RS26B_YEAST
ID RS26B_YEAST Reviewed; 119 AA.
AC P39939; A2TBN5; D3DM37; Q6B2E8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=40S ribosomal protein S26-B {ECO:0000303|PubMed:9559554};
DE AltName: Full=Small ribosomal subunit protein eS26-B {ECO:0000303|PubMed:24524803};
GN Name=RPS26B {ECO:0000303|PubMed:9559554}; OrderedLocusNames=YER131W;
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=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-88.
RC STRAIN=ATCC 201390 / BY4743;
RX PubMed=17244705; DOI=10.1073/pnas.0610354104;
RA Juneau K., Palm C., Miranda M., Davis R.W.;
RT "High-density yeast-tiling array reveals previously undiscovered introns
RT and extensive regulation of meiotic splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1522-1527(2007).
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 INTERACTION WITH TSR2.
RX PubMed=10688190; DOI=10.1038/35001009;
RA Uetz P., Giot L., Cagney G., Mansfield T.A., Judson R.S., Knight J.R.,
RA Lockshon D., Narayan V., Srinivasan M., Pochart P., Qureshi-Emili A.,
RA Li Y., Godwin B., Conover D., Kalbfleisch T., Vijayadamodar G., Yang M.,
RA Johnston M., Fields S., Rothberg J.M.;
RT "A comprehensive analysis of protein-protein interactions in Saccharomyces
RT cerevisiae.";
RL Nature 403:623-627(2000).
RN [7]
RP INTERACTION WITH TSR2.
RX PubMed=12837249; DOI=10.1016/s0092-8674(03)00466-5;
RA Peng W.-T., Robinson M.D., Mnaimneh S., Krogan N.J., Cagney G.,
RA Morris Q.D., Davierwala A.P., Grigull J., Yang X., Zhang W., Mitsakakis N.,
RA Ryan O.W., Datta N., Jojic V., Pal C., Canadien V., Richards D.P.,
RA Beattie B., Wu L.F., Altschuler S.J., Roweis S., Frey B.J., Emili A.,
RA Greenblatt J.F., Hughes T.R.;
RT "A panoramic view of yeast noncoding RNA processing.";
RL Cell 113:919-933(2003).
RN [8]
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 [9]
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 [10]
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 [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. {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). eS26 interacts with eS1 forming part of
CC the mRNA exit tunnel (PubMed:9559554, PubMed:22096102). eS26 interacts
CC with TSR2 (PubMed:10688190, PubMed:12837249).
CC {ECO:0000269|PubMed:10688190, ECO:0000269|PubMed:12837249,
CC ECO:0000269|PubMed:22096102, ECO:0000305|PubMed:9559554}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:22096102}.
CC -!- MISCELLANEOUS: Present with 503000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for eS26 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS26 family.
CC {ECO:0000305}.
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DR EMBL; U18916; AAC03229.1; -; Genomic_DNA.
DR EMBL; AY692782; AAT92801.1; -; Genomic_DNA.
DR EMBL; EF123142; ABM97486.1; -; mRNA.
DR EMBL; BK006939; DAA07791.1; -; Genomic_DNA.
DR PIR; S50634; S50634.
DR RefSeq; NP_011057.1; NM_001179021.1.
DR PDB; 4U3M; X-ray; 3.00 A; D6/d6=2-98.
DR PDB; 4U3N; X-ray; 3.20 A; D6/d6=2-98.
DR PDB; 4U3U; X-ray; 2.90 A; D6/d6=2-98.
DR PDB; 4U4N; X-ray; 3.10 A; D6/d6=2-98.
DR PDB; 4U4O; X-ray; 3.60 A; D6/d6=2-98.
DR PDB; 4U4Q; X-ray; 3.00 A; D6/d6=2-98.
DR PDB; 4U4R; X-ray; 2.80 A; D6/d6=2-98.
DR PDB; 4U4U; X-ray; 3.00 A; D6/d6=2-98.
DR PDB; 4U4Y; X-ray; 3.20 A; D6/d6=2-98.
DR PDB; 4U4Z; X-ray; 3.10 A; D6/d6=2-98.
DR PDB; 4U50; X-ray; 3.20 A; D6/d6=2-98.
DR PDB; 4U51; X-ray; 3.20 A; D6/d6=2-98.
DR PDB; 4U52; X-ray; 3.00 A; D6/d6=2-98.
DR PDB; 4U53; X-ray; 3.30 A; D6/d6=2-98.
DR PDB; 4U55; X-ray; 3.20 A; D6/d6=2-98.
DR PDB; 4U56; X-ray; 3.45 A; D6/d6=2-98.
DR PDB; 4U6F; X-ray; 3.10 A; D6/d6=2-98.
DR PDB; 5DAT; X-ray; 3.15 A; D6/d6=2-98.
DR PDB; 5DC3; X-ray; 3.25 A; D6/d6=2-98.
DR PDB; 5DGF; X-ray; 3.30 A; D6/d6=2-98.
DR PDB; 5DGV; X-ray; 3.10 A; D6/d6=2-98.
DR PDB; 5FCJ; X-ray; 3.10 A; D6/d6=2-98.
DR PDB; 5I4L; X-ray; 3.10 A; D6/d6=2-98.
DR PDB; 5LYB; X-ray; 3.25 A; D6/d6=2-98.
DR PDB; 5M1J; EM; 3.30 A; a2=2-99.
DR PDB; 5MEI; X-ray; 3.50 A; b/d6=2-98.
DR PDB; 5NDG; X-ray; 3.70 A; D6/d6=2-98.
DR PDB; 5NDV; X-ray; 3.30 A; D6/d6=2-98.
DR PDB; 5NDW; X-ray; 3.70 A; D6/d6=2-98.
DR PDB; 5OBM; X-ray; 3.40 A; D6/d6=2-98.
DR PDB; 5ON6; X-ray; 3.10 A; b/d6=2-98.
DR PDB; 5TBW; X-ray; 3.00 A; b/d6=2-98.
DR PDB; 5TGA; X-ray; 3.30 A; D6/d6=2-98.
DR PDB; 5TGM; X-ray; 3.50 A; D6/d6=2-98.
DR PDB; 6GQ1; EM; 4.40 A; AQ=2-98.
DR PDB; 6GQB; EM; 3.90 A; AQ=2-98.
DR PDB; 6GQV; EM; 4.00 A; AQ=2-98.
DR PDB; 6HHQ; X-ray; 3.10 A; b/d6=1-119.
DR PDB; 6I7O; EM; 5.30 A; e/eb=2-98.
DR PDB; 6Q8Y; EM; 3.10 A; e=2-98.
DR PDB; 6S47; EM; 3.28 A; Bb=2-119.
DR PDB; 6T4Q; EM; 2.60 A; Sa=2-98.
DR PDB; 6TB3; EM; 2.80 A; e=2-98.
DR PDB; 6TNU; EM; 3.10 A; e=2-98.
DR PDB; 6WOO; EM; 2.90 A; aa=2-98.
DR PDB; 6Z6J; EM; 3.40 A; Sa=1-119.
DR PDB; 6Z6K; EM; 3.40 A; Sa=1-119.
DR PDB; 6ZVI; EM; 3.00 A; K=2-98.
DR PDB; 7A1G; EM; 3.00 A; e=2-98.
DR PDB; 7B7D; EM; 3.30 A; e=2-98.
DR PDB; 7NRC; EM; 3.90 A; Se=2-98.
DR PDB; 7NRD; EM; 4.36 A; Se=2-98.
DR PDBsum; 4U3M; -.
DR PDBsum; 4U3N; -.
DR PDBsum; 4U3U; -.
DR PDBsum; 4U4N; -.
DR PDBsum; 4U4O; -.
DR PDBsum; 4U4Q; -.
DR PDBsum; 4U4R; -.
DR PDBsum; 4U4U; -.
DR PDBsum; 4U4Y; -.
DR PDBsum; 4U4Z; -.
DR PDBsum; 4U50; -.
DR PDBsum; 4U51; -.
DR PDBsum; 4U52; -.
DR PDBsum; 4U53; -.
DR PDBsum; 4U55; -.
DR PDBsum; 4U56; -.
DR PDBsum; 4U6F; -.
DR PDBsum; 5DAT; -.
DR PDBsum; 5DC3; -.
DR PDBsum; 5DGF; -.
DR PDBsum; 5DGV; -.
DR PDBsum; 5FCJ; -.
DR PDBsum; 5I4L; -.
DR PDBsum; 5LYB; -.
DR PDBsum; 5M1J; -.
DR PDBsum; 5MEI; -.
DR PDBsum; 5NDG; -.
DR PDBsum; 5NDV; -.
DR PDBsum; 5NDW; -.
DR PDBsum; 5OBM; -.
DR PDBsum; 5ON6; -.
DR PDBsum; 5TBW; -.
DR PDBsum; 5TGA; -.
DR PDBsum; 5TGM; -.
DR PDBsum; 6GQ1; -.
DR PDBsum; 6GQB; -.
DR PDBsum; 6GQV; -.
DR PDBsum; 6HHQ; -.
DR PDBsum; 6I7O; -.
DR PDBsum; 6Q8Y; -.
DR PDBsum; 6S47; -.
DR PDBsum; 6T4Q; -.
DR PDBsum; 6TB3; -.
DR PDBsum; 6TNU; -.
DR PDBsum; 6WOO; -.
DR PDBsum; 6Z6J; -.
DR PDBsum; 6Z6K; -.
DR PDBsum; 6ZVI; -.
DR PDBsum; 7A1G; -.
DR PDBsum; 7B7D; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR AlphaFoldDB; P39939; -.
DR SMR; P39939; -.
DR BioGRID; 36875; 163.
DR DIP; DIP-1395N; -.
DR IntAct; P39939; 10.
DR MINT; P39939; -.
DR STRING; 4932.YER131W; -.
DR CarbonylDB; P39939; -.
DR iPTMnet; P39939; -.
DR PaxDb; P39939; -.
DR PRIDE; P39939; -.
DR EnsemblFungi; YER131W_mRNA; YER131W; YER131W.
DR GeneID; 856868; -.
DR KEGG; sce:YER131W; -.
DR SGD; S000000933; RPS26B.
DR VEuPathDB; FungiDB:YER131W; -.
DR eggNOG; KOG1768; Eukaryota.
DR GeneTree; ENSGT00390000002517; -.
DR HOGENOM; CLU_129451_2_0_1; -.
DR InParanoid; P39939; -.
DR OMA; DKAICVT; -.
DR BioCyc; YEAST:G3O-30294-MON; -.
DR PRO; PR:P39939; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P39939; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; NAS:SGD.
DR GO; GO:0042255; P:ribosome assembly; IMP:SGD.
DR GO; GO:0006407; P:rRNA export from nucleus; IGI:SGD.
DR Gene3D; 3.30.1740.20; -; 1.
DR InterPro; IPR000892; Ribosomal_S26e.
DR InterPro; IPR038551; Ribosomal_S26e_sf.
DR PANTHER; PTHR12538; PTHR12538; 1.
DR Pfam; PF01283; Ribosomal_S26e; 1.
DR PROSITE; PS00733; RIBOSOMAL_S26E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT CHAIN 1..119
FT /note="40S ribosomal protein S26-B"
FT /id="PRO_0000204529"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 110
FT /note="S -> P (in Ref. 3; AAT92801)"
FT /evidence="ECO:0000305"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 37..45
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 47..51
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 75..80
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:6ZVI"
SQ SEQUENCE 119 AA; 13447 MW; 2BB61CF9B232A18E CRC64;
MPKKRASNGR NKKGRGHVKP VRCVNCSKSI PKDKAIKRMA IRNIVEAAAV RDLSEASVYP
EYALPKTYNK LHYCVSCAIH ARIVRVRSRE DRKNRAPPQR PRFNRDNKVS PAAAAKKAL
