RL26_MOUSE
ID RL26_MOUSE Reviewed; 145 AA.
AC P61255; Q02877;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=60S ribosomal protein L26;
DE AltName: Full=Silica-induced gene 20 protein;
DE Short=SIG-20;
GN Name=Rpl26;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC TISSUE=Macrophage;
RX PubMed=7868905;
RA Segade F., Claudio E., Wrobel K., Ramos S., Lazo P.S.;
RT "Isolation of nine gene sequences induced by silica in murine
RT macrophages.";
RL J. Immunol. 154:2384-2392(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-139, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [5]
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).
CC -!- FUNCTION: Component of the large ribosomal subunit (PubMed:26100019).
CC The ribosome is a large ribonucleoprotein complex responsible for the
CC synthesis of proteins in the cell (PubMed:26100019).
CC {ECO:0000305|PubMed:26100019}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (Probable). Interacts
CC with DHX33 (PubMed:26100019). {ECO:0000269|PubMed:26100019,
CC ECO:0000305|PubMed:26100019}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P61254}.
CC -!- INDUCTION: Up-regulated in silica-treated macrophages.
CC {ECO:0000269|PubMed:7868905}.
CC -!- PTM: Ufmylated by UFL1 in response to endoplasmic reticulum stress,
CC promoting reticulophagy of endoplasmic reticulum sheets.
CC {ECO:0000250|UniProtKB:P61254}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL24 family.
CC {ECO:0000305}.
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DR EMBL; X80699; CAA56716.1; -; mRNA.
DR EMBL; BC070397; AAH70397.1; -; mRNA.
DR CCDS; CCDS36187.1; -.
DR PIR; I48616; S48864.
DR RefSeq; NP_033106.1; NM_009080.2.
DR PDB; 6SWA; EM; 3.10 A; W=1-145.
DR PDB; 7CPU; EM; 2.82 A; LY=1-145.
DR PDB; 7CPV; EM; 3.03 A; LY=1-145.
DR PDB; 7LS1; EM; 3.30 A; S2=1-145.
DR PDB; 7LS2; EM; 3.10 A; S2=1-145.
DR PDBsum; 6SWA; -.
DR PDBsum; 7CPU; -.
DR PDBsum; 7CPV; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; P61255; -.
DR SMR; P61255; -.
DR BioGRID; 202973; 99.
DR ComplexPortal; CPX-5262; 60S cytosolic large ribosomal subunit.
DR CORUM; P61255; -.
DR IntAct; P61255; 1.
DR MINT; P61255; -.
DR STRING; 10090.ENSMUSP00000073175; -.
DR iPTMnet; P61255; -.
DR PhosphoSitePlus; P61255; -.
DR EPD; P61255; -.
DR jPOST; P61255; -.
DR PaxDb; P61255; -.
DR PeptideAtlas; P61255; -.
DR PRIDE; P61255; -.
DR ProteomicsDB; 299856; -.
DR TopDownProteomics; P61255; -.
DR Antibodypedia; 24664; 179 antibodies from 25 providers.
DR DNASU; 19941; -.
DR Ensembl; ENSMUST00000073471; ENSMUSP00000073175; ENSMUSG00000060938.
DR Ensembl; ENSMUST00000167436; ENSMUSP00000129072; ENSMUSG00000060938.
DR GeneID; 19941; -.
DR KEGG; mmu:19941; -.
DR UCSC; uc007joh.1; mouse.
DR CTD; 6154; -.
DR MGI; MGI:106022; Rpl26.
DR VEuPathDB; HostDB:ENSMUSG00000060938; -.
DR eggNOG; KOG3401; Eukaryota.
DR GeneTree; ENSGT00390000014165; -.
DR HOGENOM; CLU_093240_0_0_1; -.
DR InParanoid; P61255; -.
DR OMA; VRIMRGD; -.
DR OrthoDB; 1488916at2759; -.
DR PhylomeDB; P61255; -.
DR TreeFam; TF300236; -.
DR Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-MMU-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-MMU-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-MMU-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-MMU-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR BioGRID-ORCS; 19941; 24 hits in 55 CRISPR screens.
DR ChiTaRS; Rpl26; mouse.
DR PRO; PR:P61255; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P61255; protein.
DR Bgee; ENSMUSG00000060938; Expressed in medial ganglionic eminence and 246 other tissues.
DR ExpressionAtlas; P61255; baseline and differential.
DR Genevisible; P61255; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IPI:ComplexPortal.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:0071480; P:cellular response to gamma radiation; ISO:MGI.
DR GO; GO:0071479; P:cellular response to ionizing radiation; IMP:CAFA.
DR GO; GO:0034644; P:cellular response to UV; ISO:MGI.
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; IDA: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; ISO:MGI.
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; ISO:MGI.
DR GO; GO:1904803; P:regulation of translation involved in cellular response to UV; ISO:MGI.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; ISO:MGI.
DR GO; GO:0006364; P:rRNA processing; ISO:MGI.
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; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT CHAIN 1..145
FT /note="60S ribosomal protein L26"
FT /id="PRO_0000130789"
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:21183079"
FT CROSSLNK 136
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P61254"
SQ SEQUENCE 145 AA; 17258 MW; 049D53AB4E3F46B6 CRC64;
MKFNPFVTSD RSKNRKRHFN APSHIRRKIM SSPLSKELRQ KYNVRSMPIR KDDEVQVVRG
HYKGQQIGKV VQVYRKKYVI YIERVQREKA NGTTVHVGIH PSKVVITRLK LDKDRKKILE
RKAKSRQVGK EKGKYKEETI EKMQE
