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RM43_HUMAN
ID   RM43_HUMAN              Reviewed;         215 AA.
AC   Q8N983; B1AL06; B1AL07; B1AL09; B1AL10; C9J5Q3; D3DR71; Q5JW06; Q7Z719;
AC   Q7Z7H6; Q86XN1; Q9BYC7;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 163.
DE   RecName: Full=39S ribosomal protein L43, mitochondrial;
DE            Short=L43mt;
DE            Short=MRP-L43;
DE   AltName: Full=Mitochondrial large ribosomal subunit protein mL43 {ECO:0000303|PubMed:25278503};
DE   AltName: Full=Mitochondrial ribosomal protein bMRP36a;
DE   Flags: Precursor;
GN   Name=MRPL43;
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] (ISOFORM 4).
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] (ISOFORMS 1 AND 6).
RC   TISSUE=Brain;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC   TISSUE=Ovary, Pancreas, Skin, and 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   [6]
RP   TISSUE SPECIFICITY, AND COREGULATION WITH TWNK.
RX   PubMed=15509589; DOI=10.1093/hmg/ddh342;
RA   Tyynismaa H., Sembongi H., Bokori-Brown M., Granycome C., Ashley N.,
RA   Poulton J., Jalanko A., Spelbrink J.N., Holt I.J., Suomalainen A.;
RT   "Twinkle helicase is essential for mtDNA maintenance and regulates mtDNA
RT   copy number.";
RL   Hum. Mol. Genet. 13:3219-3227(2004).
RN   [7]
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   [8]
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   [9] {ECO:0007744|PDB:3J7Y}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS) OF 1-155, SUBCELLULAR
RP   LOCATION, 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   [10] {ECO:0007744|PDB:3J9M}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) OF 1-155, SUBCELLULAR
RP   LOCATION, 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   [11] {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       Q8N983; P51116: FXR2; NbExp=3; IntAct=EBI-1043145, EBI-740459;
CC       Q8N983-3; Q92993: KAT5; NbExp=3; IntAct=EBI-11109389, EBI-399080;
CC       Q8N983-3; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-11109389, EBI-11742507;
CC       Q8N983-3; P17252: PRKCA; NbExp=3; IntAct=EBI-11109389, EBI-1383528;
CC       Q8N983-3; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-11109389, EBI-9090795;
CC       Q8N983-3; P61981: YWHAG; NbExp=3; IntAct=EBI-11109389, EBI-359832;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25278503,
CC       ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=Q8N983-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8N983-2; Sequence=VSP_011026;
CC       Name=3;
CC         IsoId=Q8N983-3; Sequence=VSP_011027, VSP_011028;
CC       Name=4;
CC         IsoId=Q8N983-4; Sequence=VSP_011029, VSP_011030;
CC       Name=5;
CC         IsoId=Q8N983-6; Sequence=VSP_054092;
CC       Name=6;
CC         IsoId=Q8N983-7; Sequence=VSP_054093;
CC   -!- TISSUE SPECIFICITY: High relative levels in skeletal muscle and testis.
CC       Lower levels of expression in the heart, brain, placenta, lung, liver,
CC       kidney, pancreas, spleen, thymus, prostate, ovary, small intestine,
CC       colon and leukocytes. Expression is coregulated with TWNK.
CC       {ECO:0000269|PubMed:15509589}.
CC   -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC       mL43 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB40861.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AB049656; BAB40861.1; ALT_FRAME; mRNA.
DR   EMBL; AK095556; BAC04572.1; -; mRNA.
DR   EMBL; AK300237; BAG62005.1; -; mRNA.
DR   EMBL; AL133215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471066; EAW49795.1; -; Genomic_DNA.
DR   EMBL; CH471066; EAW49796.1; -; Genomic_DNA.
DR   EMBL; CH471066; EAW49797.1; -; Genomic_DNA.
DR   EMBL; CH471066; EAW49799.1; -; Genomic_DNA.
DR   EMBL; BC015905; AAH15905.1; -; mRNA.
DR   EMBL; BC041165; AAH41165.1; -; mRNA.
DR   EMBL; BC052639; AAH52639.1; -; mRNA.
DR   EMBL; BC053373; AAH53373.1; -; mRNA.
DR   CCDS; CCDS7502.1; -. [Q8N983-1]
DR   CCDS; CCDS7503.1; -. [Q8N983-2]
DR   CCDS; CCDS7504.1; -. [Q8N983-6]
DR   CCDS; CCDS7505.1; -. [Q8N983-4]
DR   CCDS; CCDS76331.1; -. [Q8N983-3]
DR   RefSeq; NP_001295325.1; NM_001308396.1. [Q8N983-3]
DR   RefSeq; NP_115488.2; NM_032112.2. [Q8N983-4]
DR   RefSeq; NP_789762.1; NM_176792.2. [Q8N983-1]
DR   RefSeq; NP_789763.1; NM_176793.1. [Q8N983-2]
DR   RefSeq; NP_789764.1; NM_176794.1. [Q8N983-6]
DR   RefSeq; XP_005270288.1; XM_005270231.2. [Q8N983-4]
DR   RefSeq; XP_006718098.1; XM_006718035.3. [Q8N983-4]
DR   PDB; 3J7Y; EM; 3.40 A; b=1-155.
DR   PDB; 3J9M; EM; 3.50 A; b=1-155.
DR   PDB; 5OOL; EM; 3.06 A; b=1-215.
DR   PDB; 5OOM; EM; 3.03 A; b=1-215.
DR   PDB; 6I9R; EM; 3.90 A; b=1-215.
DR   PDB; 6NU2; EM; 3.90 A; b=2-149.
DR   PDB; 6NU3; EM; 4.40 A; b=1-215.
DR   PDB; 6VLZ; EM; 2.97 A; b=1-155.
DR   PDB; 6VMI; EM; 2.96 A; b=1-155.
DR   PDB; 6ZM5; EM; 2.89 A; b=2-215.
DR   PDB; 6ZM6; EM; 2.59 A; b=2-215.
DR   PDB; 6ZS9; EM; 4.00 A; b=1-215.
DR   PDB; 6ZSA; EM; 4.00 A; b=1-215.
DR   PDB; 6ZSB; EM; 4.50 A; b=1-215.
DR   PDB; 6ZSC; EM; 3.50 A; b=1-215.
DR   PDB; 6ZSD; EM; 3.70 A; b=1-215.
DR   PDB; 6ZSE; EM; 5.00 A; b=1-215.
DR   PDB; 6ZSG; EM; 4.00 A; b=1-215.
DR   PDB; 7A5F; EM; 4.40 A; b3=1-215.
DR   PDB; 7A5G; EM; 4.33 A; b3=1-215.
DR   PDB; 7A5H; EM; 3.30 A; b=1-155.
DR   PDB; 7A5I; EM; 3.70 A; b3=1-155.
DR   PDB; 7A5J; EM; 3.10 A; b=1-155.
DR   PDB; 7A5K; EM; 3.70 A; b3=1-155.
DR   PDB; 7L08; EM; 3.49 A; b=1-155.
DR   PDB; 7L20; EM; 3.15 A; b=1-155.
DR   PDB; 7O9K; EM; 3.10 A; b=1-215.
DR   PDB; 7O9M; EM; 2.50 A; b=1-215.
DR   PDB; 7ODR; EM; 2.90 A; b=1-215.
DR   PDB; 7ODS; EM; 3.10 A; b=1-215.
DR   PDB; 7ODT; EM; 3.10 A; b=1-215.
DR   PDB; 7OF0; EM; 2.20 A; b=1-215.
DR   PDB; 7OF2; EM; 2.70 A; b=1-215.
DR   PDB; 7OF3; EM; 2.70 A; b=1-215.
DR   PDB; 7OF4; EM; 2.70 A; b=1-215.
DR   PDB; 7OF5; EM; 2.90 A; b=1-215.
DR   PDB; 7OF6; EM; 2.60 A; b=1-215.
DR   PDB; 7OF7; EM; 2.50 A; b=1-215.
DR   PDB; 7OG4; EM; 3.80 A; b=1-215.
DR   PDB; 7OI6; EM; 5.70 A; b=1-215.
DR   PDB; 7OI7; EM; 3.50 A; b=1-215.
DR   PDB; 7OI8; EM; 3.50 A; b=1-215.
DR   PDB; 7OI9; EM; 3.30 A; b=1-215.
DR   PDB; 7OIA; EM; 3.20 A; b=1-215.
DR   PDB; 7OIB; EM; 3.30 A; b=1-215.
DR   PDB; 7OIC; EM; 3.10 A; b=1-215.
DR   PDB; 7OID; EM; 3.70 A; b=1-215.
DR   PDB; 7OIE; EM; 3.50 A; b=1-215.
DR   PDB; 7PD3; EM; 3.40 A; b=1-215.
DR   PDB; 7QH6; EM; 3.08 A; b=1-215.
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; Q8N983; -.
DR   SMR; Q8N983; -.
DR   BioGRID; 124130; 187.
DR   ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR   CORUM; Q8N983; -.
DR   IntAct; Q8N983; 53.
DR   MINT; Q8N983; -.
DR   STRING; 9606.ENSP00000339844; -.
DR   GlyGen; Q8N983; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8N983; -.
DR   PhosphoSitePlus; Q8N983; -.
DR   BioMuta; MRPL43; -.
DR   DMDM; 50401603; -.
DR   EPD; Q8N983; -.
DR   jPOST; Q8N983; -.
DR   MassIVE; Q8N983; -.
DR   MaxQB; Q8N983; -.
DR   PaxDb; Q8N983; -.
DR   PeptideAtlas; Q8N983; -.
DR   PRIDE; Q8N983; -.
DR   ProteomicsDB; 3124; -.
DR   ProteomicsDB; 72499; -. [Q8N983-1]
DR   ProteomicsDB; 72500; -. [Q8N983-2]
DR   ProteomicsDB; 72501; -. [Q8N983-3]
DR   ProteomicsDB; 72502; -. [Q8N983-4]
DR   ProteomicsDB; 8648; -.
DR   TopDownProteomics; Q8N983-4; -. [Q8N983-4]
DR   Antibodypedia; 31225; 49 antibodies from 16 providers.
DR   DNASU; 84545; -.
DR   Ensembl; ENST00000299179.9; ENSP00000299179.5; ENSG00000055950.17. [Q8N983-2]
DR   Ensembl; ENST00000318325.6; ENSP00000315364.2; ENSG00000055950.17. [Q8N983-1]
DR   Ensembl; ENST00000318364.13; ENSP00000315948.8; ENSG00000055950.17. [Q8N983-4]
DR   Ensembl; ENST00000342071.5; ENSP00000339844.1; ENSG00000055950.17. [Q8N983-6]
DR   Ensembl; ENST00000370234.4; ENSP00000359254.4; ENSG00000055950.17. [Q8N983-3]
DR   Ensembl; ENST00000370236.5; ENSP00000359256.1; ENSG00000055950.17. [Q8N983-4]
DR   Ensembl; ENST00000370242.8; ENSP00000359262.4; ENSG00000055950.17. [Q8N983-7]
DR   GeneID; 84545; -.
DR   KEGG; hsa:84545; -.
DR   MANE-Select; ENST00000318364.13; ENSP00000315948.8; NM_032112.3; NP_115488.2. [Q8N983-4]
DR   UCSC; uc001kry.2; human. [Q8N983-1]
DR   CTD; 84545; -.
DR   DisGeNET; 84545; -.
DR   GeneCards; MRPL43; -.
DR   HGNC; HGNC:14517; MRPL43.
DR   HPA; ENSG00000055950; Low tissue specificity.
DR   MIM; 611848; gene.
DR   neXtProt; NX_Q8N983; -.
DR   OpenTargets; ENSG00000055950; -.
DR   PharmGKB; PA30975; -.
DR   VEuPathDB; HostDB:ENSG00000055950; -.
DR   eggNOG; KOG3445; Eukaryota.
DR   GeneTree; ENSGT00390000015375; -.
DR   HOGENOM; CLU_094620_0_0_1; -.
DR   InParanoid; Q8N983; -.
DR   OMA; ISKWIDL; -.
DR   OrthoDB; 1620056at2759; -.
DR   PhylomeDB; Q8N983; -.
DR   TreeFam; TF314535; -.
DR   PathwayCommons; Q8N983; -.
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; Q8N983; -.
DR   SIGNOR; Q8N983; -.
DR   BioGRID-ORCS; 84545; 537 hits in 1092 CRISPR screens.
DR   ChiTaRS; MRPL43; human.
DR   GenomeRNAi; 84545; -.
DR   Pharos; Q8N983; Tdark.
DR   PRO; PR:Q8N983; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q8N983; protein.
DR   Bgee; ENSG00000055950; Expressed in pancreatic ductal cell and 185 other tissues.
DR   ExpressionAtlas; Q8N983; baseline and differential.
DR   Genevisible; Q8N983; 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; IPR039927; MRPL43/MRPL51.
DR   InterPro; IPR007741; Ribosome/NADH_DH.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR21396; PTHR21396; 1.
DR   Pfam; PF05047; L51_S25_CI-B8; 1.
DR   SMART; SM00916; L51_S25_CI-B8; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Mitochondrion; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..215
FT                   /note="39S ribosomal protein L43, mitochondrial"
FT                   /id="PRO_0000030561"
FT   VAR_SEQ         156..164
FT                   /note="DTGLRLSAV -> CLLLGAVTL (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_011027"
FT   VAR_SEQ         156..159
FT                   /note="DTGL -> VQAQ (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:11279069,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_011029"
FT   VAR_SEQ         157..215
FT                   /note="TGLRLSAVAPQILLPGWPDPPDLPTVDPISSSLTSAPAPMLSAVSCLPIVPA
FT                   LTTVCSA -> AAEFLGEGAGPCWYSIVALPQKHIAIAIHPPQPAGQCHQAIGHWPETV
FT                   CSCTADPPARLARPNISSVIRSSLGKYPLPS (in isoform 5)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_054092"
FT   VAR_SEQ         157..215
FT                   /note="TGLRLSAVAPQILLPGWPDPPDLPTVDPISSSLTSAPAPMLSAVSCLPIVPA
FT                   LTTVCSA -> AAEFLGEGAGPCWYSIVALPQKHIAIAIHPPQPAGQCHQAIGHWPETV
FT                   CSCTADPPARLARPTRPPHSGSYLILIDLCSSPYAVRSFLPPDCPCTDHCVLSVKAA
FT                   (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054093"
FT   VAR_SEQ         160..215
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:11279069,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_011030"
FT   VAR_SEQ         165..215
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_011028"
FT   VAR_SEQ         177..215
FT                   /note="PDLPTVDPISSSLTSAPAPMLSAVSCLPIVPALTTVCSA -> ISVQSSDLP
FT                   WGNTHYRPEPLSSTTWL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_011026"
FT   TURN            3..5
FT                   /evidence="ECO:0007829|PDB:5OOM"
FT   STRAND          14..16
FT                   /evidence="ECO:0007829|PDB:7OIE"
FT   TURN            17..19
FT                   /evidence="ECO:0007829|PDB:5OOM"
FT   STRAND          25..32
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   HELIX           38..40
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   HELIX           41..49
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   HELIX           51..57
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          61..65
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          70..72
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          74..79
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          84..88
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   HELIX           94..106
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          113..116
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          118..120
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   TURN            132..135
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   HELIX           140..142
FT                   /evidence="ECO:0007829|PDB:7OF0"
SQ   SEQUENCE   215 AA;  23431 MW;  059C6E36FEB0D235 CRC64;
     MTARGTPSRF LASVLHNGLG RYVQQLQRLS FSVSRDGASS RGAREFVERE VIDFARRNPG
     VVIYVNSRPC CVPRVVAEYL NGAVREESIH CKSVEEISTL VQKLADQSGL DVIRIRKPFH
     TDNPSIQGQW HPFTNKPTTF RGLRPREVQD PAPAQDTGLR LSAVAPQILL PGWPDPPDLP
     TVDPISSSLT SAPAPMLSAV SCLPIVPALT TVCSA
 
 
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