RM34_HUMAN
ID RM34_HUMAN Reviewed; 92 AA.
AC Q9BQ48;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=39S ribosomal protein L34, mitochondrial;
DE Short=L34mt;
DE Short=MRP-L34;
DE AltName: Full=Mitochondrial large ribosomal subunit protein bL34m {ECO:0000303|PubMed:25278503};
DE Flags: Precursor;
GN Name=MRPL34;
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=11279069; DOI=10.1074/jbc.m100432200;
RA Suzuki T., Terasaki M., Takemoto-Hori C., Hanada T., Ueda T., Wada A.,
RA Watanabe K.;
RT "Structural compensation for the deficit of rRNA with proteins in the
RT mammalian mitochondrial ribosome. Systematic analysis of protein components
RT of the large ribosomal subunit from mammalian mitochondria.";
RL J. Biol. Chem. 276:21724-21736(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Placenta;
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 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [5]
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 [6] {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 [7] {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 [8] {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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25278503,
CC ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL34 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB049652; BAB40857.1; -; mRNA.
DR EMBL; BC000071; AAH00071.1; -; mRNA.
DR EMBL; BC021801; AAH21801.1; -; mRNA.
DR CCDS; CCDS12356.1; -.
DR RefSeq; NP_076426.1; NM_023937.3.
DR RefSeq; XP_011526491.1; XM_011528189.2.
DR PDB; 3J7Y; EM; 3.40 A; 2=1-92.
DR PDB; 3J9M; EM; 3.50 A; 2=1-92.
DR PDB; 5OOL; EM; 3.06 A; 2=1-92.
DR PDB; 5OOM; EM; 3.03 A; 2=1-92.
DR PDB; 6I9R; EM; 3.90 A; 2=1-92.
DR PDB; 6NU2; EM; 3.90 A; 2=47-92.
DR PDB; 6NU3; EM; 4.40 A; 2=1-92.
DR PDB; 6VLZ; EM; 2.97 A; 2=1-92.
DR PDB; 6VMI; EM; 2.96 A; 2=1-92.
DR PDB; 6ZM5; EM; 2.89 A; 2=1-92.
DR PDB; 6ZM6; EM; 2.59 A; 2=1-92.
DR PDB; 6ZS9; EM; 4.00 A; 2=1-92.
DR PDB; 6ZSA; EM; 4.00 A; 2=1-92.
DR PDB; 6ZSB; EM; 4.50 A; 2=1-92.
DR PDB; 6ZSC; EM; 3.50 A; 2=1-92.
DR PDB; 6ZSD; EM; 3.70 A; 2=1-92.
DR PDB; 6ZSE; EM; 5.00 A; 2=1-92.
DR PDB; 6ZSG; EM; 4.00 A; 2=1-92.
DR PDB; 7A5F; EM; 4.40 A; 23=1-92.
DR PDB; 7A5G; EM; 4.33 A; 23=1-92.
DR PDB; 7A5H; EM; 3.30 A; 2=1-92.
DR PDB; 7A5I; EM; 3.70 A; 23=1-92.
DR PDB; 7A5J; EM; 3.10 A; 2=1-92.
DR PDB; 7A5K; EM; 3.70 A; 23=1-92.
DR PDB; 7L08; EM; 3.49 A; 2=1-92.
DR PDB; 7L20; EM; 3.15 A; 2=1-92.
DR PDB; 7O9K; EM; 3.10 A; 2=1-92.
DR PDB; 7O9M; EM; 2.50 A; 2=1-92.
DR PDB; 7ODR; EM; 2.90 A; 2=1-92.
DR PDB; 7ODS; EM; 3.10 A; 2=1-92.
DR PDB; 7ODT; EM; 3.10 A; 2=1-92.
DR PDB; 7OF0; EM; 2.20 A; 2=1-92.
DR PDB; 7OF2; EM; 2.70 A; 2=1-92.
DR PDB; 7OF3; EM; 2.70 A; 2=1-92.
DR PDB; 7OF4; EM; 2.70 A; 2=1-92.
DR PDB; 7OF5; EM; 2.90 A; 2=1-92.
DR PDB; 7OF6; EM; 2.60 A; 2=1-92.
DR PDB; 7OF7; EM; 2.50 A; 2=1-92.
DR PDB; 7OG4; EM; 3.80 A; 2=1-92.
DR PDB; 7OI6; EM; 5.70 A; 2=1-92.
DR PDB; 7OI7; EM; 3.50 A; 2=1-92.
DR PDB; 7OI8; EM; 3.50 A; 2=1-92.
DR PDB; 7OI9; EM; 3.30 A; 2=1-92.
DR PDB; 7OIA; EM; 3.20 A; 2=1-92.
DR PDB; 7OIB; EM; 3.30 A; 2=1-92.
DR PDB; 7OIC; EM; 3.10 A; 2=1-92.
DR PDB; 7OID; EM; 3.70 A; 2=1-92.
DR PDB; 7OIE; EM; 3.50 A; 2=1-92.
DR PDB; 7PD3; EM; 3.40 A; 2=1-92.
DR PDB; 7QH6; EM; 3.08 A; 2=1-92.
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; Q9BQ48; -.
DR SMR; Q9BQ48; -.
DR BioGRID; 122367; 55.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q9BQ48; -.
DR IntAct; Q9BQ48; 36.
DR MINT; Q9BQ48; -.
DR STRING; 9606.ENSP00000252602; -.
DR iPTMnet; Q9BQ48; -.
DR PhosphoSitePlus; Q9BQ48; -.
DR BioMuta; MRPL34; -.
DR DMDM; 20139691; -.
DR EPD; Q9BQ48; -.
DR jPOST; Q9BQ48; -.
DR MassIVE; Q9BQ48; -.
DR MaxQB; Q9BQ48; -.
DR PaxDb; Q9BQ48; -.
DR PeptideAtlas; Q9BQ48; -.
DR PRIDE; Q9BQ48; -.
DR ProteomicsDB; 78620; -.
DR TopDownProteomics; Q9BQ48; -.
DR Antibodypedia; 43756; 84 antibodies from 21 providers.
DR DNASU; 64981; -.
DR Ensembl; ENST00000252602.2; ENSP00000252602.1; ENSG00000130312.7.
DR Ensembl; ENST00000594999.1; ENSP00000471820.1; ENSG00000130312.7.
DR Ensembl; ENST00000600434.5; ENSP00000469581.1; ENSG00000130312.7.
DR GeneID; 64981; -.
DR KEGG; hsa:64981; -.
DR MANE-Select; ENST00000252602.2; ENSP00000252602.1; NM_023937.4; NP_076426.1.
DR UCSC; uc002ngc.1; human.
DR CTD; 64981; -.
DR DisGeNET; 64981; -.
DR GeneCards; MRPL34; -.
DR HGNC; HGNC:14488; MRPL34.
DR HPA; ENSG00000130312; Low tissue specificity.
DR MIM; 611840; gene.
DR neXtProt; NX_Q9BQ48; -.
DR OpenTargets; ENSG00000130312; -.
DR PharmGKB; PA30965; -.
DR VEuPathDB; HostDB:ENSG00000130312; -.
DR eggNOG; KOG4612; Eukaryota.
DR GeneTree; ENSGT00390000012240; -.
DR HOGENOM; CLU_2372198_0_0_1; -.
DR InParanoid; Q9BQ48; -.
DR OMA; WLQPRVW; -.
DR OrthoDB; 1644259at2759; -.
DR PhylomeDB; Q9BQ48; -.
DR TreeFam; TF324478; -.
DR PathwayCommons; Q9BQ48; -.
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; Q9BQ48; -.
DR SIGNOR; Q9BQ48; -.
DR BioGRID-ORCS; 64981; 669 hits in 1092 CRISPR screens.
DR ChiTaRS; MRPL34; human.
DR GenomeRNAi; 64981; -.
DR Pharos; Q9BQ48; Tdark.
DR PRO; PR:Q9BQ48; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9BQ48; protein.
DR Bgee; ENSG00000130312; Expressed in mucosa of transverse colon and 182 other tissues.
DR ExpressionAtlas; Q9BQ48; baseline and differential.
DR Genevisible; Q9BQ48; 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:0005761; C:mitochondrial ribosome; NAS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR InterPro; IPR000271; Ribosomal_L34.
DR PANTHER; PTHR14503; PTHR14503; 1.
DR Pfam; PF00468; Ribosomal_L34; 1.
DR TIGRFAMs; TIGR01030; rpmH_bact; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT TRANSIT 1..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:A8NN94"
FT CHAIN 47..92
FT /note="39S ribosomal protein L34, mitochondrial"
FT /id="PRO_0000030520"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 66..70
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 73..85
FT /evidence="ECO:0007829|PDB:7OF0"
SQ SEQUENCE 92 AA; 10165 MW; 923C87BAFA01054C CRC64;
MAVLAGSLLG PTSRSAALLG GRWLQPRAWL GFPDAWGLPT PQQARGKARG NEYQPSNIKR
KNKHGWVRRL STPAGVQVIL RRMLKGRKSL SH