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Protein

Threonine--tRNA ligase, cytoplasmic

Gene

Tars

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr).

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Threonine--tRNA ligase, cytoplasmic (EC:6.1.1.3)
Alternative name(s):
Threonyl-tRNA synthetase
Short name:
ThrRS
Gene namesi
Name:Tars
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:106314. Tars.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 722722Threonine--tRNA ligase, cytoplasmicPRO_0000101120Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki221 – 221Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei242 – 2421N6-acetyllysineCombined sources
Modified residuei245 – 2451PhosphothreonineBy similarity
Modified residuei297 – 2971PhosphotyrosineCombined sources
Modified residuei452 – 4521PhosphothreonineBy similarity

Post-translational modificationi

ISGylated.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9D0R2.
MaxQBiQ9D0R2.
PaxDbiQ9D0R2.
PeptideAtlasiQ9D0R2.
PRIDEiQ9D0R2.

PTM databases

iPTMnetiQ9D0R2.
PhosphoSiteiQ9D0R2.
SwissPalmiQ9D0R2.

Expressioni

Gene expression databases

BgeeiQ9D0R2.
CleanExiMM_TARS.
GenevisibleiQ9D0R2. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi226055. 3 interactions.
IntActiQ9D0R2. 1 interaction.
MINTiMINT-2514453.
STRINGi10090.ENSMUSP00000022849.

Structurei

3D structure databases

ProteinModelPortaliQ9D0R2.
SMRiQ9D0R2. Positions 80-722.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1637. Eukaryota.
COG0441. LUCA.
GeneTreeiENSGT00390000002149.
HOGENOMiHOG000003878.
HOVERGENiHBG059513.
InParanoidiQ9D0R2.
KOiK01868.
OMAiYGEEKSE.
OrthoDBiEOG7JDQX3.
PhylomeDBiQ9D0R2.
TreeFamiTF300858.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
3.40.50.800. 1 hit.
HAMAPiMF_00184. Thr_tRNA_synth.
InterProiIPR002314. aa-tRNA-synt_IIb.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR012675. Beta-grasp_dom.
IPR004095. TGS.
IPR012676. TGS-like.
IPR002320. Thr-tRNA-ligase_IIa.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF03129. HGTP_anticodon. 1 hit.
PF02824. TGS. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSiPR01047. TRNASYNTHTHR.
SMARTiSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMiSSF52954. SSF52954. 1 hit.
SSF55186. SSF55186. 1 hit.
SSF81271. SSF81271. 1 hit.
TIGRFAMsiTIGR00418. thrS. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9D0R2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQEKASSPS GKMDGEKPVD ASEEKRKEGG KKKSKDGGGD GGRAELNPWP
60 70 80 90 100
EYINTRLDMY NKLKAEHDSI LAEKAAKDSK PIKVTLPDGK QVDAESWKTT
110 120 130 140 150
PYQIACGISQ GLADNTVVAK VNKVVWDLDR PLETDCTLEL LKFEDEEAQA
160 170 180 190 200
VYWHSSAHIM GEAMERVYGG CLCYGPPIEN GFYYDMYLEE GGVSSNDFSS
210 220 230 240 250
LETLCKKIIK EKQTFERLEV KKETLLEMFK YNKFKCRILN EKVNTPTTTV
260 270 280 290 300
YRCGPLIDLC RGPHVRHTGK IKTLKIHKNS STYWEGKADM ETLQRIYGIS
310 320 330 340 350
FPDPKLLKEW EKFQEEAKNR DHRKIGRDQE LYFFHELSPG SCFFLPKGAY
360 370 380 390 400
IYNTLMEFIR SEYRKRGFQE VVTPNIFNSR LWMTSGHWQH YSENMFSFEV
410 420 430 440 450
EKEQFALKPM NCPGHCLMFD HRPRSWRELP LRLADFGVLH RNELSGALTG
460 470 480 490 500
LTRVRRFQQD DAHIFCAMEQ IEDEIKGCLD FLRTVYSVFG FSFKLNLSTR
510 520 530 540 550
PEKFLGDIEI WNQAEKQLEN SLNEFGEKWE LNPGDGAFYG PKIDIQIKDA
560 570 580 590 600
IGRYHQCATI QLDFQLPIRF NLTYVSHDGD DKKRPVIVHR AILGSVERMI
610 620 630 640 650
AILTENYGGK WPFWLSPRQV MVVPVGPTCD EYAQKVRQQF HDAKFMADTD
660 670 680 690 700
LDPGCTLNKK IRNAQLAQYN FILVVGEKEK ASGTVNIRTR DNKVHGERTV
710 720
EETVRRLQQL KQTRSKQAEE EF
Length:722
Mass (Da):83,356
Last modified:March 1, 2003 - v2
Checksum:iFFBA7DC409BFD0B1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti176 – 1761P → S in BAB26799 (PubMed:16141072).Curated
Sequence conflicti271 – 2711I → T in BAB26799 (PubMed:16141072).Curated
Sequence conflicti322 – 3221H → Y in AAH55371 (PubMed:15489334).Curated
Sequence conflicti323 – 3231R → G in BAB26799 (PubMed:16141072).Curated
Sequence conflicti325 – 3251I → T in AAH55371 (PubMed:15489334).Curated
Sequence conflicti563 – 5631D → Y in BAC27235 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010256 mRNA. Translation: BAB26799.1.
AK011146 mRNA. Translation: BAB27429.2.
AK031064 mRNA. Translation: BAC27235.1.
AK152945 mRNA. Translation: BAE31616.1.
AK166693 mRNA. Translation: BAE38950.1.
AK167597 mRNA. Translation: BAE39654.1.
AK168969 mRNA. Translation: BAE40773.1.
BC055371 mRNA. Translation: AAH55371.1.
CCDSiCCDS27385.1.
RefSeqiNP_149065.2. NM_033074.3.
UniGeneiMm.286061.
Mm.474736.

Genome annotation databases

EnsembliENSMUST00000022849; ENSMUSP00000022849; ENSMUSG00000022241.
GeneIDi110960.
KEGGimmu:110960.
UCSCiuc007vhc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010256 mRNA. Translation: BAB26799.1.
AK011146 mRNA. Translation: BAB27429.2.
AK031064 mRNA. Translation: BAC27235.1.
AK152945 mRNA. Translation: BAE31616.1.
AK166693 mRNA. Translation: BAE38950.1.
AK167597 mRNA. Translation: BAE39654.1.
AK168969 mRNA. Translation: BAE40773.1.
BC055371 mRNA. Translation: AAH55371.1.
CCDSiCCDS27385.1.
RefSeqiNP_149065.2. NM_033074.3.
UniGeneiMm.286061.
Mm.474736.

3D structure databases

ProteinModelPortaliQ9D0R2.
SMRiQ9D0R2. Positions 80-722.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi226055. 3 interactions.
IntActiQ9D0R2. 1 interaction.
MINTiMINT-2514453.
STRINGi10090.ENSMUSP00000022849.

PTM databases

iPTMnetiQ9D0R2.
PhosphoSiteiQ9D0R2.
SwissPalmiQ9D0R2.

Proteomic databases

EPDiQ9D0R2.
MaxQBiQ9D0R2.
PaxDbiQ9D0R2.
PeptideAtlasiQ9D0R2.
PRIDEiQ9D0R2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022849; ENSMUSP00000022849; ENSMUSG00000022241.
GeneIDi110960.
KEGGimmu:110960.
UCSCiuc007vhc.1. mouse.

Organism-specific databases

CTDi6897.
MGIiMGI:106314. Tars.

Phylogenomic databases

eggNOGiKOG1637. Eukaryota.
COG0441. LUCA.
GeneTreeiENSGT00390000002149.
HOGENOMiHOG000003878.
HOVERGENiHBG059513.
InParanoidiQ9D0R2.
KOiK01868.
OMAiYGEEKSE.
OrthoDBiEOG7JDQX3.
PhylomeDBiQ9D0R2.
TreeFamiTF300858.

Miscellaneous databases

ChiTaRSiTars. mouse.
PROiQ9D0R2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D0R2.
CleanExiMM_TARS.
GenevisibleiQ9D0R2. MM.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
3.40.50.800. 1 hit.
HAMAPiMF_00184. Thr_tRNA_synth.
InterProiIPR002314. aa-tRNA-synt_IIb.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR012675. Beta-grasp_dom.
IPR004095. TGS.
IPR012676. TGS-like.
IPR002320. Thr-tRNA-ligase_IIa.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF03129. HGTP_anticodon. 1 hit.
PF02824. TGS. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSiPR01047. TRNASYNTHTHR.
SMARTiSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMiSSF52954. SSF52954. 1 hit.
SSF55186. SSF55186. 1 hit.
SSF81271. SSF81271. 1 hit.
TIGRFAMsiTIGR00418. thrS. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Amnion, Bone marrow, Forelimb and Heart.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C3H/He.
    Tissue: Mesenchymal stem cell.
  3. Cited for: ISGYLATION.
  4. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-297, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  5. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiSYTC_MOUSE
AccessioniPrimary (citable) accession number: Q9D0R2
Secondary accession number(s): Q3TL42
, Q7TMQ2, Q8BMI6, Q9CX03
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: March 1, 2003
Last modified: July 6, 2016
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.