RS28_HUMAN
ID RS28_HUMAN Reviewed; 69 AA.
AC P62857; P25112;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=40S ribosomal protein S28;
DE AltName: Full=Small ribosomal subunit protein eS28 {ECO:0000303|PubMed:24524803};
GN Name=RPS28;
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].
RA Bhat K.S.;
RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kim J.M., Bae Y.S.;
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
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].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell, Muscle, and Prostate;
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 [6]
RP PROTEIN SEQUENCE OF 48-68.
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 54-69.
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP INVOLVEMENT IN DBA15.
RX PubMed=24942156; DOI=10.1002/ajmg.a.36633;
RG UW Center for Mendelian Genomics;
RA Gripp K.W., Curry C., Olney A.H., Sandoval C., Fisher J., Chong J.X.,
RA Pilchman L., Sahraoui R., Stabley D.L., Sol-Church K.;
RT "Diamond-Blackfan anemia with mandibulofacial dystostosis is heterogeneous,
RT including the novel DBA genes TSR2 and RPS28.";
RL Am. J. Med. Genet. A 164A:2240-2249(2014).
RN [11]
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 [12]
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 [13]
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 [14]
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 [15] {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 [16] {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 P62857; O95273: CCNDBP1; NbExp=3; IntAct=EBI-353027, EBI-748961;
CC P62857; O75031: HSF2BP; NbExp=3; IntAct=EBI-353027, EBI-7116203;
CC P62857; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-353027, EBI-11959885;
CC P62857; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-353027, EBI-10172290;
CC P62857; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-353027, EBI-10171774;
CC P62857; P0C7H8: KRTAP2-3; NbExp=3; IntAct=EBI-353027, EBI-10196781;
CC P62857; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-353027, EBI-945833;
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:Q6QAT1}.
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:Q6QAT1,
CC ECO:0000269|PubMed:25957688}.
CC -!- DISEASE: Diamond-Blackfan anemia 15, with mandibulofacial dysostosis
CC (DBA15) [MIM:606164]: A form of Diamond-Blackfan anemia, a congenital
CC non-regenerative hypoplastic anemia that usually presents early in
CC infancy. Diamond-Blackfan anemia is characterized by a moderate to
CC severe macrocytic anemia, erythroblastopenia, and an increased risk of
CC malignancy. 30 to 40% of Diamond-Blackfan anemia patients present with
CC short stature and congenital anomalies, the most frequent being
CC craniofacial (Pierre-Robin syndrome and cleft palate), thumb and
CC urogenital anomalies. {ECO:0000269|PubMed:24942156}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS28 family.
CC {ECO:0000305}.
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DR EMBL; L05091; AAC15855.1; -; mRNA.
DR EMBL; U58682; AAB07066.1; -; mRNA.
DR EMBL; AB061846; BAB79484.1; -; Genomic_DNA.
DR EMBL; CR457055; CAG33336.1; -; mRNA.
DR EMBL; BC000354; AAH00354.1; -; mRNA.
DR EMBL; BC021239; AAH21239.1; -; mRNA.
DR EMBL; BC070217; AAH70217.1; -; mRNA.
DR EMBL; BC070218; AAH70218.1; -; mRNA.
DR EMBL; AB007164; BAA28594.1; -; Genomic_DNA.
DR CCDS; CCDS45953.1; -.
DR PIR; S68914; S68914.
DR RefSeq; NP_001022.1; NM_001031.4.
DR PDB; 4UG0; EM; -; Sc=1-69.
DR PDB; 4V6X; EM; 5.00 A; Ac=1-69.
DR PDB; 5A2Q; EM; 3.90 A; c=8-68.
DR PDB; 5AJ0; EM; 3.50 A; Bc=1-69.
DR PDB; 5FLX; EM; 3.90 A; c=1-69.
DR PDB; 5LKS; EM; 3.60 A; Sc=1-69.
DR PDB; 5OA3; EM; 4.30 A; c=8-68.
DR PDB; 5T2C; EM; 3.60 A; AF=1-69.
DR PDB; 5VYC; X-ray; 6.00 A; c1/c2/c3/c4/c5/c6=1-69.
DR PDB; 6FEC; EM; 6.30 A; l=5-68.
DR PDB; 6G18; EM; 3.60 A; c=1-69.
DR PDB; 6G4S; EM; 4.00 A; c=1-69.
DR PDB; 6G4W; EM; 4.50 A; c=1-69.
DR PDB; 6G51; EM; 4.10 A; c=1-69.
DR PDB; 6G53; EM; 4.50 A; c=1-69.
DR PDB; 6G5H; EM; 3.60 A; c=1-69.
DR PDB; 6G5I; EM; 3.50 A; c=1-69.
DR PDB; 6IP5; EM; 3.90 A; 3D=1-69.
DR PDB; 6IP6; EM; 4.50 A; 3D=1-69.
DR PDB; 6IP8; EM; 3.90 A; 3D=1-69.
DR PDB; 6OLE; EM; 3.10 A; Sc=5-68.
DR PDB; 6OLF; EM; 3.90 A; Sc=5-68.
DR PDB; 6OLG; EM; 3.40 A; Bc=7-68.
DR PDB; 6OLI; EM; 3.50 A; Sc=5-68.
DR PDB; 6OLZ; EM; 3.90 A; Bc=7-68.
DR PDB; 6OM0; EM; 3.10 A; Sc=5-68.
DR PDB; 6OM7; EM; 3.70 A; Sc=5-68.
DR PDB; 6QZP; EM; 2.90 A; Sc=5-68.
DR PDB; 6XA1; EM; 2.80 A; Sc=8-68.
DR PDB; 6Y0G; EM; 3.20 A; Sc=1-69.
DR PDB; 6Y2L; EM; 3.00 A; Sc=1-69.
DR PDB; 6Y57; EM; 3.50 A; Sc=1-69.
DR PDB; 6YBS; EM; 3.10 A; n=1-69.
DR PDB; 6Z6L; EM; 3.00 A; Sc=1-69.
DR PDB; 6Z6M; EM; 3.10 A; Sc=1-69.
DR PDB; 6Z6N; EM; 2.90 A; Sc=1-69.
DR PDB; 6ZLW; EM; 2.60 A; d=1-69.
DR PDB; 6ZM7; EM; 2.70 A; Sc=1-69.
DR PDB; 6ZME; EM; 3.00 A; Sc=1-69.
DR PDB; 6ZMI; EM; 2.60 A; Sc=1-69.
DR PDB; 6ZMO; EM; 3.10 A; Sc=1-69.
DR PDB; 6ZMT; EM; 3.00 A; d=1-69.
DR PDB; 6ZMW; EM; 3.70 A; n=1-69.
DR PDB; 6ZN5; EM; 3.20 A; d=8-68.
DR PDB; 6ZOJ; EM; 2.80 A; c=8-68.
DR PDB; 6ZOL; EM; 2.80 A; c=8-68.
DR PDB; 6ZON; EM; 3.00 A; S=1-69.
DR PDB; 6ZP4; EM; 2.90 A; S=1-69.
DR PDB; 6ZUO; EM; 3.10 A; c=1-69.
DR PDB; 6ZV6; EM; 2.90 A; c=1-69.
DR PDB; 6ZVH; EM; 2.90 A; c=5-68.
DR PDB; 6ZVJ; EM; 3.80 A; S=8-68.
DR PDB; 6ZXD; EM; 3.20 A; c=1-69.
DR PDB; 6ZXE; EM; 3.00 A; c=1-69.
DR PDB; 6ZXF; EM; 3.70 A; c=1-69.
DR PDB; 6ZXG; EM; 2.60 A; c=1-69.
DR PDB; 6ZXH; EM; 2.70 A; c=1-69.
DR PDB; 7A09; EM; 3.50 A; S=1-69.
DR PDB; 7K5I; EM; 2.90 A; c=1-69.
DR PDB; 7MQ8; EM; 3.60 A; LG=1-69.
DR PDB; 7MQ9; EM; 3.87 A; LG=1-69.
DR PDB; 7MQA; EM; 2.70 A; LG=1-69.
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; 6YBS; -.
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; 6ZOL; -.
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; P62857; -.
DR SMR; P62857; -.
DR BioGRID; 112148; 219.
DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR CORUM; P62857; -.
DR IntAct; P62857; 49.
DR MINT; P62857; -.
DR STRING; 9606.ENSP00000472469; -.
DR DrugBank; DB11638; Artenimol.
DR iPTMnet; P62857; -.
DR MetOSite; P62857; -.
DR PhosphoSitePlus; P62857; -.
DR SwissPalm; P62857; -.
DR BioMuta; RPS28; -.
DR DMDM; 51338652; -.
DR EPD; P62857; -.
DR jPOST; P62857; -.
DR MassIVE; P62857; -.
DR MaxQB; P62857; -.
DR PaxDb; P62857; -.
DR PeptideAtlas; P62857; -.
DR PRIDE; P62857; -.
DR ProteomicsDB; 57439; -.
DR TopDownProteomics; P62857; -.
DR Antibodypedia; 24844; 82 antibodies from 20 providers.
DR DNASU; 6234; -.
DR Ensembl; ENST00000600659.3; ENSP00000472469.1; ENSG00000233927.5.
DR GeneID; 6234; -.
DR KEGG; hsa:6234; -.
DR MANE-Select; ENST00000600659.3; ENSP00000472469.1; NM_001031.5; NP_001022.1.
DR UCSC; uc002mjn.4; human.
DR CTD; 6234; -.
DR DisGeNET; 6234; -.
DR GeneCards; RPS28; -.
DR GeneReviews; RPS28; -.
DR HGNC; HGNC:10418; RPS28.
DR HPA; ENSG00000233927; Low tissue specificity.
DR MalaCards; RPS28; -.
DR MIM; 603685; gene.
DR MIM; 606164; phenotype.
DR neXtProt; NX_P62857; -.
DR OpenTargets; ENSG00000233927; -.
DR Orphanet; 124; Blackfan-Diamond anemia.
DR PharmGKB; PA34825; -.
DR VEuPathDB; HostDB:ENSG00000233927; -.
DR eggNOG; KOG3502; Eukaryota.
DR GeneTree; ENSGT00910000144227; -.
DR HOGENOM; CLU_178987_1_0_1; -.
DR InParanoid; P62857; -.
DR OMA; MHGEASQ; -.
DR OrthoDB; 1578965at2759; -.
DR PhylomeDB; P62857; -.
DR TreeFam; TF300136; -.
DR PathwayCommons; P62857; -.
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; P62857; -.
DR SIGNOR; P62857; -.
DR BioGRID-ORCS; 6234; 778 hits in 1014 CRISPR screens.
DR ChiTaRS; RPS28; human.
DR GeneWiki; RPS28; -.
DR GenomeRNAi; 6234; -.
DR Pharos; P62857; Tbio.
DR PRO; PR:P62857; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P62857; protein.
DR Bgee; ENSG00000233927; Expressed in lower esophagus mucosa and 170 other tissues.
DR ExpressionAtlas; P62857; baseline and differential.
DR Genevisible; P62857; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0098556; C:cytoplasmic side of rough endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0042788; C:polysomal ribosome; IDA:UniProtKB.
DR GO; GO:0015935; C:small ribosomal subunit; HDA: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:0030490; P:maturation of SSU-rRNA; IBA:GO_Central.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:UniProtKB.
DR GO; GO:0042254; P:ribosome biogenesis; IMP:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
DR GO; GO:0006412; P:translation; IC:UniProtKB.
DR CDD; cd04457; S1_S28E; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_00292; Ribosomal_S28e; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR000289; Ribosomal_S28e.
DR InterPro; IPR028626; Ribosomal_S28e_CS.
DR PANTHER; PTHR10769; PTHR10769; 1.
DR Pfam; PF01200; Ribosomal_S28e; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS00961; RIBOSOMAL_S28E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Diamond-Blackfan anemia;
KW Direct protein sequencing; Endoplasmic reticulum; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..69
FT /note="40S ribosomal protein S28"
FT /id="PRO_0000136822"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P62859"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CONFLICT 66
FT /note="R -> P (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 16..25
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:6ZLW"
SQ SEQUENCE 69 AA; 7841 MW; 49902FE9376EB74F CRC64;
MDTSRVQPIK LARVTKVLGR TGSQGQCTQV RVEFMDDTSR SIIRNVKGPV REGDVLTLLE
SEREARRLR
