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 24-JAN-2024, entry version 163. DE RecName: Full=Large ribosomal subunit protein bL34m {ECO:0000303|PubMed:25278503}; DE AltName: Full=39S ribosomal protein L34, mitochondrial; DE Short=L34mt; DE Short=MRP-L34; 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; 7PO4; EM; 2.56 A; 2=1-92. DR PDB; 7QH6; EM; 3.08 A; 2=1-92. DR PDB; 7QH7; EM; 2.89 A; 2=48-92. DR PDB; 7QI4; EM; 2.21 A; 2=1-92. DR PDB; 7QI5; EM; 2.63 A; 2=1-92. DR PDB; 7QI6; EM; 2.98 A; 2=1-92. DR PDB; 8ANY; EM; 2.85 A; 2=1-92. DR PDB; 8OIR; EM; 3.10 A; BJ=1-92. DR PDB; 8OIT; EM; 2.90 A; BJ=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; 7PO4; -. DR PDBsum; 7QH6; -. DR PDBsum; 7QH7; -. DR PDBsum; 7QI4; -. DR PDBsum; 7QI5; -. DR PDBsum; 7QI6; -. DR PDBsum; 8ANY; -. DR PDBsum; 8OIR; -. DR PDBsum; 8OIT; -. DR AlphaFoldDB; Q9BQ48; -. DR EMDB; EMD-0514; -. DR EMDB; EMD-0515; -. DR EMDB; EMD-11278; -. DR EMDB; EMD-11279; -. DR EMDB; EMD-11390; -. DR EMDB; EMD-11391; -. DR EMDB; EMD-11392; -. DR EMDB; EMD-11393; -. DR EMDB; EMD-11394; -. DR EMDB; EMD-11395; -. DR EMDB; EMD-11397; -. DR EMDB; EMD-11641; -. DR EMDB; EMD-11642; -. DR EMDB; EMD-11643; -. DR EMDB; EMD-11644; -. DR EMDB; EMD-11645; -. DR EMDB; EMD-11646; -. DR EMDB; EMD-12763; -. DR EMDB; EMD-12764; -. DR EMDB; EMD-12845; -. DR EMDB; EMD-12846; -. DR EMDB; EMD-12847; -. DR EMDB; EMD-12865; -. DR EMDB; EMD-12867; -. DR EMDB; EMD-12868; -. DR EMDB; EMD-12869; -. DR EMDB; EMD-12870; -. DR EMDB; EMD-12871; -. DR EMDB; EMD-12872; -. DR EMDB; EMD-12877; -. DR EMDB; EMD-12919; -. DR EMDB; EMD-12920; -. DR EMDB; EMD-12921; -. DR EMDB; EMD-12922; -. DR EMDB; EMD-12923; -. DR EMDB; EMD-12924; -. DR EMDB; EMD-12925; -. DR EMDB; EMD-12926; -. DR EMDB; EMD-12927; -. DR EMDB; EMD-13329; -. DR EMDB; EMD-13562; -. DR EMDB; EMD-13965; -. DR EMDB; EMD-13967; -. DR EMDB; EMD-13980; -. DR EMDB; EMD-13981; -. DR EMDB; EMD-13982; -. DR EMDB; EMD-15544; -. DR EMDB; EMD-16897; -. DR EMDB; EMD-16899; -. DR EMDB; EMD-21233; -. DR EMDB; EMD-21242; -. DR EMDB; EMD-23096; -. DR EMDB; EMD-23121; -. DR EMDB; EMD-3842; -. DR EMDB; EMD-3843; -. DR EMDB; EMD-4434; -. DR SMR; Q9BQ48; -. DR BioGRID; 122367; 59. DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit. DR CORUM; Q9BQ48; -. DR IntAct; Q9BQ48; 37. 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; 9606-ENSP00000252602; -. DR PeptideAtlas; Q9BQ48; -. DR ProteomicsDB; 78620; -. DR Pumba; Q9BQ48; -. DR TopDownProteomics; Q9BQ48; -. DR Antibodypedia; 43756; 105 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 AGR; HGNC:14488; -. 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; LQPRVWM; -. DR OrthoDB; 3044577at2759; -. 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; 701 hits in 1171 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 184 other cell types or tissues. DR ExpressionAtlas; Q9BQ48; baseline and differential. 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; NAS:ComplexPortal. DR GO; GO:0006412; P:translation; NAS:UniProtKB. DR Gene3D; 1.10.287.3980; -; 1. DR InterPro; IPR000271; Ribosomal_bL34. DR NCBIfam; TIGR01030; rpmH_bact; 1. DR PANTHER; PTHR14503:SF4; 39S RIBOSOMAL PROTEIN L34, MITOCHONDRIAL; 1. DR PANTHER; PTHR14503; MITOCHONDRIAL RIBOSOMAL PROTEIN 34 FAMILY MEMBER; 1. DR Pfam; PF00468; Ribosomal_L34; 1. DR Genevisible; Q9BQ48; HS. 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="Large ribosomal subunit protein bL34m" 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 //