RLA4_YEAST
ID RLA4_YEAST Reviewed; 110 AA.
AC P02400; D6VT16;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=60S acidic ribosomal protein P2-beta {ECO:0000303|PubMed:9559554};
DE AltName: Full=L12eIA;
DE AltName: Full=L45;
DE AltName: Full=Large ribosomal subunit protein P2-B {ECO:0000303|PubMed:24524803};
DE Short=P2B;
DE AltName: Full=YL44C;
DE AltName: Full=YP2beta;
DE AltName: Full=YPA1;
GN Name=RPP2B {ECO:0000303|PubMed:9559554}; Synonyms=L12EIA, RPL45, RPLA4;
GN OrderedLocusNames=YDR382W;
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=2837476; DOI=10.1016/s0021-9258(19)76513-2;
RA Remacha M., Saenz-Robles M.T., Vilella M.D., Ballesta J.P.G.;
RT "Independent genes coding for three acidic proteins of the large ribosomal
RT subunit from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 263:9094-9101(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SR26-12C;
RX PubMed=2404943; DOI=10.1128/jb.172.2.579-588.1990;
RA Newton C.H., Shimmin L.C., Yee J., Dennis P.P.;
RT "A family of genes encode the multiple forms of the Saccharomyces
RT cerevisiae ribosomal proteins equivalent to the Escherichia coli L12
RT protein and a single form of the L10-equivalent ribosomal protein.";
RL J. Bacteriol. 172:579-588(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 PROTEIN SEQUENCE.
RX PubMed=7030402; DOI=10.1016/0005-2795(81)90088-x;
RA Itoh T.;
RT "Primary structure of an acidic ribosomal protein YPA1 from Saccharomyces
RT cerevisiae. Isolation and characterization of peptides and the complete
RT amino acid sequence.";
RL Biochim. Biophys. Acta 671:16-24(1981).
RN [6]
RP PROTEIN SEQUENCE OF 1-6.
RX PubMed=8476850; DOI=10.1021/bi00067a010;
RA Santos C., Ortiz-Reyes B., Naranda T., Remacha M., Ballesta J.P.G.;
RT "The acidic phosphoproteins from Saccharomyces cerevisiae ribosomes. NH2-
RT terminal acetylation is a conserved difference between P1 and P2
RT proteins.";
RL Biochemistry 32:4231-4236(1993).
RN [7]
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 [8]
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 [9]
RP INTERACTION WITH RPP1A.
RX PubMed=11431471; DOI=10.1074/jbc.m103229200;
RA Guarinos E., Remacha M., Ballesta J.P.G.;
RT "Asymmetric interactions between the acidic P1 and P2 proteins in the
RT Saccharomyces cerevisiae ribosomal stalk.";
RL J. Biol. Chem. 276:32474-32479(2001).
RN [10]
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 [11]
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 [12]
RP INTERACTION WITH RPP0 AND RPP1A.
RX PubMed=16573688; DOI=10.1111/j.1365-2958.2006.05117.x;
RA Krokowski D., Boguszewska A., Abramczyk D., Liljas A., Tchorzewski M.,
RA Grankowski N.;
RT "Yeast ribosomal P0 protein has two separate binding sites for P1/P2
RT proteins.";
RL Mol. Microbiol. 60:386-400(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION BY
RP 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 [17]
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 [18]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-49, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [19]
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). The 5
CC acidic ribosomal P-proteins form the stalk structure of the 60S
CC subunit. They are organized as a pentameric complex in which uL10/P0
CC interacts with 2 heterodimers, P1A-P2B and P1B-P2A (PubMed:16573688,
CC PubMed:11431471). {ECO:0000269|PubMed:11431471,
CC ECO:0000269|PubMed:16573688, ECO:0000269|PubMed:22096102,
CC ECO:0000305|PubMed:9559554}.
CC -!- INTERACTION:
CC P02400; P05318: RPP1A; NbExp=2; IntAct=EBI-15464, EBI-15452;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:22096102}.
CC -!- PTM: The N-terminus is not modified. {ECO:0000269|PubMed:8476850}.
CC -!- MISCELLANEOUS: The 4 small acidic ribosomal P-proteins from yeast can
CC be classified into two couples of similar but not identical sequences.
CC Each couple (P1A/P1B and P2A/P2B) is distinctly related to one of the
CC two acidic ribosomal P-proteins P1/P2 present in multicellular
CC organisms. {ECO:0000305|PubMed:2404943}.
CC -!- MISCELLANEOUS: Present with 602000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J03761; AAA34972.1; -; Genomic_DNA.
DR EMBL; M26505; AAA34732.1; -; Genomic_DNA.
DR EMBL; U28373; AAB64818.1; -; Genomic_DNA.
DR EMBL; U32274; AAB64824.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12226.1; -; Genomic_DNA.
DR PIR; A35109; R5BYA1.
DR RefSeq; NP_010670.3; NM_001180690.3.
DR PDB; 3N2D; X-ray; 2.22 A; B=100-105.
DR PDB; 3N3X; X-ray; 1.70 A; B=100-105.
DR PDBsum; 3N2D; -.
DR PDBsum; 3N3X; -.
DR AlphaFoldDB; P02400; -.
DR SMR; P02400; -.
DR BioGRID; 32443; 386.
DR DIP; DIP-580N; -.
DR IntAct; P02400; 37.
DR MINT; P02400; -.
DR STRING; 4932.YDR382W; -.
DR iPTMnet; P02400; -.
DR MaxQB; P02400; -.
DR PaxDb; P02400; -.
DR PRIDE; P02400; -.
DR TopDownProteomics; P02400; -.
DR EnsemblFungi; YDR382W_mRNA; YDR382W; YDR382W.
DR GeneID; 851990; -.
DR KEGG; sce:YDR382W; -.
DR SGD; S000002790; RPP2B.
DR VEuPathDB; FungiDB:YDR382W; -.
DR eggNOG; KOG3449; Eukaryota.
DR GeneTree; ENSGT00940000176747; -.
DR HOGENOM; CLU_114656_0_1_1; -.
DR InParanoid; P02400; -.
DR OMA; AYLMNVL; -.
DR BioCyc; YEAST:G3O-29930-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; RPP2B; yeast.
DR EvolutionaryTrace; P02400; -.
DR PRO; PR:P02400; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P02400; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0030295; F:protein kinase activator activity; IDA:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IMP:SGD.
DR GO; GO:0002182; P:cytoplasmic translational elongation; IEA:InterPro.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:SGD.
DR CDD; cd05833; Ribosomal_P2; 1.
DR Gene3D; 1.10.10.1410; -; 1.
DR HAMAP; MF_01478; Ribosomal_L12_arch; 1.
DR InterPro; IPR038716; P1/P2_N_sf.
DR InterPro; IPR027534; Ribosomal_L12/P1/P2.
DR InterPro; IPR044076; Ribosomal_P2.
DR PANTHER; PTHR21141; PTHR21141; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT CHAIN 1..110
FT /note="60S acidic ribosomal protein P2-beta"
FT /id="PRO_0000157682"
FT REGION 66..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT CROSSLNK 49
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 75..78
FT /note="AAGA -> GPAS (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 86..87
FT /note="DA -> GD (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="E -> A (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 110 AA; 11050 MW; EC45406CB5F199F4 CRC64;
MKYLAAYLLL VQGGNAAPSA ADIKAVVESV GAEVDEARIN ELLSSLEGKG SLEEIIAEGQ
KKFATVPTGG ASSAAAGAAG AAAGGDAAEE EKEEEAKEES DDDMGFGLFD
