Full text data of TARS
TARS
[Confidence: low (only semi-automatic identification from reviews)]
Threonine--tRNA ligase, cytoplasmic; 6.1.1.3 (Threonyl-tRNA synthetase; ThrRS)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Threonine--tRNA ligase, cytoplasmic; 6.1.1.3 (Threonyl-tRNA synthetase; ThrRS)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P26639
ID SYTC_HUMAN Reviewed; 723 AA.
AC P26639; A8K8I1; B4DEG8; Q96FP5; Q9BWA6;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-FEB-2005, sequence version 3.
DT 22-JAN-2014, entry version 152.
DE RecName: Full=Threonine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.3;
DE AltName: Full=Threonyl-tRNA synthetase;
DE Short=ThrRS;
GN Name=TARS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2033077;
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
RT yeast 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-222, AND MASS
RP SPECTROMETRY.
RC TISSUE=Lung adenocarcinoma;
RX PubMed=17203973; DOI=10.1021/pr060438j;
RA Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M.,
RA Haines D.S., Figeys D.;
RT "The proteomic reactor facilitates the analysis of affinity-purified
RT proteins by mass spectrometry: application for identifying
RT ubiquitinated proteins in human cells.";
RL J. Proteome Res. 6:298-305(2007).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-243, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [9]
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.,
RA Buerckstuemmer T., 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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
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.
CC -!- CATALYTIC ACTIVITY: ATP + L-threonine + tRNA(Thr) = AMP +
CC diphosphate + L-threonyl-tRNA(Thr).
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB04939.1; Type=Erroneous initiation;
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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 PIR; A38867; YSHUT.
DR RefSeq; NP_001245366.1; NM_001258437.1.
DR RefSeq; NP_001245367.1; NM_001258438.1.
DR RefSeq; NP_689508.3; NM_152295.4.
DR UniGene; Hs.481860; -.
DR PDB; 1WWT; NMR; -; A=79-153.
DR PDB; 4HWT; X-ray; 2.30 A; A/B=321-723.
DR PDBsum; 1WWT; -.
DR PDBsum; 4HWT; -.
DR ProteinModelPortal; P26639; -.
DR SMR; P26639; 81-721.
DR IntAct; P26639; 12.
DR MINT; MINT-3010570; -.
DR STRING; 9606.ENSP00000265112; -.
DR BindingDB; P26639; -.
DR ChEMBL; CHEMBL3391; -.
DR DrugBank; DB00156; L-Threonine.
DR PhosphoSite; P26639; -.
DR DMDM; 60267755; -.
DR PaxDb; P26639; -.
DR PeptideAtlas; P26639; -.
DR PRIDE; P26639; -.
DR DNASU; 6897; -.
DR Ensembl; ENST00000265112; ENSP00000265112; ENSG00000113407.
DR Ensembl; ENST00000455217; ENSP00000387710; ENSG00000113407.
DR Ensembl; ENST00000502553; ENSP00000424387; ENSG00000113407.
DR GeneID; 6897; -.
DR KEGG; hsa:6897; -.
DR UCSC; uc011coc.3; human.
DR CTD; 6897; -.
DR GeneCards; GC05P033476; -.
DR H-InvDB; HIX0004790; -.
DR HGNC; HGNC:11572; TARS.
DR HPA; HPA037425; -.
DR MIM; 187790; gene.
DR neXtProt; NX_P26639; -.
DR PharmGKB; PA36337; -.
DR eggNOG; COG0441; -.
DR HOGENOM; HOG000003878; -.
DR HOVERGEN; HBG059513; -.
DR InParanoid; P26639; -.
DR KO; K01868; -.
DR OMA; GFFYDMS; -.
DR OrthoDB; EOG7JDQX3; -.
DR PhylomeDB; P26639; -.
DR Reactome; REACT_71; Gene Expression.
DR EvolutionaryTrace; P26639; -.
DR GeneWiki; TARS_(gene); -.
DR GenomeRNAi; 6897; -.
DR NextBio; 26959; -.
DR PRO; PR:P26639; -.
DR ArrayExpress; P26639; -.
DR Bgee; P26639; -.
DR CleanEx; HS_TARS; -.
DR Genevestigator; P26639; -.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; NAS:UniProtKB.
DR GO; GO:0004829; F:threonine-tRNA ligase activity; NAS:UniProtKB.
DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; NAS:UniProtKB.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb_cons-dom.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR012675; Beta-grasp_dom.
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; IPR012947; tRNA_SAD.
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; SSF52954; 1.
DR SUPFAM; SSF55186; SSF55186; 1.
DR SUPFAM; SSF81271; SSF81271; 1.
DR TIGRFAMs; TIGR00418; thrS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing;
KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW Isopeptide bond; Ligase; Nucleotide-binding; Phosphoprotein;
KW Polymorphism; Protein biosynthesis; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1 723 Threonine--tRNA ligase, cytoplasmic.
FT /FTId=PRO_0000101119.
FT MOD_RES 243 243 N6-acetyllysine.
FT MOD_RES 298 298 Phosphotyrosine (By similarity).
FT CROSSLNK 222 222 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT VAR_SEQ 110 110 S -> SHTASCKNLSSLASLLASVAIPSSGMPWPPLFFL
FT (in isoform 2).
FT /FTId=VSP_045114.
FT VARIANT 21 21 G -> D (in dbSNP:rs34334786).
FT /FTId=VAR_034533.
FT CONFLICT 164 164 A -> G (in Ref. 1; AAB04939).
FT CONFLICT 350 350 A -> V (in Ref. 1; AAB04939).
FT CONFLICT 417 417 C -> S (in Ref. 1; AAB04939).
FT CONFLICT 439 439 V -> G (in Ref. 1; AAB04939).
FT CONFLICT 453 453 T -> I (in Ref. 5; AAH10578).
FT CONFLICT 581 581 D -> E (in Ref. 1; AAB04939).
FT CONFLICT 612 612 W -> LA (in Ref. 1; AAB04939).
FT CONFLICT 636 636 K -> N (in Ref. 1; AAB04939).
FT CONFLICT 683 683 S -> T (in Ref. 1; AAB04939).
FT STRAND 82 86
FT STRAND 92 96
FT TURN 97 99
FT HELIX 102 108
FT TURN 111 113
FT HELIX 114 116
FT STRAND 120 127
FT STRAND 129 131
FT STRAND 135 141
FT HELIX 323 329
FT STRAND 332 334
FT HELIX 347 366
FT STRAND 376 379
FT HELIX 380 385
FT HELIX 388 391
FT HELIX 393 395
FT STRAND 398 401
FT STRAND 404 408
FT HELIX 413 421
FT HELIX 427 429
FT STRAND 431 436
FT STRAND 439 441
FT HELIX 446 448
FT TURN 451 453
FT STRAND 456 459
FT STRAND 462 467
FT HELIX 469 471
FT HELIX 472 490
FT STRAND 493 499
FT HELIX 509 525
FT STRAND 530 533
FT STRAND 543 549
FT STRAND 555 565
FT HELIX 566 570
FT STRAND 587 595
FT HELIX 597 607
FT TURN 608 610
FT HELIX 614 616
FT STRAND 621 627
FT HELIX 628 630
FT HELIX 631 642
FT TURN 643 645
FT STRAND 648 650
FT HELIX 658 667
FT STRAND 671 676
FT HELIX 678 683
FT STRAND 685 690
FT STRAND 695 700
FT HELIX 701 713
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
//
ID SYTC_HUMAN Reviewed; 723 AA.
AC P26639; A8K8I1; B4DEG8; Q96FP5; Q9BWA6;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-FEB-2005, sequence version 3.
DT 22-JAN-2014, entry version 152.
DE RecName: Full=Threonine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.3;
DE AltName: Full=Threonyl-tRNA synthetase;
DE Short=ThrRS;
GN Name=TARS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2033077;
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
RT yeast 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-222, AND MASS
RP SPECTROMETRY.
RC TISSUE=Lung adenocarcinoma;
RX PubMed=17203973; DOI=10.1021/pr060438j;
RA Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M.,
RA Haines D.S., Figeys D.;
RT "The proteomic reactor facilitates the analysis of affinity-purified
RT proteins by mass spectrometry: application for identifying
RT ubiquitinated proteins in human cells.";
RL J. Proteome Res. 6:298-305(2007).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-243, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [9]
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.,
RA Buerckstuemmer T., 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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
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.
CC -!- CATALYTIC ACTIVITY: ATP + L-threonine + tRNA(Thr) = AMP +
CC diphosphate + L-threonyl-tRNA(Thr).
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB04939.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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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 PIR; A38867; YSHUT.
DR RefSeq; NP_001245366.1; NM_001258437.1.
DR RefSeq; NP_001245367.1; NM_001258438.1.
DR RefSeq; NP_689508.3; NM_152295.4.
DR UniGene; Hs.481860; -.
DR PDB; 1WWT; NMR; -; A=79-153.
DR PDB; 4HWT; X-ray; 2.30 A; A/B=321-723.
DR PDBsum; 1WWT; -.
DR PDBsum; 4HWT; -.
DR ProteinModelPortal; P26639; -.
DR SMR; P26639; 81-721.
DR IntAct; P26639; 12.
DR MINT; MINT-3010570; -.
DR STRING; 9606.ENSP00000265112; -.
DR BindingDB; P26639; -.
DR ChEMBL; CHEMBL3391; -.
DR DrugBank; DB00156; L-Threonine.
DR PhosphoSite; P26639; -.
DR DMDM; 60267755; -.
DR PaxDb; P26639; -.
DR PeptideAtlas; P26639; -.
DR PRIDE; P26639; -.
DR DNASU; 6897; -.
DR Ensembl; ENST00000265112; ENSP00000265112; ENSG00000113407.
DR Ensembl; ENST00000455217; ENSP00000387710; ENSG00000113407.
DR Ensembl; ENST00000502553; ENSP00000424387; ENSG00000113407.
DR GeneID; 6897; -.
DR KEGG; hsa:6897; -.
DR UCSC; uc011coc.3; human.
DR CTD; 6897; -.
DR GeneCards; GC05P033476; -.
DR H-InvDB; HIX0004790; -.
DR HGNC; HGNC:11572; TARS.
DR HPA; HPA037425; -.
DR MIM; 187790; gene.
DR neXtProt; NX_P26639; -.
DR PharmGKB; PA36337; -.
DR eggNOG; COG0441; -.
DR HOGENOM; HOG000003878; -.
DR HOVERGEN; HBG059513; -.
DR InParanoid; P26639; -.
DR KO; K01868; -.
DR OMA; GFFYDMS; -.
DR OrthoDB; EOG7JDQX3; -.
DR PhylomeDB; P26639; -.
DR Reactome; REACT_71; Gene Expression.
DR EvolutionaryTrace; P26639; -.
DR GeneWiki; TARS_(gene); -.
DR GenomeRNAi; 6897; -.
DR NextBio; 26959; -.
DR PRO; PR:P26639; -.
DR ArrayExpress; P26639; -.
DR Bgee; P26639; -.
DR CleanEx; HS_TARS; -.
DR Genevestigator; P26639; -.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; NAS:UniProtKB.
DR GO; GO:0004829; F:threonine-tRNA ligase activity; NAS:UniProtKB.
DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; NAS:UniProtKB.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb_cons-dom.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR012675; Beta-grasp_dom.
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; IPR012947; tRNA_SAD.
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; SSF52954; 1.
DR SUPFAM; SSF55186; SSF55186; 1.
DR SUPFAM; SSF81271; SSF81271; 1.
DR TIGRFAMs; TIGR00418; thrS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing;
KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW Isopeptide bond; Ligase; Nucleotide-binding; Phosphoprotein;
KW Polymorphism; Protein biosynthesis; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1 723 Threonine--tRNA ligase, cytoplasmic.
FT /FTId=PRO_0000101119.
FT MOD_RES 243 243 N6-acetyllysine.
FT MOD_RES 298 298 Phosphotyrosine (By similarity).
FT CROSSLNK 222 222 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT VAR_SEQ 110 110 S -> SHTASCKNLSSLASLLASVAIPSSGMPWPPLFFL
FT (in isoform 2).
FT /FTId=VSP_045114.
FT VARIANT 21 21 G -> D (in dbSNP:rs34334786).
FT /FTId=VAR_034533.
FT CONFLICT 164 164 A -> G (in Ref. 1; AAB04939).
FT CONFLICT 350 350 A -> V (in Ref. 1; AAB04939).
FT CONFLICT 417 417 C -> S (in Ref. 1; AAB04939).
FT CONFLICT 439 439 V -> G (in Ref. 1; AAB04939).
FT CONFLICT 453 453 T -> I (in Ref. 5; AAH10578).
FT CONFLICT 581 581 D -> E (in Ref. 1; AAB04939).
FT CONFLICT 612 612 W -> LA (in Ref. 1; AAB04939).
FT CONFLICT 636 636 K -> N (in Ref. 1; AAB04939).
FT CONFLICT 683 683 S -> T (in Ref. 1; AAB04939).
FT STRAND 82 86
FT STRAND 92 96
FT TURN 97 99
FT HELIX 102 108
FT TURN 111 113
FT HELIX 114 116
FT STRAND 120 127
FT STRAND 129 131
FT STRAND 135 141
FT HELIX 323 329
FT STRAND 332 334
FT HELIX 347 366
FT STRAND 376 379
FT HELIX 380 385
FT HELIX 388 391
FT HELIX 393 395
FT STRAND 398 401
FT STRAND 404 408
FT HELIX 413 421
FT HELIX 427 429
FT STRAND 431 436
FT STRAND 439 441
FT HELIX 446 448
FT TURN 451 453
FT STRAND 456 459
FT STRAND 462 467
FT HELIX 469 471
FT HELIX 472 490
FT STRAND 493 499
FT HELIX 509 525
FT STRAND 530 533
FT STRAND 543 549
FT STRAND 555 565
FT HELIX 566 570
FT STRAND 587 595
FT HELIX 597 607
FT TURN 608 610
FT HELIX 614 616
FT STRAND 621 627
FT HELIX 628 630
FT HELIX 631 642
FT TURN 643 645
FT STRAND 648 650
FT HELIX 658 667
FT STRAND 671 676
FT HELIX 678 683
FT STRAND 685 690
FT STRAND 695 700
FT HELIX 701 713
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
//
MIM
187790
*RECORD*
*FIELD* NO
187790
*FIELD* TI
*187790 THREONYL-tRNA SYNTHETASE; TARS
*FIELD* TX
Arfin et al. (1985) assigned the gene for threonyl-tRNA synthetase to
read morechromosome 5 by study of somatic cell hybrids. Of the 7 aminoacyl-tRNA
synthetase genes mapped to that time, 4 were known to be on chromosome
5, which represents only about 7% of the total human genome. By study of
human-hamster cell hybrids, Arfin et al. (1985) determined that TARS is
very closely linked to LARS (151350); the latter is located at
5pter-q11, according to Arfin et al. (1985). Gerken et al. (1986) mapped
the TARS gene to 5p13-cen by an analysis of isoelectric focusing
patterns of this enzyme from human x Chinese hamster interspecific
somatic cell hybrids. The gene is close to the gene for LARS which, they
stated, maps to 5cen-q11.
*FIELD* RF
1. Arfin, S.; Carlock, L.; Gerken, S.; Wasmuth, J.: Clustering of
genes encoding aminoacyl-tRNA synthetases on human chromosome 5.
(Abstract) Am. J. Hum. Genet. 37: A228 only, 1985.
2. Gerken, S. C.; Wasmuth, J. J.; Arfin, S. M.: Threonyl-tRNA synthetase
gene maps close to leucyl-tRNA synthetase gene on human chromosome
5. Somat. Cell Molec. Genet. 12: 519-522, 1986.
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
marie: 3/25/1988
marie: 12/16/1986
reenie: 6/2/1986
*RECORD*
*FIELD* NO
187790
*FIELD* TI
*187790 THREONYL-tRNA SYNTHETASE; TARS
*FIELD* TX
Arfin et al. (1985) assigned the gene for threonyl-tRNA synthetase to
read morechromosome 5 by study of somatic cell hybrids. Of the 7 aminoacyl-tRNA
synthetase genes mapped to that time, 4 were known to be on chromosome
5, which represents only about 7% of the total human genome. By study of
human-hamster cell hybrids, Arfin et al. (1985) determined that TARS is
very closely linked to LARS (151350); the latter is located at
5pter-q11, according to Arfin et al. (1985). Gerken et al. (1986) mapped
the TARS gene to 5p13-cen by an analysis of isoelectric focusing
patterns of this enzyme from human x Chinese hamster interspecific
somatic cell hybrids. The gene is close to the gene for LARS which, they
stated, maps to 5cen-q11.
*FIELD* RF
1. Arfin, S.; Carlock, L.; Gerken, S.; Wasmuth, J.: Clustering of
genes encoding aminoacyl-tRNA synthetases on human chromosome 5.
(Abstract) Am. J. Hum. Genet. 37: A228 only, 1985.
2. Gerken, S. C.; Wasmuth, J. J.; Arfin, S. M.: Threonyl-tRNA synthetase
gene maps close to leucyl-tRNA synthetase gene on human chromosome
5. Somat. Cell Molec. Genet. 12: 519-522, 1986.
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
marie: 3/25/1988
marie: 12/16/1986
reenie: 6/2/1986