RL6_MOUSE
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 03-AUG-2022, entry version 167.
DE RecName: 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, Pancreas,
RC 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).
CC -!- FUNCTION: Component of the large ribosomal subunit. The ribosome is a
CC large ribonucleoprotein complex responsible for the synthesis of
CC proteins in the cell. {ECO:0000250|UniProtKB:Q02878}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (By similarity). May
CC bind IPO9 with low affinity (PubMed:11823430).
CC {ECO:0000250|UniProtKB:Q02878, ECO:0000269|PubMed:11823430}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q02878}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q02878}. 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 SMR; P47911; -.
DR BioGRID; 202987; 134.
DR ComplexPortal; CPX-5262; 60S cytosolic large ribosomal subunit.
DR CORUM; P47911; -.
DR IntAct; P47911; 6.
DR STRING; 10090.ENSMUSP00000031617; -.
DR iPTMnet; P47911; -.
DR PhosphoSitePlus; P47911; -.
DR SwissPalm; P47911; -.
DR EPD; P47911; -.
DR jPOST; P47911; -.
DR PaxDb; P47911; -.
DR PeptideAtlas; P47911; -.
DR PRIDE; P47911; -.
DR ProteomicsDB; 253253; -.
DR Antibodypedia; 31186; 118 antibodies from 26 providers.
DR DNASU; 19988; -.
DR Ensembl; ENSMUST00000031617; ENSMUSP00000031617; ENSMUSG00000029614.
DR GeneID; 19988; -.
DR KEGG; mmu:19988; -.
DR UCSC; uc008ziq.3; mouse.
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; KHPLNSY; -.
DR OrthoDB; 1227453at2759; -.
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 66 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 61 other tissues.
DR ExpressionAtlas; P47911; baseline and differential.
DR Genevisible; P47911; MM.
DR GO; GO:0031672; C:A band; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
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; IPI:ComplexPortal.
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; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA: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; ISO:MGI.
DR GO; GO:0000049; F:tRNA binding; ISO:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; ISS:UniProtKB.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
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; Endoplasmic reticulum;
KW Isopeptide bond; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Ubl conjugation.
FT CHAIN 1..296
FT /note="60S ribosomal protein L6"
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
