SYTM_HUMAN
ID SYTM_HUMAN Reviewed; 718 AA.
AC Q9BW92; Q53GW7; Q96I50; Q9H9V2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Threonine--tRNA ligase, mitochondrial;
DE EC=6.1.1.3 {ECO:0000269|PubMed:26811336};
DE AltName: Full=Threonyl-tRNA synthetase;
DE Short=ThrRS;
DE AltName: Full=Threonyl-tRNA synthetase-like 1;
DE Flags: Precursor;
GN Name=TARS2; Synonyms=TARSL1;
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 [LARGE SCALE MRNA] (ISOFORM 2).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, 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 IDENTIFICATION.
RX PubMed=15779907; DOI=10.1021/bi047527z;
RA Bonnefond L., Fender A., Rudinger-Thirion J., Giege R., Florentz C.,
RA Sissler M.;
RT "Toward the full set of human mitochondrial aminoacyl-tRNA synthetases:
RT characterization of AspRS and TyrRS.";
RL Biochemistry 44:4805-4816(2005).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [9]
RP INVOLVEMENT IN COXPD21, VARIANT COXPD21 LEU-282, AND CHARACTERIZATION OF
RP VARIANT COXPD21.
RX PubMed=24827421; DOI=10.1002/humu.22590;
RA Diodato D., Melchionda L., Haack T.B., Dallabona C., Baruffini E.,
RA Donnini C., Granata T., Ragona F., Balestri P., Margollicci M.,
RA Lamantea E., Nasca A., Powell C.A., Minczuk M., Strom T.M., Meitinger T.,
RA Prokisch H., Lamperti C., Zeviani M., Ghezzi D.;
RT "VARS2 and TARS2 mutations in patients with mitochondrial
RT encephalomyopathies.";
RL Hum. Mutat. 35:983-989(2014).
RN [10]
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 [11]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP CHARACTERIZATION OF VARIANT COXPD21 LEU-282.
RX PubMed=26811336; DOI=10.1074/jbc.m115.700849;
RA Wang Y., Zhou X.L., Ruan Z.R., Liu R.J., Eriani G., Wang E.D.;
RT "A human disease-causing point mutation in mitochondrial threonyl-tRNA
RT synthetase induces both structural and functional defects.";
RL J. Biol. Chem. 291:6507-6520(2016).
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). Also edits
CC incorrectly charged tRNA(Thr) via its editing domain.
CC {ECO:0000269|PubMed:26811336}.
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:26811336};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.5 mM for L-threonine {ECO:0000269|PubMed:26811336};
CC KM=1.1 uM for tRNA(Thr) {ECO:0000269|PubMed:26811336};
CC KM=180 mM for L-serine {ECO:0000269|PubMed:26811336};
CC Note=kcat is 5.8 sec(-1) for the activation reaction of L-threonine.
CC kcat is 1.1 sec(-1) for the activation reaction of L-serine. kcat is
CC 0.061 sec(-1) for the aminoacylation of tRNA(Thr) with L-threonine.
CC {ECO:0000269|PubMed:26811336};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:26811336}.
CC -!- INTERACTION:
CC Q9BW92; Q15041: ARL6IP1; NbExp=3; IntAct=EBI-1045099, EBI-714543;
CC Q9BW92; Q9NWX5: ASB6; NbExp=3; IntAct=EBI-1045099, EBI-6425205;
CC Q9BW92; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-1045099, EBI-742054;
CC Q9BW92; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-1045099, EBI-3918971;
CC Q9BW92; Q969L2: MAL2; NbExp=3; IntAct=EBI-1045099, EBI-944295;
CC Q9BW92; O60664: PLIN3; NbExp=3; IntAct=EBI-1045099, EBI-725795;
CC Q9BW92; Q8WV19: SFT2D1; NbExp=3; IntAct=EBI-1045099, EBI-2854842;
CC Q9BW92; Q9BYT1: SLC17A9; NbExp=3; IntAct=EBI-1045099, EBI-3940816;
CC Q9BW92; Q16563: SYPL1; NbExp=3; IntAct=EBI-1045099, EBI-2800683;
CC Q9BW92; A2RTX5: TARS3; NbExp=3; IntAct=EBI-1045099, EBI-1056629;
CC Q9BW92; Q9UBN6: TNFRSF10D; NbExp=3; IntAct=EBI-1045099, EBI-1044859;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BW92-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BW92-2; Sequence=VSP_054537;
CC -!- DISEASE: Combined oxidative phosphorylation deficiency 21 (COXPD21)
CC [MIM:615918]: A mitochondrial disorder characterized by a lethal
CC encephalomyopathy. Shortly after birth, affected individuals manifest
CC axial hypotonia, limb hypertonia, psychomotor delay, and increased
CC serum lactate. Additional features include subsarcolemmal lipofuscin-
CC positive deposits in muscle, cerebral spongiosis, and hepatic
CC steatosis. {ECO:0000269|PubMed:24827421, ECO:0000269|PubMed:26811336}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AK022590; BAB14117.1; -; mRNA.
DR EMBL; AK222814; BAD96534.1; -; mRNA.
DR EMBL; AL356356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53549.1; -; Genomic_DNA.
DR EMBL; BC000541; AAH00541.1; -; mRNA.
DR EMBL; BC007824; AAH07824.2; -; mRNA.
DR EMBL; BC009997; AAH09997.1; -; mRNA.
DR CCDS; CCDS60252.1; -. [Q9BW92-2]
DR CCDS; CCDS952.1; -. [Q9BW92-1]
DR RefSeq; NP_001258825.1; NM_001271896.1. [Q9BW92-2]
DR RefSeq; NP_079426.2; NM_025150.4. [Q9BW92-1]
DR AlphaFoldDB; Q9BW92; -.
DR SMR; Q9BW92; -.
DR BioGRID; 123188; 169.
DR IntAct; Q9BW92; 37.
DR MINT; Q9BW92; -.
DR STRING; 9606.ENSP00000358060; -.
DR ChEMBL; CHEMBL3351186; -.
DR DrugBank; DB00156; Threonine.
DR GlyGen; Q9BW92; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BW92; -.
DR PhosphoSitePlus; Q9BW92; -.
DR BioMuta; TARS2; -.
DR DMDM; 74752395; -.
DR EPD; Q9BW92; -.
DR jPOST; Q9BW92; -.
DR MassIVE; Q9BW92; -.
DR MaxQB; Q9BW92; -.
DR PaxDb; Q9BW92; -.
DR PeptideAtlas; Q9BW92; -.
DR PRIDE; Q9BW92; -.
DR ProteomicsDB; 79266; -. [Q9BW92-1]
DR ProteomicsDB; 81363; -.
DR Antibodypedia; 34029; 78 antibodies from 20 providers.
DR DNASU; 80222; -.
DR Ensembl; ENST00000369054.6; ENSP00000358050.2; ENSG00000143374.18. [Q9BW92-2]
DR Ensembl; ENST00000369064.8; ENSP00000358060.3; ENSG00000143374.18. [Q9BW92-1]
DR GeneID; 80222; -.
DR KEGG; hsa:80222; -.
DR MANE-Select; ENST00000369064.8; ENSP00000358060.3; NM_025150.5; NP_079426.2.
DR UCSC; uc001euq.5; human. [Q9BW92-1]
DR CTD; 80222; -.
DR DisGeNET; 80222; -.
DR GeneCards; TARS2; -.
DR HGNC; HGNC:30740; TARS2.
DR HPA; ENSG00000143374; Low tissue specificity.
DR MalaCards; TARS2; -.
DR MIM; 612805; gene.
DR MIM; 615918; phenotype.
DR neXtProt; NX_Q9BW92; -.
DR OpenTargets; ENSG00000143374; -.
DR Orphanet; 420733; Combined oxidative phosphorylation defect type 21.
DR PharmGKB; PA162405200; -.
DR VEuPathDB; HostDB:ENSG00000143374; -.
DR eggNOG; KOG1637; Eukaryota.
DR GeneTree; ENSGT00940000161600; -.
DR HOGENOM; CLU_008554_0_3_1; -.
DR InParanoid; Q9BW92; -.
DR OMA; PILEQTC; -.
DR OrthoDB; 813937at2759; -.
DR PhylomeDB; Q9BW92; -.
DR TreeFam; TF300858; -.
DR PathwayCommons; Q9BW92; -.
DR Reactome; R-HSA-379726; Mitochondrial tRNA aminoacylation.
DR SignaLink; Q9BW92; -.
DR BioGRID-ORCS; 80222; 481 hits in 1098 CRISPR screens.
DR ChiTaRS; TARS2; human.
DR GenomeRNAi; 80222; -.
DR Pharos; Q9BW92; Tbio.
DR PRO; PR:Q9BW92; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BW92; protein.
DR Bgee; ENSG00000143374; Expressed in gastrocnemius and 175 other tissues.
DR ExpressionAtlas; Q9BW92; baseline and differential.
DR Genevisible; Q9BW92; HS.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0004829; F:threonine-tRNA ligase activity; IDA:UniProtKB.
DR GO; GO:0070159; P:mitochondrial threonyl-tRNA aminoacylation; TAS:BHF-UCL.
DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IBA:GO_Central.
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 Alternative splicing; Aminoacyl-tRNA synthetase; ATP-binding;
KW Disease variant; Ligase; Mitochondrion; Nucleotide-binding; Phosphoprotein;
KW Primary mitochondrial disease; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..718
FT /note="Threonine--tRNA ligase, mitochondrial"
FT /id="PRO_0000254586"
FT DOMAIN 55..121
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 211..340
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054537"
FT VARIANT 282
FT /note="P -> L (in COXPD21; decreased expression at mRNA and
FT protein levels; decreased threonine-tRNA ligase activity;
FT affects both Thr activation and transfer; decreased
FT aminoacyl-tRNA editing activity; decreased protein
FT stability; loss of homodimerization; dbSNP:rs587777593)"
FT /evidence="ECO:0000269|PubMed:24827421,
FT ECO:0000269|PubMed:26811336"
FT /id="VAR_071853"
FT CONFLICT 269
FT /note="A -> P (in Ref. 2; BAD96534)"
FT /evidence="ECO:0000305"
FT CONFLICT 579
FT /note="E -> G (in Ref. 2; BAD96534)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 718 AA; 81036 MW; A2F793A60483E7F9 CRC64;
MALYQRWRCL RLQGLQACRL HTAVVSTPPR WLAERLGLFE ELWAAQVKRL ASMAQKEPRT
IKISLPGGQK IDAVAWNTTP YQLARQISST LADTAVAAQV NGEPYDLERP LETDSDLRFL
TFDSPEGKAV FWHSSTHVLG AAAEQFLGAV LCRGPSTEYG FYHDFFLGKE RTIRGSELPV
LERICQELTA AARPFRRLEA SRDQLRQLFK DNPFKLHLIE EKVTGPTATV YGCGTLVDLC
QGPHLRHTGQ IGGLKLLSNS SSLWRSSGAP ETLQRVSGIS FPTTELLRVW EAWREEAELR
DHRRIGKEQE LFFFHELSPG SCFFLPRGTR VYNALVAFIR AEYAHRGFSE VKTPTLFSTK
LWEQSGHWEH YQEDMFAVQP PGSDRPPSSQ SDDSTRHITD TLALKPMNCP AHCLMFAHRP
RSWRELPLRL ADFGALHRAE ASGGLGGLTR LRCFQQDDAH IFCTTDQLEA EIQSCLDFLR
SVYAVLGFSF RLALSTRPSG FLGDPCLWDQ AEQVLKQALK EFGEPWDLNS GDGAFYGPKI
DVHLHDALGR PHQCGTIQLD FQLPLRFDLQ YKGQAGALER PVLIHRAVLG SVERLLGVLA
ESCGGKWPLW LSPFQVVVIP VGSEQEEYAK EAQQSLRAAG LVSDLDADSG LTLSRRIRRA
QLAHYNFQFV VGQKEQSKRT VNIRTRDNRR LGEWDLPEAV QRLVELQNTR VPNAEEIF
