RL34_HUMAN
ID RL34_HUMAN Reviewed; 117 AA.
AC P49207; Q6FG66; Q9BUZ2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=60S ribosomal protein L34;
DE AltName: Full=Large ribosomal subunit protein eL34 {ECO:0000303|PubMed:24524803};
GN Name=RPL34;
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=Ovary;
RX PubMed=7490091; DOI=10.1006/geno.1995.1185;
RA Rommens J.M., Durocher F., McArthur J., Tonin P., Leblanc J.-F., Allen T.,
RA Samson C., Ferri L., Narod S., Morgan K., Simard J.;
RT "Generation of a transcription map at the HSD17B locus centromeric to BRCA1
RT at 17q21.";
RL Genomics 28:530-542(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11875025; DOI=10.1101/gr.214202;
RA Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S.,
RA Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.;
RT "The human ribosomal protein genes: sequencing and comparative analysis of
RT 73 genes.";
RL Genome Res. 12:379-390(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone, and Eye;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-48.
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 [6]
RP PROTEIN SEQUENCE OF 2-12, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP AND SUBUNIT.
RX PubMed=12962325; DOI=10.1023/a:1025068419698;
RA Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R.,
RA Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B., Karpova G.G.;
RT "Characterization and analysis of posttranslational modifications of the
RT human large cytoplasmic ribosomal subunit proteins by mass spectrometry and
RT Edman sequencing.";
RL J. Protein Chem. 22:249-258(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-36, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
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 [14]
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 [15]
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 [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-108, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [17]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
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 [18] {ECO:0007744|PDB:5AJ0}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=25957688; DOI=10.1016/j.cell.2015.03.052;
RA Behrmann E., Loerke J., Budkevich T.V., Yamamoto K., Schmidt A.,
RA Penczek P.A., Vos M.R., Burger J., Mielke T., Scheerer P., Spahn C.M.;
RT "Structural snapshots of actively translating human ribosomes.";
RL Cell 161:845-857(2015).
RN [19] {ECO:0007744|PDB:4UG0}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=25901680; DOI=10.1038/nature14427;
RA Khatter H., Myasnikov A.G., Natchiar S.K., Klaholz B.P.;
RT "Structure of the human 80S ribosome.";
RL Nature 520:640-645(2015).
RN [20] {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:12962325,
CC PubMed:23636399, PubMed:25957688, PubMed:25901680, PubMed:32669547).
CC The ribosome is a large ribonucleoprotein complex responsible for the
CC synthesis of proteins in the cell (PubMed:12962325, PubMed:23636399,
CC PubMed:25957688, PubMed:25901680, PubMed:32669547).
CC {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:25901680,
CC ECO:0000269|PubMed:25957688, ECO:0000269|PubMed:32669547,
CC ECO:0000305|PubMed:12962325}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (PubMed:12962325,
CC PubMed:23636399, PubMed:25957688, PubMed:25901680, PubMed:32669547).
CC {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:25901680,
CC ECO:0000269|PubMed:25957688, ECO:0000269|PubMed:32669547,
CC ECO:0000305|PubMed:12962325}.
CC -!- INTERACTION:
CC P49207; Q5S007: LRRK2; NbExp=3; IntAct=EBI-1051893, EBI-5323863;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:25957688}.
CC Cytoplasm {ECO:0000305|PubMed:23636399, ECO:0000305|PubMed:25901680}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:Q29223}. Note=Detected on
CC cytosolic polysomes (PubMed:25957688). Detected in ribosomes that are
CC associated with the rough endoplasmic reticulum (By similarity).
CC {ECO:0000250|UniProtKB:Q29223, ECO:0000269|PubMed:25957688}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL34 family.
CC {ECO:0000305}.
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DR EMBL; L38941; AAC41916.1; -; mRNA.
DR EMBL; AB061832; BAB79470.1; -; Genomic_DNA.
DR EMBL; CR542232; CAG47028.1; -; mRNA.
DR EMBL; CR542242; CAG47038.1; -; mRNA.
DR EMBL; BC001773; AAH01773.1; -; mRNA.
DR EMBL; BC070208; AAH70208.1; -; mRNA.
DR EMBL; BC106009; AAI06010.1; -; mRNA.
DR EMBL; AB007181; BAA25840.1; -; Genomic_DNA.
DR CCDS; CCDS3680.1; -.
DR PIR; I68524; I68524.
DR RefSeq; NP_000986.2; NM_000995.4.
DR RefSeq; NP_001306161.1; NM_001319232.1.
DR RefSeq; NP_001306163.1; NM_001319234.1.
DR RefSeq; NP_001306164.1; NM_001319235.1.
DR RefSeq; NP_001306165.1; NM_001319236.1.
DR RefSeq; NP_296374.1; NM_033625.3.
DR PDB; 4UG0; EM; -; Lg=1-117.
DR PDB; 4V6X; EM; 5.00 A; Cg=1-117.
DR PDB; 5AJ0; EM; 3.50 A; Ag=1-117.
DR PDB; 5LKS; EM; 3.60 A; Lg=1-117.
DR PDB; 5T2C; EM; 3.60 A; a=1-117.
DR PDB; 6IP5; EM; 3.90 A; 2a=1-117.
DR PDB; 6IP6; EM; 4.50 A; 2a=1-117.
DR PDB; 6IP8; EM; 3.90 A; 2a=1-117.
DR PDB; 6LQM; EM; 3.09 A; F=1-117.
DR PDB; 6LSR; EM; 3.13 A; F=1-117.
DR PDB; 6LSS; EM; 3.23 A; F=1-117.
DR PDB; 6LU8; EM; 3.13 A; F=1-117.
DR PDB; 6OLE; EM; 3.10 A; h=2-115.
DR PDB; 6OLF; EM; 3.90 A; h=2-115.
DR PDB; 6OLG; EM; 3.40 A; Ag=2-115.
DR PDB; 6OLI; EM; 3.50 A; h=2-115.
DR PDB; 6OLZ; EM; 3.90 A; Ag=2-115.
DR PDB; 6OM0; EM; 3.10 A; h=2-115.
DR PDB; 6OM7; EM; 3.70 A; h=2-115.
DR PDB; 6QZP; EM; 2.90 A; Lg=2-115.
DR PDB; 6W6L; EM; 3.84 A; h=1-117.
DR PDB; 6XA1; EM; 2.80 A; Lg=2-115.
DR PDB; 6Y0G; EM; 3.20 A; Lg=1-117.
DR PDB; 6Y2L; EM; 3.00 A; Lg=1-117.
DR PDB; 6Y57; EM; 3.50 A; Lg=1-117.
DR PDB; 6Y6X; EM; 2.80 A; Lg=2-115.
DR PDB; 6Z6L; EM; 3.00 A; Lg=1-117.
DR PDB; 6Z6M; EM; 3.10 A; Lg=1-117.
DR PDB; 6Z6N; EM; 2.90 A; Lg=1-117.
DR PDB; 6ZM7; EM; 2.70 A; Lg=1-117.
DR PDB; 6ZME; EM; 3.00 A; Lg=1-117.
DR PDB; 6ZMI; EM; 2.60 A; Lg=1-117.
DR PDB; 6ZMO; EM; 3.10 A; Lg=1-117.
DR PDB; 7BHP; EM; 3.30 A; Lg=1-117.
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; P49207; -.
DR SMR; P49207; -.
DR BioGRID; 112083; 200.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR CORUM; P49207; -.
DR IntAct; P49207; 48.
DR MINT; P49207; -.
DR STRING; 9606.ENSP00000378163; -.
DR GlyGen; P49207; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P49207; -.
DR MetOSite; P49207; -.
DR PhosphoSitePlus; P49207; -.
DR SwissPalm; P49207; -.
DR BioMuta; RPL34; -.
DR EPD; P49207; -.
DR jPOST; P49207; -.
DR MassIVE; P49207; -.
DR MaxQB; P49207; -.
DR PaxDb; P49207; -.
DR PeptideAtlas; P49207; -.
DR PRIDE; P49207; -.
DR ProteomicsDB; 55970; -.
DR TopDownProteomics; P49207; -.
DR Antibodypedia; 26278; 154 antibodies from 23 providers.
DR DNASU; 6164; -.
DR Ensembl; ENST00000394665.5; ENSP00000378160.1; ENSG00000109475.17.
DR Ensembl; ENST00000394667.8; ENSP00000378162.3; ENSG00000109475.17.
DR Ensembl; ENST00000394668.2; ENSP00000378163.2; ENSG00000109475.17.
DR Ensembl; ENST00000502534.5; ENSP00000423983.1; ENSG00000109475.17.
DR Ensembl; ENST00000506397.5; ENSP00000423316.1; ENSG00000109475.17.
DR GeneID; 6164; -.
DR KEGG; hsa:6164; -.
DR MANE-Select; ENST00000394667.8; ENSP00000378162.3; NM_001319236.2; NP_001306165.1.
DR UCSC; uc003hza.4; human.
DR CTD; 6164; -.
DR DisGeNET; 6164; -.
DR GeneCards; RPL34; -.
DR HGNC; HGNC:10340; RPL34.
DR HPA; ENSG00000109475; Low tissue specificity.
DR MIM; 616862; gene.
DR neXtProt; NX_P49207; -.
DR OpenTargets; ENSG00000109475; -.
DR PharmGKB; PA34723; -.
DR VEuPathDB; HostDB:ENSG00000109475; -.
DR eggNOG; KOG1790; Eukaryota.
DR GeneTree; ENSGT00390000008294; -.
DR HOGENOM; CLU_118652_0_1_1; -.
DR InParanoid; P49207; -.
DR OMA; CGNCVKD; -.
DR OrthoDB; 1517591at2759; -.
DR PhylomeDB; P49207; -.
DR TreeFam; TF314326; -.
DR PathwayCommons; P49207; -.
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; P49207; -.
DR SIGNOR; P49207; -.
DR BioGRID-ORCS; 6164; 772 hits in 1025 CRISPR screens.
DR ChiTaRS; RPL34; human.
DR GeneWiki; RPL34; -.
DR GenomeRNAi; 6164; -.
DR Pharos; P49207; Tbio.
DR PRO; PR:P49207; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P49207; protein.
DR Bgee; ENSG00000109475; Expressed in caput epididymis and 208 other tissues.
DR ExpressionAtlas; P49207; baseline and differential.
DR Genevisible; P49207; 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:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; IC:FlyBase.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
DR InterPro; IPR008195; Ribosomal_L34Ae.
DR InterPro; IPR018065; Ribosomal_L34e_CS.
DR Pfam; PF01199; Ribosomal_L34e; 1.
DR PRINTS; PR01250; RIBOSOMALL34.
DR PROSITE; PS01145; RIBOSOMAL_L34E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Endoplasmic reticulum; Isopeptide bond; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12962325"
FT CHAIN 2..117
FT /note="60S ribosomal protein L34"
FT /id="PRO_0000131831"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 36
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 43
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D1R9"
FT CROSSLNK 108
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 52
FT /note="R -> K (in Ref. 1; AAC41916)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="A -> P (in Ref. 1; AAC41916)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="V -> I (in Ref. 1; AAC41916)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 117 AA; 13293 MW; FC09D00B98CB770C CRC64;
MVQRLTYRRR LSYNTASNKT RLSRTPGNRI VYLYTKKVGK APKSACGVCP GRLRGVRAVR
PKVLMRLSKT KKHVSRAYGG SMCAKCVRDR IKRAFLIEEQ KIVVKVLKAQ AQSQKAK
