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.
Protein type: Aminoacyl-tRNA synthetase; EC; Ligase; Translation; Translation regulation
Chromosomal Location of Human Ortholog: 15 A1|15 5.6 cM
Cellular Component:  actin cytoskeleton; cytoplasm; cytosol
Molecular Function:  aminoacyl-tRNA ligase activity; ATP binding; ligase activity; nucleotide binding; threonine-tRNA ligase activity
Biological Process:  threonyl-tRNA aminoacylation; translation; tRNA aminoacylation; tRNA aminoacylation for protein translation
Reference #:  Q9D0R2 (UniProtKB)
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
Gene Symbols: Tars
Molecular weight: 83,356 Da
Basal Isoelectric point: 7.03  Predict pI for various phosphorylation states
Select Structure to View Below


Protein Structure Not Found.

Cross-references to other databases:  STRING  |  Reactome  |  BioGPS  |  Pfam  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene