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 human Ortholog: 5p13.3 |
Cellular Component:
cytosol
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Molecular Function:
ATP binding; identical protein binding; protein binding; threonine-tRNA ligase activity; tRNA binding; zinc ion binding
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Biological Process:
threonyl-tRNA aminoacylation
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Disease: Trichothiodystrophy 7, Nonphotosensitive
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Reference #:
P26639
(UniProtKB)
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Alt. Names/Synonyms: MGC9344; SYTC; TARS; TARS1; threonine tRNA ligase 1, cytoplasmic; Threonine--tRNA ligase; Threonine--tRNA ligase 1, cytoplasmic; Threonine--tRNA ligase, cytoplasmic; threonyl-tRNA synthetase; Threonyl-tRNA synthetase 1; Threonyl-tRNA synthetase, cytoplasmic; ThrRS; TTD7
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Gene Symbols: TARS1
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Molecular weight:
83,435 Da
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Basal Isoelectric point:
6.23
Predict pI for various phosphorylation states
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