Tyrosyl-Trna Synthetase (YARS) Antibody – Rabbit Polyclonal

Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. Tyrosyl-tRNA synthetase belongs to the class I tRNA synthetase family. Cytokine activities have also been observed for the human tyrosyl-tRNA synthetase, after it is split into two parts, an N-terminal fragment that harbors the catalytic site and a C-terminal fragment found only in the mammalian enzyme. The N-terminal fragment is an interleukin-8-like cytokine, whereas the released C-terminal fragment is an EMAP II-like cytokine. [provided by RefSeq, Jul 2008]

YARS: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr). Defects in YARS are the cause of Charcot-Marie-Tooth disease dominant intermediate type C (CMTDIC). CMTDIC is a form of Charcot-Marie-Tooth disease characterized by clinical and pathologic features intermediate between demyelinating and axonal peripheral neuropathies, and motor median nerve conduction velocities ranging from 25 to 45 m/sec. Belongs to the class-I aminoacyl-tRNA synthetase family.

Protein type: Ligase; EC 6.1.1.1

Chromosomal Location of Human Ortholog: 1p35.1

Cellular Component: cytoplasm; cytosol; extracellular space; nucleus

Molecular Function: ATP binding; interleukin-8 receptor binding; signal transducer activity; tRNA binding; tyrosine-tRNA ligase activity; valine-tRNA ligase activity

Biological Process: apoptosis; gene expression; signal transduction; tRNA aminoacylation for protein translation; tyrosyl-tRNA aminoacylation

Disease: Charcot-marie-tooth Disease, Dominant Intermediate C