ID   RL6_MOUSE               Reviewed;         296 AA.
AC   P47911; Q6P5I2; Q925C3;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 176.
DE   RecName: Full=Large ribosomal subunit protein eL6 {ECO:0000305};
DE   AltName: Full=60S ribosomal protein L6;
DE   AltName: Full=TAX-responsive enhancer element-binding protein 107;
DE            Short=TAXREB107;
GN   Name=Rpl6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RA   Wang J.-S., Han H., Yang X., Li R., Zhou P.;
RL   Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 4-296.
RX   PubMed=7537974; DOI=10.1016/0167-4781(95)00046-j;
RA   Nacken W., Klempt M., Sorg C.;
RT   "The mouse homologue of the HTLV-I tax responsive element binding protein
RT   TAXREB107 is a highly conserved gene which may regulate some basal cellular
RT   functions.";
RL   Biochim. Biophys. Acta 1261:432-434(1995).
RN   [4]
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-247, SUCCINYLATION [LARGE SCALE
RP   ANALYSIS] AT LYS-102 AND LYS-215, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [7] {ECO:0007744|PDB:7CPU, ECO:0007744|PDB:7CPV}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.03 ANGSTROMS) OF RIBOSOME, FUNCTION,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=36517592; DOI=10.1038/s41586-022-05508-0;
RA   Li H., Huo Y., He X., Yao L., Zhang H., Cui Y., Xiao H., Xie W., Zhang D.,
RA   Wang Y., Zhang S., Tu H., Cheng Y., Guo Y., Cao X., Zhu Y., Jiang T.,
RA   Guo X., Qin Y., Sha J.;
RT   "A male germ-cell-specific ribosome controls male fertility.";
RL   Nature 0:0-0(2022).
CC   -!- FUNCTION: Component of the large ribosomal subunit (PubMed:36517592).
CC       The ribosome is a large ribonucleoprotein complex responsible for the
CC       synthesis of proteins in the cell (PubMed:36517592).
CC       {ECO:0000269|PubMed:36517592}.
CC   -!- SUBUNIT: Component of the large ribosomal subunit (PubMed:36517592).
CC       May bind IPO9 with low affinity (PubMed:11823430).
CC       {ECO:0000269|PubMed:11823430, ECO:0000269|PubMed:36517592}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q02878}. Cytoplasm
CC       {ECO:0000269|PubMed:36517592}. Rough endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:Q2YGT9}. Note=Detected on cytosolic polysomes
CC       (By similarity). Detected in ribosomes that are associated with the
CC       rough endoplasmic reticulum (By similarity).
CC       {ECO:0000250|UniProtKB:Q02878, ECO:0000250|UniProtKB:Q2YGT9}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL6 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA57513.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF374195; AAK56936.1; -; Genomic_DNA.
DR   EMBL; BC062880; AAH62880.1; -; mRNA.
DR   EMBL; X81987; CAA57513.1; ALT_INIT; mRNA.
DR   CCDS; CCDS19632.1; -.
DR   PIR; S55922; S55922.
DR   RefSeq; NP_035420.2; NM_011290.5.
DR   RefSeq; XP_006530290.1; XM_006530227.1.
DR   PDB; 6SWA; EM; 3.10 A; E=1-296.
DR   PDB; 7CPU; EM; 2.82 A; LE=1-296.
DR   PDB; 7CPV; EM; 3.03 A; LE=1-296.
DR   PDB; 7LS1; EM; 3.30 A; H2=1-296.
DR   PDB; 7LS2; EM; 3.10 A; H2=1-296.
DR   PDBsum; 6SWA; -.
DR   PDBsum; 7CPU; -.
DR   PDBsum; 7CPV; -.
DR   PDBsum; 7LS1; -.
DR   PDBsum; 7LS2; -.
DR   AlphaFoldDB; P47911; -.
DR   EMDB; EMD-10321; -.
DR   EMDB; EMD-23500; -.
DR   EMDB; EMD-23501; -.
DR   EMDB; EMD-30432; -.
DR   EMDB; EMD-30433; -.
DR   SMR; P47911; -.
DR   BioGRID; 202987; 137.
DR   ComplexPortal; CPX-5262; 60S cytosolic large ribosomal subunit.
DR   ComplexPortal; CPX-7662; 60S cytosolic large ribosomal subunit, testis-specific variant.
DR   ComplexPortal; CPX-7663; 60S cytosolic large ribosomal subunit, striated muscle variant.
DR   CORUM; P47911; -.
DR   IntAct; P47911; 6.
DR   STRING; 10090.ENSMUSP00000031617; -.
DR   GlyGen; P47911; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P47911; -.
DR   PhosphoSitePlus; P47911; -.
DR   SwissPalm; P47911; -.
DR   EPD; P47911; -.
DR   jPOST; P47911; -.
DR   PaxDb; 10090-ENSMUSP00000031617; -.
DR   PeptideAtlas; P47911; -.
DR   ProteomicsDB; 253253; -.
DR   Pumba; P47911; -.
DR   Antibodypedia; 31186; 134 antibodies from 26 providers.
DR   DNASU; 19988; -.
DR   Ensembl; ENSMUST00000031617.13; ENSMUSP00000031617.10; ENSMUSG00000029614.14.
DR   GeneID; 19988; -.
DR   KEGG; mmu:19988; -.
DR   UCSC; uc008ziq.3; mouse.
DR   AGR; MGI:108057; -.
DR   CTD; 6128; -.
DR   MGI; MGI:108057; Rpl6.
DR   VEuPathDB; HostDB:ENSMUSG00000029614; -.
DR   eggNOG; KOG1694; Eukaryota.
DR   GeneTree; ENSGT00390000003682; -.
DR   HOGENOM; CLU_066767_0_1_1; -.
DR   InParanoid; P47911; -.
DR   OMA; HKFLFGY; -.
DR   OrthoDB; 5483341at2759; -.
DR   PhylomeDB; P47911; -.
DR   TreeFam; TF300115; -.
DR   Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-MMU-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR   Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   Reactome; R-MMU-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-MMU-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR   Reactome; R-MMU-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR   Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   BioGRID-ORCS; 19988; 22 hits in 71 CRISPR screens.
DR   ChiTaRS; Rpl6; mouse.
DR   PRO; PR:P47911; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; P47911; Protein.
DR   Bgee; ENSMUSG00000029614; Expressed in epiblast (generic) and 64 other cell types or tissues.
DR   ExpressionAtlas; P47911; baseline and differential.
DR   GO; GO:0031672; C:A band; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR   GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
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; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0042788; C:polysomal ribosome; ISO:MGI.
DR   GO; GO:0098794; C:postsynapse; NAS:SynGO.
DR   GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR   GO; GO:0098793; C:presynapse; NAS:SynGO.
DR   GO; GO:0005840; C:ribosome; NAS:SynGO.
DR   GO; GO:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IDA:SynGO.
DR   GO; GO:1990932; F:5.8S rRNA binding; ISO:MGI.
DR   GO; GO:0003729; F:mRNA binding; ISO:MGI.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
DR   GO; GO:0000049; F:tRNA binding; ISO:MGI.
DR   GO; GO:0002181; P:cytoplasmic translation; ISS:UniProtKB.
DR   GO; GO:0140242; P:translation at postsynapse; NAS:SynGO.
DR   GO; GO:0140236; P:translation at presynapse; NAS:SynGO.
DR   CDD; cd13156; KOW_RPL6; 1.
DR   Gene3D; 2.30.30.30; -; 1.
DR   InterPro; IPR000915; 60S_ribosomal_eL6.
DR   InterPro; IPR014722; Rib_uL2_dom2.
DR   InterPro; IPR049633; Ribosomal_eL6_CS.
DR   InterPro; IPR041997; Ribosomal_eL6_KOW.
DR   InterPro; IPR005568; Ribosomal_uL6_N.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR10715; 60S RIBOSOMAL PROTEIN L6; 1.
DR   PANTHER; PTHR10715:SF0; 60S RIBOSOMAL PROTEIN L6; 1.
DR   Pfam; PF01159; Ribosomal_L6e; 1.
DR   Pfam; PF03868; Ribosomal_L6e_N; 1.
DR   SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
DR   PROSITE; PS01170; RIBOSOMAL_L6E; 1.
DR   Genevisible; P47911; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Endoplasmic reticulum;
KW   Isopeptide bond; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; Ubl conjugation.
FT   CHAIN           1..296
FT                   /note="Large ribosomal subunit protein eL6"
FT                   /id="PRO_0000171010"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..52
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         102
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         135
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q02878"
FT   MOD_RES         215
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         247
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   CROSSLNK        5
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q02878"
FT   CONFLICT        5
FT                   /note="K -> R (in Ref. 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        10
FT                   /note="K -> M (in Ref. 3; CAA57513)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        75
FT                   /note="L -> F (in Ref. 2; AAH62880)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   296 AA;  33510 MW;  D65D5EF517660836 CRC64;
     MAGEKAPDTK EKKPAAKKAG SDAAASRPRA AKVAKKVHPK GKKPKKAKPH CSRNPVLVRG
     IGRYSRSAMY SRKALYKRKY SAAKTKVEKK KKKEKVLATV TKTVGGDKNG GTRVVKLRKM
     PRYYPTEDVP RKLLSHGKKP FSQHVRRLRS SITPGTVLII LTGRHRGKRV VFLKQLDSGL
     LLVTGPLVIN RVPLRRTHQK FVIATSTKVD ISDVKIPKHL TDAYFKKKQL RKPRHQEGEI
     FDTEKEKYEI TEQRKADQKA VDLQILPKIK AVPQLQGYLR SQFSLTNGMY PHKLVF
//