RL15_MOUSE
ID RL15_MOUSE Reviewed; 204 AA.
AC Q9CZM2; Q9CWI5;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=60S ribosomal protein L15;
GN Name=Rpl15;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Embryo, Embryonic liver, Embryonic stem cell, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
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; AK002234; BAB21952.1; -; mRNA.
DR EMBL; AK010319; BAB26850.1; -; mRNA.
DR EMBL; AK010674; BAB27107.1; -; mRNA.
DR EMBL; AK010916; BAB27266.1; -; mRNA.
DR EMBL; AK010931; BAB27275.1; -; mRNA.
DR EMBL; AK012025; BAB27981.1; -; mRNA.
DR EMBL; BC079842; AAH79842.1; -; mRNA.
DR EMBL; BC081441; AAH81441.1; -; mRNA.
DR EMBL; BC081442; AAH81442.1; -; mRNA.
DR CCDS; CCDS36812.1; -.
DR RefSeq; NP_079862.1; NM_025586.3.
DR RefSeq; XP_006518143.1; XM_006518080.3.
DR RefSeq; XP_006518144.1; XM_006518081.3.
DR PDB; 6SWA; EM; 3.10 A; M=1-204.
DR PDB; 7CPU; EM; 2.82 A; LN=1-204.
DR PDB; 7CPV; EM; 3.03 A; LN=1-204.
DR PDB; 7LS1; EM; 3.30 A; H1=1-204.
DR PDB; 7LS2; EM; 3.10 A; H1=1-204.
DR PDBsum; 6SWA; -.
DR PDBsum; 7CPU; -.
DR PDBsum; 7CPV; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; Q9CZM2; -.
DR SMR; Q9CZM2; -.
DR BioGRID; 211504; 89.
DR ComplexPortal; CPX-5262; 60S cytosolic large ribosomal subunit.
DR CORUM; Q9CZM2; -.
DR IntAct; Q9CZM2; 5.
DR MINT; Q9CZM2; -.
DR STRING; 10090.ENSMUSP00000079163; -.
DR iPTMnet; Q9CZM2; -.
DR PhosphoSitePlus; Q9CZM2; -.
DR SwissPalm; Q9CZM2; -.
DR EPD; Q9CZM2; -.
DR jPOST; Q9CZM2; -.
DR MaxQB; Q9CZM2; -.
DR PaxDb; Q9CZM2; -.
DR PRIDE; Q9CZM2; -.
DR ProteomicsDB; 254889; -.
DR Antibodypedia; 11374; 251 antibodies from 30 providers.
DR DNASU; 66480; -.
DR Ensembl; ENSMUST00000079419; ENSMUSP00000078388; ENSMUSG00000012405.
DR Ensembl; ENSMUST00000080281; ENSMUSP00000079163; ENSMUSG00000012405.
DR Ensembl; ENSMUST00000100799; ENSMUSP00000098362; ENSMUSG00000012405.
DR Ensembl; ENSMUST00000112598; ENSMUSP00000108217; ENSMUSG00000012405.
DR GeneID; 66480; -.
DR KEGG; mmu:66480; -.
DR UCSC; uc007shr.1; mouse.
DR CTD; 6138; -.
DR MGI; MGI:1913730; Rpl15.
DR VEuPathDB; HostDB:ENSMUSG00000012405; -.
DR eggNOG; KOG1678; Eukaryota.
DR GeneTree; ENSGT00910000144184; -.
DR HOGENOM; CLU_080796_0_0_1; -.
DR InParanoid; Q9CZM2; -.
DR OMA; KYMQELY; -.
DR OrthoDB; 1181691at2759; -.
DR PhylomeDB; Q9CZM2; -.
DR TreeFam; TF300050; -.
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; 66480; 10 hits in 36 CRISPR screens.
DR ChiTaRS; Rpl15; mouse.
DR PRO; PR:Q9CZM2; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9CZM2; protein.
DR Bgee; ENSMUSG00000012405; Expressed in ventricular zone and 255 other tissues.
DR ExpressionAtlas; Q9CZM2; baseline and differential.
DR Genevisible; Q9CZM2; MM.
DR GO; GO:0031672; C:A band; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
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:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
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 3D-structure; Cytoplasm; Isopeptide bond; Lipoprotein; Myristate;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW 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_0000127528"
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:0000250|UniProtKB:P61314"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61313"
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"
FT CONFLICT 194
FT /note="R -> G (in Ref. 1; BAB27107)"
FT /evidence="ECO:0000305"
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
