RL6_HUMAN
ID RL6_HUMAN Reviewed; 288 AA.
AC Q02878; Q2M3Q3; Q8WW97;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 224.
DE RecName: Full=60S ribosomal protein L6;
DE AltName: Full=Large ribosomal subunit protein eL6 {ECO:0000303|PubMed:24524803};
DE AltName: Full=Neoplasm-related protein C140;
DE AltName: Full=Tax-responsive enhancer element-binding protein 107;
DE Short=TaxREB107;
GN Name=RPL6; Synonyms=TXREB1;
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].
RX PubMed=8479925; DOI=10.1093/nar/21.7.1673;
RA Zaman G.J.R.;
RT "Sequence of a cDNA encoding human ribosomal protein L26 and of a cDNA
RT probably encoding human ribosomal protein L6.";
RL Nucleic Acids Res. 21:1673-1673(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION (MICROBIAL INFECTION).
RX PubMed=8457378; DOI=10.1089/aid.1993.9.115;
RA Morita T., Sato T., Nyunoya H., Tsujimoto A., Takahara J., Irino S.,
RA Shimotohno K.;
RT "Isolation of a cDNA clone encoding DNA-binding protein (TAXREB107) that
RT binds specifically to domain C of the tax-responsive enhancer element in
RT the long terminal repeat of human T-cell leukemia virus type I.";
RL AIDS Res. Hum. Retroviruses 9:115-121(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11043511; DOI=10.1007/s100380070018;
RA Kenmochi N., Yoshihama M., Higa S., Tanaka T.;
RT "The human ribosomal protein L6 gene in a critical region for Noonan
RT syndrome.";
RL J. Hum. Genet. 45:290-293(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-227.
RC TISSUE=Brain, Liver, Lung, and Placenta;
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 [MRNA] OF 46-268.
RX PubMed=8185817; DOI=10.1677/jme.0.0120085;
RA Ohta K., Endo T., Gunji K., Onaya T.;
RT "Isolation of a cDNA whose expression is markedly increased in malignantly
RT transformed FRTL cells and neoplastic human thyroid tissues.";
RL J. Mol. Endocrinol. 12:85-92(1994).
RN [6]
RP PROTEIN SEQUENCE OF 2-10, 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 INTERACTION WITH IPO9.
RX PubMed=11823430; DOI=10.1093/emboj/21.3.377;
RA Jaekel S., Mingot J.-M., Schwarzmaier P., Hartmann E., Goerlich D.;
RT "Importins fulfill a dual function as nuclear import receptors and
RT cytoplasmic chaperones for exposed basic domains.";
RL EMBO J. 21:377-386(2002).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-239, 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 [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 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].
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 [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-5, 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 [15]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) IN COMPLEX WITH THE 80S
RP RIBOSOME, SUBUNIT, SUBCELLULAR LOCATION, AND FUNCTION.
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 [16] {ECO:0007744|PDB:5AJ0}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), SUBCELLULAR LOCATION,
RP SUBUNIT, AND FUNCTION.
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 [17] {ECO:0007744|PDB:4UG0}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), SUBUNIT, SUBCELLULAR
RP LOCATION, AND FUNCTION.
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 [18] {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).
RN [19]
RP VARIANT [LARGE SCALE ANALYSIS] GLN-100.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Component of the large ribosomal subunit (PubMed:12962325,
CC PubMed:25957688, PubMed:25901680, PubMed:32669547, PubMed:23636399).
CC The ribosome is a large ribonucleoprotein complex responsible for the
CC synthesis of proteins in the cell (PubMed:12962325, PubMed:25957688,
CC PubMed:25901680, PubMed:32669547, PubMed:23636399).
CC {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:25901680,
CC ECO:0000269|PubMed:25957688, ECO:0000269|PubMed:32669547,
CC ECO:0000305|PubMed:12962325}.
CC -!- FUNCTION: (Microbial infection) Specifically binds to domain C of the
CC Tax-responsive enhancer element in the long terminal repeat of HTLV-I
CC (PubMed:8457378). {ECO:0000269|PubMed:8457378}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (PubMed:12962325,
CC PubMed:23636399, PubMed:25957688, PubMed:25901680, PubMed:32669547).
CC May bind IPO9 with low affinity (By similarity).
CC {ECO:0000250|UniProtKB:P47911, ECO:0000269|PubMed:23636399,
CC ECO:0000269|PubMed:25901680, ECO:0000269|PubMed:25957688,
CC ECO:0000269|PubMed:32669547, ECO:0000305|PubMed:12962325}.
CC -!- INTERACTION:
CC Q02878; Q99558: MAP3K14; NbExp=3; IntAct=EBI-359655, EBI-358011;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:25957688}.
CC Cytoplasm {ECO:0000305|PubMed:23636399, ECO:0000305|PubMed:25901680}.
CC Rough endoplasmic reticulum {ECO:0000250|UniProtKB:Q2YGT9}.
CC Note=Detected on cytosolic polysomes (PubMed:25957688). Detected in
CC ribosomes that are associated with the rough endoplasmic reticulum (By
CC similarity). {ECO:0000250|UniProtKB:Q2YGT9,
CC ECO:0000269|PubMed:25957688}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL6 family.
CC {ECO:0000305}.
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DR EMBL; X69391; CAA49188.1; -; mRNA.
DR EMBL; D17554; BAA04491.1; -; mRNA.
DR EMBL; AB042820; BAB17292.1; -; Genomic_DNA.
DR EMBL; BC004138; AAH04138.1; -; mRNA.
DR EMBL; BC020679; AAH20679.1; -; mRNA.
DR EMBL; BC032299; AAH32299.1; -; mRNA.
DR EMBL; BC071912; AAH71912.1; -; mRNA.
DR EMBL; BC104824; AAI04825.1; -; mRNA.
DR EMBL; BC104826; AAI04827.1; -; mRNA.
DR EMBL; S71022; AAB30819.1; -; mRNA.
DR CCDS; CCDS9162.1; -.
DR PIR; I51803; I51803.
DR PIR; S33714; S33714.
DR RefSeq; NP_000961.2; NM_000970.4.
DR RefSeq; NP_001019833.1; NM_001024662.2.
DR RefSeq; NP_001307066.1; NM_001320137.1.
DR RefSeq; NP_001307067.1; NM_001320138.1.
DR RefSeq; NP_001307068.1; NM_001320139.1.
DR RefSeq; NP_001307069.1; NM_001320140.1.
DR RefSeq; NP_001307070.1; NM_001320141.1.
DR RefSeq; XP_016875270.1; XM_017019781.1.
DR RefSeq; XP_016875271.1; XM_017019782.1.
DR PDB; 4UG0; EM; -; LE=1-288.
DR PDB; 4V6X; EM; 5.00 A; CE=1-288.
DR PDB; 5AJ0; EM; 3.50 A; AE=1-288.
DR PDB; 5LKS; EM; 3.60 A; LE=1-288.
DR PDB; 5T2C; EM; 3.60 A; H=1-288.
DR PDB; 6IP5; EM; 3.90 A; 1H=1-288.
DR PDB; 6IP6; EM; 4.50 A; 1H=1-288.
DR PDB; 6IP8; EM; 3.90 A; 1H=1-288.
DR PDB; 6LQM; EM; 3.09 A; v=1-288.
DR PDB; 6LSR; EM; 3.13 A; v=1-288.
DR PDB; 6LSS; EM; 3.23 A; o=1-288.
DR PDB; 6LU8; EM; 3.13 A; o=1-288.
DR PDB; 6OLE; EM; 3.10 A; G=42-288.
DR PDB; 6OLF; EM; 3.90 A; G=42-288.
DR PDB; 6OLG; EM; 3.40 A; AE=95-288.
DR PDB; 6OLI; EM; 3.50 A; G=42-288.
DR PDB; 6OLZ; EM; 3.90 A; AE=42-288.
DR PDB; 6OM0; EM; 3.10 A; G=42-288.
DR PDB; 6OM7; EM; 3.70 A; G=42-288.
DR PDB; 6QZP; EM; 2.90 A; LE=42-288.
DR PDB; 6W6L; EM; 3.84 A; G=1-288.
DR PDB; 6XA1; EM; 2.80 A; LE=42-288.
DR PDB; 6Y0G; EM; 3.20 A; LE=1-288.
DR PDB; 6Y2L; EM; 3.00 A; LE=1-288.
DR PDB; 6Y57; EM; 3.50 A; LE=1-288.
DR PDB; 6Y6X; EM; 2.80 A; LE=42-288.
DR PDB; 6Z6L; EM; 3.00 A; LE=1-288.
DR PDB; 6Z6M; EM; 3.10 A; LE=1-288.
DR PDB; 6Z6N; EM; 2.90 A; LE=1-288.
DR PDB; 6ZM7; EM; 2.70 A; LE=1-288.
DR PDB; 6ZME; EM; 3.00 A; LE=1-288.
DR PDB; 6ZMI; EM; 2.60 A; LE=1-288.
DR PDB; 6ZMO; EM; 3.10 A; LE=1-288.
DR PDB; 7BHP; EM; 3.30 A; LE=1-288.
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; Q02878; -.
DR SMR; Q02878; -.
DR BioGRID; 112048; 481.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR CORUM; Q02878; -.
DR DIP; DIP-27547N; -.
DR IntAct; Q02878; 150.
DR MINT; Q02878; -.
DR STRING; 9606.ENSP00000403172; -.
DR GlyGen; Q02878; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q02878; -.
DR PhosphoSitePlus; Q02878; -.
DR SwissPalm; Q02878; -.
DR BioMuta; RPL6; -.
DR SWISS-2DPAGE; Q02878; -.
DR EPD; Q02878; -.
DR jPOST; Q02878; -.
DR MassIVE; Q02878; -.
DR MaxQB; Q02878; -.
DR PaxDb; Q02878; -.
DR PeptideAtlas; Q02878; -.
DR PRIDE; Q02878; -.
DR ProteomicsDB; 58132; -.
DR TopDownProteomics; Q02878; -.
DR Antibodypedia; 31186; 118 antibodies from 26 providers.
DR DNASU; 6128; -.
DR Ensembl; ENST00000202773.14; ENSP00000202773.9; ENSG00000089009.16.
DR Ensembl; ENST00000424576.6; ENSP00000403172.2; ENSG00000089009.16.
DR GeneID; 6128; -.
DR KEGG; hsa:6128; -.
DR MANE-Select; ENST00000202773.14; ENSP00000202773.9; NM_000970.6; NP_000961.2.
DR UCSC; uc001ttu.4; human.
DR CTD; 6128; -.
DR DisGeNET; 6128; -.
DR GeneCards; RPL6; -.
DR HGNC; HGNC:10362; RPL6.
DR HPA; ENSG00000089009; Low tissue specificity.
DR MIM; 603703; gene.
DR neXtProt; NX_Q02878; -.
DR OpenTargets; ENSG00000089009; -.
DR PharmGKB; PA34758; -.
DR VEuPathDB; HostDB:ENSG00000089009; -.
DR eggNOG; KOG1694; Eukaryota.
DR GeneTree; ENSGT00390000003682; -.
DR HOGENOM; CLU_066767_0_1_1; -.
DR InParanoid; Q02878; -.
DR OMA; KHPLNSY; -.
DR OrthoDB; 1227453at2759; -.
DR PhylomeDB; Q02878; -.
DR TreeFam; TF300115; -.
DR PathwayCommons; Q02878; -.
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; Q02878; -.
DR SIGNOR; Q02878; -.
DR BioGRID-ORCS; 6128; 787 hits in 1024 CRISPR screens.
DR ChiTaRS; RPL6; human.
DR GeneWiki; RPL6; -.
DR GenomeRNAi; 6128; -.
DR Pharos; Q02878; Tbio.
DR PRO; PR:Q02878; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q02878; protein.
DR Bgee; ENSG00000089009; Expressed in cortical plate and 107 other tissues.
DR ExpressionAtlas; Q02878; baseline and differential.
DR Genevisible; Q02878; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
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; IDA:BHF-UCL.
DR GO; GO:0042788; C:polysomal ribosome; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:ProtInc.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
DR CDD; cd13156; KOW_RPL6; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR InterPro; IPR000915; 60S_ribosomal_L6E.
DR InterPro; IPR041997; KOW_RPL6.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR005568; Ribosomal_L6_N.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR10715; PTHR10715; 1.
DR Pfam; PF01159; Ribosomal_L6e; 1.
DR Pfam; PF03868; Ribosomal_L6e_N; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR PROSITE; PS01170; RIBOSOMAL_L6E; 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..288
FT /note="60S ribosomal protein L6"
FT /id="PRO_0000171009"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..45
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 94
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47911"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17924679"
FT MOD_RES 207
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47911"
FT MOD_RES 239
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 5
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 100
FT /note="K -> Q (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036437"
FT VARIANT 227
FT /note="H -> R (in dbSNP:rs17851813)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_025313"
FT VARIANT 237
FT /note="K -> E (in dbSNP:rs16942044)"
FT /id="VAR_051810"
FT CONFLICT 43..63
FT /note="HCSRNPVLVRGIGRYSRSAMY -> PLQPQPCPSQRNWQVFPICHV (in
FT Ref. 1; CAA49188)"
FT /evidence="ECO:0000305"
FT CONFLICT 177..183
FT /note="GPLVLNR -> DLWSSIE (in Ref. 1; CAA49188)"
FT /evidence="ECO:0000305"
FT CONFLICT 181..205
FT /note="LNRVPLRRTHQKFVIATSTKIDISN -> SIEFLYEEHTRNLSLPLQPKSIS
FT AI (in Ref. 5; AAB30819)"
FT /evidence="ECO:0000305"
FT CONFLICT 252..268
FT /note="AVDSQILPKIKAIPQLQ -> LWTHKFYQKSKLFLSSS (in Ref. 1;
FT CAA49188)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 288 AA; 32728 MW; D24A6168C7D0ECBF CRC64;
MAGEKVEKPD TKEKKPEAKK VDAGGKVKKG NLKAKKPKKG KPHCSRNPVL VRGIGRYSRS
AMYSRKAMYK RKYSAAKSKV EKKKKEKVLA TVTKPVGGDK NGGTRVVKLR KMPRYYPTED
VPRKLLSHGK KPFSQHVRKL RASITPGTIL IILTGRHRGK RVVFLKQLAS GLLLVTGPLV
LNRVPLRRTH QKFVIATSTK IDISNVKIPK HLTDAYFKKK KLRKPRHQEG EIFDTEKEKY
EITEQRKIDQ KAVDSQILPK IKAIPQLQGY LRSVFALTNG IYPHKLVF
