RS26_HUMAN
ID RS26_HUMAN Reviewed; 115 AA.
AC P62854; P02383; P70394; Q06722; Q3MHD8; Q6IRY4;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=40S ribosomal protein S26;
DE AltName: Full=Small ribosomal subunit protein eS26 {ECO:0000303|PubMed:24524803};
GN Name=RPS26;
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=8464749; DOI=10.1093/nar/21.6.1498;
RA Vincent S., Marty L., Fort P.;
RT "S26 ribosomal protein RNA: an invariant control for gene regulation
RT experiments in eucaryotic cells and tissues.";
RL Nucleic Acids Res. 21:1498-1498(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=7945460;
RA Filipenko M.L., Vladimirov S.N., Muravlev A.I., Karpova G.G.,
RA Mertvetsov N.P.;
RT "Cloning cDNA of human S26 ribosomal protein and determination of its
RT primary structure.";
RL Bioorg. Khim. 20:644-649(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=9602156; DOI=10.1016/s0378-1119(98)00108-5;
RA Filipenko M.L., Vinichenko N.A., Karpova G.G., Mertvetsov N.P., Amaldi F.;
RT "Isolation, structural analysis and mapping of the functional gene of human
RT ribosomal protein S26.";
RL Gene 211:287-292(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Lymph, 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 [5]
RP PROTEIN SEQUENCE OF 2-11.
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 [6]
RP IDENTIFICATION BY MASS 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54, 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 [9]
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 [10]
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 [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 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 [13] {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 [14] {ECO:0007744|PDB:4UG0}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) IN COMPLEX WITH ZINC,
RP SUBCELLULAR 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).
RN [15]
RP INVOLVEMENT IN DBA10, AND VARIANTS DBA10 ASN-33 AND THR-115.
RX PubMed=20116044; DOI=10.1016/j.ajhg.2009.12.015;
RA Doherty L., Sheen M.R., Vlachos A., Choesmel V., O'Donohue M.F.,
RA Clinton C., Schneider H.E., Sieff C.A., Newburger P.E., Ball S.E.,
RA Niewiadomska E., Matysiak M., Glader B., Arceci R.J., Farrar J.E.,
RA Atsidaftos E., Lipton J.M., Gleizes P.E., Gazda H.T.;
RT "Ribosomal protein genes RPS10 and RPS26 are commonly mutated in Diamond-
RT Blackfan anemia.";
RL Am. J. Hum. Genet. 86:222-228(2010).
RN [16]
RP ERRATUM OF PUBMED:20116044.
RA Doherty L., Sheen M.R., Vlachos A., Choesmel V., O'Donohue M.F.,
RA Clinton C., Schneider H.E., Sieff C.A., Newburger P.E., Ball S.E.,
RA Niewiadomska E., Matysiak M., Glader B., Arceci R.J., Farrar J.E.,
RA Atsidaftos E., Lipton J.M., Gleizes P.E., Gazda H.T.;
RL Am. J. Hum. Genet. 86:655-655(2010).
RN [17]
RP INVOLVEMENT IN DBA10.
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).
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 P62854; P32243-2: OTX2; NbExp=3; IntAct=EBI-353438, EBI-9087860;
CC P62854; O00560: SDCBP; NbExp=3; IntAct=EBI-353438, EBI-727004;
CC P62854; Q969E8: TSR2; NbExp=16; IntAct=EBI-353438, EBI-746981;
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:P49171}.
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:P49171,
CC ECO:0000269|PubMed:25957688}.
CC -!- DISEASE: Diamond-Blackfan anemia 10 (DBA10) [MIM:613309]: A form of
CC Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic
CC anemia that usually presents early in infancy. Diamond-Blackfan anemia
CC is characterized by a moderate to severe macrocytic anemia,
CC erythroblastopenia, and an increased risk of malignancy. 30 to 40% of
CC Diamond-Blackfan anemia patients present with short stature and
CC congenital anomalies, the most frequent being craniofacial (Pierre-
CC Robin syndrome and cleft palate), thumb and urogenital anomalies.
CC {ECO:0000269|PubMed:20116044, ECO:0000269|PubMed:24942156}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS26 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; X69654; CAA49345.1; -; mRNA.
DR EMBL; X77770; CAA54808.1; -; mRNA.
DR EMBL; X79236; CAA55818.1; -; Genomic_DNA.
DR EMBL; U41448; AAC26987.1; -; Genomic_DNA.
DR EMBL; BC002604; AAH02604.1; -; mRNA.
DR EMBL; BC015832; AAH15832.1; -; mRNA.
DR EMBL; BC070220; AAH70220.1; -; mRNA.
DR EMBL; BC105276; AAI05277.1; -; mRNA.
DR EMBL; BC105798; AAI05799.1; -; mRNA.
DR CCDS; CCDS31832.1; -.
DR PIR; S55545; S55545.
DR PIR; T50824; T50824.
DR RefSeq; NP_001020.2; NM_001029.3.
DR RefSeq; XP_005276741.1; XM_005276684.3.
DR PDB; 4UG0; EM; -; Sa=1-115.
DR PDB; 4V6X; EM; 5.00 A; Aa=1-115.
DR PDB; 5A2Q; EM; 3.90 A; a=2-102.
DR PDB; 5AJ0; EM; 3.50 A; Ba=1-115.
DR PDB; 5FLX; EM; 3.90 A; a=1-115.
DR PDB; 5LKS; EM; 3.60 A; Sa=1-115.
DR PDB; 5OA3; EM; 4.30 A; a=2-102.
DR PDB; 5T2C; EM; 3.60 A; AE=1-115.
DR PDB; 5VYC; X-ray; 6.00 A; a1/a2/a3/a4/a5/a6=1-115.
DR PDB; 6G5H; EM; 3.60 A; a=1-115.
DR PDB; 6IP5; EM; 3.90 A; 3C=1-115.
DR PDB; 6IP6; EM; 4.50 A; 3C=1-115.
DR PDB; 6IP8; EM; 3.90 A; 3C=1-115.
DR PDB; 6OLE; EM; 3.10 A; Sa=2-103.
DR PDB; 6OLF; EM; 3.90 A; Sa=2-103.
DR PDB; 6OLG; EM; 3.40 A; Ba=2-98.
DR PDB; 6OLI; EM; 3.50 A; Sa=2-103.
DR PDB; 6OLZ; EM; 3.90 A; Ba=2-98.
DR PDB; 6OM0; EM; 3.10 A; Sa=2-103.
DR PDB; 6OM7; EM; 3.70 A; Sa=2-103.
DR PDB; 6QZP; EM; 2.90 A; Sa=2-103.
DR PDB; 6XA1; EM; 2.80 A; Sa=2-100.
DR PDB; 6Y0G; EM; 3.20 A; Sa=1-115.
DR PDB; 6Y2L; EM; 3.00 A; Sa=1-115.
DR PDB; 6Y57; EM; 3.50 A; Sa=1-115.
DR PDB; 6YBD; EM; 3.30 A; Q=1-115.
DR PDB; 6YBW; EM; 3.10 A; Q=1-115.
DR PDB; 6Z6L; EM; 3.00 A; Sa=1-115.
DR PDB; 6Z6M; EM; 3.10 A; Sa=1-115.
DR PDB; 6Z6N; EM; 2.90 A; Sa=1-115.
DR PDB; 6ZLW; EM; 2.60 A; c=1-115.
DR PDB; 6ZM7; EM; 2.70 A; Sa=1-115.
DR PDB; 6ZME; EM; 3.00 A; Sa=1-115.
DR PDB; 6ZMI; EM; 2.60 A; Sa=1-115.
DR PDB; 6ZMO; EM; 3.10 A; Sa=1-115.
DR PDB; 6ZMW; EM; 3.70 A; Q=1-115.
DR PDB; 6ZN5; EM; 3.20 A; c=2-102.
DR PDB; 6ZOJ; EM; 2.80 A; a=2-102.
DR PDB; 6ZOK; EM; 2.80 A; a=2-102.
DR PDB; 6ZON; EM; 3.00 A; Q=1-115.
DR PDB; 6ZP4; EM; 2.90 A; Q=1-115.
DR PDB; 6ZV6; EM; 2.90 A; a=1-115.
DR PDB; 6ZVH; EM; 2.90 A; a=2-103.
DR PDB; 6ZVJ; EM; 3.80 A; Q=2-102.
DR PDB; 6ZXG; EM; 2.60 A; h=1-115.
DR PDB; 6ZXH; EM; 2.70 A; h=1-115.
DR PDB; 7A09; EM; 3.50 A; Q=1-115.
DR PDB; 7K5I; EM; 2.90 A; a=1-102.
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; 6G5H; -.
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; 6ZMW; -.
DR PDBsum; 6ZN5; -.
DR PDBsum; 6ZOJ; -.
DR PDBsum; 6ZOK; -.
DR PDBsum; 6ZON; -.
DR PDBsum; 6ZP4; -.
DR PDBsum; 6ZV6; -.
DR PDBsum; 6ZVH; -.
DR PDBsum; 6ZVJ; -.
DR PDBsum; 6ZXG; -.
DR PDBsum; 6ZXH; -.
DR PDBsum; 7A09; -.
DR PDBsum; 7K5I; -.
DR AlphaFoldDB; P62854; -.
DR SMR; P62854; -.
DR BioGRID; 112145; 243.
DR BioGRID; 3193504; 66.
DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR CORUM; P62854; -.
DR IntAct; P62854; 45.
DR MINT; P62854; -.
DR STRING; 9606.ENSP00000348849; -.
DR GlyGen; P62854; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62854; -.
DR MetOSite; P62854; -.
DR PhosphoSitePlus; P62854; -.
DR SwissPalm; P62854; -.
DR BioMuta; RPS26; -.
DR DMDM; 51338650; -.
DR EPD; P62854; -.
DR jPOST; P62854; -.
DR MassIVE; P62854; -.
DR MaxQB; P62854; -.
DR PaxDb; P62854; -.
DR PeptideAtlas; P62854; -.
DR PRIDE; P62854; -.
DR ProteomicsDB; 57438; -.
DR TopDownProteomics; P62854; -.
DR Antibodypedia; 43707; 112 antibodies from 20 providers.
DR DNASU; 6231; -.
DR Ensembl; ENST00000356464.10; ENSP00000348849.5; ENSG00000197728.11.
DR Ensembl; ENST00000552361.1; ENSP00000450339.1; ENSG00000197728.11.
DR Ensembl; ENST00000646449.2; ENSP00000496643.1; ENSG00000197728.11.
DR GeneID; 6231; -.
DR KEGG; hsa:6231; -.
DR MANE-Select; ENST00000646449.2; ENSP00000496643.1; NM_001029.5; NP_001020.2.
DR UCSC; uc001sjf.4; human.
DR CTD; 6231; -.
DR DisGeNET; 6231; -.
DR GeneCards; RPS26; -.
DR GeneReviews; RPS26; -.
DR HGNC; HGNC:10414; RPS26.
DR HPA; ENSG00000197728; Low tissue specificity.
DR MalaCards; RPS26; -.
DR MIM; 603701; gene.
DR MIM; 613309; phenotype.
DR neXtProt; NX_P62854; -.
DR OpenTargets; ENSG00000197728; -.
DR Orphanet; 124; Blackfan-Diamond anemia.
DR PharmGKB; PA34818; -.
DR VEuPathDB; HostDB:ENSG00000197728; -.
DR eggNOG; KOG1768; Eukaryota.
DR GeneTree; ENSGT00390000002517; -.
DR HOGENOM; CLU_129451_0_1_1; -.
DR InParanoid; P62854; -.
DR OMA; DKAICVT; -.
DR OrthoDB; 1591366at2759; -.
DR PhylomeDB; P62854; -.
DR TreeFam; TF300234; -.
DR PathwayCommons; P62854; -.
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; P62854; -.
DR SIGNOR; P62854; -.
DR BioGRID-ORCS; 6231; 81 hits in 595 CRISPR screens.
DR ChiTaRS; RPS26; human.
DR GeneWiki; RPS26; -.
DR Pharos; P62854; Tbio.
DR PRO; PR:P62854; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P62854; protein.
DR Bgee; ENSG00000197728; Expressed in granulocyte and 93 other tissues.
DR ExpressionAtlas; P62854; baseline and differential.
DR Genevisible; P62854; 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: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:0015935; C:small ribosomal subunit; HDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0003729; F:mRNA binding; IDA: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:0033119; P:negative regulation of RNA splicing; IDA:UniProtKB.
DR GO; GO:0006412; P:translation; IC:UniProtKB.
DR Gene3D; 3.30.1740.20; -; 1.
DR InterPro; IPR000892; Ribosomal_S26e.
DR InterPro; IPR038551; Ribosomal_S26e_sf.
DR PANTHER; PTHR12538; PTHR12538; 1.
DR Pfam; PF01283; Ribosomal_S26e; 1.
DR PROSITE; PS00733; RIBOSOMAL_S26E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Diamond-Blackfan anemia;
KW Direct protein sequencing; Disease variant; Endoplasmic reticulum;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8706699"
FT CHAIN 2..115
FT /note="40S ribosomal protein S26"
FT /id="PRO_0000204509"
FT REGION 85..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..115
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 33
FT /note="D -> N (in DBA10; dbSNP:rs267607023)"
FT /evidence="ECO:0000269|PubMed:20116044"
FT /id="VAR_063580"
FT VARIANT 115
FT /note="M -> T (in DBA10)"
FT /evidence="ECO:0000269|PubMed:20116044"
FT /id="VAR_063581"
FT CONFLICT 78
FT /note="A -> V (in Ref. 2; CAA54808)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="R -> A (in Ref. 1; CAA49345)"
FT /evidence="ECO:0000305"
FT TURN 6..9
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 35..45
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 50..55
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 75..80
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:6ZLW"
SQ SEQUENCE 115 AA; 13015 MW; F60DF98F8900D968 CRC64;
MTKKRRNNGR AKKGRGHVQP IRCTNCARCV PKDKAIKKFV IRNIVEAAAV RDISEASVFD
AYVLPKLYVK LHYCVSCAIH SKVVRNRSRE ARKDRTPPPR FRPAGAAPRP PPKPM
