RL13_MOUSE
ID RL13_MOUSE Reviewed; 211 AA.
AC P47963; Q9CRZ9; Q9DCH1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=60S ribosomal protein L13;
DE AltName: Full=A52;
GN Name=Rpl13;
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].
RC STRAIN=CBA/J;
RA Palacios R., Xie X.;
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic liver, 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION BY
RP 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 -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL13 family.
CC {ECO:0000305}.
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DR EMBL; U28917; AAA69923.1; -; mRNA.
DR EMBL; AK002787; BAB22358.1; -; mRNA.
DR EMBL; AK010989; BAB27309.1; -; mRNA.
DR EMBL; BC055358; AAH55358.1; -; mRNA.
DR CCDS; CCDS22747.1; -.
DR RefSeq; NP_058018.2; NM_016738.5.
DR PDB; 6SWA; EM; 3.10 A; K=1-211.
DR PDB; 7CPU; EM; 2.82 A; LL=1-211.
DR PDB; 7CPV; EM; 3.03 A; LL=1-211.
DR PDB; 7LS1; EM; 3.30 A; F1=1-211.
DR PDB; 7LS2; EM; 3.10 A; F1=1-211.
DR PDBsum; 6SWA; -.
DR PDBsum; 7CPU; -.
DR PDBsum; 7CPV; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; P47963; -.
DR SMR; P47963; -.
DR BioGRID; 234761; 106.
DR ComplexPortal; CPX-5262; 60S cytosolic large ribosomal subunit.
DR CORUM; P47963; -.
DR IntAct; P47963; 6.
DR MINT; P47963; -.
DR STRING; 10090.ENSMUSP00000000756; -.
DR iPTMnet; P47963; -.
DR PhosphoSitePlus; P47963; -.
DR SwissPalm; P47963; -.
DR EPD; P47963; -.
DR jPOST; P47963; -.
DR MaxQB; P47963; -.
DR PaxDb; P47963; -.
DR PeptideAtlas; P47963; -.
DR PRIDE; P47963; -.
DR ProteomicsDB; 253327; -.
DR Antibodypedia; 17428; 145 antibodies from 27 providers.
DR DNASU; 270106; -.
DR Ensembl; ENSMUST00000000756; ENSMUSP00000000756; ENSMUSG00000000740.
DR GeneID; 270106; -.
DR KEGG; mmu:270106; -.
DR UCSC; uc009nue.2; mouse.
DR CTD; 6137; -.
DR MGI; MGI:105922; Rpl13.
DR VEuPathDB; HostDB:ENSMUSG00000000740; -.
DR eggNOG; KOG3295; Eukaryota.
DR GeneTree; ENSGT00390000007818; -.
DR HOGENOM; CLU_075696_1_0_1; -.
DR InParanoid; P47963; -.
DR OMA; NQQIPHN; -.
DR OrthoDB; 1239434at2759; -.
DR PhylomeDB; P47963; -.
DR TreeFam; TF300073; -.
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; 270106; 27 hits in 73 CRISPR screens.
DR ChiTaRS; Rpl13; mouse.
DR PRO; PR:P47963; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P47963; protein.
DR Bgee; ENSMUSG00000000740; Expressed in embryonic facial prominence and 67 other tissues.
DR Genevisible; P47963; MM.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IPI:ComplexPortal.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; 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:0001824; P:blastocyst development; IMP:MGI.
DR GO; GO:0060348; P:bone development; ISO:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR HAMAP; MF_00499; Ribosomal_L13e; 1.
DR InterPro; IPR001380; Ribosomal_L13e.
DR InterPro; IPR018256; Ribosomal_L13e_CS.
DR PANTHER; PTHR11722; PTHR11722; 1.
DR Pfam; PF01294; Ribosomal_L13e; 1.
DR PROSITE; PS01104; RIBOSOMAL_L13E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT CHAIN 1..211
FT /note="60S ribosomal protein L13"
FT /id="PRO_0000192920"
FT MOD_RES 16
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26373"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26373"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26373"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 177
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P26373"
FT CROSSLNK 123
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P26373"
FT CROSSLNK 145
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P26373"
FT CROSSLNK 174
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P26373"
FT CROSSLNK 174
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P26373"
FT CROSSLNK 177
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P26373"
FT CONFLICT 40
FT /note="Q -> L (in Ref. 1; AAA69923)"
FT /evidence="ECO:0000305"
FT CONFLICT 190..196
FT /note="RLFGIRA -> PTLWQSEQ (in Ref. 1; AAA69923)"
FT /evidence="ECO:0000305"
FT CONFLICT 203..211
FT /note="AEQDVEKKK -> SEQRCWKRKN (in Ref. 1; AAA69923)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 211 AA; 24305 MW; 27B1D4B97A9A1B74 CRC64;
MAPSRNGMIL KPHFHKDWQQ RVDTWFNQPA RKIRRRKARQ AKARRIAPRP ASGPIRPIVR
CPTVRYHTKV RAGRGFSLEE LRVAGIHKKV ARTIGISVDP RRRNKSTESL QANVQRLKEY
RSKLILFPRK PSAPKKGDSS AEELKLATQL TGPVMPIRNV YKKEKARVIT EEEKNFKAFA
SLRMARANAR LFGIRAKRAK EAAEQDVEKK K
