SYTC_HUMAN
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 03-AUG-2022, entry version 227.
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};
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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; 124.
DR IntAct; P26639; 37.
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; P26639; -.
DR PeptideAtlas; P26639; -.
DR PRIDE; P26639; -.
DR ProteomicsDB; 3957; -.
DR ProteomicsDB; 54357; -. [P26639-1]
DR ABCD; P26639; 2 sequenced antibodies.
DR Antibodypedia; 9874; 180 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 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; FYYDFAY; -.
DR OrthoDB; 813937at2759; -.
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 BioGRID-ORCS; 6897; 780 hits in 1085 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 204 other tissues.
DR ExpressionAtlas; P26639; baseline and differential.
DR Genevisible; P26639; HS.
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; cd00771; ThrRS_core; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 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; IPR033728; ThrRS_core.
DR InterPro; IPR012947; tRNA_SAD.
DR PANTHER; PTHR11451; PTHR11451; 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; SSF55186; SSF55186; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR SUPFAM; SSF81271; SSF81271; 1.
DR TIGRFAMs; TIGR00418; thrS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS51880; TGS; 1.
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
