RM23_HUMAN
ID RM23_HUMAN Reviewed; 153 AA.
AC Q16540; A8MT29; Q96Q71;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=39S ribosomal protein L23, mitochondrial;
DE Short=L23mt;
DE Short=MRP-L23;
DE AltName: Full=L23 mitochondrial-related protein;
DE AltName: Full=Mitochondrial large ribosomal subunit protein uL23m {ECO:0000303|PubMed:25278503};
DE AltName: Full=Ribosomal protein L23-like;
GN Name=MRPL23; Synonyms=L23MRP, RPL23L;
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=8541832; DOI=10.1093/hmg/4.9.1499;
RA Tsang P., Gilles F., Yuan L., Kuo Y., Lupu F., Samara G., Moosikasuwan J.,
RA Goy A., Zelenetz A.D., Selleri L., Tycko B.;
RT "A novel L23-related gene 40 kb downstream of the imprinted H19 gene is
RT biallelically expressed in mid-fetal and adult human tissues.";
RL Hum. Mol. Genet. 4:1499-1507(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 100-130, AND VARIANT THR-122.
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 [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 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 [8] {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 [9] {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 [10] {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 -!- INTERACTION:
CC Q16540; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-1046141, EBI-3867333;
CC Q16540; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-1046141, EBI-11959885;
CC Q16540; Q9BYR6: KRTAP3-3; NbExp=3; IntAct=EBI-1046141, EBI-3957694;
CC Q16540; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-1046141, EBI-302345;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25278503,
CC ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL23 family.
CC {ECO:0000305}.
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DR EMBL; Z49254; CAA89220.1; -; mRNA.
DR EMBL; U26596; AAC50415.1; -; mRNA.
DR EMBL; AC051649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471158; EAX02472.1; -; Genomic_DNA.
DR EMBL; BC027710; AAH27710.1; -; mRNA.
DR EMBL; AB051340; BAB54930.2; -; Genomic_DNA.
DR CCDS; CCDS31336.1; -.
DR RefSeq; NP_066957.3; NM_021134.3.
DR PDB; 3J7Y; EM; 3.40 A; U=1-153.
DR PDB; 3J9M; EM; 3.50 A; U=1-153.
DR PDB; 5OOL; EM; 3.06 A; U=1-153.
DR PDB; 5OOM; EM; 3.03 A; U=1-153.
DR PDB; 6I9R; EM; 3.90 A; U=1-153.
DR PDB; 6NU2; EM; 3.90 A; U=2-112.
DR PDB; 6NU3; EM; 4.40 A; U=1-153.
DR PDB; 6VLZ; EM; 2.97 A; U=1-153.
DR PDB; 6VMI; EM; 2.96 A; U=1-153.
DR PDB; 6ZM5; EM; 2.89 A; U=2-153.
DR PDB; 6ZM6; EM; 2.59 A; U=2-153.
DR PDB; 6ZS9; EM; 4.00 A; XU=1-153.
DR PDB; 6ZSA; EM; 4.00 A; XU=1-153.
DR PDB; 6ZSB; EM; 4.50 A; XU=1-153.
DR PDB; 6ZSC; EM; 3.50 A; XU=1-153.
DR PDB; 6ZSD; EM; 3.70 A; XU=1-153.
DR PDB; 6ZSE; EM; 5.00 A; XU=1-153.
DR PDB; 6ZSG; EM; 4.00 A; XU=1-153.
DR PDB; 7A5F; EM; 4.40 A; U3=1-153.
DR PDB; 7A5G; EM; 4.33 A; U3=1-153.
DR PDB; 7A5H; EM; 3.30 A; U=1-153.
DR PDB; 7A5I; EM; 3.70 A; U3=1-153.
DR PDB; 7A5J; EM; 3.10 A; U=1-153.
DR PDB; 7A5K; EM; 3.70 A; U3=1-153.
DR PDB; 7L08; EM; 3.49 A; U=1-153.
DR PDB; 7L20; EM; 3.15 A; U=1-153.
DR PDB; 7O9K; EM; 3.10 A; U=1-153.
DR PDB; 7O9M; EM; 2.50 A; U=1-153.
DR PDB; 7ODR; EM; 2.90 A; U=1-153.
DR PDB; 7ODS; EM; 3.10 A; U=1-153.
DR PDB; 7ODT; EM; 3.10 A; U=1-153.
DR PDB; 7OF0; EM; 2.20 A; U=1-153.
DR PDB; 7OF2; EM; 2.70 A; U=1-153.
DR PDB; 7OF3; EM; 2.70 A; U=1-153.
DR PDB; 7OF4; EM; 2.70 A; U=1-153.
DR PDB; 7OF5; EM; 2.90 A; U=1-153.
DR PDB; 7OF6; EM; 2.60 A; U=1-153.
DR PDB; 7OF7; EM; 2.50 A; U=1-153.
DR PDB; 7OG4; EM; 3.80 A; XU=1-153.
DR PDB; 7OI6; EM; 5.70 A; U=1-153.
DR PDB; 7OI7; EM; 3.50 A; U=1-153.
DR PDB; 7OI8; EM; 3.50 A; U=1-153.
DR PDB; 7OI9; EM; 3.30 A; U=1-153.
DR PDB; 7OIA; EM; 3.20 A; U=1-153.
DR PDB; 7OIB; EM; 3.30 A; U=1-153.
DR PDB; 7OIC; EM; 3.10 A; U=1-153.
DR PDB; 7OID; EM; 3.70 A; U=1-153.
DR PDB; 7OIE; EM; 3.50 A; U=1-153.
DR PDB; 7PD3; EM; 3.40 A; U=1-153.
DR PDB; 7QH6; EM; 3.08 A; U=1-153.
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; Q16540; -.
DR SMR; Q16540; -.
DR BioGRID; 112070; 208.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q16540; -.
DR IntAct; Q16540; 45.
DR MINT; Q16540; -.
DR STRING; 9606.ENSP00000380466; -.
DR GlyGen; Q16540; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q16540; -.
DR PhosphoSitePlus; Q16540; -.
DR BioMuta; MRPL23; -.
DR DMDM; 68566020; -.
DR EPD; Q16540; -.
DR jPOST; Q16540; -.
DR MassIVE; Q16540; -.
DR MaxQB; Q16540; -.
DR PaxDb; Q16540; -.
DR PeptideAtlas; Q16540; -.
DR PRIDE; Q16540; -.
DR ProteomicsDB; 60905; -.
DR TopDownProteomics; Q16540; -.
DR Antibodypedia; 42084; 53 antibodies from 21 providers.
DR DNASU; 6150; -.
DR Ensembl; ENST00000381519.5; ENSP00000370930.1; ENSG00000214026.11.
DR Ensembl; ENST00000397298.8; ENSP00000380466.3; ENSG00000214026.11.
DR Ensembl; ENST00000672185.1; ENSP00000500123.1; ENSG00000288141.1.
DR Ensembl; ENST00000672523.1; ENSP00000500896.1; ENSG00000288141.1.
DR GeneID; 6150; -.
DR KEGG; hsa:6150; -.
DR MANE-Select; ENST00000397298.8; ENSP00000380466.3; NM_021134.4; NP_066957.3.
DR UCSC; uc001lux.4; human.
DR CTD; 6150; -.
DR DisGeNET; 6150; -.
DR GeneCards; MRPL23; -.
DR HGNC; HGNC:10322; MRPL23.
DR HPA; ENSG00000214026; Low tissue specificity.
DR MalaCards; MRPL23; -.
DR MIM; 600789; gene.
DR neXtProt; NX_Q16540; -.
DR OpenTargets; ENSG00000214026; -.
DR PharmGKB; PA30953; -.
DR VEuPathDB; HostDB:ENSG00000214026; -.
DR eggNOG; KOG4089; Eukaryota.
DR GeneTree; ENSGT00390000007739; -.
DR HOGENOM; CLU_103097_1_0_1; -.
DR InParanoid; Q16540; -.
DR OMA; PGTPGWF; -.
DR OrthoDB; 1495685at2759; -.
DR PhylomeDB; Q16540; -.
DR TreeFam; TF105852; -.
DR PathwayCommons; Q16540; -.
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; Q16540; -.
DR SIGNOR; Q16540; -.
DR BioGRID-ORCS; 6150; 345 hits in 1086 CRISPR screens.
DR ChiTaRS; MRPL23; human.
DR GeneWiki; MRPL23; -.
DR GenomeRNAi; 6150; -.
DR Pharos; Q16540; Tdark.
DR PRO; PR:Q16540; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q16540; protein.
DR Bgee; ENSG00000214026; Expressed in olfactory segment of nasal mucosa and 92 other tissues.
DR ExpressionAtlas; Q16540; baseline and differential.
DR Genevisible; Q16540; HS.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
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:UniProtKB.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom_sf.
DR InterPro; IPR013025; Ribosomal_L25/23.
DR PANTHER; PTHR12059; PTHR12059; 1.
DR Pfam; PF00276; Ribosomal_L23; 1.
DR SUPFAM; SSF54189; SSF54189; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT CHAIN 1..153
FT /note="39S ribosomal protein L23, mitochondrial"
FT /id="PRO_0000129484"
FT REGION 108..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 11
FT /note="R -> Q (in dbSNP:rs34134444)"
FT /id="VAR_057197"
FT VARIANT 32
FT /note="G -> S (in dbSNP:rs2240197)"
FT /id="VAR_057198"
FT VARIANT 34
FT /note="A -> V (in dbSNP:rs6512)"
FT /id="VAR_057199"
FT VARIANT 81
FT /note="D -> N (in dbSNP:rs4930142)"
FT /id="VAR_057200"
FT VARIANT 122
FT /note="A -> T (in dbSNP:rs12812)"
FT /evidence="ECO:0000269|PubMed:11543634"
FT /id="VAR_057201"
FT STRAND 18..21
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 50..60
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 65..73
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:5OOM"
FT STRAND 92..100
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 127..135
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:7OF0"
SQ SEQUENCE 153 AA; 17781 MW; 7277C03CA224ED50 CRC64;
MARNVVYPLY RLGGPQLRVF RTNFFIQLVR PGVAQPEDTV QFRIPMEMTR VDLRNYLEGI
YNVPVAAVRT RVQHGSNKRR DHRNVRIKKP DYKVAYVQLA HGQTFTFPDL FPEKDESPEG
SAADDLYSML EEERQQRQSS DPRRGGVPSW FGL
