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Reviewed, UniProtKB/Swiss-Prot Q9D0R2 (SYTC_MOUSE)

Last modified November 3, 2009. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Threonyl-tRNA synthetase, cytoplasmic
    EC=6.1.1.3
Alternative name(s):
    Threonine--tRNA ligase
      Short name=ThrRS
Gene names
Name: Tars
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length722 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

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

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

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Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
Gene Ontology (GO)
   Biological processthreonyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

threonine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 722722Threonyl-tRNA synthetase, cytoplasmic
PRO_0000101120

Amino acid modifications

Modified residue2421N6-acetyllysine By similarity
Modified residue2971Phosphotyrosine Ref.3
Cross-link221Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Sequence conflict1761P → S in BAB26799. Ref.1
Sequence conflict2711I → T in BAB26799. Ref.1
Sequence conflict3221H → Y in AAH55371. Ref.2
Sequence conflict3231R → G in BAB26799. Ref.1
Sequence conflict3251I → T in AAH55371. Ref.2
Sequence conflict5631D → Y in BAC27235. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q9D0R2-1 [UniParc].

Last modified March 1, 2003. Version 2.
Checksum: FFBA7DC409BFD0B1

FASTA72283,356
        10         20         30         40         50         60 
MSQEKASSPS GKMDGEKPVD ASEEKRKEGG KKKSKDGGGD GGRAELNPWP EYINTRLDMY 

        70         80         90        100        110        120 
NKLKAEHDSI LAEKAAKDSK PIKVTLPDGK QVDAESWKTT PYQIACGISQ GLADNTVVAK 

       130        140        150        160        170        180 
VNKVVWDLDR PLETDCTLEL LKFEDEEAQA VYWHSSAHIM GEAMERVYGG CLCYGPPIEN 

       190        200        210        220        230        240 
GFYYDMYLEE GGVSSNDFSS LETLCKKIIK EKQTFERLEV KKETLLEMFK YNKFKCRILN 

       250        260        270        280        290        300 
EKVNTPTTTV YRCGPLIDLC RGPHVRHTGK IKTLKIHKNS STYWEGKADM ETLQRIYGIS 

       310        320        330        340        350        360 
FPDPKLLKEW EKFQEEAKNR DHRKIGRDQE LYFFHELSPG SCFFLPKGAY IYNTLMEFIR 

       370        380        390        400        410        420 
SEYRKRGFQE VVTPNIFNSR LWMTSGHWQH YSENMFSFEV EKEQFALKPM NCPGHCLMFD 

       430        440        450        460        470        480 
HRPRSWRELP LRLADFGVLH RNELSGALTG LTRVRRFQQD DAHIFCAMEQ IEDEIKGCLD 

       490        500        510        520        530        540 
FLRTVYSVFG FSFKLNLSTR PEKFLGDIEI WNQAEKQLEN SLNEFGEKWE LNPGDGAFYG 

       550        560        570        580        590        600 
PKIDIQIKDA IGRYHQCATI QLDFQLPIRF NLTYVSHDGD DKKRPVIVHR AILGSVERMI 

       610        620        630        640        650        660 
AILTENYGGK WPFWLSPRQV MVVPVGPTCD EYAQKVRQQF HDAKFMADTD LDPGCTLNKK 

       670        680        690        700        710        720 
IRNAQLAQYN FILVVGEKEK ASGTVNIRTR DNKVHGERTV EETVRRLQQL KQTRSKQAEE 


EF

« Hide

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References

[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. expand/collapse author list , 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: 16141072] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C3H/He.
Tissue: Mesenchymal stem cell.
[3]"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: 18034455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-297, MASS SPECTROMETRY.
Tissue: Brain.
+Additional computationally mapped references.

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Cross-references

Sequence databases

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.
IPIIPI00468688.
RefSeqNP_149065.2.
UniGeneMm.286061

3D structure databases

HSSPHSSP built from PDB template 1EVL based on UniProtKB P00955.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9D0R2.

PTM databases

PhosphoSiteQ9D0R2.

Proteomic databases

PRIDEQ9D0R2.

Genome annotation databases

EnsemblENSMUST00000022849; ENSMUSP00000022849; ENSMUSG00000022241; Mus musculus. [Genome view]
GeneID110960.
KEGGmmu:110960.
NMPDRfig|10090.3.peg.29705.
UCSCuc007vhc.1. mouse.

Organism-specific databases

CTD110960.
MGIMGI:106314. Tars.

Phylogenomic databases

HOGENOMQ9D0R2.
HOVERGENQ9D0R2.
OMAKLWQTSG.

Enzyme and pathway databases

BRENDA6.1.1.3. 244.

Gene expression databases

ArrayExpressQ9D0R2.
BgeeQ9D0R2.
CleanExMM_TARS.
GenevestigatorQ9D0R2.
GermOnlineENSMUSG00000022241. Mus musculus.

Family and domain databases

InterProIPR002314. aa-tRNA-synt_IIb_cons-reg.
IPR006195. aa-tRNA-synth_II_cons-reg.
IPR004154. Anticodon_bd.
IPR012675. b-grasp_ferredoxin-like.
IPR004095. TGS.
IPR002320. Thr-tRNA-synth_IIa.
IPR018158. Thr-tRNA-synth_IIa_cons-reg.
IPR012947. tRNA_SAD.
[Graphical view]
Gene3DG3DSA:3.40.50.800. Anticodon_bd. 1 hit.
G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF02824. TGS. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSPR01047. TRNASYNTHTHR.
TIGRFAMsTIGR00418. thrS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio365031.
SOURCESearch...

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Entry information

Entry nameSYTC_MOUSE
AccessionPrimary (citable) accession number: Q9D0R2
Secondary accession number(s): Q3TL42 expand/collapse secondary AC list , Q7TMQ2, Q8BMI6, Q9CX03
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: March 1, 2003
Last modified: November 3, 2009
This is version 71 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents