RS23_HUMAN
ID RS23_HUMAN Reviewed; 143 AA.
AC P62266; P39028; Q6IB08;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=40S ribosomal protein S23;
DE AltName: Full=Small ribosomal subunit protein uS12 {ECO:0000303|PubMed:24524803};
GN Name=RPS23;
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=8415000; DOI=10.1093/nar/21.18.4394;
RA Hori N., Murakawa K., Matoba R., Fukushima A., Okubo K., Matsubara K.;
RT "A cDNA sequence of human ribosomal protein, homologue of yeast S28.";
RL Nucleic Acids Res. 21:4394-4394(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 PROTEIN SEQUENCE OF 2-10.
RC TISSUE=Placenta;
RX PubMed=8706699; DOI=10.1111/j.1432-1033.1996.0144u.x;
RA Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A.,
RA Thiede B., Wittmann-Liebold B., Otto A.;
RT "Characterization of the human small-ribosomal-subunit proteins by N-
RT terminal and internal sequencing, and mass spectrometry.";
RL Eur. J. Biochem. 239:144-149(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 84-142.
RX PubMed=9582194; DOI=10.1101/gr.8.5.509;
RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J.,
RA Tanaka T., Page D.C.;
RT "A map of 75 human ribosomal protein genes.";
RL Genome Res. 8:509-523(1998).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-135, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
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 HYDROXYLATION AT PRO-62.
RX PubMed=24550462; DOI=10.1073/pnas.1311750111;
RA Loenarz C., Sekirnik R., Thalhammer A., Ge W., Spivakovsky E.,
RA Mackeen M.M., McDonough M.A., Cockman M.E., Kessler B.M., Ratcliffe P.J.,
RA Wolf A., Schofield C.J.;
RT "Hydroxylation of the eukaryotic ribosomal decoding center affects
RT translational accuracy.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:4019-4024(2014).
RN [10]
RP HYDROXYLATION AT PRO-62.
RX PubMed=24550447; DOI=10.1073/pnas.1314482111;
RA Singleton R.S., Liu-Yi P., Formenti F., Ge W., Sekirnik R., Fischer R.,
RA Adam J., Pollard P.J., Wolf A., Thalhammer A., Loenarz C., Flashman E.,
RA Yamamoto A., Coleman M.L., Kessler B.M., Wappner P., Schofield C.J.,
RA Ratcliffe P.J., Cockman M.E.;
RT "OGFOD1 catalyzes prolyl hydroxylation of RPS23 and is involved in
RT translation control and stress granule formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:4031-4036(2014).
RN [11]
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 [12]
RP FUNCTION, HYDROXYLATION AT PRO-62, INVOLVEMENT IN BTDD, VARIANTS BTDD
RP LYS-67 AND ILE-120, AND CHARACTERIZATION OF VARIANTS BTDD LYS-67 AND
RP ILE-120.
RX PubMed=28257692; DOI=10.1016/j.ajhg.2017.01.034;
RA Paolini N.A., Attwood M., Sondalle S.B., Vieira C.M., van Adrichem A.M.,
RA di Summa F.M., O'Donohue M.F., Gleizes P.E., Rachuri S., Briggs J.W.,
RA Fischer R., Ratcliffe P.J., Wlodarski M.W., Houtkooper R.H.,
RA von Lindern M., Kuijpers T.W., Dinman J.D., Baserga S.J., Cockman M.E.,
RA MacInnes A.W.;
RT "A ribosomopathy reveals decoding defective ribosomes driving human
RT dysmorphism.";
RL Am. J. Hum. Genet. 100:506-522(2017).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-37, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [14]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
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 [15] {ECO:0007744|PDB:5AJ0}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=25957688; DOI=10.1016/j.cell.2015.03.052;
RA Behrmann E., Loerke J., Budkevich T.V., Yamamoto K., Schmidt A.,
RA Penczek P.A., Vos M.R., Burger J., Mielke T., Scheerer P., Spahn C.M.;
RT "Structural snapshots of actively translating human ribosomes.";
RL Cell 161:845-857(2015).
RN [16] {ECO:0007744|PDB:4UG0}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=25901680; DOI=10.1038/nature14427;
RA Khatter H., Myasnikov A.G., Natchiar S.K., Klaholz B.P.;
RT "Structure of the human 80S ribosome.";
RL Nature 520:640-645(2015).
CC -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell (PubMed:28257692,
CC PubMed:23636399, PubMed:25957688, PubMed:25901680). The small ribosomal
CC subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded
CC message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules.
CC The large subunit (LSU) contains the ribosomal catalytic site termed
CC the peptidyl transferase center (PTC), which catalyzes the formation of
CC peptide bonds, thereby polymerizing the amino acids delivered by tRNAs
CC into a polypeptide chain. The nascent polypeptides leave the ribosome
CC through a tunnel in the LSU and interact with protein factors that
CC function in enzymatic processing, targeting, and the membrane insertion
CC of nascent chains at the exit of the ribosomal tunnel (PubMed:23636399,
CC PubMed:25957688, PubMed:25901680). Plays an important role in
CC translational accuracy (PubMed:28257692). {ECO:0000269|PubMed:23636399,
CC ECO:0000269|PubMed:25901680, ECO:0000269|PubMed:25957688,
CC ECO:0000269|PubMed:28257692}.
CC -!- SUBUNIT: Component of the 40S small ribosomal subunit.
CC {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:25901680,
CC ECO:0000269|PubMed:25957688}.
CC -!- INTERACTION:
CC P62266; P43146: DCC; NbExp=2; IntAct=EBI-353072, EBI-1222919;
CC P62266; Q5S007: LRRK2; NbExp=2; IntAct=EBI-353072, EBI-5323863;
CC P62266; Q8N543: OGFOD1; NbExp=3; IntAct=EBI-353072, EBI-13327083;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:25957688}.
CC Cytoplasm {ECO:0000305|PubMed:23636399, ECO:0000305|PubMed:25901680}.
CC Rough endoplasmic reticulum {ECO:0000250|UniProtKB:Q6SA96}.
CC Note=Detected on cytosolic polysomes (PubMed:25957688). Detected in
CC ribosomes that are associated with the rough endoplasmic reticulum (By
CC similarity). {ECO:0000250|UniProtKB:Q6SA96,
CC ECO:0000269|PubMed:25957688}.
CC -!- PTM: Hydroxylation at Pro-62 affects translation termination
CC efficiency. {ECO:0000269|PubMed:24550447, ECO:0000269|PubMed:24550462,
CC ECO:0000269|PubMed:28257692}.
CC -!- DISEASE: Brachycephaly, trichomegaly, and developmental delay (BTDD)
CC [MIM:617412]: An autosomal dominant developmental disorder
CC characterized by brachycephaly, ciliary trichomegaly, dysmorphic
CC features of the face and hands, hearing loss, and developmental delay
CC with short stature. Intellectual disability and autism spectrum
CC disorder may be present in some patients.
CC {ECO:0000269|PubMed:28257692}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS12 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; D14530; BAA03400.1; -; mRNA.
DR EMBL; CR456996; CAG33277.1; -; mRNA.
DR EMBL; BC070221; AAH70221.1; -; mRNA.
DR EMBL; AB007158; BAA25822.1; -; Genomic_DNA.
DR CCDS; CCDS47241.1; -.
DR PIR; S42105; S42105.
DR RefSeq; NP_001016.1; NM_001025.4.
DR PDB; 4CXG; EM; 8.70 A; X=1-143.
DR PDB; 4CXH; EM; 8.90 A; X=1-143.
DR PDB; 4UG0; EM; -; SX=1-143.
DR PDB; 4V6X; EM; 5.00 A; AX=1-143.
DR PDB; 5A2Q; EM; 3.90 A; X=1-143.
DR PDB; 5AJ0; EM; 3.50 A; BX=1-143.
DR PDB; 5FLX; EM; 3.90 A; X=1-143.
DR PDB; 5LKS; EM; 3.60 A; SX=1-143.
DR PDB; 5OA3; EM; 4.30 A; X=1-143.
DR PDB; 5T2C; EM; 3.60 A; AD=1-143.
DR PDB; 5VYC; X-ray; 6.00 A; X1/X2/X3/X4/X5/X6=1-143.
DR PDB; 6FEC; EM; 6.30 A; Q=1-142.
DR PDB; 6G18; EM; 3.60 A; X=1-143.
DR PDB; 6G4S; EM; 4.00 A; X=1-143.
DR PDB; 6G4W; EM; 4.50 A; X=1-143.
DR PDB; 6G51; EM; 4.10 A; X=1-143.
DR PDB; 6G53; EM; 4.50 A; X=1-143.
DR PDB; 6G5H; EM; 3.60 A; X=1-143.
DR PDB; 6G5I; EM; 3.50 A; X=1-143.
DR PDB; 6IP5; EM; 3.90 A; 3B=1-143.
DR PDB; 6IP6; EM; 4.50 A; 3B=1-143.
DR PDB; 6IP8; EM; 3.90 A; 3B=1-143.
DR PDB; 6OLE; EM; 3.10 A; SX=2-142.
DR PDB; 6OLF; EM; 3.90 A; SX=2-142.
DR PDB; 6OLG; EM; 3.40 A; BX=2-140.
DR PDB; 6OLI; EM; 3.50 A; SX=2-142.
DR PDB; 6OLZ; EM; 3.90 A; BX=2-140.
DR PDB; 6OM0; EM; 3.10 A; SX=2-142.
DR PDB; 6OM7; EM; 3.70 A; SX=2-142.
DR PDB; 6QZP; EM; 2.90 A; SX=2-142.
DR PDB; 6XA1; EM; 2.80 A; SX=2-140.
DR PDB; 6Y0G; EM; 3.20 A; SX=1-143.
DR PDB; 6Y2L; EM; 3.00 A; SX=1-143.
DR PDB; 6Y57; EM; 3.50 A; SX=1-143.
DR PDB; 6YBW; EM; 3.10 A; E=1-143.
DR PDB; 6Z6L; EM; 3.00 A; SX=1-143.
DR PDB; 6Z6M; EM; 3.10 A; SX=1-143.
DR PDB; 6Z6N; EM; 2.90 A; SX=1-143.
DR PDB; 6ZLW; EM; 2.60 A; X=1-143.
DR PDB; 6ZM7; EM; 2.70 A; SX=1-143.
DR PDB; 6ZME; EM; 3.00 A; SX=1-143.
DR PDB; 6ZMI; EM; 2.60 A; SX=1-143.
DR PDB; 6ZMO; EM; 3.10 A; SX=1-143.
DR PDB; 6ZMT; EM; 3.00 A; X=1-143.
DR PDB; 6ZMW; EM; 3.70 A; E=1-143.
DR PDB; 6ZN5; EM; 3.20 A; X=2-142.
DR PDB; 6ZOJ; EM; 2.80 A; X=1-143.
DR PDB; 6ZOK; EM; 2.80 A; X=1-143.
DR PDB; 6ZON; EM; 3.00 A; j=1-143.
DR PDB; 6ZP4; EM; 2.90 A; j=1-143.
DR PDB; 6ZUO; EM; 3.10 A; X=1-143.
DR PDB; 6ZV6; EM; 2.90 A; X=1-143.
DR PDB; 6ZVH; EM; 2.90 A; X=2-142.
DR PDB; 6ZVJ; EM; 3.80 A; j=2-140.
DR PDB; 6ZXD; EM; 3.20 A; X=1-143.
DR PDB; 6ZXE; EM; 3.00 A; X=1-143.
DR PDB; 6ZXF; EM; 3.70 A; X=1-143.
DR PDB; 6ZXG; EM; 2.60 A; X=1-143.
DR PDB; 6ZXH; EM; 2.70 A; X=1-143.
DR PDB; 7A09; EM; 3.50 A; j=1-143.
DR PDB; 7K5I; EM; 2.90 A; X=1-143.
DR PDB; 7MQ8; EM; 3.60 A; SR=1-143.
DR PDB; 7MQ9; EM; 3.87 A; SR=1-143.
DR PDB; 7MQA; EM; 2.70 A; SR=1-143.
DR PDBsum; 4CXG; -.
DR PDBsum; 4CXH; -.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 5A2Q; -.
DR PDBsum; 5AJ0; -.
DR PDBsum; 5FLX; -.
DR PDBsum; 5LKS; -.
DR PDBsum; 5OA3; -.
DR PDBsum; 5T2C; -.
DR PDBsum; 5VYC; -.
DR PDBsum; 6FEC; -.
DR PDBsum; 6G18; -.
DR PDBsum; 6G4S; -.
DR PDBsum; 6G4W; -.
DR PDBsum; 6G51; -.
DR PDBsum; 6G53; -.
DR PDBsum; 6G5H; -.
DR PDBsum; 6G5I; -.
DR PDBsum; 6IP5; -.
DR PDBsum; 6IP6; -.
DR PDBsum; 6IP8; -.
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; 6YBW; -.
DR PDBsum; 6Z6L; -.
DR PDBsum; 6Z6M; -.
DR PDBsum; 6Z6N; -.
DR PDBsum; 6ZLW; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 6ZMT; -.
DR PDBsum; 6ZMW; -.
DR PDBsum; 6ZN5; -.
DR PDBsum; 6ZOJ; -.
DR PDBsum; 6ZOK; -.
DR PDBsum; 6ZON; -.
DR PDBsum; 6ZP4; -.
DR PDBsum; 6ZUO; -.
DR PDBsum; 6ZV6; -.
DR PDBsum; 6ZVH; -.
DR PDBsum; 6ZVJ; -.
DR PDBsum; 6ZXD; -.
DR PDBsum; 6ZXE; -.
DR PDBsum; 6ZXF; -.
DR PDBsum; 6ZXG; -.
DR PDBsum; 6ZXH; -.
DR PDBsum; 7A09; -.
DR PDBsum; 7K5I; -.
DR PDBsum; 7MQ8; -.
DR PDBsum; 7MQ9; -.
DR PDBsum; 7MQA; -.
DR AlphaFoldDB; P62266; -.
DR SMR; P62266; -.
DR BioGRID; 112142; 273.
DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR CORUM; P62266; -.
DR IntAct; P62266; 57.
DR MINT; P62266; -.
DR STRING; 9606.ENSP00000296674; -.
DR GlyGen; P62266; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62266; -.
DR PhosphoSitePlus; P62266; -.
DR SwissPalm; P62266; -.
DR BioMuta; RPS23; -.
DR DMDM; 50403755; -.
DR EPD; P62266; -.
DR jPOST; P62266; -.
DR MassIVE; P62266; -.
DR MaxQB; P62266; -.
DR PaxDb; P62266; -.
DR PeptideAtlas; P62266; -.
DR PRIDE; P62266; -.
DR ProteomicsDB; 57380; -.
DR TopDownProteomics; P62266; -.
DR Antibodypedia; 24716; 142 antibodies from 22 providers.
DR DNASU; 6228; -.
DR Ensembl; ENST00000296674.13; ENSP00000296674.8; ENSG00000186468.13.
DR Ensembl; ENST00000651545.1; ENSP00000498621.1; ENSG00000186468.13.
DR GeneID; 6228; -.
DR KEGG; hsa:6228; -.
DR MANE-Select; ENST00000296674.13; ENSP00000296674.8; NM_001025.5; NP_001016.1.
DR UCSC; uc003khu.4; human.
DR CTD; 6228; -.
DR DisGeNET; 6228; -.
DR GeneCards; RPS23; -.
DR HGNC; HGNC:10410; RPS23.
DR HPA; ENSG00000186468; Low tissue specificity.
DR MalaCards; RPS23; -.
DR MIM; 603683; gene.
DR MIM; 617412; phenotype.
DR neXtProt; NX_P62266; -.
DR OpenTargets; ENSG00000186468; -.
DR PharmGKB; PA34813; -.
DR VEuPathDB; HostDB:ENSG00000186468; -.
DR eggNOG; KOG1749; Eukaryota.
DR GeneTree; ENSGT00550000074784; -.
DR HOGENOM; CLU_115574_0_1_1; -.
DR InParanoid; P62266; -.
DR OMA; KFRWSQR; -.
DR OrthoDB; 1402984at2759; -.
DR PhylomeDB; P62266; -.
DR TreeFam; TF300871; -.
DR PathwayCommons; P62266; -.
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-72649; Translation initiation complex formation.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
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-9754678; SARS-CoV-2 modulates host translation machinery.
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; P62266; -.
DR SIGNOR; P62266; -.
DR BioGRID-ORCS; 6228; 792 hits in 1054 CRISPR screens.
DR ChiTaRS; RPS23; human.
DR GeneWiki; RPS23; -.
DR GenomeRNAi; 6228; -.
DR Pharos; P62266; Tbio.
DR PRO; PR:P62266; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P62266; protein.
DR Bgee; ENSG00000186468; Expressed in skin of hip and 212 other tissues.
DR ExpressionAtlas; P62266; baseline and differential.
DR Genevisible; P62266; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0042788; C:polysomal ribosome; IDA:UniProtKB.
DR GO; GO:0005840; C:ribosome; IBA:GO_Central.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; IDA:UniProtKB.
DR GO; GO:1990145; P:maintenance of translational fidelity; IMP:UniProtKB.
DR GO; GO:0034063; P:stress granule assembly; IMP:UniProtKB.
DR GO; GO:0006412; P:translation; IMP:UniProtKB.
DR CDD; cd03367; Ribosomal_S23; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR006032; Ribosomal_S12/S23.
DR InterPro; IPR005680; Ribosomal_S23_euk/arc.
DR PANTHER; PTHR11652; PTHR11652; 1.
DR Pfam; PF00164; Ribosom_S12_S23; 1.
DR PIRSF; PIRSF002133; Ribosomal_S12/S23; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00982; uS12_E_A; 1.
DR PROSITE; PS00055; RIBOSOMAL_S12; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Deafness; Direct protein sequencing;
KW Disease variant; Dwarfism; Endoplasmic reticulum; Hydroxylation;
KW Isopeptide bond; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8706699"
FT CHAIN 2..143
FT /note="40S ribosomal protein S23"
FT /id="PRO_0000146457"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 54
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62267"
FT MOD_RES 62
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:24550447,
FT ECO:0000269|PubMed:24550462, ECO:0000269|PubMed:28257692"
FT MOD_RES 135
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 37
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 67
FT /note="R -> K (in BTDD; decreases hydroxylation of the
FT protein; decreases the accuracy of translation; decreases
FT levels of incorporation of the mutant protein into
FT ribosomes and polysomes; patient cells become highly
FT sensitive to oxidative stress; dbSNP:rs1060505034)"
FT /evidence="ECO:0000269|PubMed:28257692"
FT /id="VAR_079133"
FT VARIANT 120
FT /note="F -> I (in BTDD; decreases hydroxylation of the
FT protein; decreases the accuracy of translation; decreases
FT levels of incorporation of the mutant protein into
FT polysomes; patient cells become highly sensitive to
FT oxidative stress; dbSNP:rs1060505035)"
FT /evidence="ECO:0000269|PubMed:28257692"
FT /id="VAR_079134"
FT HELIX 10..20
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 25..31
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 34..38
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 40..43
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 45..58
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 66..74
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:6ZOJ"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:6ZN5"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 130..134
FT /evidence="ECO:0007829|PDB:6ZLW"
SQ SEQUENCE 143 AA; 15808 MW; 8417A48B8CF0A8E5 CRC64;
MGKCRGLRTA RKLRSHRRDQ KWHDKQYKKA HLGTALKANP FGGASHAKGI VLEKVGVEAK
QPNSAIRKCV RVQLIKNGKK ITAFVPNDGC LNFIEENDEV LVAGFGRKGH AVGDIPGVRF
KVVKVANVSL LALYKGKKER PRS
