RL23_MOUSE
ID RL23_MOUSE Reviewed; 140 AA.
AC P62830; P23131; P24048; Q29246; Q3THU4; Q9CZE6; Q9DCQ4;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=60S ribosomal protein L23;
GN Name=Rpl23;
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=BALB/cJ, and FVB/NJ;
RX PubMed=11124519; DOI=10.1159/000056774;
RA Kleiter N., Artner I., Copeland N.G., Gilbert D.J., Jenkins N.A.,
RA Kratochwil K.;
RT "Genomic organization and chromosome location of the murine Rpl23 gene.";
RL Cytogenet. Cell Genet. 90:227-230(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Kidney;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Mammary gland;
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 [4]
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).
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:P62829}.
CC -!- SUBUNIT: Component of the large ribosomal subunit.
CC {ECO:0000250|UniProtKB:P62829}.
CC -!- INTERACTION:
CC P62830; P23804: Mdm2; NbExp=2; IntAct=EBI-2365752, EBI-641788;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62829}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL14 family.
CC {ECO:0000305}.
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DR EMBL; AF158022; AAD42413.1; -; Genomic_DNA.
DR EMBL; AF287271; AAF88071.1; -; mRNA.
DR EMBL; AK002579; BAB22203.1; -; mRNA.
DR EMBL; AK010680; BAB27112.1; -; mRNA.
DR EMBL; AK012694; BAB28415.1; -; mRNA.
DR EMBL; AK018730; BAB31373.1; -; mRNA.
DR EMBL; AK150671; BAE29753.1; -; mRNA.
DR EMBL; AK168133; BAE40102.1; -; mRNA.
DR EMBL; BC025918; AAH25918.1; -; mRNA.
DR EMBL; BC081448; AAH81448.1; -; mRNA.
DR CCDS; CCDS25331.1; -.
DR RefSeq; NP_075029.1; NM_022891.3.
DR RefSeq; XP_003688806.1; XM_003688758.3.
DR RefSeq; XP_003689266.1; XM_003689218.3.
DR PDB; 6SWA; EM; 3.10 A; T=1-140.
DR PDB; 7CPU; EM; 2.82 A; LV=1-140.
DR PDB; 7CPV; EM; 3.03 A; LV=1-140.
DR PDB; 7LS1; EM; 3.30 A; P2=1-140.
DR PDB; 7LS2; EM; 3.10 A; P2=1-140.
DR PDBsum; 6SWA; -.
DR PDBsum; 7CPU; -.
DR PDBsum; 7CPV; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; P62830; -.
DR SMR; P62830; -.
DR BioGRID; 211121; 71.
DR BioGRID; 3404800; 2.
DR BioGRID; 787698; 3.
DR ComplexPortal; CPX-5262; 60S cytosolic large ribosomal subunit.
DR IntAct; P62830; 10.
DR MINT; P62830; -.
DR STRING; 10090.ENSMUSP00000099435; -.
DR iPTMnet; P62830; -.
DR PhosphoSitePlus; P62830; -.
DR SwissPalm; P62830; -.
DR EPD; P62830; -.
DR jPOST; P62830; -.
DR MaxQB; P62830; -.
DR PaxDb; P62830; -.
DR PeptideAtlas; P62830; -.
DR PRIDE; P62830; -.
DR ProteomicsDB; 253306; -.
DR Antibodypedia; 1251; 187 antibodies from 31 providers.
DR DNASU; 65019; -.
DR Ensembl; ENSMUST00000103146; ENSMUSP00000099435; ENSMUSG00000071415.
DR GeneID; 65019; -.
DR KEGG; mmu:65019; -.
DR UCSC; uc007leu.2; mouse.
DR CTD; 9349; -.
DR MGI; MGI:1929455; Rpl23.
DR VEuPathDB; HostDB:ENSMUSG00000071415; -.
DR eggNOG; KOG0901; Eukaryota.
DR GeneTree; ENSGT00390000004690; -.
DR HOGENOM; CLU_095071_3_0_1; -.
DR InParanoid; P62830; -.
DR OMA; AKEVLCI; -.
DR OrthoDB; 1374830at2759; -.
DR PhylomeDB; P62830; -.
DR TreeFam; TF300913; -.
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; 65019; 26 hits in 67 CRISPR screens.
DR ChiTaRS; Rpl23; mouse.
DR PRO; PR:P62830; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P62830; protein.
DR Bgee; ENSMUSG00000071415; Expressed in yolk sac and 228 other tissues.
DR ExpressionAtlas; P62830; baseline and differential.
DR Genevisible; P62830; MM.
DR GO; GO:0005737; C:cytoplasm; 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; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:0001223; F:transcription coactivator binding; 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:0072717; P:cellular response to actinomycin D; ISO:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0070314; P:G1 to G0 transition; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; 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:0008284; P:positive regulation of cell population proliferation; 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; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0032986; P:protein-DNA complex disassembly; ISO:MGI.
DR GO; GO:1903450; P:regulation of G1 to G0 transition; ISO:MGI.
DR GO; GO:0006412; P:translation; ISO:MGI.
DR Gene3D; 2.40.150.20; -; 1.
DR HAMAP; MF_01367; Ribosomal_L14; 1.
DR InterPro; IPR036853; Ribosomal_L14_sf.
DR InterPro; IPR000218; Ribosomal_L14P.
DR InterPro; IPR019972; Ribosomal_L14P_CS.
DR PANTHER; PTHR11761; PTHR11761; 1.
DR Pfam; PF00238; Ribosomal_L14; 1.
DR SMART; SM01374; Ribosomal_L14; 1.
DR SUPFAM; SSF50193; SSF50193; 1.
DR PROSITE; PS00049; RIBOSOMAL_L14; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..140
FT /note="60S ribosomal protein L23"
FT /id="PRO_0000128613"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62829"
FT MOD_RES 38
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P62829"
FT CONFLICT 53
FT /note="P -> S (in Ref. 2; BAB22203)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="M -> I (in Ref. 2; BAB28415)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 140 AA; 14865 MW; 807E14139B2EB0B5 CRC64;
MSKRGRGGSS GAKFRISLGL PVGAVINCAD NTGAKNLYII SVKGIKGRLN RLPAAGVGDM
VMATVKKGKP ELRKKVHPAV VIRQRKSYRR KDGVFLYFED NAGVIVNNKG EMKGSAITGP
VAKECADLWP RIASNAGSIA
