RL39_MOUSE
ID RL39_MOUSE Reviewed; 51 AA.
AC P62892; P02404; P39025; Q9BYF2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=60S ribosomal protein L39;
GN Name=Rpl39;
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, and NOD;
RC TISSUE=Kidney, Pancreas, Placenta, Stomach, and Thymus;
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=FVB/N-3;
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 INTERACTION WITH IMPACT.
RX PubMed=22404850; DOI=10.1111/j.1742-4658.2012.08553.x;
RA Waller T., Lee S.J., Sattlegger E.;
RT "Evidence that Yih1 resides in a complex with ribosomes.";
RL FEBS J. 279:1761-1776(2012).
CC -!- FUNCTION: RNA-binding component of the large ribosomal subunit. The
CC ribosome is a large ribonucleoprotein complex responsible for the
CC synthesis of proteins in the cell. {ECO:0000250|UniProtKB:P62891}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (By similarity).
CC Interacts with IMPACT (PubMed:22404850). {ECO:0000250|UniProtKB:P62891,
CC ECO:0000269|PubMed:22404850}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62891}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL39 family.
CC {ECO:0000305}.
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DR EMBL; AK002591; BAB22212.1; -; mRNA.
DR EMBL; AK005511; BAB24090.1; -; mRNA.
DR EMBL; AK007821; BAB25284.1; -; mRNA.
DR EMBL; AK008853; BAB25930.1; -; mRNA.
DR EMBL; AK013381; BAB28820.1; -; mRNA.
DR EMBL; AK028139; BAC25767.1; -; mRNA.
DR EMBL; AK088761; BAC40552.1; -; mRNA.
DR EMBL; BC039092; AAH39092.1; -; mRNA.
DR CCDS; CCDS40927.1; -.
DR RefSeq; NP_080331.1; NM_026055.2.
DR PDB; 6SWA; EM; 3.10 A; j=1-51.
DR PDB; 7CPU; EM; 2.82 A; Ll=1-51.
DR PDB; 7LS1; EM; 3.30 A; f2=1-51.
DR PDB; 7LS2; EM; 3.10 A; f2=1-51.
DR PDBsum; 6SWA; -.
DR PDBsum; 7CPU; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; P62892; -.
DR SMR; P62892; -.
DR BioGRID; 212046; 44.
DR ComplexPortal; CPX-5262; 60S cytosolic large ribosomal subunit.
DR STRING; 10090.ENSMUSP00000110886; -.
DR iPTMnet; P62892; -.
DR PhosphoSitePlus; P62892; -.
DR EPD; P62892; -.
DR jPOST; P62892; -.
DR PaxDb; P62892; -.
DR PeptideAtlas; P62892; -.
DR PRIDE; P62892; -.
DR ProteomicsDB; 299822; -.
DR TopDownProteomics; P62892; -.
DR DNASU; 67248; -.
DR Ensembl; ENSMUST00000115231; ENSMUSP00000110886; ENSMUSG00000079641.
DR GeneID; 67248; -.
DR KEGG; mmu:67248; -.
DR UCSC; uc009syc.1; mouse.
DR CTD; 6170; -.
DR MGI; MGI:1914498; Rpl39.
DR VEuPathDB; HostDB:ENSMUSG00000079641; -.
DR eggNOG; KOG0002; Eukaryota.
DR GeneTree; ENSGT00390000014814; -.
DR HOGENOM; CLU_181948_3_0_1; -.
DR InParanoid; P62892; -.
DR OMA; MKRRHWR; -.
DR OrthoDB; 1618745at2759; -.
DR PhylomeDB; P62892; -.
DR TreeFam; TF300223; -.
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; 67248; 7 hits in 30 CRISPR screens.
DR ChiTaRS; Rpl39; mouse.
DR PRO; PR:P62892; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P62892; protein.
DR Bgee; ENSMUSG00000079641; Expressed in yolk sac and 75 other tissues.
DR ExpressionAtlas; P62892; baseline and differential.
DR Genevisible; P62892; MM.
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:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0042788; C:polysomal ribosome; ISO:MGI.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:0019731; P:antibacterial humoral response; ISO:MGI.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; ISO:MGI.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:MGI.
DR GO; GO:0002227; P:innate immune response in mucosa; ISO:MGI.
DR Gene3D; 1.10.1620.10; -; 1.
DR HAMAP; MF_00629; Ribosomal_L39e; 1.
DR InterPro; IPR000077; Ribosomal_L39.
DR InterPro; IPR020083; Ribosomal_L39_CS.
DR InterPro; IPR023626; Ribosomal_L39e_dom_sf.
DR Pfam; PF00832; Ribosomal_L39; 1.
DR SUPFAM; SSF48662; SSF48662; 1.
DR PROSITE; PS00051; RIBOSOMAL_L39E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT CHAIN 1..51
FT /note="60S ribosomal protein L39"
FT /id="PRO_0000127025"
SQ SEQUENCE 51 AA; 6407 MW; 2023CA8590C7752C CRC64;
MSSHKTFRIK RFLAKKQKQN RPIPQWIRMK TGNKIRYNSK RRHWRRTKLG L
