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TARS
Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged tRNA(Thr) via its editing domain, at the post-transfer stage. Belongs to the class-II aminoacyl-tRNA synthetase family. 2 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
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| Protein type: Aminoacyl-tRNA synthetase; EC 6.1.1.3; Ligase; Translation; Translation regulation |
| Chromosomal Location of mouse Ortholog: 15 A1|15 5.6 cM |
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Cellular Component:
cytoplasm
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Molecular Function:
aminoacyl-tRNA ligase activity; ATP binding; identical protein binding; ligase activity; nucleotide binding; threonine-tRNA ligase activity; zinc ion binding
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Biological Process:
threonyl-tRNA aminoacylation; translation; tRNA aminoacylation; tRNA aminoacylation for protein translation
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Reference #:
Q9D0R2
(UniProtKB)
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Alt. Names/Synonyms: D15Wsu59; D15Wsu59e; SYTC; Tars; Tars1; Threonine--tRNA ligase; Threonine--tRNA ligase 1, cytoplasmic; Threonine--tRNA ligase, cytoplasmic; threonyl-tRNA synthetase; Threonyl-tRNA synthetase 1; Threonyl-tRNA synthetase, cytoplasmic; ThrRS
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Gene Symbols: Tars1
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Molecular weight:
83,356 Da
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Basal Isoelectric point:
7.03
Predict pI for various phosphorylation states
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