Protein Information

General Information
MoonProt ID393
First appeared in release2.0
Name(s)threonyl aminoacyl-tRNA synthetase, TARS, Threonine-tRNA ligase, cytoplasmic, Gene:TARS
UniProt IDP26639 (SYTC_HUMAN)
GO termsGO:0006412 translation GO:0006418 tRNA aminoacylation for protein translation GO:0006435 threonyl-tRNA aminoacylation GO:0043039 tRNA aminoacylation GO:0000166 nucleotide binding GO:0003723 RNA binding GO:0004812 aminoacyl-tRNA ligase activity GO:0005515 protein binding GO:0005524 ATP binding GO:0016874 ligase activity GO:0016876 ligase activity, forming aminoacyl-tRNA and related compounds GO:0042803 protein homodimerization activity GO:0005737 cytoplasm GO:0005829 cytosol GO:0015629 actin cytoskeleton GO:0070062 extracellular exosome GO:0001944 vasculature development
Organisms for which functions have been demonstratedHomo sapiens (human)
Sequence length723 amino acids
FASTA sequence>sp|P26639|SYTC_HUMAN Threonine--tRNA ligase, cytoplasmic OS=Homo sapiens GN=TARS PE=1 SV=3 MFEEKASSPSGKMGGEEKPIGAGEEKQKEGGKKKNKEGSGDGGRAELNPWPEYIYTRLEMYNILKAEHDSILAEKAEKDSKPIKVTLPDGKQVDAESWKTTPYQIACGISQGLADNTVIAKVNNVVWDLDRPLEEDCTLELLKFEDEEAQAVYWHSSAHIMGEAMERVYGGCLCYGPPIENGFYYDMYLEEGGVSSNDFSSLEALCKKIIKEKQAFERLEVKKETLLAMFKYNKFKCRILNEKVNTPTTTVYRCGPLIDLCRGPHVRHTGKIKALKIHKNSSTYWEGKADMETLQRIYGISFPDPKMLKEWEKFQEEAKNRDHRKIGRDQELYFFHELSPGSCFFLPKGAYIYNALIEFIRSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFEVEKELFALKPMNCPGHCLMFDHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCLDFLRTVYSVFGFSFKLNLSTRPEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFYGPKIDIQIKDAIGRYHQCATIQLDFQLPIRFNLTYVSHDGDDKKRPVIVHRAILGSVERMIAILTENYGGKWPFWLSPRQVMVVPVGPTCDEYAQKVRQQFHDAKFMADIDLDPGCTLNKKIRNAQLAQYNFILVVGEKEKISGTVNIRTRDNKVHGERTISETIERLQQLKEFRSKQAEEEF
Structure Information
PDB ID4HWT, 4TTV, 4P3N
Quaternary structure
Function 1
Function descriptionthreonyl aminoacyl-tRNA synthetase, attaches threonine to tRNA, early step in protein synthesis, ATP + L-threonine + tRNA(Thr) -> AMP + diphosphate + L-threonyl-tRNA(Thr)
References for functionCruzen, Matt E., and Stuart M. Arfin. "Nucleotide and deduced amino acid sequence of human threonyl-tRNA synthetase reveals extensive homology to the Escherichia coli and yeast enzymes." Journal of Biological Chemistry 266.15 (1991): 9919-9923.
E.C. number6.1.1.3
Location of functional site(s)
Cellular location of functioncytoplasm
Comments
Function 2
Function descriptionpromotes vascular development, demostrated this is separate from role in protein synthesis
References for function26271225
E.C. number
Location of functional site(s)
Cellular location of functionextracellular
Commentssecreted from endothelial cells in response to TNF-? and VEGF, association between TARS expression and advancing stage of ovarian cancer, mutation that prevents synthetase activity is still active in promoting vascular development, single amino acid substitutions in TARS can block the anti-angiogenic effects of BC194, indicating that TARS is the specific target of BC194