\
logo
  Home | Contact us | Browse | Quick Search by UniProtKB ID, Keyword, PDBID

Menu:

Latest news:

Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

Read more...


Protein Name: Threonine--tRNA ligase 2, cytoplasmic

UniprotKB/SwissProt ID: A2RTX5 (A2RTX5)

Gene Name: TARS3

Organism: Homo sapiens (Human)

Function: 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

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Nucleus

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR002314 aa-tRNA-synt_IIb
IPR006195 aa-tRNA-synth_II
IPR045864 aa-tRNA-synth_II/BPL/LPL
IPR004154 Anticodon-bd
IPR036621 Anticodon-bd_dom_sf
IPR012675 Beta-grasp_dom_sf
IPR004095 TGS
IPR012676 TGS-like
IPR002320 Thr-tRNA-ligase_IIa
IPR018163 Thr/Ala-tRNA-synth_IIc_edit
IPR047246 ThrRS_anticodon
IPR033728 ThrRS_core
IPR012947 tRNA_SAD

The S-nitrosylation sites of A2RTX5

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 637 IKDAIGRYHQ C ATIQLDFQLP