RM32_HUMAN
ID RM32_HUMAN Reviewed; 188 AA.
AC Q9BYC8; Q96Q68; Q9P098;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=39S ribosomal protein L32, mitochondrial;
DE Short=L32mt;
DE Short=MRP-L32;
DE AltName: Full=Mitochondrial large ribosomal subunit protein bL32m {ECO:0000303|PubMed:25278503};
DE Flags: Precursor;
GN Name=MRPL32; ORFNames=HSPC283;
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=Lymph;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-188.
RC TISSUE=Umbilical cord blood;
RA Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L.,
RA Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.;
RT "Human partial CDS from CD34+ stem cells.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 105-126.
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 [5]
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 [6]
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 [7] {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 [8] {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 [9] {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:25278503, PubMed:25838379, PubMed:28892042). 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. bL32m has a zinc binding site.
CC {ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379,
CC ECO:0000269|PubMed:28892042}.
CC -!- INTERACTION:
CC Q9BYC8; Q9GZV8: PRDM14; NbExp=3; IntAct=EBI-7825220, EBI-3957793;
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 bL32 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; AB049649; BAB40854.1; -; mRNA.
DR EMBL; BC013147; AAH13147.1; -; mRNA.
DR EMBL; AF161401; AAF28961.1; -; mRNA.
DR EMBL; AB051343; BAB54933.1; -; Genomic_DNA.
DR CCDS; CCDS5468.1; -.
DR RefSeq; NP_114109.1; NM_031903.2.
DR PDB; 3J7Y; EM; 3.40 A; 0=1-188.
DR PDB; 3J9M; EM; 3.50 A; 0=1-188.
DR PDB; 5OOL; EM; 3.06 A; 0=1-188.
DR PDB; 5OOM; EM; 3.03 A; 0=1-188.
DR PDB; 6I9R; EM; 3.90 A; 0=1-188.
DR PDB; 6NU2; EM; 3.90 A; 0=79-186.
DR PDB; 6NU3; EM; 4.40 A; 0=1-188.
DR PDB; 6VLZ; EM; 2.97 A; 0=1-188.
DR PDB; 6VMI; EM; 2.96 A; 0=1-188.
DR PDB; 6ZM5; EM; 2.89 A; 0=1-188.
DR PDB; 6ZM6; EM; 2.59 A; 0=1-188.
DR PDB; 6ZS9; EM; 4.00 A; 0=1-188.
DR PDB; 6ZSA; EM; 4.00 A; 0=1-188.
DR PDB; 6ZSB; EM; 4.50 A; 0=1-188.
DR PDB; 6ZSC; EM; 3.50 A; 0=1-188.
DR PDB; 6ZSD; EM; 3.70 A; 0=1-188.
DR PDB; 6ZSE; EM; 5.00 A; 0=1-188.
DR PDB; 6ZSG; EM; 4.00 A; 0=1-188.
DR PDB; 7A5F; EM; 4.40 A; 03=1-188.
DR PDB; 7A5G; EM; 4.33 A; 03=1-188.
DR PDB; 7A5H; EM; 3.30 A; 0=1-188.
DR PDB; 7A5I; EM; 3.70 A; 03=1-188.
DR PDB; 7A5J; EM; 3.10 A; 0=1-188.
DR PDB; 7A5K; EM; 3.70 A; 03=1-188.
DR PDB; 7L08; EM; 3.49 A; 0=1-188.
DR PDB; 7L20; EM; 3.15 A; 0=1-188.
DR PDB; 7O9K; EM; 3.10 A; 0=1-188.
DR PDB; 7O9M; EM; 2.50 A; 0=1-188.
DR PDB; 7ODR; EM; 2.90 A; 0=1-188.
DR PDB; 7ODS; EM; 3.10 A; 0=1-188.
DR PDB; 7ODT; EM; 3.10 A; 0=1-188.
DR PDB; 7OF0; EM; 2.20 A; 0=1-188.
DR PDB; 7OF2; EM; 2.70 A; 0=1-188.
DR PDB; 7OF3; EM; 2.70 A; 0=1-188.
DR PDB; 7OF4; EM; 2.70 A; 0=1-188.
DR PDB; 7OF5; EM; 2.90 A; 0=1-188.
DR PDB; 7OF6; EM; 2.60 A; 0=1-188.
DR PDB; 7OF7; EM; 2.50 A; 0=79-186.
DR PDB; 7OG4; EM; 3.80 A; 0=1-188.
DR PDB; 7OI6; EM; 5.70 A; 0=1-188.
DR PDB; 7OI7; EM; 3.50 A; 0=1-188.
DR PDB; 7OI8; EM; 3.50 A; 0=1-188.
DR PDB; 7OI9; EM; 3.30 A; 0=1-188.
DR PDB; 7OIA; EM; 3.20 A; 0=1-188.
DR PDB; 7OIB; EM; 3.30 A; 0=1-188.
DR PDB; 7OIC; EM; 3.10 A; 0=1-188.
DR PDB; 7OID; EM; 3.70 A; 0=1-188.
DR PDB; 7OIE; EM; 3.50 A; 0=1-188.
DR PDB; 7PD3; EM; 3.40 A; 0=1-188.
DR PDB; 7QH6; EM; 3.08 A; 0=1-188.
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; Q9BYC8; -.
DR SMR; Q9BYC8; -.
DR BioGRID; 122368; 131.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q9BYC8; -.
DR IntAct; Q9BYC8; 32.
DR MINT; Q9BYC8; -.
DR STRING; 9606.ENSP00000223324; -.
DR iPTMnet; Q9BYC8; -.
DR PhosphoSitePlus; Q9BYC8; -.
DR BioMuta; MRPL32; -.
DR DMDM; 22001923; -.
DR EPD; Q9BYC8; -.
DR jPOST; Q9BYC8; -.
DR MassIVE; Q9BYC8; -.
DR MaxQB; Q9BYC8; -.
DR PaxDb; Q9BYC8; -.
DR PeptideAtlas; Q9BYC8; -.
DR PRIDE; Q9BYC8; -.
DR ProteomicsDB; 79613; -.
DR Antibodypedia; 57638; 92 antibodies from 19 providers.
DR DNASU; 64983; -.
DR Ensembl; ENST00000223324.3; ENSP00000223324.2; ENSG00000106591.4.
DR GeneID; 64983; -.
DR KEGG; hsa:64983; -.
DR MANE-Select; ENST00000223324.3; ENSP00000223324.2; NM_031903.3; NP_114109.1.
DR UCSC; uc003tia.4; human.
DR CTD; 64983; -.
DR GeneCards; MRPL32; -.
DR HGNC; HGNC:14035; MRPL32.
DR HPA; ENSG00000106591; Low tissue specificity.
DR MIM; 611839; gene.
DR neXtProt; NX_Q9BYC8; -.
DR OpenTargets; ENSG00000106591; -.
DR PharmGKB; PA30963; -.
DR VEuPathDB; HostDB:ENSG00000106591; -.
DR eggNOG; KOG4080; Eukaryota.
DR GeneTree; ENSGT00390000014996; -.
DR HOGENOM; CLU_116455_1_0_1; -.
DR InParanoid; Q9BYC8; -.
DR OMA; HCYDKVR; -.
DR OrthoDB; 1600646at2759; -.
DR PhylomeDB; Q9BYC8; -.
DR TreeFam; TF106139; -.
DR PathwayCommons; Q9BYC8; -.
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; Q9BYC8; -.
DR SIGNOR; Q9BYC8; -.
DR BioGRID-ORCS; 64983; 315 hits in 1078 CRISPR screens.
DR ChiTaRS; MRPL32; human.
DR GeneWiki; MRPL32; -.
DR GenomeRNAi; 64983; -.
DR Pharos; Q9BYC8; Tdark.
DR PRO; PR:Q9BYC8; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9BYC8; protein.
DR Bgee; ENSG00000106591; Expressed in oocyte and 189 other tissues.
DR ExpressionAtlas; Q9BYC8; baseline and differential.
DR Genevisible; Q9BYC8; 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:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR InterPro; IPR002677; Ribosomal_L32p.
DR InterPro; IPR011332; Ribosomal_zn-bd.
DR Pfam; PF01783; Ribosomal_L32p; 1.
DR SUPFAM; SSF57829; SSF57829; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..188
FT /note="39S ribosomal protein L32, mitochondrial"
FT /id="PRO_0000030513"
FT REGION 164..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 11..43
FT /note="SPWSAARGVLRNYWERLLRKLPQSRPGFPSPPW -> RRGLRPGECFETTGS
FT DCYGSFRRAGRAFPVLRGV (in Ref. 3)"
FT /evidence="ECO:0000305"
FT HELIX 87..94
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 124..145
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:7OF0"
SQ SEQUENCE 188 AA; 21405 MW; 60164AD910AE3EFD CRC64;
MALAMLVLVV SPWSAARGVL RNYWERLLRK LPQSRPGFPS PPWGPALAVQ GPAMFTEPAN
DTSGSKENSS LLDSIFWMAA PKNRRTIEVN RCRRRNPQKL IKVKNNIDVC PECGHLKQKH
VLCAYCYEKV CKETAEIRRQ IGKQEGGPFK APTIETVVLY TGETPSEQDQ GKRIIERDRK
RPSWFTQN
