RL19_HUMAN
ID RL19_HUMAN Reviewed; 196 AA.
AC P84098; B2R4K2; P14118; P22908; Q502Y6; Q7Z6E4;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=60S ribosomal protein L19;
DE AltName: Full=Large ribosomal subunit protein eL19 {ECO:0000303|PubMed:24524803};
GN Name=RPL19;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1598220; DOI=10.1093/nar/20.10.2598;
RA Kumabe T., Schma Y., Yamamoto T.;
RT "Human cDNAs encoding elongation factor 1 gamma and the ribosomal protein
RT L19.";
RL Nucleic Acids Res. 20:2598-2598(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8095182;
RA Henry J.L., Coggin D.L., King C.R.;
RT "High-level expression of the ribosomal protein L19 in human breast tumors
RT that overexpress erbB-2.";
RL Cancer Res. 53:1403-1408(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Hypothalamus, and Muscle;
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 [6]
RP PROTEIN SEQUENCE OF 10-16; 22-38 AND 154-162, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Lung carcinoma;
RA Bienvenut W.V., Vousden K.H., Lukashchuk N.;
RL Submitted (MAR-2008) to UniProtKB.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND THR-187, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164 AND THR-187, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP NOMENCLATURE.
RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT "A new system for naming ribosomal proteins.";
RL Curr. Opin. Struct. Biol. 24:165-169(2014).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-181, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [16]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
RN [17] {ECO:0007744|PDB:6LQM, ECO:0007744|PDB:6LSR, ECO:0007744|PDB:6LSS, ECO:0007744|PDB:6LU8}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.09 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=32669547; DOI=10.1038/s41467-020-17237-x;
RA Liang X., Zuo M.Q., Zhang Y., Li N., Ma C., Dong M.Q., Gao N.;
RT "Structural snapshots of human pre-60S ribosomal particles before and after
RT nuclear export.";
RL Nat. Commun. 11:3542-3542(2020).
CC -!- FUNCTION: Component of the large ribosomal subunit (PubMed:23636399,
CC PubMed:32669547). The ribosome is a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell (PubMed:23636399,
CC PubMed:32669547). {ECO:0000269|PubMed:23636399,
CC ECO:0000269|PubMed:32669547}.
CC -!- SUBUNIT: Component of the large ribosomal subunit.
CC {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547}.
CC -!- INTERACTION:
CC P84098; P54253: ATXN1; NbExp=3; IntAct=EBI-916524, EBI-930964;
CC P84098; P42858: HTT; NbExp=6; IntAct=EBI-916524, EBI-466029;
CC P84098; P54274: TERF1; NbExp=2; IntAct=EBI-916524, EBI-710997;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:P84099}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL19 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD97677.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X63527; CAA45090.1; -; mRNA.
DR EMBL; S56985; AAB25672.1; -; mRNA.
DR EMBL; AK311858; BAG34799.1; -; mRNA.
DR EMBL; BX537435; CAD97677.1; ALT_INIT; mRNA.
DR EMBL; BC000530; AAH00530.1; -; mRNA.
DR EMBL; BC013016; AAH13016.1; -; mRNA.
DR EMBL; BC062709; AAH62709.1; -; mRNA.
DR EMBL; BC066315; AAH66315.1; -; mRNA.
DR EMBL; BC095445; AAH95445.1; -; mRNA.
DR CCDS; CCDS42312.1; -.
DR PIR; A48992; A48992.
DR RefSeq; NP_000972.1; NM_000981.3.
DR PDB; 4UG0; EM; -; LR=1-196.
DR PDB; 4V6X; EM; 5.00 A; CR=1-196.
DR PDB; 5A2Q; EM; 3.90 A; r=162-174.
DR PDB; 5AJ0; EM; 3.50 A; AR=1-196.
DR PDB; 5LKS; EM; 3.60 A; LR=1-196.
DR PDB; 5T2C; EM; 3.60 A; L=1-196.
DR PDB; 6IP5; EM; 3.90 A; 2L=1-196.
DR PDB; 6IP6; EM; 4.50 A; 2L=1-196.
DR PDB; 6IP8; EM; 3.90 A; 2L=1-196.
DR PDB; 6LQM; EM; 3.09 A; a=1-196.
DR PDB; 6LSR; EM; 3.13 A; a=1-196.
DR PDB; 6LSS; EM; 3.23 A; a=1-196.
DR PDB; 6LU8; EM; 3.13 A; a=1-196.
DR PDB; 6OLE; EM; 3.10 A; S=2-182.
DR PDB; 6OLF; EM; 3.90 A; S=2-182.
DR PDB; 6OLG; EM; 3.40 A; AR=2-182.
DR PDB; 6OLI; EM; 3.50 A; S=2-182.
DR PDB; 6OLZ; EM; 3.90 A; AR=2-182.
DR PDB; 6OM0; EM; 3.10 A; S=2-182.
DR PDB; 6OM7; EM; 3.70 A; S=2-182.
DR PDB; 6QZP; EM; 2.90 A; LR=2-188.
DR PDB; 6SXO; EM; 3.30 A; LR=1-196.
DR PDB; 6W6L; EM; 3.84 A; S=1-196.
DR PDB; 6XA1; EM; 2.80 A; LR=2-188.
DR PDB; 6Y0G; EM; 3.20 A; LR=1-196.
DR PDB; 6Y2L; EM; 3.00 A; LR=1-196.
DR PDB; 6Y57; EM; 3.50 A; LR=1-196.
DR PDB; 6Y6X; EM; 2.80 A; LR=2-188.
DR PDB; 6Z6L; EM; 3.00 A; LR=1-196.
DR PDB; 6Z6M; EM; 3.10 A; LR=1-196.
DR PDB; 6Z6N; EM; 2.90 A; LR=1-196.
DR PDB; 6ZM7; EM; 2.70 A; LR=1-196.
DR PDB; 6ZME; EM; 3.00 A; LR=1-196.
DR PDB; 6ZMI; EM; 2.60 A; LR=1-196.
DR PDB; 6ZMO; EM; 3.10 A; LR=1-196.
DR PDB; 7BHP; EM; 3.30 A; LR=1-196.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 5A2Q; -.
DR PDBsum; 5AJ0; -.
DR PDBsum; 5LKS; -.
DR PDBsum; 5T2C; -.
DR PDBsum; 6IP5; -.
DR PDBsum; 6IP6; -.
DR PDBsum; 6IP8; -.
DR PDBsum; 6LQM; -.
DR PDBsum; 6LSR; -.
DR PDBsum; 6LSS; -.
DR PDBsum; 6LU8; -.
DR PDBsum; 6OLE; -.
DR PDBsum; 6OLF; -.
DR PDBsum; 6OLG; -.
DR PDBsum; 6OLI; -.
DR PDBsum; 6OLZ; -.
DR PDBsum; 6OM0; -.
DR PDBsum; 6OM7; -.
DR PDBsum; 6QZP; -.
DR PDBsum; 6SXO; -.
DR PDBsum; 6W6L; -.
DR PDBsum; 6XA1; -.
DR PDBsum; 6Y0G; -.
DR PDBsum; 6Y2L; -.
DR PDBsum; 6Y57; -.
DR PDBsum; 6Y6X; -.
DR PDBsum; 6Z6L; -.
DR PDBsum; 6Z6M; -.
DR PDBsum; 6Z6N; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 7BHP; -.
DR AlphaFoldDB; P84098; -.
DR SMR; P84098; -.
DR BioGRID; 112063; 486.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR CORUM; P84098; -.
DR IntAct; P84098; 82.
DR MINT; P84098; -.
DR STRING; 9606.ENSP00000225430; -.
DR DrugBank; DB02494; (S)-3-phenyllactic acid.
DR DrugBank; DB07374; Anisomycin.
DR DrugBank; DB08437; Puromycin.
DR GlyGen; P84098; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P84098; -.
DR MetOSite; P84098; -.
DR PhosphoSitePlus; P84098; -.
DR SwissPalm; P84098; -.
DR BioMuta; RPL19; -.
DR DMDM; 51338661; -.
DR EPD; P84098; -.
DR jPOST; P84098; -.
DR MassIVE; P84098; -.
DR MaxQB; P84098; -.
DR PaxDb; P84098; -.
DR PeptideAtlas; P84098; -.
DR PRIDE; P84098; -.
DR ProteomicsDB; 57751; -.
DR TopDownProteomics; P84098; -.
DR Antibodypedia; 28221; 204 antibodies from 33 providers.
DR DNASU; 6143; -.
DR Ensembl; ENST00000225430.9; ENSP00000225430.4; ENSG00000108298.12.
DR GeneID; 6143; -.
DR KEGG; hsa:6143; -.
DR MANE-Select; ENST00000225430.9; ENSP00000225430.4; NM_000981.4; NP_000972.1.
DR UCSC; uc002hrq.1; human.
DR CTD; 6143; -.
DR DisGeNET; 6143; -.
DR GeneCards; RPL19; -.
DR HGNC; HGNC:10312; RPL19.
DR HPA; ENSG00000108298; Low tissue specificity.
DR MIM; 180466; gene.
DR neXtProt; NX_P84098; -.
DR OpenTargets; ENSG00000108298; -.
DR PharmGKB; PA34681; -.
DR VEuPathDB; HostDB:ENSG00000108298; -.
DR eggNOG; KOG1696; Eukaryota.
DR GeneTree; ENSGT00390000012628; -.
DR InParanoid; P84098; -.
DR OMA; NRVWIDP; -.
DR OrthoDB; 1437042at2759; -.
DR PhylomeDB; P84098; -.
DR TreeFam; TF313598; -.
DR PathwayCommons; P84098; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-156902; Peptide chain elongation.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-192823; Viral mRNA Translation.
DR Reactome; R-HSA-2408557; Selenocysteine synthesis.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-HSA-72764; Eukaryotic Translation Termination.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency.
DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P84098; -.
DR SIGNOR; P84098; -.
DR BioGRID-ORCS; 6143; 815 hits in 1087 CRISPR screens.
DR ChiTaRS; RPL19; human.
DR GeneWiki; RPL19; -.
DR GenomeRNAi; 6143; -.
DR Pharos; P84098; Tbio.
DR PRO; PR:P84098; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P84098; protein.
DR Bgee; ENSG00000108298; Expressed in calcaneal tendon and 208 other tissues.
DR ExpressionAtlas; P84098; baseline and differential.
DR Genevisible; P84098; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0042788; C:polysomal ribosome; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; IDA:UniProtKB.
DR GO; GO:0006412; P:translation; TAS:UniProtKB.
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_0000131169"
FT REGION 157..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:P84099"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 16
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:P84099"
FT MOD_RES 38
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:P84099"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 187
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 181
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0007744|PubMed:25114211"
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
