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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: P49588 (P49588)

Gene Name: AARS1

Organism: Homo sapiens (Human)

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) (PubMed:27622773, PubMed:27911835, PubMed:28493438, PubMed:33909043). Also edits incorrectly charged tRNA(Ala) via its editing domain (PubMed:27622773, PubMed:27911835, PubMed:28493438, PubMed:29273753). 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 (PubMed:38512451, PubMed:38653238). 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 (PubMed:38512451, PubMed:38653238, PubMed:39322678). Acts as an inhibitor of TP53/p53 activity by catalyzing lactylation of TP53/p53 (PubMed:38653238). Acts as a positive regulator of the Hippo pathway by mediating lactylation of TEAD1 and YAP1 (PubMed:38512451)

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 P49588

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 152 EAAGLEADLE C KQIWQNLGLD   
2 184 NFWEMGDTGP C GPCSEIHYDR   
3 525 FVEEVSTGQE C GVVLDKTCFY   
4 533 QECGVVLDKT C FYAEQGGQIY   
5 671 EAAKAVYTQD C PLAAAKAIQG   
6 723 PAGSLTSVEF C GGTHLRNSSH   
7 773 ALRKAESLKK C LSVMEAKVKA   
8 901 TVDNEAGKIT C LCQVPQNAAN   
9 903 DNEAGKITCL C QVPQNAANRG   
10 947 SAQATGKNVG C LQEALQLATS