RL9_HUMAN
ID RL9_HUMAN Reviewed; 192 AA.
AC P32969;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 221.
DE RecName: Full=60S ribosomal protein L9;
DE AltName: Full=Large ribosomal subunit protein uL6 {ECO:0000303|PubMed:24524803};
GN Name=RPL9; ORFNames=OK/SW-cl.103;
GN and
GN Name=RPL9P7;
GN and
GN Name=RPL9P8;
GN and
GN Name=RPL9P9;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8415001; DOI=10.1093/nar/21.18.4395;
RA Hori N., Murakawa K., Matoba R., Fukushima A., Okubo K., Matsubara K.;
RT "A new human ribosomal protein sequence, homologue of rat L9.";
RL Nucleic Acids Res. 21:4395-4395(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=8597601; DOI=10.1016/0167-4781(95)00201-4;
RA Mazuruk K., Schoen T.J., Chader G.J., Iwata T., Rodriguez I.R.;
RT "Structural organization and chromosomal localization of the human
RT ribosomal protein L9 gene.";
RL Biochim. Biophys. Acta 1305:151-162(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Williams J.H., Pearse M.J., Power D.A.;
RT "Human homolog of rat ribosomal protein L9.";
RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-reactive
RT CTL generated from TIL of colon cancer patients.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Muscle, Placenta, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 1-21; 36-51; 94-115; 142-168 AND 174-184, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Bilsland A.E., Keith W.N.;
RL Submitted (JAN-2010) to UniProtKB.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 146-192.
RX PubMed=9582194; DOI=10.1101/gr.8.5.509;
RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J.,
RA Tanaka T., Page D.C.;
RT "A map of 75 human ribosomal protein genes.";
RL Genome Res. 8:509-523(1998).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-121, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
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 [12]
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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP STRUCTURE BY NMR OF 1-87.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the N-terminal domain of human ribosomal protein
RT L9.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [16]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
RN [17] {ECO:0007744|PDB:6LQM, ECO:0007744|PDB:6LSR, ECO:0007744|PDB:6LSS, ECO:0007744|PDB:6LU8}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.09 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=32669547; DOI=10.1038/s41467-020-17237-x;
RA Liang X., Zuo M.Q., Zhang Y., Li N., Ma C., Dong M.Q., Gao N.;
RT "Structural snapshots of human pre-60S ribosomal particles before and after
RT nuclear export.";
RL Nat. Commun. 11:3542-3542(2020).
CC -!- FUNCTION: Component of the large ribosomal subunit (PubMed:23636399,
CC PubMed:32669547). The ribosome is a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell (PubMed:23636399,
CC PubMed:32669547). {ECO:0000269|PubMed:23636399,
CC ECO:0000269|PubMed:32669547}.
CC -!- SUBUNIT: Component of the large ribosomal subunit.
CC {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547}.
CC -!- INTERACTION:
CC P32969; Q9BYV9: BACH2; NbExp=3; IntAct=EBI-358122, EBI-1642333;
CC P32969; A1A5D9: BICDL2; NbExp=3; IntAct=EBI-358122, EBI-10171799;
CC P32969; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-358122, EBI-739580;
CC P32969; Q8NA61: CBY2; NbExp=3; IntAct=EBI-358122, EBI-741724;
CC P32969; Q52MB2: CCDC184; NbExp=6; IntAct=EBI-358122, EBI-10179526;
CC P32969; Q8TAP6: CEP76; NbExp=7; IntAct=EBI-358122, EBI-742887;
CC P32969; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-358122, EBI-11962928;
CC P32969; Q14247-3: CTTN; NbExp=3; IntAct=EBI-358122, EBI-12748199;
CC P32969; P49366: DHPS; NbExp=11; IntAct=EBI-358122, EBI-741925;
CC P32969; Q14919: DRAP1; NbExp=3; IntAct=EBI-358122, EBI-712941;
CC P32969; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-358122, EBI-10175124;
CC P32969; V9HW80: HEL-S-70; NbExp=3; IntAct=EBI-358122, EBI-10175326;
CC P32969; Q6NT76: HMBOX1; NbExp=6; IntAct=EBI-358122, EBI-2549423;
CC P32969; Q8IX15-3: HOMEZ; NbExp=3; IntAct=EBI-358122, EBI-10172004;
CC P32969; Q9BQD3: KXD1; NbExp=3; IntAct=EBI-358122, EBI-739657;
CC P32969; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-358122, EBI-742948;
CC P32969; Q9UL42: PNMA2; NbExp=6; IntAct=EBI-358122, EBI-302355;
CC P32969; Q86WC6: PPP1R27; NbExp=3; IntAct=EBI-358122, EBI-5235602;
CC P32969; O43586: PSTPIP1; NbExp=3; IntAct=EBI-358122, EBI-1050964;
CC P32969; Q53GL6: RALY; NbExp=3; IntAct=EBI-358122, EBI-9512693;
CC P32969; P62306: SNRPF; NbExp=3; IntAct=EBI-358122, EBI-356900;
CC P32969; Q8N9Q2: SREK1IP1; NbExp=3; IntAct=EBI-358122, EBI-10268630;
CC P32969; P84103: SRSF3; NbExp=3; IntAct=EBI-358122, EBI-372557;
CC P32969; Q96MF2: STAC3; NbExp=3; IntAct=EBI-358122, EBI-745680;
CC P32969; Q96CG3: TIFA; NbExp=6; IntAct=EBI-358122, EBI-740711;
CC P32969; Q8WVP5: TNFAIP8L1; NbExp=3; IntAct=EBI-358122, EBI-752102;
CC P32969; O94972: TRIM37; NbExp=3; IntAct=EBI-358122, EBI-741602;
CC P32969; P55072: VCP; NbExp=3; IntAct=EBI-358122, EBI-355164;
CC P32969; O43829: ZBTB14; NbExp=3; IntAct=EBI-358122, EBI-10176632;
CC P32969; O15156: ZBTB7B; NbExp=3; IntAct=EBI-358122, EBI-740434;
CC P32969; Q96BR9: ZBTB8A; NbExp=6; IntAct=EBI-358122, EBI-742740;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL6 family.
CC {ECO:0000305}.
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DR EMBL; D14531; BAA03401.1; -; mRNA.
DR EMBL; U09953; AAB01040.1; -; mRNA.
DR EMBL; U09954; AAB01041.1; -; Genomic_DNA.
DR EMBL; U21138; AAA63752.1; -; mRNA.
DR EMBL; AB062431; BAB93494.1; -; mRNA.
DR EMBL; BC000483; AAH00483.1; -; mRNA.
DR EMBL; BC004156; AAH04156.1; -; mRNA.
DR EMBL; BC004206; AAH04206.1; -; mRNA.
DR EMBL; BC007967; AAH07967.1; -; mRNA.
DR EMBL; BC012149; AAH12149.1; -; mRNA.
DR EMBL; BC031906; AAH31906.1; -; mRNA.
DR EMBL; BC066318; AAH66318.1; -; mRNA.
DR EMBL; BC070214; AAH70214.1; -; mRNA.
DR EMBL; AB007169; BAA25830.1; -; Genomic_DNA.
DR CCDS; CCDS3452.1; -.
DR PIR; S65792; S65792.
DR RefSeq; NP_000652.2; NM_000661.4.
DR RefSeq; NP_001020092.1; NM_001024921.3.
DR PDB; 2CQL; NMR; -; A=1-87.
DR PDB; 4UG0; EM; -; LH=1-192.
DR PDB; 4V6X; EM; 5.00 A; CH=1-192.
DR PDB; 5AJ0; EM; 3.50 A; AH=1-192.
DR PDB; 5LKS; EM; 3.60 A; LH=1-192.
DR PDB; 5T2C; EM; 3.60 A; o=1-192.
DR PDB; 6IP5; EM; 3.90 A; 2C=1-192.
DR PDB; 6IP6; EM; 4.50 A; 2C=1-192.
DR PDB; 6IP8; EM; 3.90 A; 2C=1-192.
DR PDB; 6LQM; EM; 3.09 A; I=1-192.
DR PDB; 6LSR; EM; 3.13 A; I=1-192.
DR PDB; 6LSS; EM; 3.23 A; I=1-192.
DR PDB; 6LU8; EM; 3.13 A; I=1-192.
DR PDB; 6OLE; EM; 3.10 A; J=1-191.
DR PDB; 6OLF; EM; 3.90 A; J=1-191.
DR PDB; 6OLG; EM; 3.40 A; AH=1-191.
DR PDB; 6OLI; EM; 3.50 A; J=1-191.
DR PDB; 6OLZ; EM; 3.90 A; AH=1-191.
DR PDB; 6OM0; EM; 3.10 A; J=1-191.
DR PDB; 6OM7; EM; 3.70 A; J=1-191.
DR PDB; 6QZP; EM; 2.90 A; LH=1-190.
DR PDB; 6W6L; EM; 3.84 A; J=1-192.
DR PDB; 6XA1; EM; 2.80 A; LH=1-190.
DR PDB; 6Y0G; EM; 3.20 A; LH=1-192.
DR PDB; 6Y2L; EM; 3.00 A; LH=1-192.
DR PDB; 6Y57; EM; 3.50 A; LH=1-192.
DR PDB; 6Y6X; EM; 2.80 A; LH=1-190.
DR PDB; 6Z6L; EM; 3.00 A; LH=1-192.
DR PDB; 6Z6M; EM; 3.10 A; LH=1-192.
DR PDB; 6Z6N; EM; 2.90 A; LH=1-192.
DR PDB; 6ZM7; EM; 2.70 A; LH=1-192.
DR PDB; 6ZME; EM; 3.00 A; LH=1-192.
DR PDB; 6ZMI; EM; 2.60 A; LH=1-192.
DR PDB; 6ZMO; EM; 3.10 A; LH=1-192.
DR PDB; 7BHP; EM; 3.30 A; LH=1-192.
DR PDBsum; 2CQL; -.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 5AJ0; -.
DR PDBsum; 5LKS; -.
DR PDBsum; 5T2C; -.
DR PDBsum; 6IP5; -.
DR PDBsum; 6IP6; -.
DR PDBsum; 6IP8; -.
DR PDBsum; 6LQM; -.
DR PDBsum; 6LSR; -.
DR PDBsum; 6LSS; -.
DR PDBsum; 6LU8; -.
DR PDBsum; 6OLE; -.
DR PDBsum; 6OLF; -.
DR PDBsum; 6OLG; -.
DR PDBsum; 6OLI; -.
DR PDBsum; 6OLZ; -.
DR PDBsum; 6OM0; -.
DR PDBsum; 6OM7; -.
DR PDBsum; 6QZP; -.
DR PDBsum; 6W6L; -.
DR PDBsum; 6XA1; -.
DR PDBsum; 6Y0G; -.
DR PDBsum; 6Y2L; -.
DR PDBsum; 6Y57; -.
DR PDBsum; 6Y6X; -.
DR PDBsum; 6Z6L; -.
DR PDBsum; 6Z6M; -.
DR PDBsum; 6Z6N; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 7BHP; -.
DR AlphaFoldDB; P32969; -.
DR SMR; P32969; -.
DR BioGRID; 112053; 316.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR CORUM; P32969; -.
DR IntAct; P32969; 89.
DR MINT; P32969; -.
DR STRING; 9606.ENSP00000400467; -.
DR GlyGen; P32969; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P32969; -.
DR MetOSite; P32969; -.
DR PhosphoSitePlus; P32969; -.
DR SwissPalm; P32969; -.
DR BioMuta; RPL9; -.
DR DMDM; 417677; -.
DR SWISS-2DPAGE; P32969; -.
DR EPD; P32969; -.
DR jPOST; P32969; -.
DR MassIVE; P32969; -.
DR PaxDb; P32969; -.
DR PeptideAtlas; P32969; -.
DR PRIDE; P32969; -.
DR ProteomicsDB; 54893; -.
DR TopDownProteomics; P32969; -.
DR Antibodypedia; 1250; 242 antibodies from 27 providers.
DR DNASU; 6133; -.
DR Ensembl; ENST00000295955.14; ENSP00000346022.7; ENSG00000163682.17.
DR Ensembl; ENST00000449470.6; ENSP00000400467.2; ENSG00000163682.17.
DR Ensembl; ENST00000645496.2; ENSP00000494697.1; ENSG00000163682.17.
DR GeneID; 6133; -.
DR KEGG; hsa:6133; -.
DR MANE-Select; ENST00000295955.14; ENSP00000346022.7; NM_000661.5; NP_000652.2.
DR CTD; 6133; -.
DR DisGeNET; 6133; -.
DR GeneCards; RPL9; -.
DR GeneCards; RPL9P7; -.
DR GeneCards; RPL9P8; -.
DR HGNC; HGNC:10369; RPL9.
DR HPA; ENSG00000163682; Low tissue specificity.
DR MIM; 603686; gene.
DR neXtProt; NX_P32969; -.
DR OpenTargets; ENSG00000163682; -.
DR PharmGKB; PA34769; -.
DR VEuPathDB; HostDB:ENSG00000163682; -.
DR eggNOG; KOG3255; Eukaryota.
DR GeneTree; ENSGT00390000015224; -.
DR InParanoid; P32969; -.
DR OMA; VFQDGIY; -.
DR OrthoDB; 1408258at2759; -.
DR PhylomeDB; P32969; -.
DR TreeFam; TF300033; -.
DR PathwayCommons; P32969; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-156902; Peptide chain elongation.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-192823; Viral mRNA Translation.
DR Reactome; R-HSA-2408557; Selenocysteine synthesis.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-HSA-72764; Eukaryotic Translation Termination.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency.
DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P32969; -.
DR SIGNOR; P32969; -.
DR BioGRID-ORCS; 6133; 477 hits in 1071 CRISPR screens.
DR ChiTaRS; RPL9; human.
DR ChiTaRS; RPL9P8; human.
DR EvolutionaryTrace; P32969; -.
DR GeneWiki; RPL9; -.
DR GenomeRNAi; 6133; -.
DR Pharos; P32969; Tbio.
DR PRO; PR:P32969; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P32969; protein.
DR Bgee; ENSG00000163682; Expressed in cortical plate and 112 other tissues.
DR ExpressionAtlas; P32969; baseline and differential.
DR Genevisible; P32969; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IPI:ComplexPortal.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0005840; C:ribosome; TAS:ProtInc.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0019843; F:rRNA binding; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
DR Gene3D; 3.90.930.12; -; 2.
DR InterPro; IPR000702; Ribosomal_L6.
DR InterPro; IPR020040; Ribosomal_L6_a/b-dom.
DR InterPro; IPR036789; Ribosomal_L6_a/b-dom_sf.
DR InterPro; IPR002359; Ribosomal_L6_CS2.
DR PANTHER; PTHR11655; PTHR11655; 1.
DR Pfam; PF00347; Ribosomal_L6; 2.
DR PIRSF; PIRSF002162; Ribosomal_L6; 1.
DR SUPFAM; SSF56053; SSF56053; 2.
DR PROSITE; PS00700; RIBOSOMAL_L6_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..192
FT /note="60S ribosomal protein L9"
FT /id="PRO_0000131097"
FT MOD_RES 121
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CONFLICT 11
FT /note="D -> E (in Ref. 2; AAB01040/AAB01041)"
FT /evidence="ECO:0000305"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:2CQL"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:2CQL"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:2CQL"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:2CQL"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:2CQL"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:2CQL"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:2CQL"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2CQL"
FT HELIX 65..85
FT /evidence="ECO:0007829|PDB:2CQL"
SQ SEQUENCE 192 AA; 21863 MW; 0249E6CA12F77934 CRC64;
MKTILSNQTV DIPENVDITL KGRTVIVKGP RGTLRRDFNH INVELSLLGK KKKRLRVDKW
WGNRKELATV RTICSHVQNM IKGVTLGFRY KMRSVYAHFP INVVIQENGS LVEIRNFLGE
KYIRRVRMRP GVACSVSQAQ KDELILEGND IELVSNSAAL IQQATTVKNK DIRKFLDGIY
VSEKGTVQQA DE
