RL26_HUMAN
ID RL26_HUMAN Reviewed; 145 AA.
AC P61254; B2R4F0; D3DTR8; Q02877; Q6IPY2;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=60S ribosomal protein L26;
DE AltName: Full=Large ribosomal subunit protein uL24 {ECO:0000303|PubMed:24524803};
GN Name=RPL26;
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=8479925; DOI=10.1093/nar/21.7.1673;
RA Zaman G.J.R.;
RT "Sequence of a cDNA encoding human ribosomal protein L26 and of a cDNA
RT probably encoding human ribosomal protein L6.";
RL Nucleic Acids Res. 21:1673-1673(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Butterfield L.H., Stephen K., Snyder C., Winston S.;
RT "Characterization of the human homologue to rat ribosomal protein L26 from
RT HL60 cells.";
RL Submitted (APR-1993) 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].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-139, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
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 INVOLVEMENT IN DBA11.
RX PubMed=22431104; DOI=10.1002/humu.22081;
RA Gazda H.T., Preti M., Sheen M.R., O'Donohue M.F., Vlachos A., Davies S.M.,
RA Kattamis A., Doherty L., Landowski M., Buros C., Ghazvinian R., Sieff C.A.,
RA Newburger P.E., Niewiadomska E., Matysiak M., Glader B., Atsidaftos E.,
RA Lipton J.M., Gleizes P.E., Beggs A.H.;
RT "Frameshift mutation in p53 regulator RPL26 is associated with multiple
RT physical abnormalities and a specific pre-ribosomal RNA processing defect
RT in diamond-blackfan anemia.";
RL Hum. Mutat. 33:1037-1044(2012).
RN [10]
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 [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-136, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-136, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [13]
RP INTERACTION WITH DHX33.
RX PubMed=26100019; DOI=10.1128/mcb.00315-15;
RA Zhang Y., You J., Wang X., Weber J.;
RT "The DHX33 RNA Helicase Promotes mRNA Translation Initiation.";
RL Mol. Cell. Biol. 35:2918-2931(2015).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-136, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-136, 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 [16]
RP UFMYLATION.
RX PubMed=32160526; DOI=10.1016/j.cell.2020.02.017;
RA Liang J.R., Lingeman E., Luong T., Ahmed S., Muhar M., Nguyen T.,
RA Olzmann J.A., Corn J.E.;
RT "A genome-wide ER-phagy screen highlights key roles of mitochondrial
RT metabolism and ER-Resident UFMylation.";
RL Cell 180:1160-1177(2020).
RN [17]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP 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 [18] {ECO:0007744|PDB:6LQM, ECO:0007744|PDB:6LSR, ECO:0007744|PDB:6LSS, ECO:0007744|PDB:6LU8}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.09 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=32669547; DOI=10.1038/s41467-020-17237-x;
RA Liang X., Zuo M.Q., Zhang Y., Li N., Ma C., Dong M.Q., Gao N.;
RT "Structural snapshots of human pre-60S ribosomal particles before and after
RT nuclear export.";
RL Nat. Commun. 11:3542-3542(2020).
CC -!- FUNCTION: Component of the large ribosomal subunit (PubMed:26100019,
CC PubMed:23636399, PubMed:32669547). The ribosome is a large
CC ribonucleoprotein complex responsible for the synthesis of proteins in
CC the cell (PubMed:26100019, PubMed:23636399, PubMed:32669547).
CC {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547,
CC ECO:0000305|PubMed:26100019}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (PubMed:26100019,
CC PubMed:23636399, PubMed:32669547). Interacts with DHX33
CC (PubMed:26100019). {ECO:0000269|PubMed:23636399,
CC ECO:0000269|PubMed:26100019, ECO:0000269|PubMed:32669547,
CC ECO:0000305|PubMed:26100019}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}.
CC -!- PTM: Ufmylated by UFL1 in response to endoplasmic reticulum stress,
CC promoting reticulophagy of endoplasmic reticulum sheets.
CC {ECO:0000269|PubMed:32160526}.
CC -!- DISEASE: Diamond-Blackfan anemia 11 (DBA11) [MIM:614900]: 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:22431104}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL24 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RPL26ID47470ch17p13.html";
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DR EMBL; X69392; CAA49189.1; -; mRNA.
DR EMBL; L07287; AAA60279.1; -; Genomic_DNA.
DR EMBL; AB061829; BAB79467.1; -; Genomic_DNA.
DR EMBL; AK311804; BAG34747.1; -; mRNA.
DR EMBL; CH471108; EAW90053.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90054.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90057.1; -; Genomic_DNA.
DR EMBL; BC071664; AAH71664.1; -; mRNA.
DR CCDS; CCDS11142.1; -.
DR PIR; S33713; S33713.
DR RefSeq; NP_000978.1; NM_000987.3.
DR RefSeq; NP_001302459.1; NM_001315530.1.
DR RefSeq; NP_001302460.1; NM_001315531.1.
DR PDB; 4UG0; EM; -; LY=1-145.
DR PDB; 4V6X; EM; 5.00 A; CY=1-145.
DR PDB; 5AJ0; EM; 3.50 A; AY=1-145.
DR PDB; 5LKS; EM; 3.60 A; LY=1-145.
DR PDB; 5T2C; EM; 3.60 A; S=1-145.
DR PDB; 6IP5; EM; 3.90 A; 2S=1-145.
DR PDB; 6IP6; EM; 4.50 A; 2S=1-145.
DR PDB; 6IP8; EM; 3.90 A; 2S=1-145.
DR PDB; 6LQM; EM; 3.09 A; h=1-145.
DR PDB; 6LSR; EM; 3.13 A; h=1-145.
DR PDB; 6LSS; EM; 3.23 A; h=1-145.
DR PDB; 6LU8; EM; 3.13 A; h=1-145.
DR PDB; 6OLE; EM; 3.10 A; Z=1-134.
DR PDB; 6OLF; EM; 3.90 A; Z=1-134.
DR PDB; 6OLG; EM; 3.40 A; AY=1-127.
DR PDB; 6OLI; EM; 3.50 A; Z=1-134.
DR PDB; 6OLZ; EM; 3.90 A; AY=1-127.
DR PDB; 6OM0; EM; 3.10 A; Z=1-134.
DR PDB; 6OM7; EM; 3.70 A; Z=1-134.
DR PDB; 6QZP; EM; 2.90 A; LY=1-134.
DR PDB; 6SXO; EM; 3.30 A; LY=1-145.
DR PDB; 6W6L; EM; 3.84 A; Z=1-145.
DR PDB; 6XA1; EM; 2.80 A; LY=1-134.
DR PDB; 6Y0G; EM; 3.20 A; LY=1-145.
DR PDB; 6Y2L; EM; 3.00 A; LY=1-145.
DR PDB; 6Y57; EM; 3.50 A; LY=1-145.
DR PDB; 6Y6X; EM; 2.80 A; LY=1-134.
DR PDB; 6Z6L; EM; 3.00 A; LY=1-145.
DR PDB; 6Z6M; EM; 3.10 A; LY=1-145.
DR PDB; 6Z6N; EM; 2.90 A; LY=1-145.
DR PDB; 6ZM7; EM; 2.70 A; LY=1-145.
DR PDB; 6ZME; EM; 3.00 A; LY=1-145.
DR PDB; 6ZMI; EM; 2.60 A; LY=1-145.
DR PDB; 6ZMO; EM; 3.10 A; LY=1-145.
DR PDB; 7BHP; EM; 3.30 A; LY=1-145.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 5AJ0; -.
DR PDBsum; 5LKS; -.
DR PDBsum; 5T2C; -.
DR PDBsum; 6IP5; -.
DR PDBsum; 6IP6; -.
DR PDBsum; 6IP8; -.
DR PDBsum; 6LQM; -.
DR PDBsum; 6LSR; -.
DR PDBsum; 6LSS; -.
DR PDBsum; 6LU8; -.
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; 6SXO; -.
DR PDBsum; 6W6L; -.
DR PDBsum; 6XA1; -.
DR PDBsum; 6Y0G; -.
DR PDBsum; 6Y2L; -.
DR PDBsum; 6Y57; -.
DR PDBsum; 6Y6X; -.
DR PDBsum; 6Z6L; -.
DR PDBsum; 6Z6M; -.
DR PDBsum; 6Z6N; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 7BHP; -.
DR AlphaFoldDB; P61254; -.
DR SMR; P61254; -.
DR BioGRID; 112073; 459.
DR CORUM; P61254; -.
DR DIP; DIP-33198N; -.
DR IntAct; P61254; 73.
DR MINT; P61254; -.
DR STRING; 9606.ENSP00000463784; -.
DR MoonProt; P61254; -.
DR GlyGen; P61254; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P61254; -.
DR MetOSite; P61254; -.
DR PhosphoSitePlus; P61254; -.
DR SwissPalm; P61254; -.
DR BioMuta; RPL26; -.
DR DMDM; 47117765; -.
DR EPD; P61254; -.
DR jPOST; P61254; -.
DR MassIVE; P61254; -.
DR MaxQB; P61254; -.
DR PaxDb; P61254; -.
DR PeptideAtlas; P61254; -.
DR PRIDE; P61254; -.
DR ProteomicsDB; 57287; -.
DR TopDownProteomics; P61254; -.
DR Antibodypedia; 24664; 179 antibodies from 25 providers.
DR DNASU; 6154; -.
DR Ensembl; ENST00000582556.5; ENSP00000463470.1; ENSG00000161970.15.
DR Ensembl; ENST00000583011.6; ENSP00000462322.1; ENSG00000161970.15.
DR Ensembl; ENST00000584164.6; ENSP00000463784.1; ENSG00000161970.15.
DR Ensembl; ENST00000648839.1; ENSP00000498177.1; ENSG00000161970.15.
DR GeneID; 6154; -.
DR KEGG; hsa:6154; -.
DR MANE-Select; ENST00000648839.1; ENSP00000498177.1; NM_000987.5; NP_000978.1.
DR UCSC; uc002glh.2; human.
DR CTD; 6154; -.
DR DisGeNET; 6154; -.
DR GeneCards; RPL26; -.
DR GeneReviews; RPL26; -.
DR HGNC; HGNC:10327; RPL26.
DR HPA; ENSG00000161970; Low tissue specificity.
DR MalaCards; RPL26; -.
DR MIM; 603704; gene.
DR MIM; 614900; phenotype.
DR neXtProt; NX_P61254; -.
DR OpenTargets; ENSG00000161970; -.
DR Orphanet; 124; Blackfan-Diamond anemia.
DR PharmGKB; PA34705; -.
DR VEuPathDB; HostDB:ENSG00000161970; -.
DR eggNOG; KOG3401; Eukaryota.
DR GeneTree; ENSGT00390000014165; -.
DR HOGENOM; CLU_093240_0_0_1; -.
DR InParanoid; P61254; -.
DR OMA; HINGLTR; -.
DR OrthoDB; 1488916at2759; -.
DR PhylomeDB; P61254; -.
DR TreeFam; TF300236; -.
DR PathwayCommons; P61254; -.
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-72689; Formation of a pool of free 40S subunits.
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-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; P61254; -.
DR SIGNOR; P61254; -.
DR BioGRID-ORCS; 6154; 771 hits in 1004 CRISPR screens.
DR ChiTaRS; RPL26; human.
DR GeneWiki; RPL26; -.
DR GenomeRNAi; 6154; -.
DR Pharos; P61254; Tbio.
DR PRO; PR:P61254; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P61254; protein.
DR Bgee; ENSG00000161970; Expressed in cortical plate and 98 other tissues.
DR ExpressionAtlas; P61254; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; HDA:UniProtKB.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:CAFA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:CAFA.
DR GO; GO:0005654; C:nucleoplasm; IDA:CAFA.
DR GO; GO:1990904; C:ribonucleoprotein complex; IMP:CAFA.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IMP:CAFA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0071480; P:cellular response to gamma radiation; IDA:CAFA.
DR GO; GO:0034644; P:cellular response to UV; IMP:CAFA.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; IMP:CAFA.
DR GO; GO:1902164; P:positive regulation of DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IMP:CAFA.
DR GO; GO:1902167; P:positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:CAFA.
DR GO; GO:0045727; P:positive regulation of translation; IMP:CAFA.
DR GO; GO:1904803; P:regulation of translation involved in cellular response to UV; IMP:CAFA.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
DR CDD; cd06089; KOW_RPL26; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR HAMAP; MF_01326_A; Ribosomal_L24_A; 1.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR041988; KOW_RPL26/RPL24.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR005825; Ribosomal_L24/26_CS.
DR InterPro; IPR005756; Ribosomal_L26/L24P_euk/arc.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR11143; PTHR11143; 1.
DR Pfam; PF00467; KOW; 1.
DR Pfam; PF16906; Ribosomal_L26; 1.
DR SMART; SM00739; KOW; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR TIGRFAMs; TIGR01080; rplX_A_E; 1.
DR PROSITE; PS01108; RIBOSOMAL_L24; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Diamond-Blackfan anemia; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT CHAIN 1..145
FT /note="60S ribosomal protein L26"
FT /id="PRO_0000130787"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 139
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 136
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CONFLICT 133
FT /note="G -> S (in Ref. 2; AAA60279)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 145 AA; 17258 MW; 049D53AB4E3F46B6 CRC64;
MKFNPFVTSD RSKNRKRHFN APSHIRRKIM SSPLSKELRQ KYNVRSMPIR KDDEVQVVRG
HYKGQQIGKV VQVYRKKYVI YIERVQREKA NGTTVHVGIH PSKVVITRLK LDKDRKKILE
RKAKSRQVGK EKGKYKEETI EKMQE
