RL5_MOUSE
ID RL5_MOUSE Reviewed; 297 AA.
AC P47962; Q9CR19;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=60S ribosomal protein L5;
GN Name=Rpl5;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Small intestine;
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 [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 [GENOMIC DNA] OF 162-179.
RX PubMed=7937132; DOI=10.1093/nar/22.20.4073;
RA Qu L.H., Nicoloso M., Michot B., Azum M.C., Caizergues-Ferrer M.,
RA Renalier M.H., Bachellerie J.-P.;
RT "U21, a novel small nucleolar RNA with a 13 nt. complementarity to 28S
RT rRNA, is encoded in an intron of ribosomal protein L5 gene in chicken and
RT mammals.";
RL Nucleic Acids Res. 22:4073-4081(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 206-297.
RC STRAIN=NMRE; TISSUE=Brain;
RA Zach O.R.F.;
RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
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-220, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell. The small
CC ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC molecules. The large subunit (LSU) contains the ribosomal catalytic
CC site termed the peptidyl transferase center (PTC), which catalyzes the
CC formation of peptide bonds, thereby polymerizing the amino acids
CC delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC leave the ribosome through a tunnel in the LSU and interact with
CC protein factors that function in enzymatic processing, targeting, and
CC the membrane insertion of nascent chains at the exit of the ribosomal
CC tunnel. As part of the 5S RNP/5S ribonucleoprotein particle it is an
CC essential component of the LSU, required for its formation and the
CC maturation of rRNAs. It also couples ribosome biogenesis to p53/TP53
CC activation. As part of the 5S RNP it accumulates in the nucleoplasm and
CC inhibits MDM2, when ribosome biogenesis is perturbed, mediating the
CC stabilization and the activation of TP53. Interacts with RRP1B.
CC {ECO:0000250|UniProtKB:P46777}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (LSU). Part of a LSU
CC subcomplex, the 5S RNP which is composed of the 5S RNA, RPL5 and RPL11.
CC Interacts with NVL in an ATP-dependent manner. Interacts with RRP1B (By
CC similarity). Interacts with IPO5, IPO7 and KPNB1; these interactions
CC may be involved in RPL5 nuclear import for the assembly of ribosomal
CC subunits (By similarity). {ECO:0000250|UniProtKB:P46777}.
CC -!- INTERACTION:
CC P47962; P23804: Mdm2; NbExp=3; IntAct=EBI-773940, EBI-641788;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P46777}.
CC Nucleus, nucleolus {ECO:0000250|UniProtKB:P46777}. Note=Although RP5 is
CC functional within the cytoplasm, the assembly of ribosomal subunits
CC occurs in the nucleus. RPL5 nuclear import is mediated by IPO5/RanBP5,
CC IPO7/RanBP7, KPNB1/importin-beta or TPNO1/Trn.
CC {ECO:0000250|UniProtKB:P46777}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL18 family.
CC {ECO:0000305}.
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DR EMBL; AK008489; BAB25695.1; -; mRNA.
DR EMBL; AK013107; BAB28652.1; -; mRNA.
DR EMBL; BC026934; AAH26934.1; -; mRNA.
DR EMBL; BC083318; AAH83318.1; -; mRNA.
DR EMBL; Z35311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X83590; CAA58570.1; -; mRNA.
DR CCDS; CCDS39199.1; -.
DR PIR; S50100; S50100.
DR RefSeq; NP_058676.1; NM_016980.2.
DR PDB; 6SWA; EM; 3.10 A; D=1-297.
DR PDB; 7CPU; EM; 2.82 A; LD=1-297.
DR PDB; 7CPV; EM; 3.03 A; LD=1-297.
DR PDB; 7LS1; EM; 3.30 A; G2=1-297.
DR PDB; 7LS2; EM; 3.10 A; G2=1-297.
DR PDBsum; 6SWA; -.
DR PDBsum; 7CPU; -.
DR PDBsum; 7CPV; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; P47962; -.
DR SMR; P47962; -.
DR BioGRID; 433810; 81.
DR ComplexPortal; CPX-5262; 60S cytosolic large ribosomal subunit.
DR CORUM; P47962; -.
DR IntAct; P47962; 8.
DR MINT; P47962; -.
DR STRING; 10090.ENSMUSP00000080854; -.
DR iPTMnet; P47962; -.
DR PhosphoSitePlus; P47962; -.
DR SwissPalm; P47962; -.
DR EPD; P47962; -.
DR jPOST; P47962; -.
DR PaxDb; P47962; -.
DR PeptideAtlas; P47962; -.
DR PRIDE; P47962; -.
DR ProteomicsDB; 299823; -.
DR Ensembl; ENSMUST00000082223; ENSMUSP00000080854; ENSMUSG00000058558.
DR GeneID; 100503670; -.
DR KEGG; mmu:100503670; -.
DR UCSC; uc008ynh.2; mouse.
DR CTD; 6125; -.
DR MGI; MGI:102854; Rpl5.
DR VEuPathDB; HostDB:ENSMUSG00000058558; -.
DR eggNOG; KOG0875; Eukaryota.
DR GeneTree; ENSGT00950000183210; -.
DR HOGENOM; CLU_056222_1_0_1; -.
DR InParanoid; P47962; -.
DR OMA; KSQFQGY; -.
DR OrthoDB; 999609at2759; -.
DR PhylomeDB; P47962; -.
DR TreeFam; TF300044; -.
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; 100503670; 25 hits in 52 CRISPR screens.
DR ChiTaRS; Rpl5; mouse.
DR PRO; PR:P47962; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P47962; protein.
DR Bgee; ENSMUSG00000058558; Expressed in epiblast (generic) and 74 other tissues.
DR ExpressionAtlas; P47962; baseline and differential.
DR Genevisible; P47962; MM.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0008097; F:5S rRNA binding; ISO:MGI.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:MGI.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; ISO:MGI.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:1990948; F:ubiquitin ligase inhibitor activity; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:2000435; P:negative regulation of protein neddylation; ISO:MGI.
DR GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:1905017; P:positive regulation of isoleucine-tRNA ligase activity; ISO:MGI.
DR GO; GO:1905020; P:positive regulation of methionine-tRNA ligase activity; ISO:MGI.
DR GO; GO:0010922; P:positive regulation of phosphatase activity; ISO:MGI.
DR GO; GO:1905023; P:positive regulation of threonine-tRNA ligase activity; ISO:MGI.
DR GO; GO:0045727; P:positive regulation of translation; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; ISO:MGI.
DR GO; GO:0000027; P:ribosomal large subunit assembly; ISO:MGI.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; ISO:MGI.
DR GO; GO:0006364; P:rRNA processing; ISO:MGI.
DR HAMAP; MF_01337_A; Ribosomal_L18_A; 1.
DR InterPro; IPR005485; Rbsml_L5_euk/L18_arc.
DR InterPro; IPR025607; Rbsml_L5e_C.
DR PANTHER; PTHR23410; PTHR23410; 1.
DR Pfam; PF14204; Ribosomal_L18_c; 1.
DR Pfam; PF17144; Ribosomal_L5e; 1.
DR PRINTS; PR00058; RIBOSOMALL5.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P46777"
FT CHAIN 2..297
FT /note="60S ribosomal protein L5"
FT /id="PRO_0000131433"
FT REGION 253..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:P46777"
FT MOD_RES 5
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P46777"
FT MOD_RES 48
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P46777"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46777"
FT MOD_RES 220
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 232
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P46777"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46777"
FT CROSSLNK 220
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P46777"
FT CROSSLNK 220
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P46777"
SQ SEQUENCE 297 AA; 34401 MW; 30D74B9E66E17C65 CRC64;
MGFVKVVKNK AYFKRYQVRF RRRREGKTDY YARKRLVIQD KNKYNTPKYR MIVRVTNRDI
ICQIAYARIE GDMIVCAAYA HELPKYGVKV GLTNYAAAYC TGLLLARRLL NRFGMDKIYE
GQVEVNGGEY NVESIDGQPG AFTCYLDAGL ARTTTGNKVF GALKGAVDGG LSIPHSTKRF
PGYDSESKEF NAEVHRKHIM GQNVADYMRY LMEEDEDAYK KQFSQYIKNN VTPDMMEEMY
KKAHAAIREN PVYEKKPKRE VKKKRWNRPK MSLAQKKDRV AQKKASFLRA QERAAES
