LARS1
entrez
51520
canonical
uniprot
Q9P2J5
canonical
ensembl
ENSG00000133706
resolver
ensp
ENSP00000377954
resolver
ensp
ENSP00000426005
resolver
ensp
ENSP00000501365
resolver
ensp
ENSP00000501376
resolver
ensp
ENSP00000501434
resolver
enst
ENST00000674270
resolver
enst
ENST00000674447
resolver
genesymbol
LARS1
resolver
genesymbol_syn
KIAA1352
resolver
genesymbol_syn
LARS
resolver
hgnc
HGNC:6512
resolver
uniprot
A0A6I8PL42
resolver
uniprot
A0A6I8PRC9
resolver
uniprot
A2RRR4
resolver
uniprot
A7E266
resolver
uniprot
B4DER1
resolver
uniprot
B4DJ10
resolver
uniprot
B4E266
resolver
uniprot
Q2TU79
resolver
uniprot
Q9NSE1
resolver
uniprot_entry
A0A6I8PL42_HUMAN
resolver
uniprot_entry
A0A6I8PRC9_HUMAN
resolver
uniprot_entry
B4DER1_HUMAN
resolver
uniprot_entry
B4E266_HUMAN
resolver
uniprot_entry
SYLC_HUMAN
resolver
uniprot_sec
A2RRR4
resolver
uniprot_sec
A7E266
resolver
uniprot_sec
B4DJ10
resolver
uniprot_sec
Q2TU79
resolver
uniprot_sec
Q9NSE1
resolver
activity_regulation
ACTIVITY REGULATION: 5-fluoro-1,3-dihydro-1-hydroxy-1,2-benzoxaborole inhibits LARS1 by forming a covalent adduct with the 3' adenosine of tRNA(Leu) at the editing site, thus locking the enzyme in an inactive conformation.
uniprot
proteins
amino_acid_sequence
MAERKGTAKVDFLKKIEKEIQQKWDTERVFEVNASNLEKQTSKGKYFVTFPYPYMNGRLHLGHTFSLSKCEFAVGYQRLKGKCCLFPFGLHCTGMPIKACADKLKREIELYGCPPDFPDEEEEEEETSVKTEDIIIKDKAKGKKSKAAAKAGSSKYQWGIMKSLGLSDEEIVKFSEAEHWLDYFPPLAIQDLKRMGLKVDWRRSFITTDVNPYYDSFVRWQFLTLRERNKIKFGKRYTIYSPKDGQPCMDHDRQTGEGVGPQEYTLLKLKVLEPYPSKLSGLKGKNIFLVAATLRPETMFGQTNCWVRPDMKYIGFETVNGDIFICTQKAARNMSYQGFTKDNGVVPVVKELMGEEILGASLSAPLTSYKVIYVLPMLTIKEDKGTGVVTSVPSDSPDDIAALRDLKKKQALRAKYGIRDDMVLPFEPVPVIEIPGFGNLSAVTICDELKIQSQNDREKLAEAKEKIYLKGFYEGIMLVDGFKGQKVQDVKKTIQKKMIDAGDALIYMEPEKQVMSRSSDECVVALCDQWYLDYGEENWKKQTSQCLKNLETFCEETRRNFEATLGWLQEHACSRTYGLGTHLPWDEQWLIESLSDSTIYMAFYTVAHLLQGGNLHGQAESPLGIRPQQMTKEVWDYVFFKEAPFPKTQIAKEKLDQLKQEFEFWYPVDLRVSGKDLVPNHLSYYLYNHVAMWPEQSDKWPTAVRANGHLLLNSEKMSKSTGNFLTLTQAIDKFSADGMRLALADAGDTVEDANFVEAMADAGILRLYTWVEWVKEMVANWDSLRSGPASTFNDRVFASELNAGIIKTDQNYEKMMFKEALKTGFFEFQAAKDKYRELAVEGMHRELVFRFIEVQTLLLAPFCPHLCEHIWTLLGKPDSIMNASWPVAGPVNEVLIHSSQYLMEVTHDLRLRLKNYMMPAKGKKTDKQPLQKPSHCTIYVAKNYPPWQHTTLSVLRKHFEANNGKLPDNKVIASELGSMPELKKYMKKVMPFVAMIKENLEKMGPRILDLQLEFDEKAVLMENIVYLTNSLELEHIEVKFASEAEDKIREDCCPGKPLNVFRIEPGVSVSLVNPQPSNGHFSTKIEIRQGDNCDSIIRRLMKMNRGIKDLSKVKLMRFDDPLLGPRRVPVLGKEYTEKTPISEHAVFNVDLMSKKIHLTENGIRVDIGDTIIYLVH
uniprot
proteins
disease_involvement
DISEASE: Infantile liver failure syndrome 1 (ILFS1) [MIM:615438]: A life-threatening disorder of hepatic function that manifests with acute liver failure in the first few months of life. Clinical features include anemia, renal tubulopathy, developmental delay, seizures, failure to thrive, and liver steatosis and fibrosis. {ECO:0000269|PubMed:22607940}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
6.1.1.4
uniprot
proteins
function
FUNCTION: Aminoacyl-tRNA synthetase that catalyzes the specific attachment of leucine to its cognate tRNA (tRNA(Leu)) (PubMed:25051973, PubMed:32232361). It performs tRNA aminoacylation in a two-step reaction: Leu is initially activated by ATP to form a leucyl-adenylate (Leu-AMP) intermediate; then the leucyl moiety is transferred to the acceptor 3' end of the tRNA to yield leucyl-tRNA (PubMed:25051973). To improve the fidelity of catalytic reactions, it is also able to hydrolyze misactivated aminoacyl-adenylate intermediates (pre-transfer editing) and mischarged aminoacyl-tRNAs (post-transfer editing) (PubMed:25051973). {ECO:0000269|PubMed:19426743, ECO:0000269|PubMed:25051973, ECO:0000269|PubMed:32232361}.
uniprot
proteins
mass_dalton
134466
uniprot
proteins
mutagenesis
MUTAGEN 236..256; /note="Missing: Loss of leucyl-tRNA ligase activity. Decreased activity in post-transfer editing of tRNA(Leu) mischarged with methionine."; /evidence="ECO:0000269|PubMed:25051973"; MUTAGEN 242; /note="P->E: Reduced leucyl-tRNA ligase activity."; /evidence="ECO:0000269|PubMed:25051973"; MUTAGEN 245; /note="G->A: No effect on leucyl-tRNA ligase activity."; /evidence="ECO:0000269|PubMed:25051973"; MUTAGEN 245; /note="G->D,R: Reduced leucyl-tRNA ligase activity."; /evidence="ECO:0000269|PubMed:25051973"; MUTAGEN 245; /note="G->P: Loss of leucyl-tRNA ligase activity."; /evidence="ECO:0000269|PubMed:25051973"; MUTAGEN 247; /note="P->A: Reduced leucyl-tRNA ligase activity."; /evidence="ECO:0000269|PubMed:25051973"; MUTAGEN 250; /note="D->A: Reduced leucyl-tRNA ligase activity. Decreased activity in pre-transfer editing and no effect on post-transfer editing of tRNA(Leu) mischarged with methionine."; /evidence="ECO:0000269|PubMed:25051973"; MUTAGEN 250; /note="D->E: No effect on leucyl-tRNA ligase activity."; /evidence="ECO:0000269|PubMed:25051973"; MUTAGEN 250; /note="D->N: Reduced leucyl-tRNA ligase activity."; /evidence="ECO:0000269|PubMed:25051973"; MUTAGEN 250; /note="D->R: Loss of leucyl-tRNA ligase activity."; /evidence="ECO:0000269|PubMed:25051973"; MUTAGEN 514..534; /note="Missing: Loss of leucyl-tRNA ligase activity. Decreased activity in post-transfer editing of tRNA(Leu) mischarged with methionine."; /evidence="ECO:0000269|PubMed:25051973"; MUTAGEN 519; /note="S->G: Reduced leucyl-tRNA ligase activity."; /evidence="ECO:0000269|PubMed:25051973"; MUTAGEN 523; /note="V->I: Reduced leucyl-tRNA ligase activity."; /evidence="ECO:0000269|PubMed:25051973"; MUTAGEN 525; /note="A->S: Reduced leucyl-tRNA ligase activity."; /evidence="ECO:0000269|PubMed:25051973"; MUTAGEN 527; /note="C->E: Reduced leucyl-tRNA ligase activity."; /evidence="ECO:0000269|PubMed:25051973
uniprot
proteins
protein_family
Class-I aminoacyl-tRNA synthetase family
uniprot
proteins
pubmed
10718198
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19426743
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22607940
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25051973
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
32232361
uniprot
proteins
sequence_length
1176
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
uniprot
proteins