EFTS_HUMAN
ID EFTS_HUMAN Reviewed; 325 AA.
AC P43897; B4E391; F5H2T7; Q561V7; Q8TBC2; Q9UQK0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Elongation factor Ts, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03135};
DE Short=EF-Ts {ECO:0000255|HAMAP-Rule:MF_03135};
DE Short=EF-TsMt {ECO:0000255|HAMAP-Rule:MF_03135};
DE Flags: Precursor;
GN Name=TSFM {ECO:0000255|HAMAP-Rule:MF_03135};
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 1).
RC TISSUE=Liver;
RA Ma L., Ma M., Spremulli L.L.;
RT "Expression of human mitochondrial translational elongation factor Ts.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Corpus callosum, and Uterus;
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=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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] (ISOFORMS 1 AND 2).
RC TISSUE=Bone marrow, and Brain;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 32-325 (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=7615523; DOI=10.1074/jbc.270.29.17243;
RA Xin H., Woriax V., Burkhart W., Spremulli L.L.;
RT "Cloning and expression of mitochondrial translational elongation factor Ts
RT from bovine and human liver.";
RL J. Biol. Chem. 270:17243-17249(1995).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-324, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
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 [12]
RP STRUCTURE BY NMR OF 43-95.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RSGI RUH-042, a UBA domain from human mitochondrial
RT elongation factor TS.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [13]
RP VARIANT COXPD3 TRP-312, AND INVOLVEMENT IN COXPD3.
RX PubMed=17033963; DOI=10.1086/508434;
RA Smeitink J.A.M., Elpeleg O., Antonicka H., Diepstra H., Saada A., Smits P.,
RA Sasarman F., Vriend G., Jacob-Hirsch J., Shaag A., Rechavi G., Welling B.,
RA Horst J., Rodenburg R.J., van den Heuvel B., Shoubridge E.A.;
RT "Distinct clinical phenotypes associated with a mutation in the
RT mitochondrial translation elongation factor EFTs.";
RL Am. J. Hum. Genet. 79:869-877(2006).
RN [14]
RP VARIANT COXPD3 TRP-312.
RX PubMed=22499341; DOI=10.1136/jmedgenet-2012-100836;
RA Shamseldin H.E., Alshammari M., Al-Sheddi T., Salih M.A., Alkhalidi H.,
RA Kentab A., Repetto G.M., Hashem M., Alkuraya F.S.;
RT "Genomic analysis of mitochondrial diseases in a consanguineous population
RT reveals novel candidate disease genes.";
RL J. Med. Genet. 49:234-241(2012).
RN [15]
RP VARIANT COXPD3 SER-240, CHARACTERIZATION OF VARIANT COXPD3 SER-240, AND
RP FUNCTION.
RX PubMed=27677415; DOI=10.1038/ejhg.2016.124;
RA Emperador S., Bayona-Bafaluy M.P., Fernandez-Marmiesse A., Pineda M.,
RA Felgueroso B., Lopez-Gallardo E., Artuch R., Roca I., Ruiz-Pesini E.,
RA Couce M.L., Montoya J.;
RT "Molecular-genetic characterization and rescue of a TSFM mutation causing
RT childhood-onset ataxia and nonobstructive cardiomyopathy.";
RL Eur. J. Hum. Genet. 25:153-156(2016).
CC -!- FUNCTION: Associates with the EF-Tu.GDP complex and induces the
CC exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-
CC Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
CC {ECO:0000255|HAMAP-Rule:MF_03135, ECO:0000269|PubMed:27677415}.
CC -!- INTERACTION:
CC P43897; Q8N998: CCDC89; NbExp=3; IntAct=EBI-1049298, EBI-12814117;
CC P43897; Q8NHQ1: CEP70; NbExp=4; IntAct=EBI-1049298, EBI-739624;
CC P43897; Q6PUV4: CPLX2; NbExp=3; IntAct=EBI-1049298, EBI-2689453;
CC P43897; O95995: GAS8; NbExp=3; IntAct=EBI-1049298, EBI-1052570;
CC P43897; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-1049298, EBI-5916454;
CC P43897; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-1049298, EBI-11959885;
CC P43897; Q99750: MDFI; NbExp=3; IntAct=EBI-1049298, EBI-724076;
CC P43897; Q15311: RALBP1; NbExp=4; IntAct=EBI-1049298, EBI-749285;
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P43897-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P43897-2; Sequence=VSP_001364;
CC Name=3;
CC IsoId=P43897-3; Sequence=VSP_043517, VSP_043518;
CC Name=4;
CC IsoId=P43897-4; Sequence=VSP_045283, VSP_045284;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues, with the highest levels
CC of expression in skeletal muscle, liver and kidney.
CC -!- DISEASE: Combined oxidative phosphorylation deficiency 3 (COXPD3)
CC [MIM:610505]: A mitochondrial disease resulting in severe metabolic
CC acidosis with encephalomyopathy or with hypertrophic cardiomyopathy.
CC Patients show a severe defect in mitochondrial translation leading to a
CC failure to assemble adequate amounts of three of the oxidative
CC phosphorylation complexes. {ECO:0000269|PubMed:17033963,
CC ECO:0000269|PubMed:22499341, ECO:0000269|PubMed:27677415}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the EF-Ts family. {ECO:0000255|HAMAP-
CC Rule:MF_03135}.
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DR EMBL; AF110399; AAD20224.1; -; mRNA.
DR EMBL; AK304621; BAG65403.1; -; mRNA.
DR EMBL; AK308981; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC025165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW97075.1; -; Genomic_DNA.
DR EMBL; BC022862; AAH22862.1; -; mRNA.
DR EMBL; BC093068; AAH93068.1; -; mRNA.
DR EMBL; L37936; AAC37577.1; -; mRNA.
DR CCDS; CCDS53809.1; -. [P43897-2]
DR CCDS; CCDS53810.1; -. [P43897-4]
DR CCDS; CCDS53811.1; -. [P43897-3]
DR CCDS; CCDS8958.2; -. [P43897-1]
DR PIR; I84606; I84606.
DR RefSeq; NP_001166166.1; NM_001172695.1. [P43897-3]
DR RefSeq; NP_001166167.1; NM_001172696.1. [P43897-2]
DR RefSeq; NP_001166168.1; NM_001172697.1. [P43897-4]
DR RefSeq; NP_005717.3; NM_005726.5. [P43897-1]
DR PDB; 2CP9; NMR; -; A=45-95.
DR PDBsum; 2CP9; -.
DR AlphaFoldDB; P43897; -.
DR SMR; P43897; -.
DR BioGRID; 115409; 387.
DR IntAct; P43897; 38.
DR MINT; P43897; -.
DR STRING; 9606.ENSP00000313877; -.
DR GlyGen; P43897; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P43897; -.
DR MetOSite; P43897; -.
DR PhosphoSitePlus; P43897; -.
DR SwissPalm; P43897; -.
DR BioMuta; TSFM; -.
DR DMDM; 12644268; -.
DR EPD; P43897; -.
DR jPOST; P43897; -.
DR MassIVE; P43897; -.
DR MaxQB; P43897; -.
DR PeptideAtlas; P43897; -.
DR PRIDE; P43897; -.
DR ProteomicsDB; 26068; -.
DR ProteomicsDB; 55655; -. [P43897-1]
DR ProteomicsDB; 55656; -. [P43897-2]
DR ProteomicsDB; 55657; -. [P43897-3]
DR Antibodypedia; 1781; 149 antibodies from 25 providers.
DR DNASU; 10102; -.
DR Ensembl; ENST00000323833.12; ENSP00000313877.8; ENSG00000123297.20. [P43897-2]
DR Ensembl; ENST00000540550.6; ENSP00000440987.1; ENSG00000123297.20. [P43897-3]
DR Ensembl; ENST00000543727.5; ENSP00000439342.1; ENSG00000123297.20. [P43897-4]
DR Ensembl; ENST00000652027.2; ENSP00000499171.2; ENSG00000123297.20. [P43897-1]
DR GeneID; 10102; -.
DR KEGG; hsa:10102; -.
DR MANE-Select; ENST00000652027.2; ENSP00000499171.2; NM_005726.6; NP_005717.3.
DR UCSC; uc001sqh.4; human. [P43897-1]
DR CTD; 10102; -.
DR DisGeNET; 10102; -.
DR GeneCards; TSFM; -.
DR HGNC; HGNC:12367; TSFM.
DR HPA; ENSG00000123297; Low tissue specificity.
DR MalaCards; TSFM; -.
DR MIM; 604723; gene.
DR MIM; 610505; phenotype.
DR neXtProt; NX_P43897; -.
DR OpenTargets; ENSG00000123297; -.
DR Orphanet; 168566; Fatal mitochondrial disease due to combined oxidative phosphorylation defect type 3.
DR PharmGKB; PA37037; -.
DR VEuPathDB; HostDB:ENSG00000123297; -.
DR eggNOG; KOG1071; Eukaryota.
DR GeneTree; ENSGT00390000016293; -.
DR HOGENOM; CLU_047155_4_0_1; -.
DR InParanoid; P43897; -.
DR OMA; HTTRQLC; -.
DR OrthoDB; 1048278at2759; -.
DR PhylomeDB; P43897; -.
DR TreeFam; TF314154; -.
DR PathwayCommons; P43897; -.
DR Reactome; R-HSA-5389840; Mitochondrial translation elongation.
DR SignaLink; P43897; -.
DR BioGRID-ORCS; 10102; 369 hits in 1089 CRISPR screens.
DR ChiTaRS; TSFM; human.
DR EvolutionaryTrace; P43897; -.
DR GeneWiki; TSFM; -.
DR GenomeRNAi; 10102; -.
DR Pharos; P43897; Tbio.
DR PRO; PR:P43897; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P43897; protein.
DR Bgee; ENSG00000123297; Expressed in right adrenal gland and 100 other tissues.
DR ExpressionAtlas; P43897; baseline and differential.
DR Genevisible; P43897; HS.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0070125; P:mitochondrial translational elongation; IBA:GO_Central.
DR GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; TAS:ProtInc.
DR GO; GO:0070129; P:regulation of mitochondrial translation; IDA:UniProtKB.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR Gene3D; 3.30.479.20; -; 2.
DR HAMAP; MF_00050; EF_Ts; 1.
DR InterPro; IPR036402; EF-Ts_dimer_sf.
DR InterPro; IPR001816; Transl_elong_EFTs/EF1B.
DR InterPro; IPR014039; Transl_elong_EFTs/EF1B_dimer.
DR InterPro; IPR018101; Transl_elong_Ts_CS.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR11741; PTHR11741; 1.
DR Pfam; PF00889; EF_TS; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54713; SSF54713; 2.
DR PROSITE; PS01126; EF_TS_1; 1.
DR PROSITE; PS01127; EF_TS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cardiomyopathy; Disease variant;
KW Elongation factor; Mitochondrion; Phosphoprotein;
KW Primary mitochondrial disease; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..45
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03135"
FT CHAIN 46..325
FT /note="Elongation factor Ts, mitochondrial"
FT /id="PRO_0000007468"
FT MOD_RES 76
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZR8"
FT MOD_RES 133
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZR8"
FT MOD_RES 192
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZR8"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 324
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 161
FT /note="K -> KVQWLTPVNLALWEAEAGGSLE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_001364"
FT VAR_SEQ 162..167
FT /note="GFLNSS -> ENWEKT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043517"
FT VAR_SEQ 168..325
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043518"
FT VAR_SEQ 192..215
FT /note="KLGENMILKRAAWVKVPSGFYVGS -> LPFQIGAVSELQLPESNFLQNTSS
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045283"
FT VAR_SEQ 216..325
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045284"
FT VARIANT 240
FT /note="C -> S (in COXPD3; decreased protein abundance;
FT decreased mitochondrial translation products; patient
FT fibroblast phenotype can be rescued by coexpression with
FT wild-type TSFM; dbSNP:rs750799705)"
FT /evidence="ECO:0000269|PubMed:27677415"
FT /id="VAR_077697"
FT VARIANT 312
FT /note="R -> W (in COXPD3; dbSNP:rs121909485)"
FT /evidence="ECO:0000269|PubMed:17033963,
FT ECO:0000269|PubMed:22499341"
FT /id="VAR_068973"
FT CONFLICT 32..34
FT /note="HTF -> ARV (in Ref. 6; AAC37577)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="N -> T (in Ref. 5; AAH93068)"
FT /evidence="ECO:0000305"
FT HELIX 48..57
FT /evidence="ECO:0007829|PDB:2CP9"
FT HELIX 61..71
FT /evidence="ECO:0007829|PDB:2CP9"
FT HELIX 75..89
FT /evidence="ECO:0007829|PDB:2CP9"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:2CP9"
SQ SEQUENCE 325 AA; 35391 MW; 671645764A9CB31C CRC64;
MSLLRSLRVF LVARTGSYPA GSLLRQSPQP RHTFYAGPRL SASASSKELL MKLRRKTGYS
FVNCKKALET CGGDLKQAEI WLHKEAQKEG WSKAAKLQGR KTKEGLIGLL QEGNTTVLVE
VNCETDFVSR NLKFQLLVQQ VALGTMMHCQ TLKDQPSAYS KGFLNSSELS GLPAGPDREG
SLKDQLALAI GKLGENMILK RAAWVKVPSG FYVGSYVHGA MQSPSLHKLV LGKYGALVIC
ETSEQKTNLE DVGRRLGQHV VGMAPLSVGS LDDEPGGEAE TKMLSQPYLL DPSITLGQYV
QPQGVSVVDF VRFECGEGEE AAETE
