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Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7

DescriptionRecName: Full=60S ribosomal protein L32;
MyHits logo
MyHits synonymsRL32_MOUSE , P62911 , P02433 , Q3UFJ7 , EDEE48446483966E
match map segment
ismart:Ribosomal_L32e ipfam:Ribosomal_L32e ipat:RIBOSOMAL_L32E  
Legends: 1, INIT_MET Removed. {ECO:0000250|UniProtKB:P62910}; 2, N6-succinyllysine. {ECO:0000244|PubMed:23806337}; 3, Phosphoserine. {ECO:0000250|UniProtKB:P62910}; 4, ipat:RIBOSOMAL_L32E [T].
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   30-NOV-2016, entry version 110.
DE   RecName: Full=60S ribosomal protein L32;
GN   Name=Rpl32;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: 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,
RC   Pancreas, 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-50, AND IDENTIFICATION BY
RP   MASS 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.,
RA   Zhang Y., 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   -!- SIMILARITY: Belongs to the ribosomal protein L32e family.
CC       {ECO:0000305}.
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   UniGene; Mm.104368; -.
DR   ProteinModelPortal; P62911; -.
DR   SMR; P62911; -.
DR   BioGrid; 202982; 3.
DR   IntAct; P62911; 2.
DR   MINT; MINT-1854367; -.
DR   STRING; 10090.ENSMUSP00000080523; -.
DR   iPTMnet; P62911; -.
DR   PhosphoSitePlus; P62911; -.
DR   SwissPalm; P62911; -.
DR   EPD; P62911; -.
DR   MaxQB; P62911; -.
DR   PaxDb; P62911; -.
DR   PeptideAtlas; P62911; -.
DR   PRIDE; P62911; -.
DR   TopDownProteomics; P62911; -.
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   eggNOG; KOG0878; Eukaryota.
DR   eggNOG; COG1717; LUCA.
DR   GeneTree; ENSGT00390000014729; -.
DR   HOGENOM; HOG000231288; -.
DR   HOVERGEN; HBG056057; -.
DR   InParanoid; P62911; -.
DR   KO; K02912; -.
DR   OMA; KVLVHNV; -.
DR   OrthoDB; EOG091G0XS4; -.
DR   PhylomeDB; P62911; -.
DR   TreeFam; TF314947; -.
DR   Reactome; R-MMU-1799339; SRP-dependent cotranslational protein targeting to membrane.
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   ChiTaRS; Rpl32; mouse.
DR   PRO; PR:P62911; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   Bgee; ENSMUSG00000057841; -.
DR   CleanEx; MM_RPL32; -.
DR   Genevisible; P62911; MM.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:MGI.
DR   GO; GO:0003735; F:structural constituent of ribosome; IC:MGI.
DR   GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
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   Pfam; PF01655; Ribosomal_L32e; 1.
DR   ProDom; PD003823; 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   Complete proteome; Phosphoprotein; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:P62910}.
FT   CHAIN         2    135       60S ribosomal protein L32.
FT                                /FTId=PRO_0000131115.
FT   MOD_RES      50     50       N6-succinyllysine.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES      62     62       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P62910}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        17    124       ismart:Ribosomal_L32e [T]
FT   MYHIT        17    124       ipfam:Ribosomal_L32e [T]
FT   MYHIT        20     40       ipat:RIBOSOMAL_L32E [T]
SQ   SEQUENCE   135 AA;  15860 MW;  EDEE48446483966E CRC64;
     MAALRPLVKP KIVKKRTKKF IRHQSDRYVK IKRNWRKPRG IDNRVRRRFK GQILMPNIGY
     GSNKKTKHML PSGFRKFLVH NVKELEVLLM CNKSYCAEIA HNVSSKNRKA IVERAAQLAI
     RVTNPNARLR SEENE
//