ID SYTC_HUMAN Reviewed; 723 AA. AC P26639; A8K8I1; B4DEG8; Q96FP5; Q9BWA6; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 3. DT 27-MAR-2024, entry version 236. DE RecName: Full=Threonine--tRNA ligase 1, cytoplasmic {ECO:0000305}; DE EC=6.1.1.3 {ECO:0000269|PubMed:25824639}; DE AltName: Full=Threonyl-tRNA synthetase; DE Short=ThrRS; DE AltName: Full=Threonyl-tRNA synthetase 1 {ECO:0000312|HGNC:HGNC:11572}; GN Name=TARS1 {ECO:0000312|HGNC:HGNC:11572}; Synonyms=TARS; 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). RX PubMed=2033077; DOI=10.1016/s0021-9258(18)92906-6; RA Cruzen M.E., Arfin S.M.; RT "Nucleotide and deduced amino acid sequence of human threonyl-tRNA RT synthetase reveals extensive homology to the Escherichia coli and yeast RT enzymes."; RL J. Biol. Chem. 266:9919-9923(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Cerebellum, and Testis; 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=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(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] (ISOFORM 1). RC TISSUE=Cervix, and Lung; 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 ISGYLATION. RX PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132; RA Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., RA Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.; RT "Proteomic identification of proteins conjugated to ISG15 in mouse and RT human cells."; RL Biochem. Biophys. Res. Commun. 336:496-506(2005). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-243, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(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-39; THR-246; TYR-298; THR-453 RP AND SER-702, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 STRUCTURE BY NMR OF 79-153. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the TGS domain from human threonyl-tRNA RT synthetase."; RL Submitted (JUL-2005) to the PDB data bank. RN [11] {ECO:0007744|PDB:4P3N} RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 322-723 IN COMPLEX WITH RP BORRELIDIN INHIBITOR, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, RP SUBUNIT, AND MUTAGENESIS OF TYR-392; PHE-458; ASP-462 AND LEU-567. RX PubMed=25824639; DOI=10.1038/ncomms7402; RA Fang P., Yu X., Jeong S.J., Mirando A., Chen K., Chen X., Kim S., RA Francklyn C.S., Guo M.; RT "Structural basis for full-spectrum inhibition of translational functions RT on a tRNA synthetase."; RL Nat. Commun. 6:6402-6402(2015). RN [12] RP INVOLVEMENT IN TTD7, VARIANTS TTD7 PRO-227; GLU-276 AND 638-ARG--PHE-723 RP DEL, CHARACTERIZATION OF VARIANT TTD7 PRO-227, AND FUNCTION. RX PubMed=31374204; DOI=10.1016/j.ajhg.2019.06.017; RA Theil A.F., Botta E., Raams A., Smith D.E.C., Mendes M.I., Caligiuri G., RA Giachetti S., Bione S., Carriero R., Liberi G., Zardoni L., RA Swagemakers S.M.A., Salomons G.S., Sarasin A., Lehmann A., RA van der Spek P.J., Ogi T., Hoeijmakers J.H.J., Vermeulen W., Orioli D.; RT "Bi-allelic TARS Mutations Are Associated with Brittle Hair Phenotype."; RL Am. J. Hum. Genet. 105:434-440(2019). CC -!- FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a two- CC step reaction: threonine is first activated by ATP to form Thr-AMP and CC then transferred to the acceptor end of tRNA(Thr) (PubMed:25824639, CC PubMed:31374204). Also edits incorrectly charged tRNA(Thr) via its CC editing domain, at the post-transfer stage (By similarity). CC {ECO:0000250|UniProtKB:Q9D0R2, ECO:0000269|PubMed:25824639, CC ECO:0000269|PubMed:31374204}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L- CC threonyl-tRNA(Thr); Xref=Rhea:RHEA:24624, Rhea:RHEA-COMP:9670, CC Rhea:RHEA-COMP:9704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:78442, CC ChEBI:CHEBI:78534, ChEBI:CHEBI:456215; EC=6.1.1.3; CC Evidence={ECO:0000269|PubMed:25824639}; CC -!- ACTIVITY REGULATION: Inhibited by borrelidin (BN, IC 50 is 7 nM), which CC binds to 4 distinct subsites in the protein, preventing binding of all CC 3 substrates (PubMed:25824639). {ECO:0000269|PubMed:25824639}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:25824639}. CC -!- INTERACTION: CC P26639; Q9BPX7: C7orf25; NbExp=3; IntAct=EBI-1042683, EBI-718586; CC P26639; Q96CV9: OPTN; NbExp=3; IntAct=EBI-1042683, EBI-748974; CC P26639; O43704: SULT1B1; NbExp=3; IntAct=EBI-1042683, EBI-10179062; CC P26639; A2RTX5: TARS3; NbExp=6; IntAct=EBI-1042683, EBI-1056629; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9D0R2}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P26639-1; Sequence=Displayed; CC Name=2; CC IsoId=P26639-2; Sequence=VSP_045114; CC -!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}. CC -!- DISEASE: Trichothiodystrophy 7, non-photosensitive (TTD7) [MIM:618546]: CC A form of trichothiodystrophy, a disease characterized by sulfur- CC deficient brittle hair and multisystem variable abnormalities. The CC spectrum of clinical features varies from mild disease with only hair CC involvement to severe disease with cutaneous, neurologic and profound CC developmental defects. Ichthyosis, intellectual and developmental CC disabilities, decreased fertility, abnormal characteristics at birth, CC ocular abnormalities, short stature, and infections are common CC manifestations. There are both photosensitive and non-photosensitive CC forms of the disorder. TTD7 patients do not manifest cutaneous CC photosensitivity. They have cysteine- and threonine-deficient hair with CC alternating light and dark 'tiger-tail' banding pattern observed under CC polarization microscopy. Inheritance pattern is autosomal recessive. CC {ECO:0000269|PubMed:31374204}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB04939.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; M63180; AAB04939.1; ALT_INIT; mRNA. DR EMBL; AK292346; BAF85035.1; -; mRNA. DR EMBL; AK293620; BAG57079.1; -; mRNA. DR EMBL; AC025441; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC034231; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471118; EAX10804.1; -; Genomic_DNA. DR EMBL; BC000517; AAH00517.2; -; mRNA. DR EMBL; BC010578; AAH10578.2; -; mRNA. DR CCDS; CCDS3899.1; -. [P26639-1] DR CCDS; CCDS58943.1; -. [P26639-2] DR PIR; A38867; YSHUT. DR RefSeq; NP_001245366.1; NM_001258437.1. [P26639-1] DR RefSeq; NP_001245367.1; NM_001258438.1. [P26639-2] DR RefSeq; NP_689508.3; NM_152295.4. [P26639-1] DR PDB; 1WWT; NMR; -; A=79-153. DR PDB; 4HWT; X-ray; 2.30 A; A/B=321-723. DR PDB; 4P3N; X-ray; 2.60 A; A/B/C/D=322-723. DR PDB; 4TTV; X-ray; 2.80 A; A/B/C/D=322-723. DR PDB; 5XLN; X-ray; 1.90 A; B=30-74. DR PDBsum; 1WWT; -. DR PDBsum; 4HWT; -. DR PDBsum; 4P3N; -. DR PDBsum; 4TTV; -. DR PDBsum; 5XLN; -. DR AlphaFoldDB; P26639; -. DR SMR; P26639; -. DR BioGRID; 112760; 150. DR IntAct; P26639; 41. DR MINT; P26639; -. DR STRING; 9606.ENSP00000387710; -. DR BindingDB; P26639; -. DR ChEMBL; CHEMBL3391; -. DR DrugBank; DB00156; Threonine. DR MoonProt; P26639; -. DR GlyGen; P26639; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P26639; -. DR MetOSite; P26639; -. DR PhosphoSitePlus; P26639; -. DR SwissPalm; P26639; -. DR BioMuta; TARS; -. DR DMDM; 60267755; -. DR CPTAC; CPTAC-1194; -. DR CPTAC; CPTAC-1195; -. DR CPTAC; CPTAC-278; -. DR CPTAC; CPTAC-279; -. DR EPD; P26639; -. DR jPOST; P26639; -. DR MassIVE; P26639; -. DR MaxQB; P26639; -. DR PaxDb; 9606-ENSP00000387710; -. DR PeptideAtlas; P26639; -. DR ProteomicsDB; 3957; -. DR ProteomicsDB; 54357; -. [P26639-1] DR Pumba; P26639; -. DR ABCD; P26639; 2 sequenced antibodies. DR Antibodypedia; 9874; 195 antibodies from 30 providers. DR DNASU; 6897; -. DR Ensembl; ENST00000265112.8; ENSP00000265112.3; ENSG00000113407.14. [P26639-1] DR Ensembl; ENST00000455217.6; ENSP00000387710.2; ENSG00000113407.14. [P26639-2] DR Ensembl; ENST00000502553.5; ENSP00000424387.1; ENSG00000113407.14. [P26639-1] DR GeneID; 6897; -. DR KEGG; hsa:6897; -. DR MANE-Select; ENST00000265112.8; ENSP00000265112.3; NM_152295.5; NP_689508.3. DR UCSC; uc003jhy.5; human. [P26639-1] DR AGR; HGNC:11572; -. DR CTD; 6897; -. DR DisGeNET; 6897; -. DR GeneCards; TARS1; -. DR HGNC; HGNC:11572; TARS1. DR HPA; ENSG00000113407; Low tissue specificity. DR MalaCards; TARS1; -. DR MIM; 187790; gene. DR MIM; 618546; phenotype. DR neXtProt; NX_P26639; -. DR OpenTargets; ENSG00000113407; -. DR Orphanet; 33364; Trichothiodystrophy. DR PharmGKB; PA36337; -. DR VEuPathDB; HostDB:ENSG00000113407; -. DR eggNOG; KOG1637; Eukaryota. DR GeneTree; ENSGT00940000154969; -. DR HOGENOM; CLU_008554_0_1_1; -. DR InParanoid; P26639; -. DR OMA; CEAQLAK; -. DR OrthoDB; 1119631at2759; -. DR PhylomeDB; P26639; -. DR TreeFam; TF300858; -. DR BRENDA; 6.1.1.3; 2681. DR PathwayCommons; P26639; -. DR Reactome; R-HSA-379716; Cytosolic tRNA aminoacylation. DR SignaLink; P26639; -. DR SIGNOR; P26639; -. DR BioGRID-ORCS; 6897; 801 hits in 1159 CRISPR screens. DR ChiTaRS; TARS; human. DR EvolutionaryTrace; P26639; -. DR GeneWiki; TARS_(gene); -. DR GenomeRNAi; 6897; -. DR Pharos; P26639; Tchem. DR PRO; PR:P26639; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; P26639; Protein. DR Bgee; ENSG00000113407; Expressed in sural nerve and 206 other cell types or tissues. DR ExpressionAtlas; P26639; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IMP:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB. DR GO; GO:0004829; F:threonine-tRNA ligase activity; IDA:UniProtKB. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IDA:UniProtKB. DR CDD; cd01667; TGS_ThrRS; 1. DR CDD; cd00860; ThrRS_anticodon; 1. DR CDD; cd00771; ThrRS_core; 1. DR Gene3D; 3.10.20.30; -; 1. DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1. DR HAMAP; MF_00184; Thr_tRNA_synth; 1. DR InterPro; IPR002314; aa-tRNA-synt_IIb. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL. DR InterPro; IPR004154; Anticodon-bd. DR InterPro; IPR036621; Anticodon-bd_dom_sf. DR InterPro; IPR012675; Beta-grasp_dom_sf. DR InterPro; IPR004095; TGS. DR InterPro; IPR012676; TGS-like. DR InterPro; IPR002320; Thr-tRNA-ligase_IIa. DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit. DR InterPro; IPR047246; ThrRS_anticodon. DR InterPro; IPR033728; ThrRS_core. DR InterPro; IPR012947; tRNA_SAD. DR NCBIfam; TIGR00418; thrS; 1. DR PANTHER; PTHR11451:SF36; THREONINE--TRNA LIGASE 1, CYTOPLASMIC; 1. DR PANTHER; PTHR11451; THREONINE-TRNA LIGASE; 1. DR Pfam; PF03129; HGTP_anticodon; 1. DR Pfam; PF02824; TGS; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR Pfam; PF07973; tRNA_SAD; 1. DR PRINTS; PR01047; TRNASYNTHTHR. DR SMART; SM00863; tRNA_SAD; 1. DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1. DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1. DR SUPFAM; SSF81271; TGS-like; 1. DR SUPFAM; SSF55186; ThrRS/AlaRS common domain; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. DR PROSITE; PS51880; TGS; 1. DR Genevisible; P26639; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Aminoacyl-tRNA synthetase; KW ATP-binding; Cytoplasm; Disease variant; Ligase; Nucleotide-binding; KW Phosphoprotein; Protein biosynthesis; Reference proteome; RNA-binding; KW tRNA-binding; Ubl conjugation. FT CHAIN 1..723 FT /note="Threonine--tRNA ligase 1, cytoplasmic" FT /id="PRO_0000101119" FT DOMAIN 79..143 FT /note="TGS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228" FT REGION 1..46 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 18..41 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 39 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 243 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 246 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 298 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 453 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 702 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 110 FT /note="S -> SHTASCKNLSSLASLLASVAIPSSGMPWPPLFFL (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045114" FT VARIANT 21 FT /note="G -> D (in dbSNP:rs34334786)" FT /id="VAR_034533" FT VARIANT 227 FT /note="L -> P (in TTD7; loss of protein stability; loss of FT threonine-tRNA ligase activity)" FT /evidence="ECO:0000269|PubMed:31374204" FT /id="VAR_083226" FT VARIANT 276 FT /note="K -> E (in TTD7)" FT /evidence="ECO:0000269|PubMed:31374204" FT /id="VAR_083227" FT VARIANT 638..723 FT /note="Missing (in TTD7)" FT /evidence="ECO:0000269|PubMed:31374204" FT /id="VAR_083228" FT MUTAGEN 392 FT /note="Y->E: Partially restores in vitro translation." FT /evidence="ECO:0000269|PubMed:25824639" FT MUTAGEN 458 FT /note="F->A: Partially restores in vitro translation." FT /evidence="ECO:0000269|PubMed:25824639" FT MUTAGEN 462 FT /note="D->L: Does not restore in vitro translation, FT probably does not bind BN." FT /evidence="ECO:0000269|PubMed:25824639" FT MUTAGEN 567 FT /note="L->R,W: Does not restore in vitro translation, does FT not replace endogenous yeast enzyme." FT /evidence="ECO:0000269|PubMed:25824639" FT MUTAGEN 567 FT /note="L->V: Replaces endogenous yeast enzyme." FT /evidence="ECO:0000269|PubMed:25824639" FT CONFLICT 164 FT /note="A -> G (in Ref. 1; AAB04939)" FT /evidence="ECO:0000305" FT CONFLICT 350 FT /note="A -> V (in Ref. 1; AAB04939)" FT /evidence="ECO:0000305" FT CONFLICT 417 FT /note="C -> S (in Ref. 1; AAB04939)" FT /evidence="ECO:0000305" FT CONFLICT 439 FT /note="V -> G (in Ref. 1; AAB04939)" FT /evidence="ECO:0000305" FT CONFLICT 453 FT /note="T -> I (in Ref. 5; AAH10578)" FT /evidence="ECO:0000305" FT CONFLICT 581 FT /note="D -> E (in Ref. 1; AAB04939)" FT /evidence="ECO:0000305" FT CONFLICT 612 FT /note="W -> LA (in Ref. 1; AAB04939)" FT /evidence="ECO:0000305" FT CONFLICT 636 FT /note="K -> N (in Ref. 1; AAB04939)" FT /evidence="ECO:0000305" FT CONFLICT 683 FT /note="S -> T (in Ref. 1; AAB04939)" FT /evidence="ECO:0000305" FT HELIX 57..69 FT /evidence="ECO:0007829|PDB:5XLN" FT STRAND 82..86 FT /evidence="ECO:0007829|PDB:1WWT" FT STRAND 92..96 FT /evidence="ECO:0007829|PDB:1WWT" FT TURN 97..99 FT /evidence="ECO:0007829|PDB:1WWT" FT HELIX 102..108 FT /evidence="ECO:0007829|PDB:1WWT" FT TURN 111..113 FT /evidence="ECO:0007829|PDB:1WWT" FT HELIX 114..116 FT /evidence="ECO:0007829|PDB:1WWT" FT STRAND 120..127 FT /evidence="ECO:0007829|PDB:1WWT" FT STRAND 129..131 FT /evidence="ECO:0007829|PDB:1WWT" FT STRAND 135..141 FT /evidence="ECO:0007829|PDB:1WWT" FT HELIX 323..329 FT /evidence="ECO:0007829|PDB:4HWT" FT STRAND 332..334 FT /evidence="ECO:0007829|PDB:4HWT" FT HELIX 347..366 FT /evidence="ECO:0007829|PDB:4HWT" FT STRAND 376..379 FT /evidence="ECO:0007829|PDB:4HWT" FT HELIX 380..385 FT /evidence="ECO:0007829|PDB:4HWT" FT HELIX 388..391 FT /evidence="ECO:0007829|PDB:4HWT" FT HELIX 393..395 FT /evidence="ECO:0007829|PDB:4HWT" FT STRAND 398..401 FT /evidence="ECO:0007829|PDB:4HWT" FT STRAND 404..408 FT /evidence="ECO:0007829|PDB:4HWT" FT HELIX 413..421 FT /evidence="ECO:0007829|PDB:4HWT" FT HELIX 427..429 FT /evidence="ECO:0007829|PDB:4HWT" FT STRAND 431..436 FT /evidence="ECO:0007829|PDB:4HWT" FT STRAND 439..441 FT /evidence="ECO:0007829|PDB:4HWT" FT HELIX 446..448 FT /evidence="ECO:0007829|PDB:4HWT" FT TURN 451..453 FT /evidence="ECO:0007829|PDB:4HWT" FT STRAND 456..459 FT /evidence="ECO:0007829|PDB:4HWT" FT STRAND 462..467 FT /evidence="ECO:0007829|PDB:4HWT" FT HELIX 469..471 FT /evidence="ECO:0007829|PDB:4HWT" FT HELIX 472..490 FT /evidence="ECO:0007829|PDB:4HWT" FT STRAND 493..499 FT /evidence="ECO:0007829|PDB:4HWT" FT HELIX 509..525 FT /evidence="ECO:0007829|PDB:4HWT" FT STRAND 530..533 FT /evidence="ECO:0007829|PDB:4HWT" FT STRAND 543..549 FT /evidence="ECO:0007829|PDB:4HWT" FT STRAND 555..565 FT /evidence="ECO:0007829|PDB:4HWT" FT HELIX 566..570 FT /evidence="ECO:0007829|PDB:4HWT" FT STRAND 587..595 FT /evidence="ECO:0007829|PDB:4HWT" FT HELIX 597..607 FT /evidence="ECO:0007829|PDB:4HWT" FT TURN 608..610 FT /evidence="ECO:0007829|PDB:4HWT" FT HELIX 614..616 FT /evidence="ECO:0007829|PDB:4HWT" FT STRAND 621..627 FT /evidence="ECO:0007829|PDB:4HWT" FT HELIX 628..630 FT /evidence="ECO:0007829|PDB:4HWT" FT HELIX 631..642 FT /evidence="ECO:0007829|PDB:4HWT" FT TURN 643..645 FT /evidence="ECO:0007829|PDB:4HWT" FT STRAND 648..650 FT /evidence="ECO:0007829|PDB:4HWT" FT HELIX 658..667 FT /evidence="ECO:0007829|PDB:4HWT" FT STRAND 671..676 FT /evidence="ECO:0007829|PDB:4HWT" FT HELIX 678..683 FT /evidence="ECO:0007829|PDB:4HWT" FT STRAND 685..690 FT /evidence="ECO:0007829|PDB:4HWT" FT STRAND 695..700 FT /evidence="ECO:0007829|PDB:4HWT" FT HELIX 701..713 FT /evidence="ECO:0007829|PDB:4HWT" FT HELIX 719..722 FT /evidence="ECO:0007829|PDB:4P3N" SQ SEQUENCE 723 AA; 83435 MW; 885745118972C5A9 CRC64; MFEEKASSPS GKMGGEEKPI GAGEEKQKEG GKKKNKEGSG DGGRAELNPW PEYIYTRLEM YNILKAEHDS ILAEKAEKDS KPIKVTLPDG KQVDAESWKT TPYQIACGIS QGLADNTVIA KVNNVVWDLD RPLEEDCTLE LLKFEDEEAQ AVYWHSSAHI MGEAMERVYG GCLCYGPPIE NGFYYDMYLE EGGVSSNDFS SLEALCKKII KEKQAFERLE VKKETLLAMF KYNKFKCRIL NEKVNTPTTT VYRCGPLIDL CRGPHVRHTG KIKALKIHKN SSTYWEGKAD METLQRIYGI SFPDPKMLKE WEKFQEEAKN RDHRKIGRDQ ELYFFHELSP GSCFFLPKGA YIYNALIEFI RSEYRKRGFQ EVVTPNIFNS RLWMTSGHWQ HYSENMFSFE VEKELFALKP MNCPGHCLMF DHRPRSWREL PLRLADFGVL HRNELSGALT GLTRVRRFQQ DDAHIFCAME QIEDEIKGCL DFLRTVYSVF GFSFKLNLST RPEKFLGDIE VWDQAEKQLE NSLNEFGEKW ELNSGDGAFY GPKIDIQIKD AIGRYHQCAT IQLDFQLPIR FNLTYVSHDG DDKKRPVIVH RAILGSVERM IAILTENYGG KWPFWLSPRQ VMVVPVGPTC DEYAQKVRQQ FHDAKFMADI DLDPGCTLNK KIRNAQLAQY NFILVVGEKE KISGTVNIRT RDNKVHGERT ISETIERLQQ LKEFRSKQAE EEF //