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Details on Person UniProt:Q5JTZ9 AARS2
| Class:Id | ReferenceGeneProduct:250002 |
|---|---|
| _chainChangeLog | transit peptide:1-23 added on Fri February 6 2015;chain:24-985 added on Fri February 6 2015 |
| _displayName | UniProt:Q5JTZ9 AARS2 |
| _timestamp | 2025-02-21 20:15:05 |
| chain | transit peptide:1-23 chain:24-985 |
| checksum | 721368BD05474F86 |
| comment | 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 (PubMed:21549344). In presence of high levels of lactate, also acts as a protein lactyltransferase that mediates lactylation of lysine residues in target proteins, such as CGAS (PubMed:39322678). Acts as an inhibitor of cGAS/STING signaling by catalyzing lactylation of CGAS, preventing the formation of liquid-like droplets in which CGAS is activated (PubMed:39322678).CATALYTIC ACTIVITY tRNA(Ala) + L-alanine + ATP = L-alanyl-tRNA(Ala) + AMP + diphosphateCATALYTIC ACTIVITY (S)-lactate + ATP + H(+) = (S)-lactoyl-AMP + diphosphateCATALYTIC ACTIVITY (S)-lactoyl-AMP + L-lysyl-[protein] = N(6)-[(S)-lactoyl]-L-lysyl-[protein] + AMP + 2 H(+)COFACTOR Binds 1 zinc ion per subunit.SUBUNIT Monomer.INTERACTION Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE The disease is caused by variants affecting the gene represented in this entry.SIMILARITY Belongs to the class-II aminoacyl-tRNA synthetase family.CAUTION Given that AARS2 is a mitochondrial protein, it is unclear how it can mediate lactylation of CGAS, which localizes in the cytosol and nucleus.SEQUENCE CAUTION Extended N-terminus. |
| created | [InstanceEdit:217385] Schmidt, EE, 2008-03-27 06:23:53 |
| description | recommendedName: fullName evidence="2"Alanine--tRNA ligase, mitochondrial ecNumber evidence="2"6.1.1.7 alternativeName: fullName evidence="2"Alanyl-tRNA synthetase shortName evidence="2"AlaRS alternativeName: fullName evidence="9"Protein lactyltransferase AARS2 ecNumber evidence="8"6.-.-.- |
| geneName | AARS2 AARSL KIAA1270 |
| identifier | Q5JTZ9 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Aminoacyl-tRNA synthetase ATP-binding Cardiomyopathy Disease variant Ligase Metal-binding Mitochondrion Neurodegeneration Nucleotide-binding Premature ovarian failure Primary mitochondrial disease Protein biosynthesis Proteomics identification Reference proteome RNA-binding Transit peptide tRNA-binding Zinc |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9862192] Weiser, Joel, 2024-02-26 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21 |
| name | AARS2 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8990434] ENSEMBL:ENSG00000124608 AARS2 [Homo sapiens] |
| secondaryIdentifier | SYAM_HUMAN A2RRN5 Q8N198 Q96D02 Q9ULF0 |
| sequenceLength | 985 |
| species | [Species:48887] Homo sapiens |
| (referenceEntity) | [EntityWithAccessionedSequence:379653] AARS2 [mitochondrial matrix] [Homo sapiens] |
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No pathways have been reviewed or authored by UniProt:Q5JTZ9 AARS2 (250002)
