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RL13B_YEAST
ID   RL13B_YEAST             Reviewed;         199 AA.
AC   P40212; D6VZW4;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 162.
DE   RecName: Full=60S ribosomal protein L13-B {ECO:0000303|PubMed:9559554};
DE   AltName: Full=Large ribosomal subunit protein eL13-B {ECO:0000303|PubMed:24524803};
GN   Name=RPL13B {ECO:0000303|PubMed:9559554}; Synonyms=RPL13;
GN   OrderedLocusNames=YMR142C; ORFNames=YM9375.11C;
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   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   [5]
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-144 AND THR-152, 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   [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   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 large ribosomal subunit (LSU). 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       {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 54200 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- MISCELLANEOUS: There are 2 genes for eL13 in yeast. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL13 family.
CC       {ECO:0000305}.
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DR   EMBL; Z47071; CAA87356.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA10038.1; -; Genomic_DNA.
DR   PIR; S50398; S50398.
DR   RefSeq; NP_013862.1; NM_001182644.1.
DR   PDB; 4V91; EM; 3.70 A; L=1-199.
DR   PDBsum; 4V91; -.
DR   AlphaFoldDB; P40212; -.
DR   SMR; P40212; -.
DR   BioGRID; 35318; 90.
DR   DIP; DIP-2591N; -.
DR   IntAct; P40212; 61.
DR   MINT; P40212; -.
DR   STRING; 4932.YMR142C; -.
DR   iPTMnet; P40212; -.
DR   MaxQB; P40212; -.
DR   PaxDb; P40212; -.
DR   PRIDE; P40212; -.
DR   TopDownProteomics; P40212; -.
DR   EnsemblFungi; YMR142C_mRNA; YMR142C; YMR142C.
DR   GeneID; 855173; -.
DR   KEGG; sce:YMR142C; -.
DR   SGD; S000004750; RPL13B.
DR   VEuPathDB; FungiDB:YMR142C; -.
DR   eggNOG; KOG3295; Eukaryota.
DR   GeneTree; ENSGT00390000007818; -.
DR   HOGENOM; CLU_075696_1_0_1; -.
DR   InParanoid; P40212; -.
DR   OMA; NQQIPHN; -.
DR   BioCyc; YEAST:G3O-32834-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-72689; Formation of a pool of free 40S subunits.
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   ChiTaRS; RPL16A; yeast.
DR   PRO; PR:P40212; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P40212; protein.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
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:0002181; P:cytoplasmic translation; IC:SGD.
DR   GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR   HAMAP; MF_00499; Ribosomal_L13e; 1.
DR   InterPro; IPR001380; Ribosomal_L13e.
DR   InterPro; IPR018256; Ribosomal_L13e_CS.
DR   PANTHER; PTHR11722; PTHR11722; 1.
DR   Pfam; PF01294; Ribosomal_L13e; 1.
DR   PROSITE; PS01104; RIBOSOMAL_L13E; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Phosphoprotein; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein.
FT   CHAIN           1..199
FT                   /note="60S ribosomal protein L13-B"
FT                   /id="PRO_0000192939"
FT   MOD_RES         144
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         152
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   199 AA;  22525 MW;  BEA3B423EE76EF23 CRC64;
     MAISKNLPIL KNHFRKHWQE RVKVHFDQAG KKVSRRNARA ARAAKIAPRP LDLLRPVVRA
     PTVKYNRKVR AGRGFTLAEV KAAGLTAAYA RTIGIAVDHR RQNRNQEIFD ANVQRLKEYQ
     SKIIVFPRDG KAPEAEQVLS AAATFPIAQP ATDVEARAVQ DNGESAFRTL RLARSEKKFR
     GIREKRAREK AEAEAEKKK
 
 
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