GTPB3_HUMAN
ID GTPB3_HUMAN Reviewed; 492 AA.
AC Q969Y2; A6NFH1; A6NIG5; A6NKR4; A8K7B4; B7Z4V8; Q8TCY6; Q8WUW9; Q969G4;
AC Q9BX61;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=tRNA modification GTPase GTPBP3, mitochondrial;
DE AltName: Full=GTP-binding protein 3;
DE AltName: Full=Mitochondrial GTP-binding protein 1;
DE Flags: Precursor;
GN Name=GTPBP3; Synonyms=MTGP1;
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 [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3), PROBABLE
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, POSSIBLE INVOLVEMENT IN
RP AID, AND VARIANT ALA-250.
RX PubMed=12370316; DOI=10.1128/mcb.22.21.7701-7711.2002;
RA Li X., Guan M.-X.;
RT "A human mitochondrial GTP binding protein related to tRNA modification may
RT modulate phenotypic expression of the deafness-associated mitochondrial 12S
RT rRNA mutation.";
RL Mol. Cell. Biol. 22:7701-7711(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT
RP ALA-250.
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], AND VARIANT ALA-250.
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ALA-250 AND HIS-368.
RC TISSUE=Brain, and 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 [6]
RP INVOLVEMENT IN AID, AND VARIANT ALA-250.
RX PubMed=15542390; DOI=10.1016/j.ymgme.2004.07.009;
RA Bykhovskaya Y., Mengesha E., Wang D., Yang H., Estivill X., Shohat M.,
RA Fischel-Ghodsian N.;
RT "Phenotype of non-syndromic deafness associated with the mitochondrial
RT A1555G mutation is modulated by mitochondrial RNA modifying enzymes MTO1
RT and GTPBP3.";
RL Mol. Genet. Metab. 83:199-206(2004).
RN [7]
RP INVOLVEMENT IN COXPD23, VARIANTS COXPD23 LEU-3; LYS-142; VAL-159; PRO-162;
RP GLY-222; HIS-257; GLY-312--VAL-319 DEL; HIS-337 AND LYS-459, AND VARIANTS
RP LYS-225 AND PRO-322.
RX PubMed=25434004; DOI=10.1016/j.ajhg.2014.10.017;
RA Kopajtich R., Nicholls T.J., Rorbach J., Metodiev M.D., Freisinger P.,
RA Mandel H., Vanlander A., Ghezzi D., Carrozzo R., Taylor R.W., Marquard K.,
RA Murayama K., Wieland T., Schwarzmayr T., Mayr J.A., Pearce S.F.,
RA Powell C.A., Saada A., Ohtake A., Invernizzi F., Lamantea E.,
RA Sommerville E.W., Pyle A., Chinnery P.F., Crushell E., Okazaki Y.,
RA Kohda M., Kishita Y., Tokuzawa Y., Assouline Z., Rio M., Feillet F.,
RA Mousson de Camaret B., Chretien D., Munnich A., Menten B., Sante T.,
RA Smet J., Regal L., Lorber A., Khoury A., Zeviani M., Strom T.M.,
RA Meitinger T., Bertini E.S., Van Coster R., Klopstock T., Rotig A.,
RA Haack T.B., Minczuk M., Prokisch H.;
RT "Mutations in GTPBP3 cause a mitochondrial translation defect associated
RT with hypertrophic cardiomyopathy, lactic acidosis, and encephalopathy.";
RL Am. J. Hum. Genet. 95:708-720(2014).
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]
RP VARIANT COXPD23 LEU-3.
RX PubMed=26741492; DOI=10.1371/journal.pgen.1005679;
RA Kohda M., Tokuzawa Y., Kishita Y., Nyuzuki H., Moriyama Y., Mizuno Y.,
RA Hirata T., Yatsuka Y., Yamashita-Sugahara Y., Nakachi Y., Kato H.,
RA Okuda A., Tamaru S., Borna N.N., Banshoya K., Aigaki T., Sato-Miyata Y.,
RA Ohnuma K., Suzuki T., Nagao A., Maehata H., Matsuda F., Higasa K.,
RA Nagasaki M., Yasuda J., Yamamoto M., Fushimi T., Shimura M.,
RA Kaiho-Ichimoto K., Harashima H., Yamazaki T., Mori M., Murayama K.,
RA Ohtake A., Okazaki Y.;
RT "A comprehensive genomic analysis reveals the genetic landscape of
RT mitochondrial respiratory chain complex deficiencies.";
RL PLoS Genet. 12:E1005679-E1005679(2016).
CC -!- FUNCTION: GTPase involved in the 5-carboxymethylaminomethyl
CC modification (mnm(5)s(2)U34) of the wobble uridine base in
CC mitochondrial tRNAs. {ECO:0000305}.
CC -!- INTERACTION:
CC Q969Y2; O95994: AGR2; NbExp=3; IntAct=EBI-740290, EBI-712648;
CC Q969Y2; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-740290, EBI-10181188;
CC Q969Y2; P20807-4: CAPN3; NbExp=3; IntAct=EBI-740290, EBI-11532021;
CC Q969Y2; Q9BV29: CCDC32; NbExp=3; IntAct=EBI-740290, EBI-2874058;
CC Q969Y2; Q92905: COPS5; NbExp=3; IntAct=EBI-740290, EBI-594661;
CC Q969Y2; Q96D03: DDIT4L; NbExp=5; IntAct=EBI-740290, EBI-742054;
CC Q969Y2; Q7L190: DPPA4; NbExp=3; IntAct=EBI-740290, EBI-710457;
CC Q969Y2; Q9Y223: GNE; NbExp=3; IntAct=EBI-740290, EBI-4291090;
CC Q969Y2; Q0VD86: INCA1; NbExp=3; IntAct=EBI-740290, EBI-6509505;
CC Q969Y2; Q13352: ITGB3BP; NbExp=3; IntAct=EBI-740290, EBI-712105;
CC Q969Y2; Q8WWY6: MBD3L1; NbExp=3; IntAct=EBI-740290, EBI-12516603;
CC Q969Y2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-740290, EBI-16439278;
CC Q969Y2; Q14696: MESD; NbExp=3; IntAct=EBI-740290, EBI-6165891;
CC Q969Y2; Q9NR21-1: PARP11; NbExp=7; IntAct=EBI-740290, EBI-17644640;
CC Q969Y2; P17858: PFKL; NbExp=3; IntAct=EBI-740290, EBI-487243;
CC Q969Y2; Q8WUT1: POLDIP3; NbExp=3; IntAct=EBI-740290, EBI-10276663;
CC Q969Y2; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-740290, EBI-2557469;
CC Q969Y2; Q53GL6: RALY; NbExp=5; IntAct=EBI-740290, EBI-9512693;
CC Q969Y2; Q15293: RCN1; NbExp=3; IntAct=EBI-740290, EBI-948278;
CC Q969Y2; Q9UJW9: SERTAD3; NbExp=3; IntAct=EBI-740290, EBI-748621;
CC Q969Y2; Q13148: TARDBP; NbExp=6; IntAct=EBI-740290, EBI-372899;
CC Q969Y2; Q6DHY5: TBC1D3G; NbExp=3; IntAct=EBI-740290, EBI-13092532;
CC Q969Y2; Q99081-3: TCF12; NbExp=3; IntAct=EBI-740290, EBI-11952764;
CC Q969Y2; Q8TF47: ZFP90; NbExp=3; IntAct=EBI-740290, EBI-11419867;
CC Q969Y2; Q9UC07-2: ZNF69; NbExp=3; IntAct=EBI-740290, EBI-12310821;
CC Q969Y2; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-740290, EBI-10251462;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12370316}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=V;
CC IsoId=Q969Y2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q969Y2-2; Sequence=VSP_023583;
CC Name=3; Synonyms=IV;
CC IsoId=Q969Y2-3; Sequence=VSP_023584;
CC Name=4;
CC IsoId=Q969Y2-4; Sequence=VSP_045050;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:12370316}.
CC -!- POLYMORPHISM: Val-250 variation may influence aminoglycoside-induced
CC deafness (AID) [MIM:580000]. AID is characterized by deafness, varying
CC from profond congenital hearing loss to normal hearing, and is caused
CC by homoplasmic A1555G mutation in the mitochondrial 12S rRNA. Val-250
CC may affect the accuracy of codon-anticodon interaction, leading to
CC modulate the translational efficiency and thereby affecting the
CC severity of deafness in patients homozygous for 12S rRNA A1555G
CC mutation.
CC -!- DISEASE: Combined oxidative phosphorylation deficiency 23 (COXPD23)
CC [MIM:616198]: An autosomal recessive mitochondrial disorder
CC characterized by hypertrophic cardiomyopathy and/or neurologic symptoms
CC with onset in early childhood. Disease features include hypertrophic
CC cardiomyopathy, hypotonia, delayed psychomotor development, lactic
CC acidosis, impaired activities of respiratory complexes I and IV, and
CC defective translation of mitochondrial proteins. Disease severity is
CC variable, ranging from death in early infancy to survival into the
CC second decade of life. {ECO:0000269|PubMed:25434004,
CC ECO:0000269|PubMed:26741492}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. TrmE GTPase family. {ECO:0000305}.
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DR EMBL; AF360742; AAK39555.1; -; mRNA.
DR EMBL; AF361481; AAK37568.1; -; Genomic_DNA.
DR EMBL; AF360743; AAK39556.1; -; mRNA.
DR EMBL; AF360744; AAK39557.1; -; mRNA.
DR EMBL; AY078987; AAL85492.1; -; mRNA.
DR EMBL; AY078988; AAL85493.1; -; mRNA.
DR EMBL; AK027606; BAB55228.1; -; mRNA.
DR EMBL; AK291929; BAF84618.1; -; mRNA.
DR EMBL; AK297953; BAH12694.1; -; mRNA.
DR EMBL; AC010463; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84597.1; -; Genomic_DNA.
DR EMBL; BC017207; AAH17207.1; -; mRNA.
DR EMBL; BC019261; AAH19261.1; -; mRNA.
DR CCDS; CCDS32950.1; -. [Q969Y2-2]
DR CCDS; CCDS32951.1; -. [Q969Y2-1]
DR CCDS; CCDS56088.1; -. [Q969Y2-4]
DR CCDS; CCDS59364.1; -. [Q969Y2-3]
DR RefSeq; NP_001122327.1; NM_001128855.2. [Q969Y2-3]
DR RefSeq; NP_001182351.1; NM_001195422.1. [Q969Y2-4]
DR RefSeq; NP_116009.2; NM_032620.3. [Q969Y2-1]
DR RefSeq; NP_598399.2; NM_133644.3. [Q969Y2-2]
DR AlphaFoldDB; Q969Y2; -.
DR SMR; Q969Y2; -.
DR BioGRID; 124216; 79.
DR IntAct; Q969Y2; 41.
DR MINT; Q969Y2; -.
DR STRING; 9606.ENSP00000351644; -.
DR GlyGen; Q969Y2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q969Y2; -.
DR PhosphoSitePlus; Q969Y2; -.
DR BioMuta; GTPBP3; -.
DR DMDM; 313104112; -.
DR EPD; Q969Y2; -.
DR jPOST; Q969Y2; -.
DR MassIVE; Q969Y2; -.
DR MaxQB; Q969Y2; -.
DR PeptideAtlas; Q969Y2; -.
DR PRIDE; Q969Y2; -.
DR ProteomicsDB; 1268; -.
DR ProteomicsDB; 75877; -. [Q969Y2-1]
DR ProteomicsDB; 75878; -. [Q969Y2-2]
DR ProteomicsDB; 75879; -. [Q969Y2-3]
DR Antibodypedia; 27650; 110 antibodies from 22 providers.
DR DNASU; 84705; -.
DR Ensembl; ENST00000324894.13; ENSP00000313818.7; ENSG00000130299.17. [Q969Y2-1]
DR Ensembl; ENST00000358792.11; ENSP00000351644.6; ENSG00000130299.17. [Q969Y2-2]
DR Ensembl; ENST00000361619.9; ENSP00000354598.4; ENSG00000130299.17. [Q969Y2-4]
DR Ensembl; ENST00000600625.5; ENSP00000473150.1; ENSG00000130299.17. [Q969Y2-3]
DR GeneID; 84705; -.
DR KEGG; hsa:84705; -.
DR MANE-Select; ENST00000324894.13; ENSP00000313818.7; NM_032620.4; NP_116009.2.
DR UCSC; uc002ngg.5; human. [Q969Y2-1]
DR CTD; 84705; -.
DR DisGeNET; 84705; -.
DR GeneCards; GTPBP3; -.
DR HGNC; HGNC:14880; GTPBP3.
DR HPA; ENSG00000130299; Low tissue specificity.
DR MalaCards; GTPBP3; -.
DR MIM; 580000; phenotype.
DR MIM; 608536; gene.
DR MIM; 616198; phenotype.
DR neXtProt; NX_Q969Y2; -.
DR OpenTargets; ENSG00000130299; -.
DR Orphanet; 444013; Combined oxidative phosphorylation defect type 23.
DR PharmGKB; PA134883205; -.
DR VEuPathDB; HostDB:ENSG00000130299; -.
DR eggNOG; KOG1191; Eukaryota.
DR GeneTree; ENSGT00390000016851; -.
DR HOGENOM; CLU_019624_3_1_1; -.
DR InParanoid; Q969Y2; -.
DR OMA; CEIQCHG; -.
DR PhylomeDB; Q969Y2; -.
DR TreeFam; TF313153; -.
DR PathwayCommons; Q969Y2; -.
DR Reactome; R-HSA-6787450; tRNA modification in the mitochondrion.
DR SignaLink; Q969Y2; -.
DR BioGRID-ORCS; 84705; 36 hits in 1082 CRISPR screens.
DR ChiTaRS; GTPBP3; human.
DR GeneWiki; GTPBP3; -.
DR GenomeRNAi; 84705; -.
DR Pharos; Q969Y2; Tbio.
DR PRO; PR:Q969Y2; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q969Y2; protein.
DR Bgee; ENSG00000130299; Expressed in buccal mucosa cell and 185 other tissues.
DR ExpressionAtlas; Q969Y2; baseline and differential.
DR Genevisible; Q969Y2; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central.
DR CDD; cd04164; trmE; 1.
DR Gene3D; 1.20.120.430; -; 1.
DR Gene3D; 3.30.1360.120; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00379; GTPase_MnmE; 1.
DR InterPro; IPR031168; G_TrmE.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR018948; GTP-bd_TrmE_N.
DR InterPro; IPR004520; GTPase_MnmE.
DR InterPro; IPR027368; MnmE_dom2.
DR InterPro; IPR025867; MnmE_helical.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR Pfam; PF12631; MnmE_helical; 1.
DR Pfam; PF10396; TrmE_N; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51709; G_TRME; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cardiomyopathy; Disease variant; GTP-binding;
KW Mitochondrion; Nucleotide-binding; Primary mitochondrial disease;
KW Reference proteome; Transit peptide; tRNA processing.
FT TRANSIT 1..81
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 82..492
FT /note="tRNA modification GTPase GTPBP3, mitochondrial"
FT /id="PRO_0000280265"
FT DOMAIN 249..416
FT /note="TrmE-type G"
FT BINDING 256..263
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 303..307
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 374..377
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..18
FT /note="MWRGLWTLAAQAARGPRR -> MVHSPTCPHPCFLLVPASEPQFPHLQTPDP
FT GDAVWNVRWA (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045050"
FT VAR_SEQ 221
FT /note="Q -> QGGSTWWWGRKTPHISPQRLPSLSLSACLLSPT (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:12370316"
FT /id="VSP_023583"
FT VAR_SEQ 325..345
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12370316"
FT /id="VSP_023584"
FT VARIANT 3
FT /note="R -> L (in COXPD23; unknown pathological
FT significance; dbSNP:rs1057518138)"
FT /evidence="ECO:0000269|PubMed:25434004,
FT ECO:0000269|PubMed:26741492"
FT /id="VAR_073298"
FT VARIANT 142
FT /note="E -> K (in COXPD23)"
FT /evidence="ECO:0000269|PubMed:25434004"
FT /id="VAR_073299"
FT VARIANT 159
FT /note="E -> V (in COXPD23; dbSNP:rs730880255)"
FT /evidence="ECO:0000269|PubMed:25434004"
FT /id="VAR_073300"
FT VARIANT 162
FT /note="A -> P (in COXPD23)"
FT /evidence="ECO:0000269|PubMed:25434004"
FT /id="VAR_073301"
FT VARIANT 222
FT /note="A -> G (in COXPD23; dbSNP:rs373370177)"
FT /evidence="ECO:0000269|PubMed:25434004"
FT /id="VAR_073302"
FT VARIANT 225
FT /note="E -> K (in dbSNP:rs778983997)"
FT /evidence="ECO:0000269|PubMed:25434004"
FT /id="VAR_073303"
FT VARIANT 250
FT /note="V -> A (in dbSNP:rs3810206)"
FT /evidence="ECO:0000269|PubMed:12370316,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15057824,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:15542390"
FT /id="VAR_031103"
FT VARIANT 257
FT /note="P -> H (in COXPD23)"
FT /evidence="ECO:0000269|PubMed:25434004"
FT /id="VAR_073304"
FT VARIANT 312..319
FT /note="Missing (in COXPD23)"
FT /evidence="ECO:0000269|PubMed:25434004"
FT /id="VAR_073305"
FT VARIANT 322
FT /note="A -> P (in dbSNP:rs372174278)"
FT /evidence="ECO:0000269|PubMed:25434004"
FT /id="VAR_073306"
FT VARIANT 337
FT /note="D -> H (in COXPD23; dbSNP:rs886037735)"
FT /evidence="ECO:0000269|PubMed:25434004"
FT /id="VAR_073307"
FT VARIANT 368
FT /note="R -> H (in dbSNP:rs3745193)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031104"
FT VARIANT 459
FT /note="E -> K (in COXPD23; dbSNP:rs886037734)"
FT /evidence="ECO:0000269|PubMed:25434004"
FT /id="VAR_073308"
SQ SEQUENCE 492 AA; 52058 MW; F39EA7990A1F6494 CRC64;
MWRGLWTLAA QAARGPRRLC TRRSSGAPAP GSGATIFALS SGQGRCGIAV IRTSGPASGH
ALRILTAPRD LPLARHASLR LLSDPRSGEP LDRALVLWFP GPQSFTGEDC VEFHVHGGPA
VVSGVLQALG SVPGLRPAEA GEFTRRAFAN GKLNLTEVEG LADLIHAETE AQRRQALRQL
DGELGHLCRG WAETLTKALA HVEAYIDFGE DDNLEEGVLE QADIEVRALQ VALGAHLRDA
RRGQRLRSGV HVVVTGPPNA GKSSLVNLLS RKPVSIVSPE PGTTRDVLET PVDLAGFPVL
LSDTAGLREG VGPVEQEGVR RARERLEQAD LILAMLDASD LASPSSCNFL ATVVASVGAQ
SPSDSSQRLL LVLNKSDLLS PEGPGPGPDL PPHLLLSCLT GEGLDGLLEA LRKELAAVCG
DPSTDPPLLT RARHQHHLQG CLDALGHYKQ SKDLALAAEA LRVARGHLTR LTGGGGTEEI
LDIIFQDFCV GK
