RL15_RAT
ID RL15_RAT Reviewed; 204 AA.
AC P61314; P39030; P41051; Q96C44; Q9H2E5;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=60S ribosomal protein L15;
GN Name=Rpl15;
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 PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Sprague-Dawley;
RX PubMed=8198562; DOI=10.1006/bbrc.1994.1675;
RA Chan Y.-L., Olvera J., Wool I.G.;
RT "The primary structure of rat ribosomal protein L15.";
RL Biochem. Biophys. Res. Commun. 201:108-114(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 SER-34 AND SER-97, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:P61313}.
CC -!- SUBUNIT: Component of the large ribosomal subunit. Interacts with IFIT1
CC (via TPR repeats 1-4). {ECO:0000250|UniProtKB:P61313}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P61313}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL15 family.
CC {ECO:0000305}.
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DR EMBL; X78167; CAA55026.1; -; mRNA.
DR EMBL; BC078724; AAH78724.1; -; mRNA.
DR PIR; JC2369; JC2369.
DR RefSeq; NP_620814.1; NM_139114.3.
DR AlphaFoldDB; P61314; -.
DR SMR; P61314; -.
DR BioGRID; 251470; 1.
DR IntAct; P61314; 4.
DR STRING; 10116.ENSRNOP00000010759; -.
DR iPTMnet; P61314; -.
DR PhosphoSitePlus; P61314; -.
DR SwissPalm; P61314; -.
DR jPOST; P61314; -.
DR PaxDb; P61314; -.
DR PRIDE; P61314; -.
DR Ensembl; ENSRNOT00000010759; ENSRNOP00000010759; ENSRNOG00000008140.
DR GeneID; 245981; -.
DR KEGG; rno:245981; -.
DR UCSC; RGD:621181; rat.
DR CTD; 6138; -.
DR RGD; 621181; Rpl15.
DR eggNOG; KOG1678; Eukaryota.
DR GeneTree; ENSGT00910000144184; -.
DR HOGENOM; CLU_080796_0_0_1; -.
DR InParanoid; P61314; -.
DR OMA; KYMQELY; -.
DR OrthoDB; 1181691at2759; -.
DR PhylomeDB; P61314; -.
DR TreeFam; TF300050; -.
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:P61314; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000008140; Expressed in spleen and 20 other tissues.
DR Genevisible; P61314; RN.
DR GO; GO:0031672; C:A band; IDA:RGD.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:RGD.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:RGD.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR Gene3D; 3.40.1120.10; -; 1.
DR InterPro; IPR024794; Rbsml_L15e_core_dom_sf.
DR InterPro; IPR000439; Ribosomal_L15e.
DR InterPro; IPR020925; Ribosomal_L15e_CS.
DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom_sf.
DR PANTHER; PTHR11847; PTHR11847; 1.
DR Pfam; PF00827; Ribosomal_L15e; 1.
DR SMART; SM01384; Ribosomal_L15e; 1.
DR SUPFAM; SSF54189; SSF54189; 1.
DR PROSITE; PS01194; RIBOSOMAL_L15E; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Isopeptide bond; Lipoprotein;
KW Myristate; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P61313"
FT CHAIN 2..204
FT /note="60S ribosomal protein L15"
FT /id="PRO_0000127531"
FT REGION 165..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..186
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61313"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P61313"
FT CROSSLNK 83
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P61313"
SQ SEQUENCE 204 AA; 24146 MW; A6E3AD1A76C9506F CRC64;
MGAYKYIQEL WRKKQSDVMR FLLRVRCWQY RQLSALHRAP RPTRPDKARR LGYKAKQGYV
IYRIRVRRGG RKRPVPKGAT YGKPVHHGVN QLKFARSLQS VAEERAGRHC GALRVLNSYW
VGEDSTYKFF EVILIDPFHK AIRRNPDTQW ITKPVHKHRE MRGLTSAGRK SRGLGKGHKF
HHTIGGSRRA AWRRRNTLQL HRYR
