RS10B_YEAST
ID RS10B_YEAST Reviewed; 105 AA.
AC P46784; D6W055;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=40S ribosomal protein S10-B {ECO:0000303|PubMed:9559554};
DE AltName: Full=Small ribosomal subunit protein eS10-B {ECO:0000303|PubMed:24524803};
GN Name=RPS10B {ECO:0000303|PubMed:9559554}; OrderedLocusNames=YMR230W;
GN ORFNames=YM9959.12;
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=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 [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 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 [4]
RP ANALYSIS OF N-TERMINUS.
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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
RP FUNCTION, AND INTERACTION WITH GCN1.
RX PubMed=25437641; DOI=10.1042/bj20140782;
RA Lee S.J., Swanson M.J., Sattlegger E.;
RT "Gcn1 contacts the small ribosomal protein Rps10, which is required for
RT full activation of the protein kinase Gcn2.";
RL Biochem. J. 466:547-559(2015).
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). eS10 plays a role as a positive regulator of
CC the GCN2 kinase activity by stimulating GCN1-mediated GCN2 activation
CC (PubMed:25437641). {ECO:0000269|PubMed:25437641,
CC 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). eS10
CC interacts with GCN1 (via middle region); this interaction is direct and
CC promotes GCN2 kinase activity (PubMed:25437641).
CC {ECO:0000269|PubMed:22096102, ECO:0000269|PubMed:25437641,
CC ECO:0000305|PubMed:9559554}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:22096102}.
CC -!- PTM: The N-terminus is not modified. {ECO:0000269|PubMed:10601260}.
CC -!- MISCELLANEOUS: Present with 7650 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for eS10 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS10 family.
CC {ECO:0000305}.
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DR EMBL; Z49939; CAA90201.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10129.1; -; Genomic_DNA.
DR PIR; S57597; S57597.
DR RefSeq; NP_013957.1; NM_001182737.1.
DR PDB; 4U3M; X-ray; 3.00 A; C0/c0=1-105.
DR PDBsum; 4U3M; -.
DR AlphaFoldDB; P46784; -.
DR SMR; P46784; -.
DR BioGRID; 35408; 228.
DR IntAct; P46784; 9.
DR MINT; P46784; -.
DR STRING; 4932.YMR230W; -.
DR iPTMnet; P46784; -.
DR MaxQB; P46784; -.
DR PaxDb; P46784; -.
DR PRIDE; P46784; -.
DR TopDownProteomics; P46784; -.
DR EnsemblFungi; YMR230W_mRNA; YMR230W; YMR230W.
DR GeneID; 855270; -.
DR KEGG; sce:YMR230W; -.
DR SGD; S000004843; RPS10B.
DR VEuPathDB; FungiDB:YMR230W; -.
DR eggNOG; KOG3344; Eukaryota.
DR GeneTree; ENSGT00940000166022; -.
DR HOGENOM; CLU_089349_4_1_1; -.
DR InParanoid; P46784; -.
DR OMA; NWQHLYF; -.
DR BioCyc; YEAST:G3O-32911-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:P46784; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P46784; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0034198; P:cellular response to amino acid starvation; IDA:UniProtKB.
DR GO; GO:0002181; P:cytoplasmic translation; NAS:SGD.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0006407; P:rRNA export from nucleus; IGI:SGD.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR037447; Rps10.
DR InterPro; IPR005326; S10_plectin_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12146; PTHR12146; 1.
DR Pfam; PF03501; S10_plectin; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT CHAIN 1..105
FT /note="40S ribosomal protein S10-B"
FT /id="PRO_0000116377"
FT HELIX 5..18
FT /evidence="ECO:0007829|PDB:4U3M"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:4U3M"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:4U3M"
FT HELIX 39..51
FT /evidence="ECO:0007829|PDB:4U3M"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:4U3M"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:4U3M"
FT HELIX 70..79
FT /evidence="ECO:0007829|PDB:4U3M"
SQ SEQUENCE 105 AA; 12738 MW; BE50B625869963CF CRC64;
MLMPKQERNK IHQYLFQEGV VVAKKDFNQA KHEEIDTKNL YVIKALQSLT SKGYVKTQFS
WQYYYYTLTE EGVEYLREYL NLPEHIVPGT YIQERNPSQR PQRRY
