RM15_HUMAN
ID RM15_HUMAN Reviewed; 296 AA.
AC Q9P015; Q96Q54; Q9H0Y1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=39S ribosomal protein L15, mitochondrial;
DE Short=L15mt;
DE Short=MRP-L15;
DE AltName: Full=Mitochondrial large ribosomal subunit protein uL15m {ECO:0000303|PubMed:25278503};
DE Flags: Precursor;
GN Name=MRPL15; ORFNames=HSPC145;
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 MRNA].
RC TISSUE=Blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 259-296.
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 [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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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 Q9P015; O95273: CCNDBP1; NbExp=7; IntAct=EBI-2371967, EBI-748961;
CC Q9P015; Q59EK9: RUNDC3A; NbExp=3; IntAct=EBI-2371967, EBI-747225;
CC Q9P015; P09012: SNRPA; NbExp=3; IntAct=EBI-2371967, EBI-607085;
CC Q9P015; P26368-2: U2AF2; NbExp=3; IntAct=EBI-2371967, EBI-11097439;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25278503,
CC ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL15 family.
CC {ECO:0000305}.
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DR EMBL; AF161494; AAF29109.1; -; mRNA.
DR EMBL; AL136665; CAB66600.1; -; mRNA.
DR EMBL; CR533531; CAG38562.1; -; mRNA.
DR EMBL; BC000891; AAH00891.1; -; mRNA.
DR EMBL; AB051619; BAB54947.1; -; Genomic_DNA.
DR CCDS; CCDS6158.1; -.
DR RefSeq; NP_054894.1; NM_014175.3.
DR PDB; 3J7Y; EM; 3.40 A; M=1-296.
DR PDB; 3J9M; EM; 3.50 A; M=1-296.
DR PDB; 5OOL; EM; 3.06 A; M=1-296.
DR PDB; 5OOM; EM; 3.03 A; M=1-296.
DR PDB; 6I9R; EM; 3.90 A; M=1-296.
DR PDB; 6NU2; EM; 3.90 A; M=10-296.
DR PDB; 6NU3; EM; 4.40 A; M=1-296.
DR PDB; 6VLZ; EM; 2.97 A; M=1-296.
DR PDB; 6VMI; EM; 2.96 A; M=1-296.
DR PDB; 6ZM5; EM; 2.89 A; M=1-296.
DR PDB; 6ZM6; EM; 2.59 A; M=1-296.
DR PDB; 6ZS9; EM; 4.00 A; XM=1-296.
DR PDB; 6ZSA; EM; 4.00 A; XM=1-296.
DR PDB; 6ZSB; EM; 4.50 A; XM=1-296.
DR PDB; 6ZSC; EM; 3.50 A; XM=1-296.
DR PDB; 6ZSD; EM; 3.70 A; XM=1-296.
DR PDB; 6ZSE; EM; 5.00 A; XM=1-296.
DR PDB; 6ZSG; EM; 4.00 A; XM=1-296.
DR PDB; 7A5F; EM; 4.40 A; M3=1-296.
DR PDB; 7A5G; EM; 4.33 A; M3=1-296.
DR PDB; 7A5H; EM; 3.30 A; M=1-296.
DR PDB; 7A5I; EM; 3.70 A; M3=1-296.
DR PDB; 7A5J; EM; 3.10 A; M=1-296.
DR PDB; 7A5K; EM; 3.70 A; M3=1-296.
DR PDB; 7L08; EM; 3.49 A; M=1-296.
DR PDB; 7L20; EM; 3.15 A; M=1-296.
DR PDB; 7O9K; EM; 3.10 A; M=1-296.
DR PDB; 7O9M; EM; 2.50 A; M=1-296.
DR PDB; 7ODR; EM; 2.90 A; M=1-296.
DR PDB; 7ODS; EM; 3.10 A; M=1-296.
DR PDB; 7ODT; EM; 3.10 A; M=1-296.
DR PDB; 7OF0; EM; 2.20 A; M=1-296.
DR PDB; 7OF2; EM; 2.70 A; M=1-296.
DR PDB; 7OF3; EM; 2.70 A; M=1-296.
DR PDB; 7OF4; EM; 2.70 A; M=1-296.
DR PDB; 7OF5; EM; 2.90 A; M=1-296.
DR PDB; 7OF6; EM; 2.60 A; M=1-296.
DR PDB; 7OF7; EM; 2.50 A; M=1-296.
DR PDB; 7OG4; EM; 3.80 A; XM=1-296.
DR PDB; 7OI6; EM; 5.70 A; M=1-296.
DR PDB; 7OI7; EM; 3.50 A; M=1-296.
DR PDB; 7OI8; EM; 3.50 A; M=1-296.
DR PDB; 7OI9; EM; 3.30 A; M=1-296.
DR PDB; 7OIA; EM; 3.20 A; M=1-296.
DR PDB; 7OIB; EM; 3.30 A; M=1-296.
DR PDB; 7OIC; EM; 3.10 A; M=1-296.
DR PDB; 7OID; EM; 3.70 A; M=1-296.
DR PDB; 7OIE; EM; 3.50 A; M=1-296.
DR PDB; 7PD3; EM; 3.40 A; M=1-296.
DR PDB; 7QH6; EM; 3.08 A; M=1-296.
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; Q9P015; -.
DR SMR; Q9P015; -.
DR BioGRID; 118857; 202.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q9P015; -.
DR IntAct; Q9P015; 52.
DR MINT; Q9P015; -.
DR STRING; 9606.ENSP00000260102; -.
DR GlyGen; Q9P015; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9P015; -.
DR PhosphoSitePlus; Q9P015; -.
DR SwissPalm; Q9P015; -.
DR BioMuta; MRPL15; -.
DR DMDM; 74734761; -.
DR EPD; Q9P015; -.
DR jPOST; Q9P015; -.
DR MassIVE; Q9P015; -.
DR MaxQB; Q9P015; -.
DR PaxDb; Q9P015; -.
DR PeptideAtlas; Q9P015; -.
DR PRIDE; Q9P015; -.
DR ProteomicsDB; 83533; -.
DR Antibodypedia; 24498; 188 antibodies from 25 providers.
DR DNASU; 29088; -.
DR Ensembl; ENST00000260102.9; ENSP00000260102.4; ENSG00000137547.9.
DR GeneID; 29088; -.
DR KEGG; hsa:29088; -.
DR MANE-Select; ENST00000260102.9; ENSP00000260102.4; NM_014175.4; NP_054894.1.
DR UCSC; uc003xsa.3; human.
DR CTD; 29088; -.
DR GeneCards; MRPL15; -.
DR HGNC; HGNC:14054; MRPL15.
DR HPA; ENSG00000137547; Tissue enhanced (skeletal muscle, tongue).
DR MIM; 611828; gene.
DR neXtProt; NX_Q9P015; -.
DR OpenTargets; ENSG00000137547; -.
DR PharmGKB; PA30944; -.
DR VEuPathDB; HostDB:ENSG00000137547; -.
DR eggNOG; KOG0846; Eukaryota.
DR GeneTree; ENSGT00390000009040; -.
DR InParanoid; Q9P015; -.
DR OMA; KGHHLKR; -.
DR OrthoDB; 930708at2759; -.
DR PhylomeDB; Q9P015; -.
DR TreeFam; TF105918; -.
DR PathwayCommons; Q9P015; -.
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; Q9P015; -.
DR SIGNOR; Q9P015; -.
DR BioGRID-ORCS; 29088; 335 hits in 1082 CRISPR screens.
DR ChiTaRS; MRPL15; human.
DR GeneWiki; MRPL15; -.
DR GenomeRNAi; 29088; -.
DR Pharos; Q9P015; Tdark.
DR PRO; PR:Q9P015; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9P015; protein.
DR Bgee; ENSG00000137547; Expressed in heart right ventricle and 202 other tissues.
DR ExpressionAtlas; Q9P015; baseline and differential.
DR Genevisible; Q9P015; 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:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR HAMAP; MF_01341; Ribosomal_L15; 1.
DR InterPro; IPR036227; L18e/L15P_sf.
DR InterPro; IPR030878; Ribosomal_L15.
DR InterPro; IPR005749; Ribosomal_L15_bac-type.
DR InterPro; IPR021131; Ribosomal_L18e/L15P.
DR PANTHER; PTHR12934; PTHR12934; 1.
DR Pfam; PF00828; Ribosomal_L27A; 1.
DR SUPFAM; SSF52080; SSF52080; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Transit peptide.
FT TRANSIT 1..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:Q0VC21"
FT CHAIN 22..296
FT /note="39S ribosomal protein L15, mitochondrial"
FT /id="PRO_0000257838"
FT REGION 22..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..58
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 96
FT /note="L -> M (in Ref. 2; CAB66600 and 3; CAG38562)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="G -> D (in Ref. 2; CAB66600 and 3; CAG38562)"
FT /evidence="ECO:0000305"
FT HELIX 11..18
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:7OIB"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:5OOL"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:7OI9"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:3J7Y"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 98..106
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:3J7Y"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:7OIB"
FT HELIX 118..123
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 161..169
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 181..188
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 190..195
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 211..215
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 217..220
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:7OI9"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 229..240
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 253..257
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 277..280
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 288..295
FT /evidence="ECO:0007829|PDB:7OF0"
SQ SEQUENCE 296 AA; 33420 MW; D7396086F808A72C CRC64;
MAGPLQGGGA RALDLLRGLP RVSLANLKPN PGSKKPERRP RGRRRGRKCG RGHKGERQRG
TRPRLGFEGG QTPFYIRIPK YGFNEGHSFR RQYKPLSLNR LQYLIDLGRV DPSQPIDLTQ
LVNGRGVTIQ PLKRDYGVQL VEEGADTFTA KVNIEVQLAS ELAIAAIEKN GGVVTTAFYD
PRSLDIVCKP VPFFLRGQPI PKRMLPPEEL VPYYTDAKNR GYLADPAKFP EARLELARKY
GYILPDITKD ELFKMLCTRK DPRQIFFGLA PGWVVNMADK KILKPTDENL LKYYTS
