ID   RL11_MOUSE              Reviewed;         178 AA.
AC   Q9CXW4; Q3TPE3; Q6ZWY0;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   27-MAR-2024, entry version 174.
DE   RecName: Full=Large ribosomal subunit protein uL5 {ECO:0000305};
DE   AltName: Full=60S ribosomal protein L11;
GN   Name=Rpl11;
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, and NOD;
RC   TISSUE=Bone marrow, Brain, Embryonic head, Eye, Small intestine, and
RC   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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon, 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   [3]
RP   FUNCTION, INTERACTION WITH PML AND MDM2, AND SUBCELLULAR LOCATION.
RX   PubMed=15195100; DOI=10.1038/ncb1147;
RA   Bernardi R., Scaglioni P.P., Bergmann S., Horn H.F., Vousden K.H.,
RA   Pandolfi P.P.;
RT   "PML regulates p53 stability by sequestering Mdm2 to the nucleolus.";
RL   Nat. Cell Biol. 6:665-672(2004).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MDM2 AND NOP53.
RX   PubMed=21804542; DOI=10.1038/nm.2392;
RA   Sasaki M., Kawahara K., Nishio M., Mimori K., Kogo R., Hamada K., Itoh B.,
RA   Wang J., Komatsu Y., Yang Y.R., Hikasa H., Horie Y., Yamashita T.,
RA   Kamijo T., Zhang Y., Zhu Y., Prives C., Nakano T., Mak T.W., Sasaki T.,
RA   Maehama T., Mori M., Suzuki A.;
RT   "Regulation of the MDM2-P53 pathway and tumor growth by PICT1 via nucleolar
RT   RPL11.";
RL   Nat. Med. 17:944-951(2011).
RN   [5] {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 ribosome, a large ribonucleoprotein complex
CC       responsible for the synthesis of proteins in the cell
CC       (PubMed:36517592). The small ribosomal subunit (SSU) binds messenger
CC       RNAs (mRNAs) and translates the encoded message by selecting cognate
CC       aminoacyl-transfer RNA (tRNA) molecules (PubMed:36517592). The large
CC       subunit (LSU) contains the ribosomal catalytic site termed the peptidyl
CC       transferase center (PTC), which catalyzes the formation of peptide
CC       bonds, thereby polymerizing the amino acids delivered by tRNAs into a
CC       polypeptide chain (PubMed:36517592). The nascent polypeptides leave the
CC       ribosome through a tunnel in the LSU and interact with protein factors
CC       that function in enzymatic processing, targeting, and the membrane
CC       insertion of nascent chains at the exit of the ribosomal tunnel
CC       (PubMed:36517592). As part of the 5S RNP/5S ribonucleoprotein particle
CC       it is an essential component of the LSU, required for its formation and
CC       the maturation of rRNAs (PubMed:36517592). It also couples ribosome
CC       biogenesis to p53/TP53 activation (PubMed:21804542). As part of the 5S
CC       RNP it accumulates in the nucleoplasm and inhibits MDM2, when ribosome
CC       biogenesis is perturbed, mediating the stabilization and the activation
CC       of TP53 (PubMed:21804542). Promotes nucleolar location of PML
CC       (PubMed:15195100). {ECO:0000269|PubMed:15195100,
CC       ECO:0000269|PubMed:21804542, ECO:0000269|PubMed:36517592}.
CC   -!- SUBUNIT: Component of the large ribosomal subunit (LSU)
CC       (PubMed:36517592). Part of a LSU subcomplex, the 5S RNP which is
CC       composed of the 5S RNA, RPL5 and RPL11 (By similarity). Interacts with
CC       PML (PubMed:15195100). Interacts with MDM2; negatively regulates MDM2-
CC       mediated TP53 ubiquitination and degradation (PubMed:15195100,
CC       PubMed:21804542). Interacts with NOP53; retains RPL11 into the
CC       nucleolus (PubMed:21804542). {ECO:0000250|UniProtKB:P62913,
CC       ECO:0000269|PubMed:15195100, ECO:0000269|PubMed:21804542,
CC       ECO:0000269|PubMed:36517592}.
CC   -!- INTERACTION:
CC       Q9CXW4; P23804: Mdm2; NbExp=4; IntAct=EBI-1548890, EBI-641788;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:15195100,
CC       ECO:0000269|PubMed:21804542}. Cytoplasm {ECO:0000269|PubMed:21804542,
CC       ECO:0000269|PubMed:36517592}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL5 family.
CC       {ECO:0000305}.
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DR   EMBL; AK002998; BAB22504.1; -; mRNA.
DR   EMBL; AK008422; BAB25660.1; -; mRNA.
DR   EMBL; AK011211; BAB27470.1; -; mRNA.
DR   EMBL; AK011800; BAB27850.1; -; mRNA.
DR   EMBL; AK013923; BAB29059.1; -; mRNA.
DR   EMBL; AK088967; BAC40676.1; -; mRNA.
DR   EMBL; AK153486; BAE32034.1; -; mRNA.
DR   EMBL; AK164445; BAE37793.1; -; mRNA.
DR   EMBL; AK169053; BAE40841.1; -; mRNA.
DR   EMBL; BC025077; AAH25077.1; -; mRNA.
DR   EMBL; BC069896; AAH69896.1; -; mRNA.
DR   CCDS; CCDS18799.1; -.
DR   RefSeq; NP_080195.1; NM_025919.2.
DR   PDB; 6SWA; EM; 3.10 A; J=1-178.
DR   PDB; 7CPU; EM; 2.82 A; LJ=1-178.
DR   PDB; 7CPV; EM; 3.03 A; LJ=1-178.
DR   PDB; 7LS1; EM; 3.30 A; E1=1-178.
DR   PDB; 7LS2; EM; 3.10 A; E1=1-178.
DR   PDBsum; 6SWA; -.
DR   PDBsum; 7CPU; -.
DR   PDBsum; 7CPV; -.
DR   PDBsum; 7LS1; -.
DR   PDBsum; 7LS2; -.
DR   AlphaFoldDB; Q9CXW4; -.
DR   EMDB; EMD-10321; -.
DR   EMDB; EMD-23500; -.
DR   EMDB; EMD-23501; -.
DR   EMDB; EMD-30432; -.
DR   EMDB; EMD-30433; -.
DR   SMR; Q9CXW4; -.
DR   BioGRID; 211883; 99.
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; Q9CXW4; -.
DR   IntAct; Q9CXW4; 3.
DR   MINT; Q9CXW4; -.
DR   STRING; 10090.ENSMUSP00000099595; -.
DR   MoonProt; Q9CXW4; -.
DR   GlyGen; Q9CXW4; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9CXW4; -.
DR   PhosphoSitePlus; Q9CXW4; -.
DR   SwissPalm; Q9CXW4; -.
DR   EPD; Q9CXW4; -.
DR   jPOST; Q9CXW4; -.
DR   MaxQB; Q9CXW4; -.
DR   PaxDb; 10090-ENSMUSP00000099595; -.
DR   PeptideAtlas; Q9CXW4; -.
DR   ProteomicsDB; 253326; -.
DR   Pumba; Q9CXW4; -.
DR   Antibodypedia; 1241; 361 antibodies from 31 providers.
DR   DNASU; 67025; -.
DR   Ensembl; ENSMUST00000102536.11; ENSMUSP00000099595.5; ENSMUSG00000059291.16.
DR   GeneID; 67025; -.
DR   KEGG; mmu:67025; -.
DR   UCSC; uc008vhr.1; mouse.
DR   AGR; MGI:1914275; -.
DR   CTD; 6135; -.
DR   MGI; MGI:1914275; Rpl11.
DR   VEuPathDB; HostDB:ENSMUSG00000059291; -.
DR   eggNOG; KOG0397; Eukaryota.
DR   GeneTree; ENSGT00910000144211; -.
DR   InParanoid; Q9CXW4; -.
DR   OMA; NPMKELK; -.
DR   OrthoDB; 5473480at2759; -.
DR   PhylomeDB; Q9CXW4; -.
DR   TreeFam; TF300017; -.
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; 67025; 23 hits in 74 CRISPR screens.
DR   ChiTaRS; Rpl11; mouse.
DR   PRO; PR:Q9CXW4; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q9CXW4; Protein.
DR   Bgee; ENSMUSG00000059291; Expressed in yolk sac and 145 other cell types or tissues.
DR   ExpressionAtlas; Q9CXW4; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
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; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0042788; C:polysomal ribosome; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0045202; C:synapse; ISO:MGI.
DR   GO; GO:0008097; F:5S rRNA binding; ISO:MGI.
DR   GO; GO:0042975; F:peroxisome proliferator activated receptor 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: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; ISO:MGI.
DR   GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR   GO; GO:2000435; P:negative regulation of protein neddylation; 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:1901798; P:positive regulation of signal transduction by p53 class mediator; IMP:UniProtKB.
DR   GO; GO:0034504; P:protein localization to nucleus; IMP:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR   GO; GO:0006605; P:protein targeting; ISO:MGI.
DR   GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; ISO:MGI.
DR   GO; GO:0042273; P:ribosomal large subunit biogenesis; ISO:MGI.
DR   GO; GO:0006364; P:rRNA processing; ISO:MGI.
DR   Gene3D; 3.30.1440.10; -; 1.
DR   InterPro; IPR002132; Ribosomal_uL5.
DR   InterPro; IPR031309; Ribosomal_uL5_C.
DR   InterPro; IPR020929; Ribosomal_uL5_CS.
DR   InterPro; IPR022803; Ribosomal_uL5_dom_sf.
DR   InterPro; IPR031310; Ribosomal_uL5_N.
DR   PANTHER; PTHR11994:SF8; 60S RIBOSOMAL PROTEIN L11; 1.
DR   PANTHER; PTHR11994; 60S RIBOSOMAL PROTEIN L11-RELATED; 1.
DR   Pfam; PF00281; Ribosomal_L5; 1.
DR   Pfam; PF00673; Ribosomal_L5_C; 1.
DR   PIRSF; PIRSF002161; Ribosomal_L5; 1.
DR   SUPFAM; SSF55282; RL5-like; 1.
DR   PROSITE; PS00358; RIBOSOMAL_L5; 1.
DR   Genevisible; Q9CXW4; MM.
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:P62913"
FT   CHAIN           2..178
FT                   /note="Large ribosomal subunit protein uL5"
FT                   /id="PRO_0000125083"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P62913"
FT   MOD_RES         44
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P62913"
FT   MOD_RES         47
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P62913"
FT   MOD_RES         52
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62913"
FT   MOD_RES         85
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62913"
FT   CROSSLNK        38
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P62913"
FT   CROSSLNK        52
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62913"
FT   CROSSLNK        154
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P62913"
FT   CONFLICT        48
FT                   /note="P -> Q (in Ref. 1; BAB29059)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   178 AA;  20252 MW;  26EC965C9239774E CRC64;
     MAQDQGEKEN PMRELRIRKL CLNICVGESG DRLTRAAKVL EQLTGQTPVF SKARYTVRSF
     GIRRNEKIAV HCTVRGAKAE EILEKGLKVR EYELRKNNFS DTGNFGFGIQ EHIDLGIKYD
     PSIGIYGLDF YVVLGRPGFS IADKKRRTGC IGAKHRISKE EAMRWFQQKY DGIILPGK
//