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 6.1.1.3; Ligase; Translation; Translation regulation
Chromosomal Location of Human Ortholog: 5p13.3
Cellular Component:  actin cytoskeleton; cytoplasm; cytosol
Molecular Function:  ATP binding; protein binding; protein homodimerization activity; threonine-tRNA ligase activity; tRNA binding
Biological Process:  threonyl-tRNA aminoacylation; translation; tRNA aminoacylation for protein translation
Disease: Trichothiodystrophy 7, Nonphotosensitive
Reference #:  P26639 (UniProtKB)
Alt. Names/Synonyms: MGC9344; SYTC; TARS; threonine tRNA ligase 1, cytoplasmic; Threonine--tRNA ligase; Threonine--tRNA ligase, cytoplasmic; threonyl-tRNA synthetase; Threonyl-tRNA synthetase, cytoplasmic; ThrRS
Gene Symbols: TARS
Molecular weight: 83,435 Da
Basal Isoelectric point: 6.23  Predict pI for various phosphorylation states
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TARS

Protein Structure Not Found.


Cross-references to other databases:  STRING  |  cBioPortal  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  InnateDB