AARS2
entrez
57505
canonical
uniprot
Q5JTZ9
canonical
ensembl
ENSG00000124608
resolver
ensp
ENSP00000244571
resolver
ensp
ENSP00000526794
resolver
enst
ENST00000244571
resolver
genesymbol
AARS2
resolver
genesymbol_syn
AARSL
resolver
genesymbol_syn
KIAA1270
resolver
hgnc
HGNC:21022
resolver
uniprot
A2RRN5
resolver
uniprot
Q8N198
resolver
uniprot
Q96D02
resolver
uniprot
Q9ULF0
resolver
uniprot_entry
SYAM_HUMAN
resolver
uniprot_sec
A2RRN5
resolver
uniprot_sec
Q8N198
resolver
uniprot_sec
Q96D02
resolver
uniprot_sec
Q9ULF0
resolver
amino_acid_sequence
MAASVAAAARRLRRAIRRSPAWRGLSHRPLSSEPPAAKASAVRAAFLNFFRDRHGHRLVPSASVRPRGDPSLLFVNAGMNQFKPIFLGTVDPRSEMAGFRRVANSQKCVRAGGHHNDLEDVGRDLSHHTFFEMLGNWAFGGEYFKEEACNMAWELLTQVYGIPEERLWISYFDGDPKAGLDPDLETRDIWLSLGVPASRVLSFGPQENFWEMGDTGPCGPCTEIHYDLAGGVGAPQLVELWNLVFMQHNREADGSLQPLPQRHVDTGMGLERLVAVLQGKHSTYDTDLFSPLLNAIQQGCRAPPYLGRVGVADEGRTDTAYRVVADHIRTLSVCISDGIFPGMSGPPLVLRRILRRAVRFSMEILKAPPGFLGSLVPVVVETLGDAYPELQRNSAQIANLVSEDEAAFLASLERGRRIIDRTLRTLGPSDMFPAEVAWSLSLCGDLGLPLDMVELMLEEKGVQLDSAGLERLAQEEAQHRARQAEPVQKQGLWLDVHALGELQRQGVPPTDDSPKYNYSLRPSGSYEFGTCEAQVLQLYTEDGTAVASVGKGQRCGLLLDRTNFYAEQGGQASDRGYLVRAGQEDVLFPVARAQVCGGFILHEAVAPECLRLGDQVQLHVDEAWRLGCMAKHTATHLLNWALRQTLGPGTEQQGSHLNPEQLRLDVTTQTPLTPEQLRAVENTVQEAVGQDEAVYMEEVPLALTAQVPGLRSLDEVYPDPVRVVSVGVPVAHALDPASQAALQTSVELCCGTHLLRTGAVGDLVIIGDRQLSKGTTRLLAVTGEQAQQARELGQSLAQEVKAATERLSLGSRDVAEALRLSKDIGRLIEAVETAVMPQWQRRELLATVKMLQRRANTAIRKLQMGQAAKKTQELLERHSKGPLIVDTVSAESLSVLVKVVRQLCEQAPSTSVLLLSPQPMGKVLCACQVAQGAMPTFTAEAWALAVCSHMGGKAWGSRVVAQGTGSTTDLEAALSIAQTYALSQL
uniprot
proteins
disease_involvement
DISEASE: Combined oxidative phosphorylation deficiency 8 (COXPD8) [MIM:614096]: A mitochondrial disease characterized by a lethal infantile hypertrophic cardiomyopathy, generalized muscle dysfunction and some neurologic involvement. The liver is not affected. {ECO:0000269|PubMed:21549344}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Leukoencephalopathy, progressive, with ovarian failure (LKENP) [MIM:615889]: An autosomal recessive neurodegenerative disorder characterized by childhood- to adulthood-onset of signs of neurologic deterioration consisting of ataxia, spasticity, and cognitive decline with features of frontal lobe dysfunction. Brain MRI shows leukoencephalopathy with striking involvement of deep white matter, and cerebellar atrophy. All female patients develop premature ovarian failure. {ECO:0000269|PubMed:24808023}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
6.-.-.-
uniprot
proteins
ec_number
6.1.1.7
uniprot
proteins
function
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). {ECO:0000269|PubMed:21549344, ECO:0000269|PubMed:39322678}.
uniprot
proteins
mass_dalton
107340
uniprot
proteins
mutagenesis
MUTAGEN 79; /note="M->A: In mutant 5A; abolished binding to lactate and protein lactylation; when associated with A-110, A-242 and 265-A--A-267."; /evidence="ECO:0000269|PubMed:39322678"; MUTAGEN 110; /note="R->A: In mutant 5A; abolished binding to lactate and protein lactylation; when associated with A-79, A-242 and 265-A--A-267. In ATP-binding mutant; abolished ability to mediate protein lactylation; when associated with A-210 and A-269."; /evidence="ECO:0000269|PubMed:39322678"; MUTAGEN 210; /note="W->A: In ATP-binding mutant; abolished ability to mediate protein lactylation; when associated with A-110 and A-269."; /evidence="ECO:0000269|PubMed:39322678"; MUTAGEN 242; /note="N->A: In mutant 5A; abolished binding to lactate and protein lactylation; when associated with A-79, A-110 and 265-A--A-267."; /evidence="ECO:0000269|PubMed:39322678"; MUTAGEN 265..267; /note="DTG->ATA: In mutant 5A; abolished binding to lactate and protein lactylation; when associated with A-79, A-110 and A-242."; /evidence="ECO:0000269|PubMed:39322678"; MUTAGEN 269; /note="G->A: In ATP-binding mutant; abolished ability to mediate protein lactylation; when associated with A-110 and A-210."; /evidence="ECO:0000269|PubMed:39322678
uniprot
proteins
protein_family
Class-II aminoacyl-tRNA synthetase family
uniprot
proteins
pubmed
10574462
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15779907
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21549344
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24808023
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
34585293
uniprot
proteins
pubmed
39322678
uniprot
proteins
sequence_length
985
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03133, ECO:0000269|PubMed:21549344}.
uniprot
proteins