RL1A_YEAST
ID RL1A_YEAST Reviewed; 217 AA.
AC P0CX43; D6VU14; P53030;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=60S ribosomal protein L1-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=L10a;
DE AltName: Full=Large ribosomal subunit protein uL1-A {ECO:0000303|PubMed:24524803};
GN Name=RPL1A {ECO:0000303|PubMed:9559554}; Synonyms=SSM1, SSM1A;
GN OrderedLocusNames=YPL220W;
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].
RC STRAIN=ATCC 28383 / FL100 / VTT C-80102;
RX PubMed=7651424; DOI=10.1128/mcb.15.9.5071;
RA Petitjean A., Bonneaud N., Lacroute F.;
RT "The duplicated Saccharomyces cerevisiae gene SSM1 encodes a eucaryotic
RT homolog of the eubacterial and archaebacterial L1 ribosomal proteins.";
RL Mol. Cell. Biol. 15:5071-5081(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
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 [4]
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 [5]
RP CLEAVAGE OF INITIATOR METHIONINE, AND ACETYLATION AT SER-2 BY NATA.
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 [6]
RP MASS SPECTROMETRY.
RX PubMed=11983894; DOI=10.1073/pnas.082119899;
RA Lee S.-W., Berger S.J., Martinovic S., Pasa-Tolic L., Anderson G.A.,
RA Shen Y., Zhao R., Smith R.D.;
RT "Direct mass spectrometric analysis of intact proteins of the yeast large
RT ribosomal subunit using capillary LC/FTICR.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:5942-5947(2002).
RN [7]
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, 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 [10]
RP IDENTIFICATION BY 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79 AND SER-86, 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 [12]
RP METHYLATION AT LYS-47, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21460220; DOI=10.1074/jbc.m110.200410;
RA Webb K.J., Al-Hadid Q., Zurita-Lopez C.I., Young B.D., Lipson R.S.,
RA Clarke S.G.;
RT "The ribosomal L1 protuberance in yeast is methylated on a lysine residue
RT catalyzed by a seven beta-strand methyltransferase.";
RL J. Biol. Chem. 286:18405-18413(2011).
RN [13]
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [15]
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 [16]
RP 3D-STRUCTURE MODELING OF 4-216, AND ELECTRON MICROSCOPY.
RX PubMed=11701127; DOI=10.1016/s0092-8674(01)00539-6;
RA Spahn C.M.T., Beckmann R., Eswar N., Penczek P.A., Sali A., Blobel G.,
RA Frank J.;
RT "Structure of the 80S ribosome from Saccharomyces cerevisiae -- tRNA-
RT ribosome and subunit-subunit interactions.";
RL Cell 107:373-386(2001).
RN [17]
RP 3D-STRUCTURE MODELING, AND ELECTRON MICROSCOPY.
RX PubMed=14976550; DOI=10.1038/sj.emboj.7600102;
RA Spahn C.M.T., Gomez-Lorenzo M.G., Grassucci R.A., Joergensen R.,
RA Andersen G.R., Beckmann R., Penczek P.A., Ballesta J.P.G., Frank J.;
RT "Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome
RT facilitate tRNA translocation.";
RL EMBO J. 23:1008-1019(2004).
RN [18]
RP STRUCTURE BY ELECTRON MICROSCOPY (7.3 ANGSTROMS) OF 4-216.
RX PubMed=17115051; DOI=10.1038/nsmb1177;
RA Schueler M., Connell S.R., Lescoute A., Giesebrecht J., Dabrowski M.,
RA Schroeer B., Mielke T., Penczek P.A., Westhof E., Spahn C.M.T.;
RT "Structure of the ribosome-bound cricket paralysis virus IRES RNA.";
RL Nat. Struct. Mol. Biol. 13:1092-1096(2006).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS) OF 80S RIBOSOME.
RX PubMed=21109664; DOI=10.1126/science.1194294;
RA Ben-Shem A., Jenner L., Yusupova G., Yusupov M.;
RT "Crystal structure of the eukaryotic ribosome.";
RL Science 330:1203-1209(2010).
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. uL1 forms part of the L1 stalk, a mobile element that plays a
CC role in evacuating the exit-site tRNA. {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). uL1 forms part of the L1 stalk
CC (PubMed:9559554, PubMed:22096102). {ECO:0000269|PubMed:22096102,
CC ECO:0000305|PubMed:9559554}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:22096102}.
CC -!- PTM: N-terminally acetylated by acetyltransferase NatA.
CC {ECO:0000269|PubMed:10601260}.
CC -!- MASS SPECTROMETRY: Mass=24410.862; Method=Electrospray; Note=Average
CC mass with 1 acetylation and 1 methylation modification.;
CC Evidence={ECO:0000269|PubMed:11983894};
CC -!- MISCELLANEOUS: Present with 116000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for uL1 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family.
CC {ECO:0000305}.
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DR EMBL; X70985; CAA50314.1; -; Genomic_DNA.
DR EMBL; Z73576; CAA97935.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11216.1; -; Genomic_DNA.
DR PIR; S53893; S53893.
DR RefSeq; NP_011380.3; NM_001181000.3.
DR RefSeq; NP_015104.1; NM_001184034.1.
DR PDB; 2NOQ; EM; 7.30 A; G=4-216.
DR PDB; 3J0P; EM; 10.60 A; B=4-216.
DR PDB; 3J0Q; EM; 10.60 A; B=4-216.
DR PDB; 3J6X; EM; 6.10 A; L1=1-217.
DR PDB; 3J6Y; EM; 6.10 A; L1=1-217.
DR PDB; 3J77; EM; 6.20 A; L1=1-217.
DR PDB; 3J78; EM; 6.30 A; L1=1-217.
DR PDB; 4V4B; EM; 11.70 A; BA=1-217.
DR PDB; 4V6I; EM; 8.80 A; BA=1-217.
DR PDB; 4V7F; EM; 8.70 A; A=1-217.
DR PDB; 4V7H; EM; 8.90 A; A=4-216.
DR PDB; 4V7R; X-ray; 4.00 A; BA/DA=1-217.
DR PDB; 4V91; EM; 3.70 A; t=1-217.
DR PDB; 5JCS; EM; 9.50 A; I=1-217.
DR PDB; 5JUO; EM; 4.00 A; E=1-217.
DR PDB; 5JUP; EM; 3.50 A; E=1-217.
DR PDB; 5JUS; EM; 4.20 A; E=1-217.
DR PDB; 5JUT; EM; 4.00 A; E=1-217.
DR PDB; 5JUU; EM; 4.00 A; E=1-217.
DR PDB; 6GQB; EM; 3.90 A; BA=13-216.
DR PDB; 6GQV; EM; 4.00 A; BA=13-216.
DR PDB; 6OIG; EM; 3.80 A; z=13-216.
DR PDB; 6R84; EM; 3.60 A; L=13-216.
DR PDB; 6R86; EM; 3.40 A; L=13-216.
DR PDB; 6R87; EM; 3.40 A; L=13-216.
DR PDB; 6TB3; EM; 2.80 A; BT=13-216.
DR PDB; 6WOO; EM; 2.90 A; q=1-217.
DR PDB; 6YLG; EM; 3.00 A; o=1-217.
DR PDB; 6YLH; EM; 3.10 A; o=1-217.
DR PDBsum; 2NOQ; -.
DR PDBsum; 3J0P; -.
DR PDBsum; 3J0Q; -.
DR PDBsum; 3J6X; -.
DR PDBsum; 3J6Y; -.
DR PDBsum; 3J77; -.
DR PDBsum; 3J78; -.
DR PDBsum; 4V4B; -.
DR PDBsum; 4V6I; -.
DR PDBsum; 4V7F; -.
DR PDBsum; 4V7H; -.
DR PDBsum; 4V7R; -.
DR PDBsum; 4V91; -.
DR PDBsum; 5JCS; -.
DR PDBsum; 5JUO; -.
DR PDBsum; 5JUP; -.
DR PDBsum; 5JUS; -.
DR PDBsum; 5JUT; -.
DR PDBsum; 5JUU; -.
DR PDBsum; 6GQB; -.
DR PDBsum; 6GQV; -.
DR PDBsum; 6OIG; -.
DR PDBsum; 6R84; -.
DR PDBsum; 6R86; -.
DR PDBsum; 6R87; -.
DR PDBsum; 6TB3; -.
DR PDBsum; 6WOO; -.
DR PDBsum; 6YLG; -.
DR PDBsum; 6YLH; -.
DR AlphaFoldDB; P0CX43; -.
DR SMR; P0CX43; -.
DR BioGRID; 33117; 190.
DR BioGRID; 35965; 159.
DR IntAct; P0CX43; 7.
DR MINT; P0CX43; -.
DR STRING; 4932.YGL135W; -.
DR iPTMnet; P0CX43; -.
DR MaxQB; P0CX43; -.
DR PaxDb; P0CX43; -.
DR PRIDE; P0CX43; -.
DR TopDownProteomics; P0CX43; -.
DR EnsemblFungi; YGL135W_mRNA; YGL135W; YGL135W.
DR EnsemblFungi; YPL220W_mRNA; YPL220W; YPL220W.
DR GeneID; 852742; -.
DR GeneID; 855881; -.
DR KEGG; sce:YGL135W; -.
DR KEGG; sce:YPL220W; -.
DR SGD; S000006141; RPL1A.
DR VEuPathDB; FungiDB:YGL135W; -.
DR VEuPathDB; FungiDB:YPL220W; -.
DR eggNOG; KOG1570; Eukaryota.
DR HOGENOM; CLU_062853_3_0_1; -.
DR InParanoid; P0CX43; -.
DR OMA; TMAINFL; -.
DR BioCyc; YEAST:G3O-34109-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; RPL1A; yeast.
DR EvolutionaryTrace; P0CX43; -.
DR PRO; PR:P0CX43; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P0CX43; protein.
DR ExpressionAtlas; P0CX43; baseline and differential.
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; IC:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:SGD.
DR CDD; cd00403; Ribosomal_L1; 1.
DR Gene3D; 3.40.50.790; -; 1.
DR InterPro; IPR002143; Ribosomal_L1.
DR InterPro; IPR023674; Ribosomal_L1-like.
DR InterPro; IPR028364; Ribosomal_L1/biogenesis.
DR InterPro; IPR016095; Ribosomal_L1_3-a/b-sand.
DR InterPro; IPR023673; Ribosomal_L1_CS.
DR Pfam; PF00687; Ribosomal_L1; 1.
DR PIRSF; PIRSF002155; Ribosomal_L1; 1.
DR SUPFAM; SSF56808; SSF56808; 1.
DR PROSITE; PS01199; RIBOSOMAL_L1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Methylation; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..217
FT /note="60S ribosomal protein L1-A"
FT /id="PRO_0000125842"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:10601260,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 47
FT /note="N6-methyllysine; by RKM5"
FT /evidence="ECO:0000269|PubMed:21460220"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 217 AA; 24486 MW; C890A90505655F2A CRC64;
MSKITSSQVR EHVKELLKYS NETKKRNFLE TVELQVGLKN YDPQRDKRFS GSLKLPNCPR
PNMSICIFGD AFDVDRAKSC GVDAMSVDDL KKLNKNKKLI KKLSKKYNAF IASEVLIKQV
PRLLGPQLSK AGKFPTPVSH NDDLYGKVTD VRSTIKFQLK KVLCLAVAVG NVEMEEDVLV
NQILMSVNFF VSLLKKNWQN VGSLVVKSSM GPAFRLY
