RL11_MOUSE
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 03-AUG-2022, entry version 165.
DE RecName: 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).
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 (PubMed:21804542). Promotes
CC nucleolar location of PML (PubMed:15195100).
CC {ECO:0000269|PubMed:15195100, ECO:0000269|PubMed:21804542}.
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 (By similarity). Interacts with PML (PubMed:15195100). Interacts with
CC MDM2; negatively regulates MDM2-mediated TP53 ubiquitination and
CC degradation (PubMed:15195100, PubMed:21804542). Interacts with NOP53;
CC retains RPL11 into the nucleolus (PubMed:21804542).
CC {ECO:0000250|UniProtKB:P62913, ECO:0000269|PubMed:15195100,
CC ECO:0000269|PubMed:21804542}.
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 -!- 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 SMR; Q9CXW4; -.
DR BioGRID; 211883; 96.
DR ComplexPortal; CPX-5262; 60S cytosolic large ribosomal subunit.
DR CORUM; Q9CXW4; -.
DR IntAct; Q9CXW4; 3.
DR MINT; Q9CXW4; -.
DR STRING; 10090.ENSMUSP00000099595; -.
DR MoonProt; Q9CXW4; -.
DR iPTMnet; Q9CXW4; -.
DR PhosphoSitePlus; Q9CXW4; -.
DR SwissPalm; Q9CXW4; -.
DR EPD; Q9CXW4; -.
DR jPOST; Q9CXW4; -.
DR MaxQB; Q9CXW4; -.
DR PaxDb; Q9CXW4; -.
DR PeptideAtlas; Q9CXW4; -.
DR PRIDE; Q9CXW4; -.
DR ProteomicsDB; 253326; -.
DR Antibodypedia; 1241; 332 antibodies from 31 providers.
DR DNASU; 67025; -.
DR Ensembl; ENSMUST00000102536; ENSMUSP00000099595; ENSMUSG00000059291.
DR GeneID; 67025; -.
DR KEGG; mmu:67025; -.
DR UCSC; uc008vhr.1; mouse.
DR CTD; 6135; -.
DR MGI; MGI:1914275; Rpl11.
DR VEuPathDB; HostDB:ENSMUSG00000059291; -.
DR eggNOG; KOG0397; Eukaryota.
DR GeneTree; ENSGT00910000144211; -.
DR InParanoid; Q9CXW4; -.
DR OMA; QTETIKW; -.
DR OrthoDB; 1340833at2759; -.
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 70 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 142 other tissues.
DR ExpressionAtlas; Q9CXW4; baseline and differential.
DR Genevisible; Q9CXW4; MM.
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; IPI:ComplexPortal.
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; 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; ISO:MGI.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; 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: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:1902255; P:positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator; IMP:CAFA.
DR GO; GO:0032092; P:positive regulation of protein binding; 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: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 Gene3D; 3.30.1440.10; -; 1.
DR InterPro; IPR002132; Ribosomal_L5.
DR InterPro; IPR031309; Ribosomal_L5_C.
DR InterPro; IPR020929; Ribosomal_L5_CS.
DR InterPro; IPR022803; Ribosomal_L5_dom_sf.
DR InterPro; IPR031310; Ribosomal_L5_N.
DR PANTHER; PTHR11994; PTHR11994; 1.
DR Pfam; PF00281; Ribosomal_L5; 1.
DR Pfam; PF00673; Ribosomal_L5_C; 1.
DR PIRSF; PIRSF002161; Ribosomal_L5; 1.
DR SUPFAM; SSF55282; SSF55282; 1.
DR PROSITE; PS00358; RIBOSOMAL_L5; 1.
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="60S ribosomal protein L11"
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
