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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}.
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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
 
 
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