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 02-SEP-2026, entry version 189. DE RecName: Full=Small ribosomal subunit protein eS26 {ECO:0000303|PubMed:24524803}; DE AltName: Full=40S ribosomal protein S26; 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) OF RIBOSOME, FUNCTION, RP SUBUNIT, AND 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 [13] {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 [14] {ECO:0007744|PDB:4UG0} RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) IN COMPLEX WITH ZINC, RP FUNCTION, 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 -!- FUNCTION: Component of the small ribosomal subunit (PubMed:23636399, CC PubMed:25901680, PubMed:25957688). The ribosome is a large CC ribonucleoprotein complex responsible for the synthesis of proteins in CC the cell (PubMed:23636399, PubMed:25901680, PubMed:25957688). CC {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:25901680, CC ECO:0000269|PubMed:25957688}. 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=17; 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]: An autosomal CC dominant form of Diamond-Blackfan anemia, a congenital non-regenerative CC hypoplastic anemia that usually presents early in infancy. Diamond- CC Blackfan anemia is characterized by a moderate to severe macrocytic CC anemia, erythroblastopenia, and an increased risk of malignancy. 30 to CC 40% of 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_001029.5. DR RefSeq; XP_054228811.1; XM_054372836.1. DR PDB; 22TU; EM; 3.00 A; Sa=1-115. 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 PDB; 7QP6; EM; 4.70 A; Q=1-115. DR PDB; 7QP7; EM; 3.70 A; Q=1-115. DR PDB; 7R4X; EM; 2.15 A; a=1-115. DR PDB; 7TQL; EM; 3.40 A; c=2-100. DR PDB; 7XNX; EM; 2.70 A; Sa=1-115. DR PDB; 7XNY; EM; 2.50 A; Sa=1-115. DR PDB; 8G5Y; EM; 2.29 A; Sa=1-115. DR PDB; 8G5Z; EM; 2.64 A; Sa=2-100. DR PDB; 8G60; EM; 2.54 A; Sa=1-115. DR PDB; 8G61; EM; 2.94 A; Sa=1-115. DR PDB; 8G6J; EM; 2.80 A; Sa=1-115. DR PDB; 8GLP; EM; 1.67 A; Sa=1-115. DR PDB; 8IFD; EM; 2.59 A; 3C=1-115. DR PDB; 8IFE; EM; 2.57 A; 3C=1-115. DR PDB; 8JDJ; EM; 2.50 A; AM=1-115. DR PDB; 8JDK; EM; 2.26 A; AM=1-115. DR PDB; 8JDL; EM; 2.42 A; AM=1-115. DR PDB; 8JDM; EM; 2.67 A; AM=1-115. DR PDB; 8K2C; EM; 2.40 A; Sa=1-115. DR PDB; 8OZ0; EM; 3.50 A; R=1-115. DR PDB; 8PJ1; EM; 3.40 A; Q=1-115. DR PDB; 8PJ2; EM; 3.40 A; Q=1-115. DR PDB; 8PJ3; EM; 3.70 A; Q=1-115. DR PDB; 8PJ4; EM; 3.20 A; Q=1-115. DR PDB; 8PJ5; EM; 2.90 A; Q=1-115. DR PDB; 8PJ6; EM; 2.90 A; Q=1-115. DR PDB; 8PPK; EM; 2.98 A; a=1-115. DR PDB; 8PPL; EM; 2.65 A; Aa=1-115. DR PDB; 8QOI; EM; 1.90 A; Sa=1-115. DR PDB; 8RG0; EM; 3.40 A; Q=1-115. DR PDB; 8T4S; EM; 2.60 A; a=1-115. DR PDB; 8UKB; EM; 3.05 A; Sa=2-103. DR PDB; 8XP2; EM; 3.20 A; Sa=1-115. DR PDB; 8XP3; EM; 3.40 A; Sa=1-115. DR PDB; 8XSX; EM; 2.40 A; Sa=1-115. DR PDB; 8XSY; EM; 3.00 A; Sa=1-115. DR PDB; 8XSZ; EM; 3.20 A; Sa=1-115. DR PDB; 8XXL; EM; 2.90 A; Sa=1-115. DR PDB; 8XXM; EM; 3.20 A; Sa=1-115. DR PDB; 8XXN; EM; 3.60 A; Sa=1-115. DR PDB; 8Y0W; EM; 3.40 A; Sa=1-115. DR PDB; 8Y0X; EM; 3.30 A; Sa=1-115. DR PDB; 8YOO; EM; 2.00 A; Sa=1-115. DR PDB; 8YOP; EM; 2.20 A; Sa=1-115. DR PDB; 8ZDB; EM; 3.60 A; a=1-115. DR PDB; 9B0P; EM; 2.82 A; Sa=2-103. DR PDB; 9B0Q; EM; 3.20 A; Sa/sa=2-103. DR PDB; 9B0S; EM; 3.80 A; Sa/sa=2-103. DR PDB; 9BKD; EM; 2.60 A; Q=1-115. DR PDB; 9BLN; EM; 3.90 A; Q=1-115. DR PDB; 9C3H; EM; 2.00 A; Sa=1-115. DR PDB; 9ED0; EM; 2.80 A; a=1-115. DR PDB; 9FQZ; EM; 2.85 A; Sa=1-115. DR PDB; 9G8M; EM; 3.30 A; Sa=1-115. DR PDB; 9G8O; EM; 3.40 A; Sa=1-115. DR PDB; 9I14; EM; 3.34 A; Sa=1-115. DR PDB; 9I2D; EM; 2.19 A; Sa=1-115. DR PDB; 9I2E; EM; 2.95 A; Sa=1-115. DR PDB; 9KKF; EM; 3.30 A; Sa=1-115. DR PDB; 9KMT; EM; 2.81 A; a=2-102. DR PDB; 9KMU; EM; 2.87 A; a=2-102. DR PDB; 9KMV; EM; 2.65 A; a=2-102. DR PDB; 9KMW; EM; 2.73 A; a=2-102. DR PDB; 9KMX; EM; 2.89 A; a=2-102. DR PDB; 9KMY; EM; 2.70 A; a=2-101. DR PDB; 9KMZ; EM; 2.78 A; a=2-102. DR PDB; 9KN0; EM; 2.65 A; a=2-102. DR PDB; 9KN5; EM; 3.20 A; Sa=1-115. DR PDB; 9KN6; EM; 3.30 A; Sa=1-115. DR PDB; 9KRP; EM; 3.20 A; Sa=1-115. DR PDB; 9KZU; EM; 3.00 A; Sa=1-115. DR PDB; 9KZX; EM; 3.30 A; Sa=1-115. DR PDB; 9M0P; EM; 2.78 A; Sa=1-115. DR PDB; 9O3W; EM; 1.90 A; Sa=1-115. DR PDB; 9O3Y; EM; 2.20 A; Sa=1-115. DR PDB; 9P6Z; EM; 2.97 A; Sa=2-103. DR PDB; 9P72; EM; 2.80 A; Sa=2-103. DR PDB; 9P73; EM; 2.66 A; Sa=2-103. DR PDB; 9P76; EM; 2.83 A; Sa=2-103. DR PDB; 9P78; EM; 2.90 A; Sa=2-103. DR PDB; 9P79; EM; 3.10 A; Sa=2-103. DR PDB; 9P7A; EM; 2.81 A; Sa=2-103. DR PDB; 9P7C; EM; 2.78 A; Sa=2-103. DR PDB; 9P7D; EM; 2.57 A; Sa=2-103. DR PDB; 9P7E; EM; 2.59 A; Sa=2-103. DR PDB; 9P7F; EM; 3.56 A; Sa=2-103. DR PDB; 9P7G; EM; 3.54 A; Sa=2-103. DR PDB; 9P7H; EM; 3.68 A; Sa=2-103. DR PDB; 9P7I; EM; 3.69 A; Sa=2-103. DR PDB; 9P7J; EM; 3.91 A; Sa=2-103. DR PDB; 9P7K; EM; 2.80 A; Sa=2-103. DR PDB; 9P7L; EM; 2.92 A; Sa=2-103. DR PDB; 9P7N; EM; 2.83 A; Sa=2-103. DR PDB; 9P7O; EM; 2.65 A; Sa=2-103. DR PDB; 9P7W; EM; 2.93 A; Sa=2-103. DR PDB; 9P7X; EM; 2.83 A; Sa=2-103. DR PDB; 9P7Y; EM; 2.75 A; Sa=2-103. DR PDB; 9P8B; EM; 2.48 A; Sa=2-103. DR PDB; 9P8C; EM; 3.11 A; Sa=2-103. DR PDB; 9P8H; EM; 2.98 A; Sa=2-103. DR PDB; 9P8I; EM; 3.89 A; Sa=2-103. DR PDB; 9P9H; EM; 2.84 A; Sa=2-103. DR PDB; 9P9I; EM; 2.77 A; Sa=2-103. DR PDB; 9PA7; EM; 2.67 A; Sa=2-103. DR PDB; 9PBE; EM; 2.19 A; Sa=2-103. DR PDB; 9PKG; EM; 3.26 A; Sa=2-103. DR PDB; 9QLO; EM; 2.47 A; Sa=1-115. DR PDB; 9QLP; EM; 2.75 A; Sa=1-115. DR PDB; 9QLQ; EM; 2.57 A; Sa=1-115. DR PDB; 9RPV; EM; 2.35 A; Ra/Sa=1-115. DR PDB; 9S3B; EM; 2.38 A; Sa=1-115. DR PDB; 9S3C; EM; 2.42 A; Sa=1-115. DR PDB; 9S3D; EM; 2.32 A; Sa=1-115. DR PDB; 9SPF; EM; 2.40 A; Sa=1-115. DR PDB; 9SPI; EM; 2.40 A; Sa=1-115. DR PDB; 9SYR; EM; 3.55 A; Sj=1-115. DR AlphaFoldDB; P62854; -. DR EMDB; EMD-10668; -. DR EMDB; EMD-10674; -. DR EMDB; EMD-10690; -. DR EMDB; EMD-10769; -. DR EMDB; EMD-10775; -. DR EMDB; EMD-11098; -. DR EMDB; EMD-11099; -. DR EMDB; EMD-11100; -. DR EMDB; EMD-11276; -. DR EMDB; EMD-11288; -. DR EMDB; EMD-11289; -. DR EMDB; EMD-11292; -. DR EMDB; EMD-11299; -. DR EMDB; EMD-11302; -. DR EMDB; EMD-11310; -. DR EMDB; EMD-11320; -. DR EMDB; EMD-11321; -. DR EMDB; EMD-11325; -. DR EMDB; EMD-11335; -. DR EMDB; EMD-11441; -. DR EMDB; EMD-11456; -. DR EMDB; EMD-11458; -. DR EMDB; EMD-11520; -. DR EMDB; EMD-11521; -. DR EMDB; EMD-11602; -. DR EMDB; EMD-14113; -. DR EMDB; EMD-14114; -. DR EMDB; EMD-14317; -. DR EMDB; EMD-17297; -. DR EMDB; EMD-17696; -. DR EMDB; EMD-17697; -. DR EMDB; EMD-17698; -. DR EMDB; EMD-17699; -. DR EMDB; EMD-17700; -. DR EMDB; EMD-17701; -. DR EMDB; EMD-17804; -. DR EMDB; EMD-17805; -. DR EMDB; EMD-18539; -. DR EMDB; EMD-19128; -. DR EMDB; EMD-22681; -. DR EMDB; EMD-26067; -. DR EMDB; EMD-29757; -. DR EMDB; EMD-29758; -. DR EMDB; EMD-29759; -. DR EMDB; EMD-29760; -. DR EMDB; EMD-29771; -. DR EMDB; EMD-33329; -. DR EMDB; EMD-33330; -. DR EMDB; EMD-35413; -. DR EMDB; EMD-35414; -. DR EMDB; EMD-36178; -. DR EMDB; EMD-36179; -. DR EMDB; EMD-36180; -. DR EMDB; EMD-36181; -. DR EMDB; EMD-36838; -. DR EMDB; EMD-3770; -. DR EMDB; EMD-38548; -. DR EMDB; EMD-38549; -. DR EMDB; EMD-38629; -. DR EMDB; EMD-38630; -. DR EMDB; EMD-38631; -. DR EMDB; EMD-38752; -. DR EMDB; EMD-38753; -. DR EMDB; EMD-38754; -. DR EMDB; EMD-3883; -. DR EMDB; EMD-39455; -. DR EMDB; EMD-39456; -. DR EMDB; EMD-39956; -. DR EMDB; EMD-40205; -. DR EMDB; EMD-4070; -. DR EMDB; EMD-41039; -. DR EMDB; EMD-42297; -. DR EMDB; EMD-42351; -. DR EMDB; EMD-4352; -. DR EMDB; EMD-44014; -. DR EMDB; EMD-44049; -. DR EMDB; EMD-44050; -. DR EMDB; EMD-44052; -. DR EMDB; EMD-44641; -. DR EMDB; EMD-44671; -. DR EMDB; EMD-45170; -. DR EMDB; EMD-47929; -. DR EMDB; EMD-50673; -. DR EMDB; EMD-51132; -. DR EMDB; EMD-51134; -. DR EMDB; EMD-52565; -. DR EMDB; EMD-52581; -. DR EMDB; EMD-52582; -. DR EMDB; EMD-53230; -. DR EMDB; EMD-53231; -. DR EMDB; EMD-53232; -. DR EMDB; EMD-54172; -. DR EMDB; EMD-54528; -. DR EMDB; EMD-54529; -. DR EMDB; EMD-54530; -. DR EMDB; EMD-55083; -. DR EMDB; EMD-55091; -. DR EMDB; EMD-55351; -. DR EMDB; EMD-62386; -. DR EMDB; EMD-62444; -. DR EMDB; EMD-62445; -. DR EMDB; EMD-62446; -. DR EMDB; EMD-62447; -. DR EMDB; EMD-62448; -. DR EMDB; EMD-62449; -. DR EMDB; EMD-62450; -. DR EMDB; EMD-62451; -. DR EMDB; EMD-62453; -. DR EMDB; EMD-62454; -. DR EMDB; EMD-62535; -. DR EMDB; EMD-62671; -. DR EMDB; EMD-62679; -. DR EMDB; EMD-63560; -. DR EMDB; EMD-68666; -. DR EMDB; EMD-70083; -. DR EMDB; EMD-70084; -. DR EMDB; EMD-70086; -. DR EMDB; EMD-71329; -. DR EMDB; EMD-71331; -. DR EMDB; EMD-71332; -. DR EMDB; EMD-71333; -. DR EMDB; EMD-71334; -. DR EMDB; EMD-71335; -. DR EMDB; EMD-71336; -. DR EMDB; EMD-71337; -. DR EMDB; EMD-71338; -. DR EMDB; EMD-71339; -. DR EMDB; EMD-71340; -. DR EMDB; EMD-71341; -. DR EMDB; EMD-71342; -. DR EMDB; EMD-71343; -. DR EMDB; EMD-71344; -. DR EMDB; EMD-71345; -. DR EMDB; EMD-71346; -. DR EMDB; EMD-71348; -. DR EMDB; EMD-71349; -. DR EMDB; EMD-71355; -. DR EMDB; EMD-71356; -. DR EMDB; EMD-71357; -. DR EMDB; EMD-71371; -. DR EMDB; EMD-71372; -. DR EMDB; EMD-71377; -. DR EMDB; EMD-71378; -. DR EMDB; EMD-71411; -. DR EMDB; EMD-71412; -. DR EMDB; EMD-71435; -. DR EMDB; EMD-71477; -. DR EMDB; EMD-71696; -. DR EMDB; EMD-9701; -. DR EMDB; EMD-9702; -. DR EMDB; EMD-9703; -. DR SMR; P62854; -. DR BioGRID; 112145; 355. DR BioGRID; 3193504; 66. DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit. DR CORUM; P62854; -. DR FunCoup; P62854; 1264. DR IntAct; P62854; 107. DR MINT; P62854; -. DR NDEx; IQUERY-CP-RPS26; 5 NDEx IQuery Curated Pathways. 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 jPOST; P62854; -. DR MassIVE; P62854; -. DR PaxDb; 9606-ENSP00000348849; -. DR PeptideAtlas; P62854; -. DR ProteomicsDB; 57438; -. DR Pumba; P62854; -. DR TopDownProteomics; P62854; -. DR Antibodypedia; 43707; 110 antibodies from 21 providers. DR DNASU; 6231; -. DR Ensembl; ENST00000356464.10; ENSP00000348849.5; ENSG00000197728.12. DR Ensembl; ENST00000552361.1; ENSP00000450339.1; ENSG00000197728.12. DR Ensembl; ENST00000646449.2; ENSP00000496643.1; ENSG00000197728.12. 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 AGR; HGNC:10414; -. DR ClinPGx; PA34818; -. 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 OpenTargets; ENSG00000197728; -. DR Orphanet; 124; Diamond-Blackfan anemia. DR VEuPathDB; HostDB:ENSG00000197728; -. DR eggNOG; KOG1768; Eukaryota. DR GeneTree; ENSGT00390000002517; -. DR HOGENOM; CLU_129451_0_1_1; -. DR InParanoid; P62854; -. DR OMA; KCYCVSC; -. DR OrthoDB; 9831170at2759; -. DR PAN-GO; P62854; 3 GO annotations based on evolutionary models. DR PhylomeDB; P62854; -. 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-9735869; SARS-CoV-1 modulates host translation machinery. 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 Reactome; R-HSA-9954714; PELO:HBS1L and ABCE1 dissociate a ribosome on a non-stop mRNA. DR Reactome; R-HSA-9954716; ZNF598 and the Ribosome-associated Quality Trigger (RQT) complex dissociate a ribosome stalled on a no-go mRNA. DR SignaLink; P62854; -. DR SIGNOR; P62854; -. DR Agora; ENSG00000197728; -. DR BioGRID-ORCS; 6231; 95 hits in 653 CRISPR screens. DR ChiTaRS; RPS26; human. DR EvolutionaryTrace; P62854; -. 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 95 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; NAS:ComplexPortal. DR GO; GO:0098556; C:cytoplasmic side of rough endoplasmic reticulum membrane; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005840; C:ribosome; IDA:UniProtKB. DR GO; GO:0005791; C:rough endoplasmic reticulum; ISS: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 FunFam; 3.30.1740.20:FF:000001; 40S ribosomal protein S26; 1. DR Gene3D; 3.30.1740.20; Ribosomal protein S26e; 1. DR InterPro; IPR000892; Ribosomal_eS26. DR InterPro; IPR047864; Ribosomal_eS26_CS. DR InterPro; IPR038551; Ribosomal_eS26_sf. DR PANTHER; PTHR12538; 40S RIBOSOMAL PROTEIN S26; 1. DR PANTHER; PTHR12538:SF7; SMALL RIBOSOMAL SUBUNIT PROTEIN ES26-RELATED; 1. DR Pfam; PF01283; Ribosomal_S26e; 1. DR PROSITE; PS00733; RIBOSOMAL_S26E; 1. DR PDBsum; 22TU; -. 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 PDBsum; 7QP6; -. DR PDBsum; 7QP7; -. DR PDBsum; 7R4X; -. DR PDBsum; 7TQL; -. DR PDBsum; 7XNX; -. DR PDBsum; 7XNY; -. DR PDBsum; 8G5Y; -. DR PDBsum; 8G5Z; -. DR PDBsum; 8G60; -. DR PDBsum; 8G61; -. DR PDBsum; 8G6J; -. DR PDBsum; 8GLP; -. DR PDBsum; 8IFD; -. DR PDBsum; 8IFE; -. DR PDBsum; 8JDJ; -. DR PDBsum; 8JDK; -. DR PDBsum; 8JDL; -. DR PDBsum; 8JDM; -. DR PDBsum; 8K2C; -. DR PDBsum; 8OZ0; -. DR PDBsum; 8PJ1; -. DR PDBsum; 8PJ2; -. DR PDBsum; 8PJ3; -. DR PDBsum; 8PJ4; -. DR PDBsum; 8PJ5; -. DR PDBsum; 8PJ6; -. DR PDBsum; 8PPK; -. DR PDBsum; 8PPL; -. DR PDBsum; 8QOI; -. DR PDBsum; 8RG0; -. DR PDBsum; 8T4S; -. DR PDBsum; 8UKB; -. DR PDBsum; 8XP2; -. DR PDBsum; 8XP3; -. DR PDBsum; 8XSX; -. DR PDBsum; 8XSY; -. DR PDBsum; 8XSZ; -. DR PDBsum; 8XXL; -. DR PDBsum; 8XXM; -. DR PDBsum; 8XXN; -. DR PDBsum; 8Y0W; -. DR PDBsum; 8Y0X; -. DR PDBsum; 8YOO; -. DR PDBsum; 8YOP; -. DR PDBsum; 8ZDB; -. DR PDBsum; 9B0P; -. DR PDBsum; 9B0Q; -. DR PDBsum; 9B0S; -. DR PDBsum; 9BKD; -. DR PDBsum; 9BLN; -. DR PDBsum; 9C3H; -. DR PDBsum; 9ED0; -. DR PDBsum; 9FQZ; -. DR PDBsum; 9G8M; -. DR PDBsum; 9G8O; -. DR PDBsum; 9I14; -. DR PDBsum; 9I2D; -. DR PDBsum; 9I2E; -. DR PDBsum; 9KKF; -. DR PDBsum; 9KMT; -. DR PDBsum; 9KMU; -. DR PDBsum; 9KMV; -. DR PDBsum; 9KMW; -. DR PDBsum; 9KMX; -. DR PDBsum; 9KMY; -. DR PDBsum; 9KMZ; -. DR PDBsum; 9KN0; -. DR PDBsum; 9KN5; -. DR PDBsum; 9KN6; -. DR PDBsum; 9KRP; -. DR PDBsum; 9KZU; -. DR PDBsum; 9KZX; -. DR PDBsum; 9M0P; -. DR PDBsum; 9O3W; -. DR PDBsum; 9O3Y; -. DR PDBsum; 9P6Z; -. DR PDBsum; 9P72; -. DR PDBsum; 9P73; -. DR PDBsum; 9P76; -. DR PDBsum; 9P78; -. DR PDBsum; 9P79; -. DR PDBsum; 9P7A; -. DR PDBsum; 9P7C; -. DR PDBsum; 9P7D; -. DR PDBsum; 9P7E; -. DR PDBsum; 9P7F; -. DR PDBsum; 9P7G; -. DR PDBsum; 9P7H; -. DR PDBsum; 9P7I; -. DR PDBsum; 9P7J; -. DR PDBsum; 9P7K; -. DR PDBsum; 9P7L; -. DR PDBsum; 9P7N; -. DR PDBsum; 9P7O; -. DR PDBsum; 9P7W; -. DR PDBsum; 9P7X; -. DR PDBsum; 9P7Y; -. DR PDBsum; 9P8B; -. DR PDBsum; 9P8C; -. DR PDBsum; 9P8H; -. DR PDBsum; 9P8I; -. DR PDBsum; 9P9H; -. DR PDBsum; 9P9I; -. DR PDBsum; 9PA7; -. DR PDBsum; 9PBE; -. DR PDBsum; 9PKG; -. DR PDBsum; 9QLO; -. DR PDBsum; 9QLP; -. DR PDBsum; 9QLQ; -. DR PDBsum; 9RPV; -. DR PDBsum; 9S3B; -. DR PDBsum; 9S3C; -. DR PDBsum; 9S3D; -. DR PDBsum; 9SPF; -. DR PDBsum; 9SPI; -. DR PDBsum; 9SYR; -. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Diamond-Blackfan anemia; KW Direct protein sequencing; Disease variant; Endoplasmic reticulum; KW Phosphoprotein; Proteomics identification; Reference proteome; KW Ribonucleoprotein; Ribosomal protein. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:8706699" FT CHAIN 2..115 FT /note="Small ribosomal subunit protein eS26" FT /id="PRO_0000204509" FT REGION 85..115 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 87..97 FT /note="Basic and acidic 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:8GLP" FT STRAND 13..16 FT /evidence="ECO:0007829|PDB:5AJ0" FT STRAND 20..22 FT /evidence="ECO:0007829|PDB:8GLP" FT TURN 24..26 FT /evidence="ECO:0007829|PDB:8GLP" FT STRAND 28..31 FT /evidence="ECO:0007829|PDB:8GLP" FT TURN 32..34 FT /evidence="ECO:0007829|PDB:8GLP" FT STRAND 35..45 FT /evidence="ECO:0007829|PDB:8GLP" FT HELIX 47..56 FT /evidence="ECO:0007829|PDB:8GLP" FT STRAND 57..61 FT /evidence="ECO:0007829|PDB:8GLP" FT HELIX 62..65 FT /evidence="ECO:0007829|PDB:8GLP" FT STRAND 66..73 FT /evidence="ECO:0007829|PDB:8GLP" FT HELIX 75..80 FT /evidence="ECO:0007829|PDB:8GLP" FT HELIX 85..88 FT /evidence="ECO:0007829|PDB:5AJ0" FT HELIX 91..93 FT /evidence="ECO:0007829|PDB:8GLP" FT HELIX 96..99 FT /evidence="ECO:0007829|PDB:8GLP" SQ SEQUENCE 115 AA; 13015 MW; F60DF98F8900D968 CRC64; MTKKRRNNGR AKKGRGHVQP IRCTNCARCV PKDKAIKKFV IRNIVEAAAV RDISEASVFD AYVLPKLYVK LHYCVSCAIH SKVVRNRSRE ARKDRTPPPR FRPAGAAPRP PPKPM //