RM19_HUMAN
ID RM19_HUMAN Reviewed; 292 AA.
AC P49406; Q53TX9; Q96Q52;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=39S ribosomal protein L19, mitochondrial;
DE Short=L19mt;
DE Short=MRP-L19;
DE AltName: Full=39S ribosomal protein L15, mitochondrial;
DE Short=L15mt;
DE Short=MRP-L15;
DE AltName: Full=Mitochondrial large ribosomal subunit protein bL19m {ECO:0000303|PubMed:25278503};
DE Flags: Precursor;
GN Name=MRPL19; Synonyms=KIAA0104, MRPL15;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-292.
RC TISSUE=Bone marrow;
RX PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S.,
RA Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III. The
RT coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 257-292, AND SUBCELLULAR LOCATION.
RX PubMed=11543634; DOI=10.1006/geno.2001.6622;
RA Kenmochi N., Suzuki T., Uechi T., Magoori M., Kuniba M., Higa S.,
RA Watanabe K., Tanaka T.;
RT "The human mitochondrial ribosomal protein genes: mapping of 54 genes to
RT the chromosomes and implications for human disorders.";
RL Genomics 77:65-70(2001).
RN [5]
RP IDENTIFICATION AS A RIBOSOMAL PROTEIN, AND SUBCELLULAR LOCATION.
RX PubMed=10600119; DOI=10.1021/bi991543s;
RA Graack H.R., Bryant M.L., O'Brien T.W.;
RT "Identification of mammalian mitochondrial ribosomal proteins (MRPs) by N-
RT terminal sequencing of purified bovine MRPs and comparison to data bank
RT sequences: the large subribosomal particle.";
RL Biochemistry 38:16569-16577(1999).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [8]
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 [9] {ECO:0007744|PDB:3J7Y}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RX PubMed=25278503; DOI=10.1126/science.1258026;
RA Brown A., Amunts A., Bai X.C., Sugimoto Y., Edwards P.C., Murshudov G.,
RA Scheres S.H., Ramakrishnan V.;
RT "Structure of the large ribosomal subunit from human mitochondria.";
RL Science 346:718-722(2014).
RN [10] {ECO:0007744|PDB:3J9M}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RX PubMed=25838379; DOI=10.1126/science.aaa1193;
RA Amunts A., Brown A., Toots J., Scheres S.H., Ramakrishnan V.;
RT "Ribosome. The structure of the human mitochondrial ribosome.";
RL Science 348:95-98(2015).
RN [11] {ECO:0007744|PDB:5OOL, ECO:0007744|PDB:5OOM}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.03 ANGSTROMS), SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RX PubMed=28892042; DOI=10.1038/nsmb.3464;
RA Brown A., Rathore S., Kimanius D., Aibara S., Bai X.C., Rorbach J.,
RA Amunts A., Ramakrishnan V.;
RT "Structures of the human mitochondrial ribosome in native states of
RT assembly.";
RL Nat. Struct. Mol. Biol. 24:866-869(2017).
CC -!- SUBUNIT: Component of the mitochondrial large ribosomal subunit (mt-
CC LSU) (PubMed:28892042, PubMed:25838379, PubMed:25278503). Mature
CC mammalian 55S mitochondrial ribosomes consist of a small (28S) and a
CC large (39S) subunit. The 28S small subunit contains a 12S ribosomal RNA
CC (12S mt-rRNA) and 30 different proteins. The 39S large subunit contains
CC a 16S rRNA (16S mt-rRNA), a copy of mitochondrial valine transfer RNA
CC (mt-tRNA(Val)), which plays an integral structural role, and 52
CC different proteins. {ECO:0000269|PubMed:25278503,
CC ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
CC -!- INTERACTION:
CC P49406; Q5S007: LRRK2; NbExp=3; IntAct=EBI-1188518, EBI-5323863;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10600119,
CC ECO:0000269|PubMed:11543634, ECO:0000269|PubMed:25278503,
CC ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL19 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY14972.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA03494.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC005034; AAY14972.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC030144; AAH30144.2; -; mRNA.
DR EMBL; D14660; BAA03494.1; ALT_INIT; mRNA.
DR EMBL; AB051621; BAB54949.1; -; Genomic_DNA.
DR CCDS; CCDS1960.2; -.
DR RefSeq; NP_055578.2; NM_014763.3.
DR PDB; 3J7Y; EM; 3.40 A; Q=1-292.
DR PDB; 3J9M; EM; 3.50 A; Q=1-292.
DR PDB; 5OOL; EM; 3.06 A; Q=1-292.
DR PDB; 5OOM; EM; 3.03 A; Q=1-292.
DR PDB; 6I9R; EM; 3.90 A; Q=1-292.
DR PDB; 6NU2; EM; 3.90 A; Q=74-292.
DR PDB; 6NU3; EM; 4.40 A; Q=74-292.
DR PDB; 6VLZ; EM; 2.97 A; Q=1-292.
DR PDB; 6VMI; EM; 2.96 A; Q=1-292.
DR PDB; 6ZM5; EM; 2.89 A; Q=1-292.
DR PDB; 6ZM6; EM; 2.59 A; Q=1-292.
DR PDB; 6ZS9; EM; 4.00 A; XQ=1-292.
DR PDB; 6ZSA; EM; 4.00 A; XQ=1-292.
DR PDB; 6ZSB; EM; 4.50 A; XQ=1-292.
DR PDB; 6ZSC; EM; 3.50 A; XQ=1-292.
DR PDB; 6ZSD; EM; 3.70 A; XQ=1-292.
DR PDB; 6ZSE; EM; 5.00 A; XQ=1-292.
DR PDB; 6ZSG; EM; 4.00 A; XQ=1-292.
DR PDB; 7A5F; EM; 4.40 A; Q3=1-292.
DR PDB; 7A5G; EM; 4.33 A; Q3=1-292.
DR PDB; 7A5H; EM; 3.30 A; Q=1-292.
DR PDB; 7A5I; EM; 3.70 A; Q3=1-292.
DR PDB; 7A5J; EM; 3.10 A; Q=1-292.
DR PDB; 7A5K; EM; 3.70 A; Q3=1-292.
DR PDB; 7L08; EM; 3.49 A; Q=1-292.
DR PDB; 7L20; EM; 3.15 A; Q=1-292.
DR PDB; 7O9K; EM; 3.10 A; Q=1-292.
DR PDB; 7O9M; EM; 2.50 A; Q=1-292.
DR PDB; 7ODR; EM; 2.90 A; Q=1-292.
DR PDB; 7ODS; EM; 3.10 A; Q=1-292.
DR PDB; 7ODT; EM; 3.10 A; Q=1-292.
DR PDB; 7OF0; EM; 2.20 A; Q=1-292.
DR PDB; 7OF2; EM; 2.70 A; Q=1-292.
DR PDB; 7OF3; EM; 2.70 A; Q=1-292.
DR PDB; 7OF4; EM; 2.70 A; Q=1-292.
DR PDB; 7OF5; EM; 2.90 A; Q=1-292.
DR PDB; 7OF6; EM; 2.60 A; Q=1-292.
DR PDB; 7OF7; EM; 2.50 A; Q=1-292.
DR PDB; 7OG4; EM; 3.80 A; XQ=1-292.
DR PDB; 7OI6; EM; 5.70 A; Q=1-292.
DR PDB; 7OI7; EM; 3.50 A; Q=1-292.
DR PDB; 7OI8; EM; 3.50 A; Q=1-292.
DR PDB; 7OI9; EM; 3.30 A; Q=1-292.
DR PDB; 7OIA; EM; 3.20 A; Q=1-292.
DR PDB; 7OIB; EM; 3.30 A; Q=1-292.
DR PDB; 7OIC; EM; 3.10 A; Q=1-292.
DR PDB; 7OID; EM; 3.70 A; Q=1-292.
DR PDB; 7OIE; EM; 3.50 A; Q=1-292.
DR PDB; 7PD3; EM; 3.40 A; Q=1-292.
DR PDB; 7QH6; EM; 3.08 A; Q=1-292.
DR PDBsum; 3J7Y; -.
DR PDBsum; 3J9M; -.
DR PDBsum; 5OOL; -.
DR PDBsum; 5OOM; -.
DR PDBsum; 6I9R; -.
DR PDBsum; 6NU2; -.
DR PDBsum; 6NU3; -.
DR PDBsum; 6VLZ; -.
DR PDBsum; 6VMI; -.
DR PDBsum; 6ZM5; -.
DR PDBsum; 6ZM6; -.
DR PDBsum; 6ZS9; -.
DR PDBsum; 6ZSA; -.
DR PDBsum; 6ZSB; -.
DR PDBsum; 6ZSC; -.
DR PDBsum; 6ZSD; -.
DR PDBsum; 6ZSE; -.
DR PDBsum; 6ZSG; -.
DR PDBsum; 7A5F; -.
DR PDBsum; 7A5G; -.
DR PDBsum; 7A5H; -.
DR PDBsum; 7A5I; -.
DR PDBsum; 7A5J; -.
DR PDBsum; 7A5K; -.
DR PDBsum; 7L08; -.
DR PDBsum; 7L20; -.
DR PDBsum; 7O9K; -.
DR PDBsum; 7O9M; -.
DR PDBsum; 7ODR; -.
DR PDBsum; 7ODS; -.
DR PDBsum; 7ODT; -.
DR PDBsum; 7OF0; -.
DR PDBsum; 7OF2; -.
DR PDBsum; 7OF3; -.
DR PDBsum; 7OF4; -.
DR PDBsum; 7OF5; -.
DR PDBsum; 7OF6; -.
DR PDBsum; 7OF7; -.
DR PDBsum; 7OG4; -.
DR PDBsum; 7OI6; -.
DR PDBsum; 7OI7; -.
DR PDBsum; 7OI8; -.
DR PDBsum; 7OI9; -.
DR PDBsum; 7OIA; -.
DR PDBsum; 7OIB; -.
DR PDBsum; 7OIC; -.
DR PDBsum; 7OID; -.
DR PDBsum; 7OIE; -.
DR PDBsum; 7PD3; -.
DR PDBsum; 7QH6; -.
DR AlphaFoldDB; P49406; -.
DR SMR; P49406; -.
DR BioGRID; 115142; 161.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; P49406; -.
DR IntAct; P49406; 46.
DR MINT; P49406; -.
DR STRING; 9606.ENSP00000377486; -.
DR ChEMBL; CHEMBL4295771; -.
DR GlyGen; P49406; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P49406; -.
DR MetOSite; P49406; -.
DR PhosphoSitePlus; P49406; -.
DR BioMuta; MRPL19; -.
DR DMDM; 92090636; -.
DR EPD; P49406; -.
DR jPOST; P49406; -.
DR MassIVE; P49406; -.
DR MaxQB; P49406; -.
DR PaxDb; P49406; -.
DR PeptideAtlas; P49406; -.
DR PRIDE; P49406; -.
DR ProteomicsDB; 56000; -.
DR Antibodypedia; 31651; 184 antibodies from 23 providers.
DR DNASU; 9801; -.
DR Ensembl; ENST00000393909.7; ENSP00000377486.2; ENSG00000115364.14.
DR Ensembl; ENST00000409374.5; ENSP00000387284.1; ENSG00000115364.14.
DR GeneID; 9801; -.
DR KEGG; hsa:9801; -.
DR MANE-Select; ENST00000393909.7; ENSP00000377486.2; NM_014763.4; NP_055578.2.
DR UCSC; uc002snl.4; human.
DR CTD; 9801; -.
DR DisGeNET; 9801; -.
DR GeneCards; MRPL19; -.
DR HGNC; HGNC:14052; MRPL19.
DR HPA; ENSG00000115364; Low tissue specificity.
DR MIM; 611832; gene.
DR neXtProt; NX_P49406; -.
DR OpenTargets; ENSG00000115364; -.
DR PharmGKB; PA30948; -.
DR VEuPathDB; HostDB:ENSG00000115364; -.
DR eggNOG; KOG1698; Eukaryota.
DR GeneTree; ENSGT00390000009415; -.
DR HOGENOM; CLU_076988_1_0_1; -.
DR InParanoid; P49406; -.
DR OMA; IDHQGME; -.
DR OrthoDB; 1387536at2759; -.
DR PhylomeDB; P49406; -.
DR TreeFam; TF320270; -.
DR PathwayCommons; P49406; -.
DR Reactome; R-HSA-5368286; Mitochondrial translation initiation.
DR Reactome; R-HSA-5389840; Mitochondrial translation elongation.
DR Reactome; R-HSA-5419276; Mitochondrial translation termination.
DR SignaLink; P49406; -.
DR SIGNOR; P49406; -.
DR BioGRID-ORCS; 9801; 259 hits in 1100 CRISPR screens.
DR ChiTaRS; MRPL19; human.
DR GeneWiki; MRPL19; -.
DR GenomeRNAi; 9801; -.
DR Pharos; P49406; Tbio.
DR PRO; PR:P49406; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P49406; protein.
DR Bgee; ENSG00000115364; Expressed in adrenal tissue and 197 other tissues.
DR ExpressionAtlas; P49406; baseline and differential.
DR Genevisible; P49406; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR Gene3D; 2.30.30.790; -; 1.
DR InterPro; IPR038657; L19_sf.
DR InterPro; IPR001857; Ribosomal_L19.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR15680; PTHR15680; 1.
DR Pfam; PF01245; Ribosomal_L19; 1.
DR PRINTS; PR00061; RIBOSOMALL19.
DR SUPFAM; SSF50104; SSF50104; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..292
FT /note="39S ribosomal protein L19, mitochondrial"
FT /id="PRO_0000030473"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:7OIA"
FT HELIX 89..103
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 116..141
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 158..165
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:5OOM"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 251..257
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 276..289
FT /evidence="ECO:0007829|PDB:7OF0"
SQ SEQUENCE 292 AA; 33535 MW; 4056F39694284A9F CRC64;
MAACIAAGHW AAMGLGRSFQ AARTLLPPPA SIACRVHAGP VRQQSTGPSE PGAFQPPPKP
VIVDKHRPVE PERRFLSPEF IPRRGRTDPL KFQIERKDML ERRKVLHIPE FYVGSILRVT
TADPYASGKI SQFLGICIQR SGRGLGATFI LRNVIEGQGV EICFELYNPR VQEIQVVKLE
KRLDDSLLYL RDALPEYSTF DVNMKPVVQE PNQKVPVNEL KVKMKPKPWS KRWERPNFNI
KGIRFDLCLT EQQMKEAQKW NQPWLEFDMM REYDTSKIEA AIWKEIEASK RS
