RM12_HUMAN
ID RM12_HUMAN Reviewed; 198 AA.
AC P52815; Q969U0; Q9HCA2; Q9UQJ3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=39S ribosomal protein L12, mitochondrial;
DE Short=L12mt;
DE Short=MRP-L12;
DE AltName: Full=5c5-2;
DE AltName: Full=Mitochondrial large ribosomal subunit protein bL12m {ECO:0000303|PubMed:25278503};
DE Flags: Precursor;
GN Name=MRPL12; Synonyms=MRPL7, RPML12;
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], SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=8626705; DOI=10.1074/jbc.271.19.11468;
RA Marty L., Fort P.;
RT "A delayed-early response nuclear gene encoding MRPL12, the mitochondrial
RT homologue to the bacterial translational regulator L7/L12 protein.";
RL J. Biol. Chem. 271:11468-11476(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Liu J., Barnoski B.L., O'Brien T.W.;
RT "Genomic structure and chromosomal localization of human mitochondrial
RT ribosomal protein L12.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 47-198.
RA Ma F.-R., Yan M., Zhu L.-P.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH NOA1.
RX PubMed=19103604; DOI=10.1074/jbc.m807797200;
RA Tang T., Zheng B., Chen S.H., Murphy A.N., Kudlicka K., Zhou H.,
RA Farquhar M.G.;
RT "hNOA1 interacts with complex I and DAP3 and regulates mitochondrial
RT respiration and apoptosis.";
RL J. Biol. Chem. 284:5414-5424(2009).
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 FUNCTION.
RX PubMed=22003127; DOI=10.1073/pnas.1108852108;
RA Surovtseva Y.V., Shutt T.E., Cotney J., Cimen H., Chen S.Y., Koc E.C.,
RA Shadel G.S.;
RT "Mitochondrial ribosomal protein L12 selectively associates with human
RT mitochondrial RNA polymerase to activate transcription.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:17921-17926(2011).
RN [8]
RP FUNCTION, INVOLVEMENT IN COXPD45, VARIANT COXPD45 VAL-181, AND
RP CHARACTERIZATION OF VARIANT COXPD45 VAL-181.
RX PubMed=23603806; DOI=10.1016/j.bbadis.2013.04.014;
RA Serre V., Rozanska A., Beinat M., Chretien D., Boddaert N., Munnich A.,
RA Roetig A., Chrzanowska-Lightowlers Z.M.;
RT "Mutations in mitochondrial ribosomal protein MRPL12 leads to growth
RT retardation, neurological deterioration and mitochondrial translation
RT deficiency.";
RL Biochim. Biophys. Acta 1832:1304-1312(2013).
RN [9]
RP NOMENCLATURE.
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]
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).
CC -!- FUNCTION: As a component of the mitochondrial large ribosomal subunit,
CC it plays a role in mitochondrial translation (PubMed:23603806).
CC Associates with mitochondrial RNA polymerase to activate transcription.
CC {ECO:0000269|PubMed:22003127, ECO:0000269|PubMed:23603806}.
CC -!- SUBUNIT: Component of the mitochondrial large ribosomal subunit (mt-
CC LSU) (PubMed:8626705). Mature mammalian 55S mitochondrial ribosomes
CC consist of a small (28S) and a large (39S) subunit. The 28S small
CC subunit contains a 12S ribosomal RNA (12S mt-rRNA) and 30 different
CC proteins. The 39S large subunit contains a 16S rRNA (16S mt-rRNA), a
CC copy of mitochondrial valine transfer RNA (mt-tRNA(Val)), which plays
CC an integral structural role, and 52 different proteins (Probable).
CC bL12m interacts with NOA1 (PubMed:19103604).
CC {ECO:0000269|PubMed:19103604, ECO:0000269|PubMed:8626705,
CC ECO:0000305|PubMed:25278503}.
CC -!- INTERACTION:
CC P52815; Q13185: CBX3; NbExp=3; IntAct=EBI-358272, EBI-78176;
CC P52815; Q5VUJ9-2: EFCAB2; NbExp=3; IntAct=EBI-358272, EBI-13317131;
CC P52815; O95967: EFEMP2; NbExp=3; IntAct=EBI-358272, EBI-743414;
CC P52815; Q2M3D2: EXOC3L2; NbExp=3; IntAct=EBI-358272, EBI-14890134;
CC P52815; P23142-4: FBLN1; NbExp=3; IntAct=EBI-358272, EBI-11956479;
CC P52815; Q9UPY8: MAPRE3; NbExp=3; IntAct=EBI-358272, EBI-726739;
CC P52815; Q9UBU8-2: MORF4L1; NbExp=3; IntAct=EBI-358272, EBI-10288852;
CC P52815; Q15014: MORF4L2; NbExp=3; IntAct=EBI-358272, EBI-399257;
CC P52815; P41271-2: NBL1; NbExp=3; IntAct=EBI-358272, EBI-12135485;
CC P52815; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-358272, EBI-741158;
CC P52815; Q9P121-3: NTM; NbExp=3; IntAct=EBI-358272, EBI-12027160;
CC P52815; O00411: POLRMT; NbExp=5; IntAct=EBI-358272, EBI-355145;
CC P52815; Q96I34: PPP1R16A; NbExp=3; IntAct=EBI-358272, EBI-710402;
CC P52815; P21673: SAT1; NbExp=3; IntAct=EBI-358272, EBI-711613;
CC P52815; Q8WYJ6: SEPTIN1; NbExp=3; IntAct=EBI-358272, EBI-693002;
CC P52815; Q8IWR1: TRIM59; NbExp=3; IntAct=EBI-358272, EBI-10262539;
CC P52815; O14530: TXNDC9; NbExp=3; IntAct=EBI-358272, EBI-707554;
CC P52815; P36508: ZNF76; NbExp=3; IntAct=EBI-358272, EBI-7254550;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:8626705}.
CC -!- DISEASE: Combined oxidative phosphorylation deficiency 45 (COXPD45)
CC [MIM:618951]: An autosomal recessive mitochondrial disorder with onset
CC in utero and characterized by poor overall growth, failure to thrive,
CC global developmental delay, poor or absent speech, seizures, hypotonia,
CC loss of walking, acute progressive neurologic deterioration, brain
CC lesions, and facial dysmorphism. Laboratory studies show increased
CC serum lactate and decreased mitochondrial respiratory chain enzyme
CC activity in patient tissues. {ECO:0000269|PubMed:23603806}. Note=The
CC disease may be caused by variants affecting the gene represented in
CC this entry.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL12 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD16894.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X79865; CAA56249.1; -; mRNA.
DR EMBL; AF059736; AAG32154.1; -; Genomic_DNA.
DR EMBL; BC002344; AAH02344.1; -; mRNA.
DR EMBL; BC007497; AAH07497.1; -; mRNA.
DR EMBL; AF105278; AAD16894.1; ALT_FRAME; mRNA.
DR CCDS; CCDS11785.1; -.
DR RefSeq; NP_002940.2; NM_002949.3.
DR PDB; 6VLZ; EM; 2.97 A; TA/TB/TC=1-198.
DR PDB; 6VMI; EM; 2.96 A; TA/TB/TC=1-198.
DR PDB; 6ZM5; EM; 2.89 A; t1/t2/t3/t4/t5/t6=1-198.
DR PDB; 6ZM6; EM; 2.59 A; t1/t2/t3/t4/t5/t6=1-198.
DR PDB; 6ZS9; EM; 4.00 A; t1/t2/t3/t4/t5/t6=1-198.
DR PDB; 6ZSA; EM; 4.00 A; t1/t2/t3/t4/t5/t6=1-198.
DR PDB; 6ZSB; EM; 4.50 A; t1/t2/t3/t4/t5/t6=1-198.
DR PDB; 6ZSC; EM; 3.50 A; t1/t2/t3/t4/t5/t6=1-198.
DR PDB; 6ZSD; EM; 3.70 A; t1/t2/t3/t4/t5/t6=1-198.
DR PDB; 6ZSE; EM; 5.00 A; t1/t2/t3/t4/t5/t6=1-198.
DR PDB; 6ZSG; EM; 4.00 A; t1/t2/t3/t4/t5/t6=1-198.
DR PDB; 7L08; EM; 3.49 A; TA/TB=1-198.
DR PDB; 7L20; EM; 3.15 A; TA/TB/TC=1-198.
DR PDB; 7O9K; EM; 3.10 A; FF/t1/t2/t3/t4/t5/t6=1-198.
DR PDB; 7O9M; EM; 2.50 A; t1/t2/t3/t4/t5/t6=1-198.
DR PDB; 7OG4; EM; 3.80 A; t1/t2/t3/t4/t5/t6=1-198.
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; 7L08; -.
DR PDBsum; 7L20; -.
DR PDBsum; 7O9K; -.
DR PDBsum; 7O9M; -.
DR PDBsum; 7OG4; -.
DR AlphaFoldDB; P52815; -.
DR SMR; P52815; -.
DR BioGRID; 112097; 322.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; P52815; -.
DR DIP; DIP-50865N; -.
DR IntAct; P52815; 175.
DR MINT; P52815; -.
DR STRING; 9606.ENSP00000333837; -.
DR ChEMBL; CHEMBL4295780; -.
DR iPTMnet; P52815; -.
DR PhosphoSitePlus; P52815; -.
DR SwissPalm; P52815; -.
DR BioMuta; MRPL12; -.
DR DMDM; 20981709; -.
DR DOSAC-COBS-2DPAGE; P52815; -.
DR SWISS-2DPAGE; P52815; -.
DR EPD; P52815; -.
DR jPOST; P52815; -.
DR MassIVE; P52815; -.
DR MaxQB; P52815; -.
DR PaxDb; P52815; -.
DR PeptideAtlas; P52815; -.
DR PRIDE; P52815; -.
DR ProteomicsDB; 56540; -.
DR TopDownProteomics; P52815; -.
DR Antibodypedia; 60242; 242 antibodies from 30 providers.
DR DNASU; 6182; -.
DR Ensembl; ENST00000333676.8; ENSP00000333837.3; ENSG00000262814.8.
DR GeneID; 6182; -.
DR KEGG; hsa:6182; -.
DR MANE-Select; ENST00000333676.8; ENSP00000333837.3; NM_002949.4; NP_002940.2.
DR UCSC; uc002kbh.3; human.
DR CTD; 6182; -.
DR DisGeNET; 6182; -.
DR GeneCards; MRPL12; -.
DR HGNC; HGNC:10378; MRPL12.
DR HPA; ENSG00000262814; Low tissue specificity.
DR MalaCards; MRPL12; -.
DR MIM; 602375; gene.
DR MIM; 618951; phenotype.
DR neXtProt; NX_P52815; -.
DR OpenTargets; ENSG00000262814; -.
DR PharmGKB; PA30941; -.
DR VEuPathDB; HostDB:ENSG00000262814; -.
DR eggNOG; KOG1715; Eukaryota.
DR GeneTree; ENSGT00390000000190; -.
DR HOGENOM; CLU_086499_0_2_1; -.
DR InParanoid; P52815; -.
DR OMA; LEDKWGV; -.
DR OrthoDB; 1626139at2759; -.
DR PhylomeDB; P52815; -.
DR TreeFam; TF105997; -.
DR PathwayCommons; P52815; -.
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; P52815; -.
DR SIGNOR; P52815; -.
DR BioGRID-ORCS; 6182; 425 hits in 1061 CRISPR screens.
DR ChiTaRS; MRPL12; human.
DR GeneWiki; MRPL12; -.
DR GenomeRNAi; 6182; -.
DR Pharos; P52815; Tbio.
DR PRO; PR:P52815; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P52815; protein.
DR Bgee; ENSG00000262814; Expressed in apex of heart and 109 other tissues.
DR Genevisible; P52815; 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:HGNC-UCL.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0006390; P:mitochondrial transcription; IDA:HGNC-UCL.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:HGNC-UCL.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR CDD; cd00387; Ribosomal_L7_L12; 1.
DR Gene3D; 1.20.5.710; -; 1.
DR Gene3D; 3.30.1390.10; -; 1.
DR HAMAP; MF_00368; Ribosomal_L7_L12; 1.
DR InterPro; IPR000206; Ribosomal_L7/12.
DR InterPro; IPR014719; Ribosomal_L7/12_C/ClpS-like.
DR InterPro; IPR013823; Ribosomal_L7/L12_C.
DR InterPro; IPR008932; Ribosomal_L7/L12_oligo.
DR InterPro; IPR036235; Ribosomal_L7/L12_oligo_N_sf.
DR PANTHER; PTHR45987; PTHR45987; 1.
DR Pfam; PF00542; Ribosomal_L12; 1.
DR Pfam; PF16320; Ribosomal_L12_N; 1.
DR SUPFAM; SSF48300; SSF48300; 1.
DR SUPFAM; SSF54736; SSF54736; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Disease variant; Mitochondrion;
KW Primary mitochondrial disease; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Transit peptide.
FT TRANSIT 1..45
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 46..198
FT /note="39S ribosomal protein L12, mitochondrial"
FT /id="PRO_0000030458"
FT MOD_RES 138
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB15"
FT MOD_RES 150
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB15"
FT MOD_RES 162
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB15"
FT MOD_RES 178
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB15"
FT VARIANT 105
FT /note="S -> P (in dbSNP:rs11546280)"
FT /id="VAR_052001"
FT VARIANT 181
FT /note="A -> V (in COXPD45; MRPL12 steady state level are
FT reduced in patient fibroblasts; results in defective mt-LSU
FT assembly; reduced mitochondrial translation with a
FT significant decrease of synthesis of COXI, COXII and COXIII
FT subunits; dbSNP:rs577290119)"
FT /evidence="ECO:0000269|PubMed:23603806"
FT /id="VAR_084463"
FT CONFLICT 33
FT /note="A -> T (in Ref. 1; CAA56249)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 198 AA; 21348 MW; 7F26BEDE9218CEF0 CRC64;
MLPAAARPLW GPCLGLRAAA FRLARRQVPC VCAVRHMRSS GHQRCEALAG APLDNAPKEY
PPKIQQLVQD IASLTLLEIS DLNELLKKTL KIQDVGLVPM GGVMSGAVPA AAAQEAVEED
IPIAKERTHF TVRLTEAKPV DKVKLIKEIK NYIQGINLVQ AKKLVESLPQ EIKANVAKAE
AEKIKAALEA VGGTVVLE
