RL3_MOUSE
ID RL3_MOUSE Reviewed; 403 AA.
AC P27659; O89071; Q91VJ6;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=60S ribosomal protein L3;
DE AltName: Full=J1 protein;
GN Name=Rpl3;
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 [MRNA].
RX PubMed=2628163; DOI=10.1101/gad.3.12b.2062;
RA Peckham I., Sobel S., Comer J., Jaenisch R., Barklis E.;
RT "Retrovirus activation in embryonal carcinoma cells by cellular
RT promoters.";
RL Genes Dev. 3:2062-2071(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1711497; DOI=10.1016/0378-1119(91)90409-5;
RA Petersen R., Sobel S., Wang C.T., Jaenisch R., Barklis E.;
RT "Cellular transcripts encoded at a locus which permits retrovirus
RT expression in mouse embryonic cells.";
RL Gene 101:177-183(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, C57BL/6J, DBA/2J, and NOD;
RC TISSUE=Bone marrow, Brain cortex, Heart, Kidney, Liver, Lung,
RC Mammary gland, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Limb, and Mammary tumor;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 183-299.
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=9798653; DOI=10.1016/s0161-5890(98)00031-5;
RA Chu C.C., Paul W.E.;
RT "Expressed genes in interleukin-4 treated B cells identified by cDNA
RT representational difference analysis.";
RL Mol. Immunol. 35:487-502(1998).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-136; LYS-286 AND LYS-373, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [10]
RP INTERACTION WITH DHX33.
RX PubMed=26100019; DOI=10.1128/mcb.00315-15;
RA Zhang Y., You J., Wang X., Weber J.;
RT "The DHX33 RNA Helicase Promotes mRNA Translation Initiation.";
RL Mol. Cell. Biol. 35:2918-2931(2015).
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:P39023}.
CC -!- SUBUNIT: Component of the large ribosomal subunit. Interacts with DHX33
CC (PubMed:26100019). {ECO:0000250|UniProtKB:P39023,
CC ECO:0000269|PubMed:26100019}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P39023}. Cytoplasm
CC {ECO:0000250|UniProtKB:P39023}.
CC -!- PTM: Constitutively monomethylated at His-245 by METTL18. Regulates the
CC function of RPL3 in the dynamics of pre-rRNA processing, ribosome
CC biogenesis, and translation. It is not required for incorporation of
CC RPL3 into ribosomes. {ECO:0000250|UniProtKB:P39023}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y00225; CAA68370.1; -; mRNA.
DR EMBL; U89417; AAC36524.1; -; mRNA.
DR EMBL; AK088993; BAC40691.1; -; mRNA.
DR EMBL; AK144518; BAE25922.1; -; mRNA.
DR EMBL; AK144816; BAE26078.1; -; mRNA.
DR EMBL; AK146502; BAE27217.1; -; mRNA.
DR EMBL; AK149494; BAE28917.1; -; mRNA.
DR EMBL; AK151596; BAE30536.1; -; mRNA.
DR EMBL; AK166433; BAE38773.1; -; mRNA.
DR EMBL; AK166825; BAE39049.1; -; mRNA.
DR EMBL; AK167787; BAE39818.1; -; mRNA.
DR EMBL; AK167947; BAE39950.1; -; mRNA.
DR EMBL; AK168040; BAE40022.1; -; mRNA.
DR EMBL; AK168059; BAE40037.1; -; mRNA.
DR EMBL; AK168126; BAE40095.1; -; mRNA.
DR EMBL; AK168128; BAE40097.1; -; mRNA.
DR EMBL; AK168224; BAE40178.1; -; mRNA.
DR EMBL; AK168744; BAE40585.1; -; mRNA.
DR EMBL; AK169060; BAE40848.1; -; mRNA.
DR EMBL; AK169235; BAE41003.1; -; mRNA.
DR EMBL; AK169321; BAE41075.1; -; mRNA.
DR EMBL; AK170819; BAE42051.1; -; mRNA.
DR EMBL; CH466550; EDL04616.1; -; Genomic_DNA.
DR EMBL; BC009655; AAH09655.1; -; mRNA.
DR EMBL; BC083134; AAH83134.1; -; mRNA.
DR EMBL; BC094059; AAH94059.1; -; mRNA.
DR EMBL; BC158039; AAI58040.1; -; mRNA.
DR CCDS; CCDS37144.1; -.
DR RefSeq; NP_038790.2; NM_013762.2.
DR PDB; 6SWA; EM; 3.10 A; B=1-403.
DR PDB; 7CPU; EM; 2.82 A; LB=1-403.
DR PDB; 7CPV; EM; 3.03 A; LB=1-403.
DR PDB; 7LS1; EM; 3.30 A; E2=1-403.
DR PDB; 7LS2; EM; 3.10 A; E2=1-403.
DR PDBsum; 6SWA; -.
DR PDBsum; 7CPU; -.
DR PDBsum; 7CPV; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; P27659; -.
DR SMR; P27659; -.
DR BioGRID; 205174; 89.
DR ComplexPortal; CPX-5262; 60S cytosolic large ribosomal subunit.
DR CORUM; P27659; -.
DR IntAct; P27659; 3.
DR MINT; P27659; -.
DR STRING; 10090.ENSMUSP00000080354; -.
DR iPTMnet; P27659; -.
DR PhosphoSitePlus; P27659; -.
DR SwissPalm; P27659; -.
DR EPD; P27659; -.
DR jPOST; P27659; -.
DR MaxQB; P27659; -.
DR PaxDb; P27659; -.
DR PeptideAtlas; P27659; -.
DR PRIDE; P27659; -.
DR ProteomicsDB; 299902; -.
DR Antibodypedia; 1245; 294 antibodies from 30 providers.
DR DNASU; 27367; -.
DR Ensembl; ENSMUST00000081650; ENSMUSP00000080354; ENSMUSG00000060036.
DR GeneID; 27367; -.
DR KEGG; mmu:27367; -.
DR UCSC; uc007wvb.2; mouse.
DR CTD; 6122; -.
DR MGI; MGI:1351605; Rpl3.
DR VEuPathDB; HostDB:ENSMUSG00000060036; -.
DR eggNOG; KOG0746; Eukaryota.
DR GeneTree; ENSGT00390000017606; -.
DR HOGENOM; CLU_033361_2_1_1; -.
DR InParanoid; P27659; -.
DR OMA; HQRTEYN; -.
DR OrthoDB; 793191at2759; -.
DR PhylomeDB; P27659; -.
DR TreeFam; TF300555; -.
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; 27367; 22 hits in 52 CRISPR screens.
DR ChiTaRS; Rpl3; mouse.
DR PRO; PR:P27659; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P27659; protein.
DR Bgee; ENSMUSG00000060036; Expressed in ventricular zone and 63 other tissues.
DR ExpressionAtlas; P27659; baseline and differential.
DR Genevisible; P27659; MM.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005840; C:ribosome; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0008097; F:5S rRNA 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:0071353; P:cellular response to interleukin-4; IDA:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 4.10.960.10; -; 1.
DR InterPro; IPR045077; L3_arc_euk.
DR InterPro; IPR000597; Ribosomal_L3.
DR InterPro; IPR019926; Ribosomal_L3_CS.
DR InterPro; IPR044892; Ribosomal_L3_dom_3_arc_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR11363; PTHR11363; 1.
DR Pfam; PF00297; Ribosomal_L3; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR PROSITE; PS00474; RIBOSOMAL_L3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Isopeptide bond; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Ubl conjugation.
FT CHAIN 1..403
FT /note="60S ribosomal protein L3"
FT /id="PRO_0000077229"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 136
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 245
FT /note="Tele-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:P39023"
FT MOD_RES 286
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 294
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P39023"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39023"
FT MOD_RES 366
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P39023"
FT MOD_RES 373
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CROSSLNK 39
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P39023"
FT CROSSLNK 224
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P39023"
FT CROSSLNK 226
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P39023"
FT CROSSLNK 286
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P39023"
FT CROSSLNK 294
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P39023"
FT CROSSLNK 366
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P39023"
FT CROSSLNK 386
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P39023"
FT CROSSLNK 393
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P39023"
FT CROSSLNK 399
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P39023"
FT CONFLICT 265
FT /note="S -> T (in Ref. 1; CAA68370)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 403 AA; 46110 MW; 87AA82D9B2A8481E CRC64;
MSHRKFSAPR HGSLGFLPRK RSSRHRGKVK SFPKDDASKP VHLTAFLGYK AGMTHIVREV
DRPGSKVNKK EVVEAVTIVE TPPMVVVGIV GYVETPRGLR TFKTVFAEHI SDECKRRFYK
NWHKSKKKAF TKYCKKWQDD TGKKQLEKDF NSMKKYCQVI RIIAHTQMRL LPLRQKKAHL
MEIQVNGGTV AEKLDWARER LEQQVPVNQV FGQDEMIDVI GVTKGKGYKG VTSRWHTKKL
PRKTHRGLRK VACIGAWHPA RVAFSVARAG QKGYHHRTEI NKKIYKIGQG YLIKDGKLIK
NNASTDYDLS DKSINPLGGF VHYGEVTNDF IMLKGCVVGT KKRVLTLRKS LLVQTKRRAL
EKIDLKFIDT TSKFGHGRFQ TMEEKKAFMG PLKKDRIAKE EGA
