RL19_MOUSE
ID RL19_MOUSE Reviewed; 196 AA.
AC P84099; P14118; P22908;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=60S ribosomal protein L19;
GN Name=Rpl19;
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].
RX PubMed=1702292; DOI=10.1089/dna.1990.9.697;
RA Nakamura T., Onno M., Mariage-Samson R., Hillova J., Hill M.;
RT "Nucleotide sequence of mouse L19 ribosomal protein cDNA isolated in
RT screening with tre oncogene probes.";
RL DNA Cell Biol. 9:697-703(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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].
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 PROTEIN SEQUENCE OF 187-195, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
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 [6]
RP CITRULLINATION AT ARG-5; ARG-16 AND ARG-38.
RX PubMed=24463520; DOI=10.1038/nature12942;
RA Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S.,
RA Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C.,
RA Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.;
RT "Citrullination regulates pluripotency and histone H1 binding to
RT chromatin.";
RL Nature 507:104-108(2014).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 137-145 IN COMPLEX WITH MHC.
RX PubMed=11738047; DOI=10.1016/s0969-2126(01)00689-x;
RA He X., Tabaczewski P., Ho J., Stroynowski I., Garcia K.C.;
RT "Promiscuous antigen presentation by the nonclassical MHC Ib Qa-2 is
RT enabled by a shallow, hydrophobic groove and self-stabilized peptide
RT conformation.";
RL Structure 9:1213-1224(2001).
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:P84098}.
CC -!- SUBUNIT: Component of the large ribosomal subunit.
CC {ECO:0000250|UniProtKB:P84098}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P84098}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL19 family.
CC {ECO:0000305}.
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DR EMBL; M62952; AAB48630.1; -; mRNA.
DR EMBL; AK010440; BAB26941.1; -; mRNA.
DR EMBL; BC010710; AAH10710.1; -; mRNA.
DR EMBL; BC083131; AAH83131.1; -; mRNA.
DR CCDS; CCDS25337.1; -.
DR PIR; A36554; A36554.
DR RefSeq; NP_033104.2; NM_009078.2.
DR PDB; 1K8D; X-ray; 2.30 A; P=137-145.
DR PDB; 6SWA; EM; 3.10 A; o=1-196.
DR PDB; 7LS1; EM; 3.30 A; L2=1-196.
DR PDB; 7LS2; EM; 3.10 A; L2=1-196.
DR PDBsum; 1K8D; -.
DR PDBsum; 6SWA; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; P84099; -.
DR SMR; P84099; -.
DR BioGRID; 202969; 86.
DR ComplexPortal; CPX-5262; 60S cytosolic large ribosomal subunit.
DR CORUM; P84099; -.
DR IntAct; P84099; 4.
DR STRING; 10090.ENSMUSP00000017548; -.
DR iPTMnet; P84099; -.
DR PhosphoSitePlus; P84099; -.
DR SwissPalm; P84099; -.
DR EPD; P84099; -.
DR jPOST; P84099; -.
DR PaxDb; P84099; -.
DR PRIDE; P84099; -.
DR ProteomicsDB; 253248; -.
DR TopDownProteomics; P84099; -.
DR Antibodypedia; 28221; 204 antibodies from 33 providers.
DR DNASU; 19921; -.
DR Ensembl; ENSMUST00000017548; ENSMUSP00000017548; ENSMUSG00000017404.
DR GeneID; 19921; -.
DR KEGG; mmu:19921; -.
DR UCSC; uc007lfj.2; mouse.
DR CTD; 6143; -.
DR MGI; MGI:98020; Rpl19.
DR VEuPathDB; HostDB:ENSMUSG00000017404; -.
DR eggNOG; KOG1696; Eukaryota.
DR GeneTree; ENSGT00390000012628; -.
DR InParanoid; P84099; -.
DR OMA; NRVWIDP; -.
DR OrthoDB; 1437042at2759; -.
DR PhylomeDB; P84099; -.
DR TreeFam; TF313598; -.
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; 19921; 26 hits in 70 CRISPR screens.
DR ChiTaRS; Rpl19; mouse.
DR EvolutionaryTrace; P84099; -.
DR PRO; PR:P84099; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P84099; protein.
DR Bgee; ENSMUSG00000017404; Expressed in ectoplacental cone and 62 other tissues.
DR ExpressionAtlas; P84099; baseline and differential.
DR Genevisible; P84099; MM.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:MGI.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0042788; C:polysomal ribosome; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:1990932; F:5.8S rRNA binding; ISO:MGI.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; ISO:MGI.
DR GO; GO:0006412; P:translation; IC:MGI.
DR CDD; cd01417; Ribosomal_L19e_E; 1.
DR Gene3D; 1.10.1650.10; -; 1.
DR HAMAP; MF_01475; Ribosomal_L19e; 1.
DR InterPro; IPR035970; 60S_ribosomal_L19/L19e_sf.
DR InterPro; IPR000196; Ribosomal_L19/L19e.
DR InterPro; IPR023638; Ribosomal_L19/L19e_CS.
DR InterPro; IPR015972; Ribosomal_L19/L19e_dom1.
DR InterPro; IPR033935; Ribosomal_L19_euka.
DR InterPro; IPR039547; RPL19.
DR PANTHER; PTHR10722; PTHR10722; 1.
DR Pfam; PF01280; Ribosomal_L19e; 1.
DR SMART; SM01416; Ribosomal_L19e; 1.
DR SUPFAM; SSF48140; SSF48140; 1.
DR PROSITE; PS00526; RIBOSOMAL_L19E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Citrullination; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Ubl conjugation.
FT CHAIN 1..196
FT /note="60S ribosomal protein L19"
FT /id="PRO_0000131171"
FT REGION 157..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:24463520"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P84098"
FT MOD_RES 16
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:24463520"
FT MOD_RES 38
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:24463520"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P84098"
FT MOD_RES 187
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P84098"
FT CROSSLNK 181
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:P84098"
FT CONFLICT 179
FT /note="A -> S (in Ref. 1; AAB48630)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 196 AA; 23466 MW; 4AF506393E526216 CRC64;
MSMLRLQKRL ASSVLRCGKK KVWLDPNETN EIANANSRQQ IRKLIKDGLI IRKPVTVHSR
ARCRKNTLAR RKGRHMGIGK RKGTANARMP EKVTWMRRMR ILRRLLRRYR ESKKIDRHMY
HSLYLKVKGN VFKNKRILME HIHKLKADKA RKKLLADQAE ARRSKTKEAR KRREERLQAK
KEEIIKTLSK EEETKK
