Leucyl-tRNA synthetase

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LARS1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesLARS1, Leucyl-tRNA synthetase, ILFS1, HSPC192, LARS, leucyl-tRNA synthetase 1, LRS, LEUS, LFIS, PIG44, hr025Cl, LEURS, RNTLS
External IDsOMIM: 151350 MGI: 1913808 HomoloGene: 7083 GeneCards: LARS1
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_020117
NM_001317964
NM_001317965
NM_016460

NM_134137

RefSeq (protein)

NP_001304893
NP_001304894
NP_057544
NP_064502

NP_598898

Location (UCSC)Chr 5: 146.11 – 146.18 MbChr 18: 42.34 – 42.4 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Leucyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the LARS gene.[5][6]

Function

This gene encodes a cytosolic leucine-tRNA synthetase, a member of the class I aminoacyl-tRNA synthetase family. The encoded enzyme catalyzes the ATP-dependent ligation of L-leucine to tRNA(Leu). It is found in the cytoplasm as part of a multisynthetase complex and interacts with the arginyl-tRNA synthetase through its C-terminal domain. Alternatively spliced transcript variants of this gene have been found; however, their full-length nature is not known.[6]

Interactions

Leucyl-tRNA synthetase has been shown to interact with EEF1G.[7]

Inhibitors

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000133706 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000024493 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Giles RE, Shimizu N, Ruddle FH (September 1980). "Assignment of a human genetic locus to chromosome 5 which corrects the heat sensitive lesion associated with reduced leucyl-tRNA synthetase activity in ts025Cl Chinese hamster cells". Somatic Cell Genetics. 6 (5): 667–687. doi:10.1007/BF01538645. PMID 6933703. S2CID 11128003.
  6. ^ a b "Entrez Gene: LARS leucyl-tRNA synthetase".
  7. ^ Sang Lee J, Gyu Park S, Park H, Seol W, Lee S, Kim S (February 2002). "Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex". Biochemical and Biophysical Research Communications. 291 (1): 158–164. doi:10.1006/bbrc.2002.6398. PMID 11829477.
  8. ^ Markinson B, Ghannoum M, Winter T, Rycerz A, Rock F, Gupta AK (January 2018). "Examining the Benefits of the Boron-Based Mechanism of Action and Physicochemical Properties of Tavaborole in the Treatment of Onychomycosis". Journal of the American Podiatric Medical Association. 108 (1): 12–19. doi:10.7547/16-154. PMID 29547036.

Further reading