RS26A_YEAST
ID RS26A_YEAST Reviewed; 119 AA.
AC P39938; A2TBN5; D6VTW5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=40S ribosomal protein S26-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=Small ribosomal subunit protein eS26-A {ECO:0000303|PubMed:24524803};
GN Name=RPS26A {ECO:0000303|PubMed:9559554}; Synonyms=RPS26;
GN OrderedLocusNames=YGL189C; ORFNames=G1355;
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=7821815; DOI=10.1016/0378-1119(94)90461-8;
RA Wu M., Tan H.;
RT "The Saccharomyces cerevisiae homologue of ribosomal protein S26.";
RL Gene 150:401-402(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9046087;
RX DOI=10.1002/(sici)1097-0061(199701)13:1<55::aid-yea48>3.0.co;2-9;
RA Coglievina M., Klima R., Bertani I., Delneri D., Zaccaria P., Bruschi C.V.;
RT "Sequencing of a 40.5 kb fragment located on the left arm of chromosome VII
RT from Saccharomyces cerevisiae.";
RL Yeast 13:55-64(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
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 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 [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 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 [8]
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 [9]
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 [10]
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 [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).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 80S RIBOSOME, SUBUNIT, AND
RP 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).
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 16300 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; U10563; AAA66066.1; -; Genomic_DNA.
DR EMBL; X91489; CAA62786.1; -; Genomic_DNA.
DR EMBL; Z72711; CAA96901.1; -; Genomic_DNA.
DR EMBL; EF123138; ABM97482.1; -; mRNA.
DR EMBL; BK006941; DAA07926.1; -; Genomic_DNA.
DR PIR; S47942; S47942.
DR RefSeq; NP_011326.1; NM_001181054.1.
DR PDB; 3J6X; EM; 6.10 A; 26=1-119.
DR PDB; 3J6Y; EM; 6.10 A; 26=1-119.
DR PDB; 3J77; EM; 6.20 A; 26=1-119.
DR PDB; 3J78; EM; 6.30 A; 26=1-119.
DR PDB; 4V88; X-ray; 3.00 A; Aa/Ca=1-119.
DR PDB; 4V8Y; EM; 4.30 A; A0=1-119.
DR PDB; 4V8Z; EM; 6.60 A; A0=1-119.
DR PDB; 4V92; EM; 3.70 A; a=2-98.
DR PDB; 5DGE; X-ray; 3.45 A; D6/d6=2-98.
DR PDB; 5FCI; X-ray; 3.40 A; D6/d6=2-98.
DR PDB; 5JUO; EM; 4.00 A; XB=1-119.
DR PDB; 5JUP; EM; 3.50 A; XB=1-119.
DR PDB; 5JUS; EM; 4.20 A; XB=1-119.
DR PDB; 5JUT; EM; 4.00 A; XB=1-119.
DR PDB; 5JUU; EM; 4.00 A; XB=1-119.
DR PDB; 5LL6; EM; 3.90 A; e=1-119.
DR PDB; 5MC6; EM; 3.80 A; e=1-119.
DR PDB; 6G04; NMR; -; B=100-119.
DR PDB; 6SNT; EM; 2.80 A; a=1-119.
DR PDB; 6SV4; EM; 3.30 A; e/eb/ec=1-119.
DR PDB; 6T7I; EM; 3.20 A; Sa=1-119.
DR PDB; 6T7T; EM; 3.10 A; Sa=1-119.
DR PDB; 6T83; EM; 4.00 A; 1/ab=1-119.
DR PDB; 6ZCE; EM; 5.30 A; b=1-119.
DR PDB; 6ZU9; EM; 6.20 A; e=1-119.
DR PDBsum; 3J6X; -.
DR PDBsum; 3J6Y; -.
DR PDBsum; 3J77; -.
DR PDBsum; 3J78; -.
DR PDBsum; 4V88; -.
DR PDBsum; 4V8Y; -.
DR PDBsum; 4V8Z; -.
DR PDBsum; 4V92; -.
DR PDBsum; 5DGE; -.
DR PDBsum; 5FCI; -.
DR PDBsum; 5JUO; -.
DR PDBsum; 5JUP; -.
DR PDBsum; 5JUS; -.
DR PDBsum; 5JUT; -.
DR PDBsum; 5JUU; -.
DR PDBsum; 5LL6; -.
DR PDBsum; 5MC6; -.
DR PDBsum; 6G04; -.
DR PDBsum; 6SNT; -.
DR PDBsum; 6SV4; -.
DR PDBsum; 6T7I; -.
DR PDBsum; 6T7T; -.
DR PDBsum; 6T83; -.
DR PDBsum; 6ZCE; -.
DR PDBsum; 6ZU9; -.
DR AlphaFoldDB; P39938; -.
DR SMR; P39938; -.
DR BioGRID; 33067; 93.
DR DIP; DIP-1396N; -.
DR IntAct; P39938; 10.
DR MINT; P39938; -.
DR STRING; 4932.YGL189C; -.
DR iPTMnet; P39938; -.
DR MaxQB; P39938; -.
DR PaxDb; P39938; -.
DR PRIDE; P39938; -.
DR EnsemblFungi; YGL189C_mRNA; YGL189C; YGL189C.
DR GeneID; 852686; -.
DR KEGG; sce:YGL189C; -.
DR SGD; S000003157; RPS26A.
DR VEuPathDB; FungiDB:YGL189C; -.
DR eggNOG; KOG1768; Eukaryota.
DR GeneTree; ENSGT00390000002517; -.
DR HOGENOM; CLU_129451_2_0_1; -.
DR InParanoid; P39938; -.
DR OMA; GGRCKHN; -.
DR BioCyc; YEAST:G3O-30672-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:P39938; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P39938; 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-A"
FT /id="PRO_0000204528"
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..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:6G04"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:6G04"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:6G04"
SQ SEQUENCE 119 AA; 13505 MW; 2BB61CF9B233E3FE CRC64;
MPKKRASNGR NKKGRGHVKP VRCVNCSKSI PKDKAIKRMA IRNIVEAAAV RDLSEASVYP
EYALPKTYNK LHYCVSCAIH ARIVRVRSRE DRKNRAPPQR PRFNRENKVS PADAAKKAL
