RL23_HUMAN
ID RL23_HUMAN Reviewed; 140 AA.
AC P62829; P23131; P24048; Q29246; Q3SWV7; Q6P5S1;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=60S ribosomal protein L23;
DE AltName: Full=60S ribosomal protein L17;
DE AltName: Full=Large ribosomal subunit protein uL14 {ECO:0000303|PubMed:24524803};
GN Name=RPL23;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1861993; DOI=10.1093/nar/19.14.4001;
RA Herault Y., Michel D., Chatelain G., Brun G.;
RT "cDNA and predicted amino acid sequences of the human ribosomal protein
RT genes rpS12 and rpL17.";
RL Nucleic Acids Res. 19:4001-4001(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1874450; DOI=10.1016/0378-1119(91)90091-o;
RA Berchtold M.W., Berger M.C.;
RT "Isolation and analysis of a human cDNA highly homologous to the yeast gene
RT encoding L17A ribosomal protein.";
RL Gene 102:283-288(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11875025; DOI=10.1101/gr.214202;
RA Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S.,
RA Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.;
RT "The human ribosomal protein genes: sequencing and comparative analysis of
RT 73 genes.";
RL Genome Res. 12:379-390(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Kidney, and Uterus;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-38, AND IDENTIFICATION BY
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP NOMENCLATURE.
RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT "A new system for naming ribosomal proteins.";
RL Curr. Opin. Struct. Biol. 24:165-169(2014).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [11]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
RN [12] {ECO:0007744|PDB:6LQM, ECO:0007744|PDB:6LSR, ECO:0007744|PDB:6LSS, ECO:0007744|PDB:6LU8}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.09 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=32669547; DOI=10.1038/s41467-020-17237-x;
RA Liang X., Zuo M.Q., Zhang Y., Li N., Ma C., Dong M.Q., Gao N.;
RT "Structural snapshots of human pre-60S ribosomal particles before and after
RT nuclear export.";
RL Nat. Commun. 11:3542-3542(2020).
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:0000269|PubMed:23636399,
CC ECO:0000269|PubMed:32669547}.
CC -!- SUBUNIT: Component of the large ribosomal subunit.
CC {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547}.
CC -!- INTERACTION:
CC P62829; Q9P287: BCCIP; NbExp=7; IntAct=EBI-353303, EBI-711154;
CC P62829; Q00987: MDM2; NbExp=3; IntAct=EBI-353303, EBI-389668;
CC P62829; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-353303, EBI-16439278;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL14 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; X52839; CAA37023.1; -; mRNA.
DR EMBL; X55954; CAA39417.1; -; mRNA.
DR EMBL; AB061827; BAB79465.1; -; Genomic_DNA.
DR EMBL; BC010114; AAH10114.1; -; mRNA.
DR EMBL; BC062716; AAH62716.1; -; mRNA.
DR EMBL; BC104651; AAI04652.1; -; mRNA.
DR EMBL; BC106061; AAI06062.1; -; mRNA.
DR CCDS; CCDS11330.1; -.
DR PIR; S18815; R5HU23.
DR RefSeq; NP_000969.1; NM_000978.3.
DR PDB; 4UG0; EM; -; LV=1-140.
DR PDB; 4V6X; EM; 5.00 A; CV=1-140.
DR PDB; 5AJ0; EM; 3.50 A; AV=1-140.
DR PDB; 5LKS; EM; 3.60 A; LV=1-140.
DR PDB; 5T2C; EM; 3.60 A; P=1-140.
DR PDB; 6IP5; EM; 3.90 A; 2P=1-140.
DR PDB; 6IP6; EM; 4.50 A; 2P=1-140.
DR PDB; 6IP8; EM; 3.90 A; 2P=1-140.
DR PDB; 6LQM; EM; 3.09 A; e=1-140.
DR PDB; 6LSR; EM; 3.13 A; e=1-140.
DR PDB; 6LSS; EM; 3.23 A; e=1-140.
DR PDB; 6LU8; EM; 3.13 A; e=1-140.
DR PDB; 6OLE; EM; 3.10 A; W=12-140.
DR PDB; 6OLF; EM; 3.90 A; W=12-140.
DR PDB; 6OLG; EM; 3.40 A; AV=12-140.
DR PDB; 6OLI; EM; 3.50 A; W=12-140.
DR PDB; 6OLZ; EM; 3.90 A; AV=12-140.
DR PDB; 6OM0; EM; 3.10 A; W=12-140.
DR PDB; 6OM7; EM; 3.70 A; W=12-140.
DR PDB; 6QZP; EM; 2.90 A; LV=10-140.
DR PDB; 6XA1; EM; 2.80 A; LV=10-140.
DR PDB; 6Y0G; EM; 3.20 A; LV=1-140.
DR PDB; 6Y2L; EM; 3.00 A; LV=1-140.
DR PDB; 6Y57; EM; 3.50 A; LV=1-140.
DR PDB; 6Y6X; EM; 2.80 A; LV=10-140.
DR PDB; 6Z6L; EM; 3.00 A; LV=1-140.
DR PDB; 6Z6M; EM; 3.10 A; LV=1-140.
DR PDB; 6Z6N; EM; 2.90 A; LV=1-140.
DR PDB; 6ZM7; EM; 2.70 A; LV=1-140.
DR PDB; 6ZME; EM; 3.00 A; LV=1-140.
DR PDB; 6ZMI; EM; 2.60 A; LV=1-140.
DR PDB; 6ZMO; EM; 3.10 A; LV=1-140.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 5AJ0; -.
DR PDBsum; 5LKS; -.
DR PDBsum; 5T2C; -.
DR PDBsum; 6IP5; -.
DR PDBsum; 6IP6; -.
DR PDBsum; 6IP8; -.
DR PDBsum; 6LQM; -.
DR PDBsum; 6LSR; -.
DR PDBsum; 6LSS; -.
DR PDBsum; 6LU8; -.
DR PDBsum; 6OLE; -.
DR PDBsum; 6OLF; -.
DR PDBsum; 6OLG; -.
DR PDBsum; 6OLI; -.
DR PDBsum; 6OLZ; -.
DR PDBsum; 6OM0; -.
DR PDBsum; 6OM7; -.
DR PDBsum; 6QZP; -.
DR PDBsum; 6XA1; -.
DR PDBsum; 6Y0G; -.
DR PDBsum; 6Y2L; -.
DR PDBsum; 6Y57; -.
DR PDBsum; 6Y6X; -.
DR PDBsum; 6Z6L; -.
DR PDBsum; 6Z6M; -.
DR PDBsum; 6Z6N; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR AlphaFoldDB; P62829; -.
DR SMR; P62829; -.
DR BioGRID; 114752; 469.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR CORUM; P62829; -.
DR DIP; DIP-33156N; -.
DR IntAct; P62829; 119.
DR MINT; P62829; -.
DR STRING; 9606.ENSP00000420311; -.
DR DrugBank; DB02494; (S)-3-phenyllactic acid.
DR DrugBank; DB07374; Anisomycin.
DR DrugBank; DB08437; Puromycin.
DR MoonProt; P62829; -.
DR GlyGen; P62829; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62829; -.
DR MetOSite; P62829; -.
DR PhosphoSitePlus; P62829; -.
DR SwissPalm; P62829; -.
DR BioMuta; RPL23; -.
DR DMDM; 51338639; -.
DR SWISS-2DPAGE; P62829; -.
DR EPD; P62829; -.
DR jPOST; P62829; -.
DR MassIVE; P62829; -.
DR MaxQB; P62829; -.
DR PaxDb; P62829; -.
DR PeptideAtlas; P62829; -.
DR PRIDE; P62829; -.
DR ProteomicsDB; 57430; -.
DR TopDownProteomics; P62829; -.
DR Antibodypedia; 1251; 187 antibodies from 31 providers.
DR DNASU; 9349; -.
DR Ensembl; ENST00000394332.5; ENSP00000377865.1; ENSG00000125691.14.
DR Ensembl; ENST00000479035.7; ENSP00000420311.2; ENSG00000125691.14.
DR GeneID; 9349; -.
DR KEGG; hsa:9349; -.
DR MANE-Select; ENST00000479035.7; ENSP00000420311.2; NM_000978.4; NP_000969.1.
DR UCSC; uc002hqx.2; human.
DR CTD; 9349; -.
DR DisGeNET; 9349; -.
DR GeneCards; RPL23; -.
DR HGNC; HGNC:10316; RPL23.
DR HPA; ENSG00000125691; Low tissue specificity.
DR MIM; 603662; gene.
DR neXtProt; NX_P62829; -.
DR OpenTargets; ENSG00000125691; -.
DR PharmGKB; PA34690; -.
DR VEuPathDB; HostDB:ENSG00000125691; -.
DR eggNOG; KOG0901; Eukaryota.
DR GeneTree; ENSGT00390000004690; -.
DR HOGENOM; CLU_095071_3_0_1; -.
DR InParanoid; P62829; -.
DR OMA; AKEVLCI; -.
DR OrthoDB; 1374830at2759; -.
DR PhylomeDB; P62829; -.
DR TreeFam; TF300913; -.
DR PathwayCommons; P62829; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-156902; Peptide chain elongation.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-192823; Viral mRNA Translation.
DR Reactome; R-HSA-2408557; Selenocysteine synthesis.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-HSA-72764; Eukaryotic Translation Termination.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency.
DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P62829; -.
DR SIGNOR; P62829; -.
DR BioGRID-ORCS; 9349; 805 hits in 1021 CRISPR screens.
DR ChiTaRS; RPL23; human.
DR GeneWiki; RPL23; -.
DR GenomeRNAi; 9349; -.
DR Pharos; P62829; Tbio.
DR PRO; PR:P62829; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P62829; protein.
DR Bgee; ENSG00000125691; Expressed in ganglionic eminence and 128 other tissues.
DR ExpressionAtlas; P62829; baseline and differential.
DR Genevisible; P62829; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
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; IDA:FlyBase.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:CAFA.
DR GO; GO:0005654; C:nucleoplasm; IDA:CAFA.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0005840; C:ribosome; NAS:UniProtKB.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0001223; F:transcription coactivator binding; IPI:CAFA.
DR GO; GO:1990948; F:ubiquitin ligase inhibitor activity; IDA:CAFA.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:CAFA.
DR GO; GO:0072717; P:cellular response to actinomycin D; IMP:CAFA.
DR GO; GO:0002181; P:cytoplasmic translation; IC:FlyBase.
DR GO; GO:0070314; P:G1 to G0 transition; IMP:CAFA.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:CAFA.
DR GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; IDA:CAFA.
DR GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; IDA:CAFA.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:CAFA.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:CAFA.
DR GO; GO:1901798; P:positive regulation of signal transduction by p53 class mediator; IMP:CAFA.
DR GO; GO:0050821; P:protein stabilization; IMP:CAFA.
DR GO; GO:0032986; P:protein-DNA complex disassembly; IDA:CAFA.
DR GO; GO:1903450; P:regulation of G1 to G0 transition; IMP:CAFA.
DR GO; GO:0006610; P:ribosomal protein import into nucleus; NAS:UniProtKB.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
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_0000128612"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 38
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT CONFLICT 77
FT /note="H -> R (in Ref. 4; AAH62716)"
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
