RS21_HUMAN
ID RS21_HUMAN Reviewed; 83 AA.
AC P63220; P35265;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=40S ribosomal protein S21;
DE AltName: Full=Small ribosomal subunit protein eS21 {ECO:0000303|PubMed:24524803};
GN Name=RPS21;
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=8332502; DOI=10.1093/nar/21.12.2939;
RA Bhat K.S., Morrison S.G.;
RT "Primary structure of human ribosomal protein S21.";
RL Nucleic Acids Res. 21:2939-2939(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10900511;
RA Smirnova E.V., Rakitina T.V., Evtodienko A.Y., Kostanian I.A., Lipkin V.M.;
RT "Cloning and characterization of the human ribosomal protein S21 gene.";
RL Bioorg. Khim. 26:392-396(2000).
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 GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 21-74.
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 PROTEIN SEQUENCE OF 1-15, ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=T-cell;
RA Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
RL Submitted (MAY-2006) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 42-47.
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81, 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 [10]
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
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 [14]
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 [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-41, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [17]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS), SUBCELLULAR LOCATION, AND
RP 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 [18] {ECO:0007744|PDB:5AJ0}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), SUBCELLULAR LOCATION,
RP 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 [19] {ECO:0007744|PDB:4UG0}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), SUBCELLULAR LOCATION,
RP 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 -!- 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 P63220; Q5TD97: FHL5; NbExp=3; IntAct=EBI-714051, EBI-750641;
CC P63220; Q9H8W4: PLEKHF2; NbExp=6; IntAct=EBI-714051, EBI-742388;
CC P63220; P36508: ZNF76; NbExp=3; IntAct=EBI-714051, EBI-7254550;
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:P63221}.
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:P63221,
CC ECO:0000269|PubMed:25957688}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS21 family.
CC {ECO:0000305}.
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DR EMBL; L04483; AAA99893.1; -; mRNA.
DR EMBL; AJ250907; CAB83213.1; -; Genomic_DNA.
DR EMBL; AB061843; BAB79481.1; -; Genomic_DNA.
DR EMBL; AL121832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB007157; BAA25821.1; -; Genomic_DNA.
DR CCDS; CCDS13497.1; -.
DR PIR; S34108; S34108.
DR RefSeq; NP_001015.1; NM_001024.3.
DR PDB; 4UG0; EM; -; SV=1-83.
DR PDB; 4V6X; EM; 5.00 A; AV=1-83.
DR PDB; 5A2Q; EM; 3.90 A; V=1-83.
DR PDB; 5AJ0; EM; 3.50 A; BV=1-83.
DR PDB; 5FLX; EM; 3.90 A; V=1-83.
DR PDB; 5LKS; EM; 3.60 A; SV=1-83.
DR PDB; 5OA3; EM; 4.30 A; V=1-83.
DR PDB; 5T2C; EM; 3.60 A; AC=1-83.
DR PDB; 5VYC; X-ray; 6.00 A; V1/V2/V3/V4/V5/V6=1-83.
DR PDB; 6G18; EM; 3.60 A; V=1-83.
DR PDB; 6G4S; EM; 4.00 A; V=1-83.
DR PDB; 6G51; EM; 4.10 A; V=1-83.
DR PDB; 6G53; EM; 4.50 A; V=1-83.
DR PDB; 6G5H; EM; 3.60 A; V=1-83.
DR PDB; 6G5I; EM; 3.50 A; V=1-83.
DR PDB; 6IP5; EM; 3.90 A; 3A=1-83.
DR PDB; 6IP6; EM; 4.50 A; 3A=1-83.
DR PDB; 6IP8; EM; 3.90 A; 3A=1-83.
DR PDB; 6OLE; EM; 3.10 A; SV=1-82.
DR PDB; 6OLF; EM; 3.90 A; SV=1-82.
DR PDB; 6OLG; EM; 3.40 A; BV=1-81.
DR PDB; 6OLI; EM; 3.50 A; SV=1-82.
DR PDB; 6OLZ; EM; 3.90 A; BV=1-81.
DR PDB; 6OM0; EM; 3.10 A; SV=1-82.
DR PDB; 6OM7; EM; 3.70 A; SV=1-82.
DR PDB; 6QZP; EM; 2.90 A; SV=1-83.
DR PDB; 6XA1; EM; 2.80 A; SV=1-83.
DR PDB; 6Y0G; EM; 3.20 A; SV=1-83.
DR PDB; 6Y2L; EM; 3.00 A; SV=1-83.
DR PDB; 6Y57; EM; 3.50 A; SV=1-83.
DR PDB; 6YBD; EM; 3.30 A; K=1-83.
DR PDB; 6YBW; EM; 3.10 A; K=1-83.
DR PDB; 6Z6L; EM; 3.00 A; SV=1-83.
DR PDB; 6Z6M; EM; 3.10 A; SV=1-83.
DR PDB; 6Z6N; EM; 2.90 A; SV=1-83.
DR PDB; 6ZLW; EM; 2.60 A; Z=1-83.
DR PDB; 6ZM7; EM; 2.70 A; SV=1-83.
DR PDB; 6ZME; EM; 3.00 A; SV=1-83.
DR PDB; 6ZMI; EM; 2.60 A; SV=1-83.
DR PDB; 6ZMO; EM; 3.10 A; SV=1-83.
DR PDB; 6ZMT; EM; 3.00 A; Z=1-83.
DR PDB; 6ZMW; EM; 3.70 A; K=1-83.
DR PDB; 6ZN5; EM; 3.20 A; Z=1-82.
DR PDB; 6ZOJ; EM; 2.80 A; V=1-83.
DR PDB; 6ZOK; EM; 2.80 A; V=1-83.
DR PDB; 6ZON; EM; 3.00 A; y=1-83.
DR PDB; 6ZP4; EM; 2.90 A; y=1-83.
DR PDB; 6ZUO; EM; 3.10 A; V=1-83.
DR PDB; 6ZV6; EM; 2.90 A; V=1-83.
DR PDB; 6ZVH; EM; 2.90 A; V=1-83.
DR PDB; 6ZVJ; EM; 3.80 A; y=1-82.
DR PDB; 6ZXD; EM; 3.20 A; V=1-83.
DR PDB; 6ZXE; EM; 3.00 A; V=1-83.
DR PDB; 6ZXF; EM; 3.70 A; V=1-83.
DR PDB; 6ZXG; EM; 2.60 A; V=1-83.
DR PDB; 6ZXH; EM; 2.70 A; V=1-83.
DR PDB; 7A09; EM; 3.50 A; y=1-83.
DR PDB; 7JQB; EM; 2.70 A; W=1-83.
DR PDB; 7JQC; EM; 3.30 A; W=1-83.
DR PDB; 7K5I; EM; 2.90 A; V=1-83.
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; 6G18; -.
DR PDBsum; 6G4S; -.
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; 6YBD; -.
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; 7JQB; -.
DR PDBsum; 7JQC; -.
DR PDBsum; 7K5I; -.
DR AlphaFoldDB; P63220; -.
DR SMR; P63220; -.
DR BioGRID; 112141; 190.
DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR CORUM; P63220; -.
DR IntAct; P63220; 33.
DR MINT; P63220; -.
DR STRING; 9606.ENSP00000345957; -.
DR iPTMnet; P63220; -.
DR MetOSite; P63220; -.
DR PhosphoSitePlus; P63220; -.
DR SwissPalm; P63220; -.
DR BioMuta; RPS21; -.
DR DMDM; 52783792; -.
DR EPD; P63220; -.
DR jPOST; P63220; -.
DR MassIVE; P63220; -.
DR PaxDb; P63220; -.
DR PeptideAtlas; P63220; -.
DR PRIDE; P63220; -.
DR ProteomicsDB; 57509; -.
DR TopDownProteomics; P63220; -.
DR Antibodypedia; 1249; 149 antibodies from 28 providers.
DR DNASU; 6227; -.
DR Ensembl; ENST00000343986.9; ENSP00000345957.3; ENSG00000171858.18.
DR GeneID; 6227; -.
DR KEGG; hsa:6227; -.
DR MANE-Select; ENST00000343986.9; ENSP00000345957.3; NM_001024.4; NP_001015.1.
DR CTD; 6227; -.
DR DisGeNET; 6227; -.
DR GeneCards; RPS21; -.
DR HGNC; HGNC:10409; RPS21.
DR HPA; ENSG00000171858; Low tissue specificity.
DR MIM; 180477; gene.
DR neXtProt; NX_P63220; -.
DR OpenTargets; ENSG00000171858; -.
DR PharmGKB; PA34812; -.
DR VEuPathDB; HostDB:ENSG00000171858; -.
DR eggNOG; KOG3486; Eukaryota.
DR GeneTree; ENSGT00390000017515; -.
DR InParanoid; P63220; -.
DR OMA; ALCGYIR; -.
DR OrthoDB; 1571849at2759; -.
DR PhylomeDB; P63220; -.
DR TreeFam; TF300167; -.
DR PathwayCommons; P63220; -.
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; P63220; -.
DR SIGNOR; P63220; -.
DR BioGRID-ORCS; 6227; 692 hits in 1082 CRISPR screens.
DR ChiTaRS; RPS21; human.
DR GeneWiki; RPS21; -.
DR GenomeRNAi; 6227; -.
DR Pharos; P63220; Tbio.
DR PRO; PR:P63220; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; P63220; protein.
DR Bgee; ENSG00000171858; Expressed in nipple and 207 other tissues.
DR ExpressionAtlas; P63220; baseline and differential.
DR Genevisible; P63220; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0042788; C:polysomal ribosome; IDA:UniProtKB.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0015935; C:small ribosomal subunit; HDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
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:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0000461; P:endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR Gene3D; 3.30.1230.20; -; 1.
DR InterPro; IPR001931; Ribosomal_S21e.
DR InterPro; IPR018279; Ribosomal_S21e_CS.
DR InterPro; IPR038579; Ribosomal_S21e_sf.
DR PANTHER; PTHR10442; PTHR10442; 1.
DR Pfam; PF01249; Ribosomal_S21e; 1.
DR PIRSF; PIRSF002148; Ribosomal_S21e; 1.
DR PROSITE; PS00996; RIBOSOMAL_S21E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Endoplasmic reticulum; Isopeptide bond; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT CHAIN 1..83
FT /note="40S ribosomal protein S21"
FT /id="PRO_0000194730"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 81
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 41
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25114211"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:6YBW"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 46..55
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 65..75
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:6YBD"
SQ SEQUENCE 83 AA; 9111 MW; 6794AC1292A06BD3 CRC64;
MQNDAGEFVD LYVPRKCSAS NRIIGAKDHA SIQMNVAEVD KVTGRFNGQF KTYAICGAIR
RMGESDDSIL RLAKADGIVS KNF
