30 A; Z/Zb=11-138.
DR PDB; 6Q8Y; EM; 3.10 A; Z=12-138.
DR PDB; 6T4Q; EM; 2.60 A; SO=12-138.
DR PDB; 6TB3; EM; 2.80 A; Z=12-138.
DR PDB; 6TNU; EM; 3.10 A; Z=12-138.
DR PDB; 6WOO; EM; 2.90 A; OO=12-138.
DR PDB; 6XIQ; EM; 4.20 A; AE=1-138.
DR PDB; 6XIR; EM; 3.20 A; AE=1-138.
DR PDB; 6ZVI; EM; 3.00 A; w=11-138.
DR PDB; 7A1G; EM; 3.00 A; Z=12-138.
DR PDB; 7B7D; EM; 3.30 A; Z=12-138.
DR PDB; 7NRC; EM; 3.90 A; SZ=12-138.
DR PDB; 7NRD; EM; 4.36 A; SZ=11-138.
DR PDBsum; 5I4L; -.
DR PDBsum; 5MEI; -.
DR PDBsum; 5NDV; -.
DR PDBsum; 5NDW; -.
DR PDBsum; 5OBM; -.
DR PDBsum; 5ON6; -.
DR PDBsum; 5TBW; -.
DR PDBsum; 5TGA; -.
DR PDBsum; 6GQ1; -.
DR PDBsum; 6GQB; -.
DR PDBsum; 6GQV; -.
DR PDBsum; 6HHQ; -.
DR PDBsum; 6I7O; -.
DR PDBsum; 6Q8Y; -.
DR PDBsum; 6T4Q; -.
DR PDBsum; 6TB3; -.
DR PDBsum; 6TNU; -.
DR PDBsum; 6WOO; -.
DR PDBsum; 6XIQ; -.
DR PDBsum; 6XIR; -.
DR PDBsum; 6ZVI; -.
DR PDBsum; 7A1G; -.
DR PDBsum; 7B7D; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR AlphaFoldDB; P39516; -.
DR SMR; P39516; -.
DR BioGRID; 33572; 111.
DR DIP; DIP-5688N; -.
DR IntAct; P39516; 27.
DR MINT; P39516; -.
DR STRING; 4932.YJL191W; -.
DR MaxQB; P39516; -.
DR PaxDb; P39516; -.
DR PRIDE; P39516; -.
DR EnsemblFungi; YJL191W_mRNA; YJL191W; YJL191W.
DR GeneID; 853248; -.
DR KEGG; sce:YJL191W; -.
DR SGD; S000003727; RPS14B.
DR VEuPathDB; FungiDB:YJL191W; -.
DR eggNOG; KOG0407; Eukaryota.
DR GeneTree; ENSGT00390000000703; -.
DR HOGENOM; CLU_072439_6_0_1; -.
DR InParanoid; P39516; -.
DR OMA; KWGVAHI; -.
DR BioCyc; YEAST:G3O-31623-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:P39516; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P39516; 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:0048027; F:mRNA 5'-UTR binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IDA:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; NAS:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IMP:UniProtKB.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IMP:UniProtKB.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 3.30.420.80; -; 1.
DR HAMAP; MF_01310; Ribosomal_S11; 1.
DR InterPro; IPR001971; Ribosomal_S11.
DR InterPro; IPR018102; Ribosomal_S11_CS.
DR InterPro; IPR036967; Ribosomal_S11_sf.
DR PANTHER; PTHR11759; PTHR11759; 1.
DR Pfam; PF00411; Ribosomal_S11; 1.
DR PIRSF; PIRSF002131; Ribosomal_S11; 1.
DR PROSITE; PS00054; RIBOSOMAL_S11; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Ribosome biogenesis; rRNA processing.
FT CHAIN 1..138
FT /note="40S ribosomal protein S14-B"
FT /id="PRO_0000123360"
FT REGION 118..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 3
FT /note="N -> K (in Ref. 2; CAA54769)"
FT /evidence="ECO:0000305"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 58..75
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:6ZVI"
SQ SEQUENCE 138 AA; 14650 MW; 6BBACF61D38538AA CRC64;
MANDLVQARD NSQVFGVARI YASFNDTFVH VTDLSGKETI ARVTGGMKVK ADRDESSPYA
AMLAAQDVAA KCKEVGITAV HVKIRATGGT RTKTPGPGGQ AALRALARSG LRIGRIEDVT
PVPSDSTRKK GGRRGRRL
