RL26_RAT
ID RL26_RAT Reviewed; 145 AA.
AC P12749;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=60S ribosomal protein L26;
GN Name=Rpl26;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-13.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=2546830; DOI=10.1016/0014-5793(89)81434-6;
RA Paz V., Olvera J., Chan Y.-L., Wool I.G.;
RT "The primary structure of rat ribosomal protein L26.";
RL FEBS Lett. 251:89-93(1989).
CC -!- FUNCTION: Component of the large ribosomal subunit. The ribosome is a
CC large ribonucleoprotein complex responsible for the synthesis of
CC proteins in the cell. {ECO:0000250|UniProtKB:P61254}.
CC -!- SUBUNIT: Component of the large ribosomal subunit. Interacts with
CC DHX33. {ECO:0000250|UniProtKB:P61254}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P61254}.
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; X14671; CAA32801.1; -; mRNA.
DR PIR; S05024; R5RT26.
DR AlphaFoldDB; P12749; -.
DR SMR; P12749; -.
DR IntAct; P12749; 3.
DR MINT; P12749; -.
DR STRING; 10116.ENSRNOP00000005588; -.
DR iPTMnet; P12749; -.
DR PhosphoSitePlus; P12749; -.
DR jPOST; P12749; -.
DR PaxDb; P12749; -.
DR PRIDE; P12749; -.
DR UCSC; RGD:1310607; rat.
DR RGD; 1310607; Rpl26.
DR eggNOG; KOG3401; Eukaryota.
DR InParanoid; P12749; -.
DR PhylomeDB; P12749; -.
DR Reactome; R-RNO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-RNO-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-RNO-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-RNO-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-RNO-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-RNO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:P12749; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:RGD.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:RGD.
DR GO; GO:0005730; C:nucleolus; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; ISO:RGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:RGD.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:RGD.
DR GO; GO:0071480; P:cellular response to gamma radiation; ISO:RGD.
DR GO; GO:0071479; P:cellular response to ionizing radiation; ISO:RGD.
DR GO; GO:0034644; P:cellular response to UV; ISO:RGD.
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; ISO:RGD.
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:RGD.
DR GO; GO:1902167; P:positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISO:RGD.
DR GO; GO:0045727; P:positive regulation of translation; ISO:RGD.
DR GO; GO:1904803; P:regulation of translation involved in cellular response to UV; ISO:RGD.
DR GO; GO:1990928; P:response to amino acid starvation; IEP:RGD.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; ISO:RGD.
DR GO; GO:0006364; P:rRNA processing; ISO:RGD.
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 Cytoplasm; Direct protein sequencing; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT CHAIN 1..145
FT /note="60S ribosomal protein L26"
FT /id="PRO_0000130790"
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:0000250|UniProtKB:P61254"
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; 17277 MW; A8FD53AB4E227A45 CRC64;
MKFNPFVTSD RSKNRKRHFN APSHIRRKIM SSPLSKELRQ KYNVRSMPIR KDDEVQVVRG
HYKGQQIGKV VQVYRKKYVI YIERVQREKA NGTTVHVGIR PSKVVITRLK LDKDRKKILE
RKAKSRQVGK EKGKYKEETI EKMQE
