RL32_MOUSE
ID RL32_MOUSE Reviewed; 135 AA.
AC P62911; P02433; Q3UFJ7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=60S ribosomal protein L32;
GN Name=Rpl32;
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 [GENOMIC DNA].
RX PubMed=6327068; DOI=10.1016/0092-8674(84)90376-3;
RA Dudov K.P., Perry R.P.;
RT "The gene family encoding the mouse ribosomal protein L32 contains a
RT uniquely expressed intron-containing gene and an unmutated processed
RT gene.";
RL Cell 37:457-468(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, and C57BL/6J;
RC TISSUE=Bone marrow, Kidney, Liver, Pancreas, and Stomach;
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=Colon;
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 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).
RN [5]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-50, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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:P62910}.
CC -!- SUBUNIT: Component of the large ribosomal subunit.
CC {ECO:0000250|UniProtKB:P62910}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62910}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL32 family.
CC {ECO:0000305}.
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DR EMBL; K02060; AAC28897.1; -; Genomic_DNA.
DR EMBL; AK002353; BAB22032.1; -; mRNA.
DR EMBL; AK011017; BAB27335.1; -; mRNA.
DR EMBL; AK012525; BAB28296.1; -; mRNA.
DR EMBL; AK028204; BAC25812.1; -; mRNA.
DR EMBL; AK146768; BAE27419.1; -; mRNA.
DR EMBL; AK148453; BAE28563.1; -; mRNA.
DR EMBL; AK150705; BAE29784.1; -; mRNA.
DR EMBL; AK168282; BAE40228.1; -; mRNA.
DR EMBL; BC046339; AAH46339.1; -; mRNA.
DR CCDS; CCDS20443.1; -.
DR PIR; A02829; R5MS32.
DR RefSeq; NP_742083.1; NM_172086.2.
DR PDB; 6SWA; EM; 3.10 A; c=1-135.
DR PDB; 7CPU; EM; 2.82 A; Le=1-135.
DR PDB; 7CPV; EM; 3.03 A; Le=1-135.
DR PDB; 7LS1; EM; 3.30 A; Y2=1-135.
DR PDB; 7LS2; EM; 3.10 A; Y2=1-135.
DR PDBsum; 6SWA; -.
DR PDBsum; 7CPU; -.
DR PDBsum; 7CPV; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; P62911; -.
DR SMR; P62911; -.
DR BioGRID; 202982; 79.
DR ComplexPortal; CPX-5262; 60S cytosolic large ribosomal subunit.
DR IntAct; P62911; 1.
DR MINT; P62911; -.
DR STRING; 10090.ENSMUSP00000080523; -.
DR iPTMnet; P62911; -.
DR PhosphoSitePlus; P62911; -.
DR SwissPalm; P62911; -.
DR EPD; P62911; -.
DR jPOST; P62911; -.
DR MaxQB; P62911; -.
DR PaxDb; P62911; -.
DR PeptideAtlas; P62911; -.
DR PRIDE; P62911; -.
DR ProteomicsDB; 260974; -.
DR TopDownProteomics; P62911; -.
DR Antibodypedia; 10834; 100 antibodies from 24 providers.
DR DNASU; 19951; -.
DR Ensembl; ENSMUST00000081840; ENSMUSP00000080523; ENSMUSG00000057841.
DR Ensembl; ENSMUST00000203816; ENSMUSP00000145350; ENSMUSG00000057841.
DR GeneID; 19951; -.
DR KEGG; mmu:19951; -.
DR UCSC; uc009djc.1; mouse.
DR CTD; 6161; -.
DR MGI; MGI:98038; Rpl32.
DR VEuPathDB; HostDB:ENSMUSG00000057841; -.
DR eggNOG; KOG0878; Eukaryota.
DR GeneTree; ENSGT00940000153973; -.
DR HOGENOM; CLU_071479_4_1_1; -.
DR InParanoid; P62911; -.
DR OMA; HPSGYEE; -.
DR OrthoDB; 1460684at2759; -.
DR PhylomeDB; P62911; -.
DR TreeFam; TF314947; -.
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; 19951; 26 hits in 54 CRISPR screens.
DR ChiTaRS; Rpl32; mouse.
DR PRO; PR:P62911; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P62911; protein.
DR Bgee; ENSMUSG00000057841; Expressed in ventricular zone and 65 other tissues.
DR Genevisible; P62911; 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; IDA:MGI.
DR GO; GO:0022626; C:cytosolic ribosome; 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:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
DR GO; GO:0002181; P:cytoplasmic translation; ISO:MGI.
DR GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
DR GO; GO:0006412; P:translation; IC:MGI.
DR CDD; cd00513; Ribosomal_L32_L32e; 1.
DR InterPro; IPR001515; Ribosomal_L32e.
DR InterPro; IPR018263; Ribosomal_L32e_CS.
DR InterPro; IPR036351; Ribosomal_L32e_sf.
DR PANTHER; PTHR23413; PTHR23413; 1.
DR Pfam; PF01655; Ribosomal_L32e; 1.
DR SMART; SM01393; Ribosomal_L32e; 1.
DR SUPFAM; SSF52042; SSF52042; 1.
DR PROSITE; PS00580; RIBOSOMAL_L32E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT CHAIN 1..135
FT /note="60S ribosomal protein L32"
FT /id="PRO_0000131115"
FT MOD_RES 50
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62910"
FT CROSSLNK 9
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P62910"
SQ SEQUENCE 135 AA; 15860 MW; EDEE48446483966E CRC64;
MAALRPLVKP KIVKKRTKKF IRHQSDRYVK IKRNWRKPRG IDNRVRRRFK GQILMPNIGY
GSNKKTKHML PSGFRKFLVH NVKELEVLLM CNKSYCAEIA HNVSSKNRKA IVERAAQLAI
RVTNPNARLR SEENE
