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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.

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Protein Name: Alanine--tRNA ligase, cytoplasmic

UniprotKB/SwissProt ID: P50475 (P50475)

Gene Name: Aars1

Organism: Rattus norvegicus (Rat)

Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain. In presence of high levels of lactate, also acts as a protein lactyltransferase that mediates lactylation of lysine residues in target proteins, such as TEAD1, TP53/p53 and YAP1. Protein lactylation takes place in a two-step reaction: lactate is first activated by ATP to form lactate-AMP and then transferred to lysine residues of target proteins. Acts as an inhibitor of TP53/p53 activity by catalyzing lactylation of TP53/p53. Acts as a positive regulator of the Hippo pathway by mediating lactylation of TEAD1 and YAP1

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Nucleus

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR045864 aa-tRNA-synth_II/BPL/LPL
IPR002318 Ala-tRNA-lgiase_IIc
IPR018162 Ala-tRNA-ligase_IIc_anticod-bd
IPR018165 Ala-tRNA-synth_IIc_core
IPR018164 Ala-tRNA-synth_IIc_N
IPR050058 Ala-tRNA_ligase
IPR023033 Ala_tRNA_ligase_euk/bac
IPR003156 DHHA1_dom
IPR018163 Thr/Ala-tRNA-synth_IIc_edit
IPR009000 Transl_B-barrel_sf
IPR012947 tRNA_SAD

The S-nitrosylation sites of P50475

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 501 SDSSGSYVFE C TVATVLALRR   
2 533 QECGVVLDKT C FYAEQGGQIF   
3 901 TVDNEAGKIT C LCQVPQNAAN