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Information on EC 6.1.1.6 - lysine-tRNA ligase and Organism(s) Homo sapiens and UniProt Accession Q15046
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6.1.1.6 lysine-tRNA ligaseSpecify your search results
Word Map
- 6.1.1.6
- synthetases
- aminoacylation
- lysylation
-
anticodon
-
aarss
-
isoacceptors
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diadenosine
- aspartyl-trna
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gagpol
- tetraphosphate
- trnalys3
- prors
- valrs
- leurs
- arginyl-trna
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isoleucyl-trna
- glnrs
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atp-ppi
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anticodon-binding
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prolyl-trna
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multi-trna
- asprs
- diagnostics
- pharmacology
- medicine
- drug development
- synthesis
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
lysyl-trna synthetase, lysrs, lysrs1, lysrs2, lysyl trna synthetase, mitochondrial lysyl-trna synthetase, cytoplasmic lysyl-trna synthetase, class i lysrs, premsk1p, pfkrs, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
LysRS
Lysyl-tRNA synthetase
L-Lysine-transfer RNA ligase
Lysine translase
Lysine--tRNA ligase
Lysine-tRNA synthetase
LysRS
Lysyl-transfer ribonucleate synthetase
Lysyl-transfer RNA synthetase
Lysyl-tRNA synthetase
Synthetase, lysyl-transfer ribonucleate
Lysyl-tRNA synthetase
-
Lysyl-tRNA synthetase
interacts with EF1alpha, aspartyl-tRNA synthetase (EC 6.1.1.12) and p38 in vitro
L-Lysine-transfer RNA ligase
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Lysine translase
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Lysine--tRNA ligase
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Lysine-tRNA synthetase
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LysRS
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LysRS
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Lysyl-transfer ribonucleate synthetase
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Lysyl-transfer RNA synthetase
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Lysyl-tRNA synthetase
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Lysyl-tRNA synthetase
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Synthetase, lysyl-transfer ribonucleate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
esterification
Aminoacylation
esterification
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-
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Aminoacylation
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-
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SYSTEMATIC NAME
IUBMB Comments
L-lysine:tRNALys ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY
9031-26-9
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
-
?
ATP + lysine + tRNALys,3'-59mer
AMP + L-lysyl-tRNALys, 3'-59mer + diphosphate
-
human tRNALys mutant
-
?
ATP + lysine + tRNALysU35A
AMP + L-lysyl-tRNALysU35A + diphosphate
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human tRNALys mutant, from in vitro translation, very low activity
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?
ATP + lysine + tRNALysU35C
AMP + L-lysyl-tRNALysU35C + diphosphate
-
human tRNALys mutant, from in vitro translation, 153fold decreased activity compared to the wild-type
-
?
ATP + lysine + tRNALysU36A
AMP + L-lysyl-tRNALysU36A + diphosphate
-
human tRNALys mutant, from in vitro translation, 182fold decreased activity compared to the wild-type
-
?
ATP + lysine + tRNALysU36C
AMP + L-lysyl-tRNALysU36C + diphosphate
-
human tRNALys mutant, from in vitro translation, 11fold decreased activity compared to the wild-type
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
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-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
isozyme shows different activities with cytoplasmic and mitochondrial tRNALys
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?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
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-
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
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during early assembly of human immunodeficiency virus type 1, an assembly complex is formed, the components of which include genomic RNA, Gag, Gag-Pol, tRNALys, and lysyl tRNA synthetase. Directly increasing or decreasing cellular expression of LysRS results in corresponding changes in viral infectivity and in the viral concentrations of LysRS, tRNALys, and reverse transcriptase. Overexpression of LysRS in the cell reduces viral protease activity
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-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
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enzyme facilitates the selective packaging of tRNA3 Lys. Newly synthesized LysRS is associated with Gag protein after a 10 minute pulse with [35 S]cysteine/methionine. Incorporation of LysRS into HIV-1 is very sensitive to the inhibition of new synthesis of LysRS
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-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
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the enzyme is secreted to trigger proinflammatory response. TNF-alpha induces secretion of lysyl-tRNA synthetase. The secreted enzyme binds to macrophages and peripheral blood mononuclear cell to enhance the TNF-alpha production and their migration. The mitogen-activated protein kinases, extracellular signal-regulated kinase, p38 mitogen-activated protein kinase and inhibitory protein Galphai are involved in the signal transduction triggered by lysyl-tRNA synthetase. Lysyl-tRNA synthetase may work as a signaling molecule, inducing immune response through the activation of monocyte/macrophages
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-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
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LysRS plays a key role via Ap4A as an important signaling molecule in transcriptional activity of microphthalmia transcription factor
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-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
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pathology-related human mitochondrial tRNA(Lys) variants as substrates. G8313A or G8328A mutations in tRNA(Lys) lead to drastic decreases (500fold to 7000fold) in lysylation efficiency. Mutations in tRNA(Lys) that have no effect on aminoacylation: A8296G, U8316G, G8342A, U8356C, U8362G, G8363A
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-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
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accepts tRNA nucleotide 73 variants: G73, A73, C73 and U73, E. coli tRNA is aminoacylated
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-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
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human tRNALys wild-type
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?
additional information
?
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selective binding of the C-terminal region of 37 kDa laminin receptor precursor 37LRP to the KRS anticodon-binding domain, surface plasmon resonance
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-
?
additional information
?
-
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substrate specificity, no activity with human tRNALysU35G mutant
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?
additional information
?
-
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enzyme is selectively packaged into virions during assembly of the human immunodeficiency virus type 1, i.e. HIV-1, through interaction with the viral Pr55gag protein, overview
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?
additional information
?
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the enzyme signals and mediates the selective recognition and packaging of tRNALys isoacceptors into HIV particles, the human enzyme is selectively packaged into virions of the human immunodeficiency virus during virus assembly, along with and independent of its cognate tRNALys isoacceptors, packaging is mediated by the viral protein Gag, which alone is sufficient for the incorporation, determination of interaction regions
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?
additional information
?
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enzyme KRS accomplishes catalysis in two steps. The first reaction involves the activation of lysine, where KRS selectively binds lysine by using one molecule of ATP. The second reaction involves the transfer of the activated lysine (lysine-AMP) to the acceptor end of tRNALys
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
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during early assembly of human immunodeficiency virus type 1, an assembly complex is formed, the components of which include genomic RNA, Gag, Gag-Pol, tRNALys, and lysyl tRNA synthetase. Directly increasing or decreasing cellular expression of LysRS results in corresponding changes in viral infectivity and in the viral concentrations of LysRS, tRNALys, and reverse transcriptase. Overexpression of LysRS in the cell reduces viral protease activity
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
enzyme facilitates the selective packaging of tRNA3 Lys. Newly synthesized LysRS is associated with Gag protein after a 10 minute pulse with [35 S]cysteine/methionine. Incorporation of LysRS into HIV-1 is very sensitive to the inhibition of new synthesis of LysRS
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
the enzyme is secreted to trigger proinflammatory response. TNF-alpha induces secretion of lysyl-tRNA synthetase. The secreted enzyme binds to macrophages and peripheral blood mononuclear cell to enhance the TNF-alpha production and their migration. The mitogen-activated protein kinases, extracellular signal-regulated kinase, p38 mitogen-activated protein kinase and inhibitory protein Galphai are involved in the signal transduction triggered by lysyl-tRNA synthetase. Lysyl-tRNA synthetase may work as a signaling molecule, inducing immune response through the activation of monocyte/macrophages
-
-
?
additional information
?
-
-
enzyme is selectively packaged into virions during assembly of the human immunodeficiency virus type 1, i.e. HIV-1, through interaction with the viral Pr55gag protein, overview
-
?
additional information
?
-
-
the enzyme signals and mediates the selective recognition and packaging of tRNALys isoacceptors into HIV particles, the human enzyme is selectively packaged into virions of the human immunodeficiency virus during virus assembly, along with and independent of its cognate tRNALys isoacceptors, packaging is mediated by the viral protein Gag, which alone is sufficient for the incorporation, determination of interaction regions
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
BC-K-01
the inhibitor interferes with the binding between enzyme KRS and laminin receptor 37LRP domain
BC-K-YH16899
the inhibitor interferes with the binding between enzyme KRS and laminin receptor 37LRP domain
2-(5,6-difluoro-2-([3-(trifluoromethyl)benzoyl]imino)benzo[d]thiazol-3(2H)-yl)butanoic acid
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i.e. BC-K-YH16899, shows three to sixfold better inhibition of KRS as BC-K01 in most of the assays and better volume of distribution in vivo
human tRNALys anticodon domain
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from wild-type tRNALys, N-terminally truncated mutant enzyme
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human tRNALys-3'oxidized
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3'-oxidized by periodate, N-terminally truncated mutant enzyme
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human tRNALysU35G mutant
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defective substrate in both binding and catalysis, N-terminally truncated mutant enzyme
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YH16899
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KRS is the main target of YH16899. YH16899 inhibits enzyme KRS and KRS-mediated metastasis, it also reduces pulmonary nodule formation by approximately 70% without any effects on bodyweight. While YH16899 does not affect cancer cell viability, it inhibits the H226 cell migration with an IC50 of 0.0085 mM
additional information
the complex formation among KRS, p67LR, and integrins alpha6 and beta1 upon cell adhesion can be disrupted by YH16899 treatment. SW620 cells with inhibitors U1026 or YH16899 blocks dissemination. Blockade of dissemination of KRS-suppressed cells is relieved by ERK1/2 and/or paxillin expression
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
aspartyl-tRNA synthetase
EC 6.1.1.12, AspRS, from the multi-synthetase complex. HKRS and hKRSDELTA60 are differentially stimulated by
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epidermal growth factor receptor
activation of LysRS by epidermal growth factor receptor (EGFR)
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syntenin-1
tandem PDZ protein, regulates KRS activity, adaptor modulating the activity of KRS. A point mutation in the PDZ2 domain of syntenin-1 abrogates interaction with KRS
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translation elongation factor 1alpha
EF1alpha, hKRSDELTA60 binds to EF1alpha and is stimulated by EF1alpha in vitro
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additional information
the non-synthetase protein from the multi-synthetase complex p38 alone does not affect hKRS lysylation but inhibited the AspRS-mediated stimulation of hKRS
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additional information
-
the non-synthetase protein from the multi-synthetase complex p38 alone does not affect hKRS lysylation but inhibited the AspRS-mediated stimulation of hKRS
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additional information
-
specific binding to HIV Gag protein, thereby signaling and mediation of selective recognition and packaging of tRNALys isoacceptors as well as the enzyme itself into HIV particles, the Gag protein alone is sufficient for the incorporation, determination and mapping of interaction regions
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0034
tRNALys
-
human wild-type tRNALys, 30°C, wild-type and N-terminally truncated mutant enzymes
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.08
tRNALys,3'-59mer
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human tRNALys mutant + human tRNALys,3'-14mer mutant, 20°C, wild-type enzyme
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0.0079
tRNALysU35C
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human mutant tRNALys, 30°C, N-terminally truncated mutant enzyme
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0.0068
tRNALysU36A
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human mutant tRNALys, 30°C, N-terminally truncated mutant enzyme
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0.046
tRNALysU36C
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human mutant tRNALys, 30°C, N-terminally truncated mutant enzyme
-
0.38
tRNALys
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human wild-type tRNALys, 30°C, N-terminally truncated mutant enzyme
0.00026
tRNALys,3'-59mer
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human tRNALys mutant + human tRNALys,3'-7mer mutant, 20°C, wild-type enzyme
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0.88
tRNALys,3'-59mer
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human tRNALys mutant + human tRNALys,3'-14mer mutant, 20°C, wild-type enzyme
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1.5
tRNALys,3'-59mer
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human tRNALys mutant + human tRNALys,3'-17mer mutant, 20°C, wild-type enzyme
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.005
human tRNALys anticodon domain
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30°C, N-terminally truncated mutant enzyme
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0.0013
human tRNALys-3'oxidized
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3'-oxidized by periodate, 30°C, N-terminally truncated mutant enzyme
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0.005
human tRNALysU35G anticodon domain
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30°C, N-terminally truncated mutant enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
1 gene encodes a cytoplasmic isozyme, the second encodes both a cytoplasmic and mitochondrial isozyme, which are differenciated by alternative splicing
SwissProt
1 gene encodes a cytoplasmic isozyme, the second encodes both a cytoplasmic and mitochondrial isozyme, which are differentiated by alternative splicing
SwissProt
sequence alignment of class II LysRS from Homo sapiens, Drosophila melanogaster, Saccharomyces cerevisiae, and Escherichia coli shown
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
high expression of KRS in tumor cells is noted in 43.3 % (198 of 457) of the cases. High expression of KRS in tumor-associated inflammatory cells including macrophages/monocytes, CD4-positive T cells, and/or neutrophils is observed in 37.2 % (170 of 457) of the cases, overview
KRS protein is expressed with a fine granular pattern in the cytoplasm of the tumor cells
significantly higher staining levels of phosphos207-LysRS are observed in both the cytoplasm and the nuclei of cancerous tissues compared to healthy tissues
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among human ARSs, cytosolic lysyl-tRNA synthetase (KRS) is often highly expressed in cancer cells and tissues, and facilitates cancer cell migration and invasion through the interaction with the 67 kDa laminin receptor on the plasma membrane. KRS is often highly expressed in cancer cells
additional information
-
infected with HIV-1, during early assembly of human immunodeficiency virus type 1, an assembly complex is formed, the components of which include genomic RNA, Gag, Gag-Pol, tRNALys, and lysyl tRNA synthetase. Directly increasing or decreasing cellular expression of LysRS results in corresponding changes in viral infectivity and in the viral concentrations of LysRS, tRNALys, and reverse transcriptase. Overexpression of LysRS in the cell reduces viral protease activity
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
KRS is released fromMSC and translocates to the cell membrane, where it binds to p67LR
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KRS is normally located in the cytosol as a component of the multitRNA synthetase complex (MSC) that consists of nine different ARSs and three auxiliary factors named AIMP1, 2 and 3
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dissociation of lysyl-tRNA synthetase (KRS) from the multi-aminoacyl-tRNA synthetase complex in human macrophage-like differentiated THP-1 cells and its subsequent secretion, can be triggered by Shiga toxins
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in response to immunological challenge of mast cells, LysRS is phosphorylated on residue Ser207 in a MAPK-dependent manner, released from the multisynthetase complex, and translocated into the nucleus
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associated with plasma membrane of HIV-1-producing 293FT cells
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
metabolism
physiological function
additional information
malfunction
aberrant expression of aminoacyl-tRNA synthetases is associated with various human cancers. Enzyme status and clinicopathological parameters reveal that the enzyme expression is correlated with a shorter overall survival. Enzyme KRS has an oncogenic role, it binds microphthalmia-associated transcription factor (MITF), which is an oncogenic transcriptional activator observed in the development of melanoma
malfunction
congenital visual impairment and progressive microcephaly due to lysyl-transfer RNA synthetase (KARS) mutations, expanding phenotype with severe infantile visual loss, progressive microcephaly, developmental delay, seizures, and abnormal subcortical white matter, overview
malfunction
KRS-suppressed HCT-116 cells show increased mesenchymal markers and decreased epithelial markers 24 h after embedding of colon cancer spheroids in 3D collagen I gels. KRS-positive cells are sensitive to laminin treatment for p67LR stabilization, KRS-suppressed cells are insensitive to the laminin treatment. KRS-expressing parental cells show disseminative margins that are positive for E-cadherin expression, whereas KRS-suppressed cells show neither. Specific effect of KRS suppression on paxillin. KRS suppression decreases the phosphorylations of vinculin Tyr822 and tensin2 Tyr483, but not of talin Ser425. KRS-suppression decreases ERK1/2 phosphorylation, ERK1/2 phosphorylation is increased by KRS overexpression. Treating SW620 cells with inhibitors U1026 or YH16899 blocks dissemination
metabolism
LysRS enzyme phosphorylation on residue Ser207 is correlated to activity of epidermal growth factor receptor and level of lymph node metastases, e.g. in lung cancer, overview. The MAPK-ERK pathway leads to the phosphorylation of LysRS and its release from the MSC in activated mast cells. Lysyl-tRNA synthetase phosphorylated on Ser207 (P-s207 LysRS) is released from the cytoplasmic multi-tRNA synthetase complex (MSC) into the nucleus, where it activates the microphthalmia-associated transcription factor (MITF) in stimulated cultured mast cells and cardiomyocytes. This specific phosphorylation results in LysRS losing its ability to acetylate tRNA but enhances its production of the second messenger diadenosine tetraphosphate (Ap4A). Ap4A has been shown to bind to the tumor suppressor Hint-1, releasing its inhibition on MITF. Patients with EGFR mutations without lymph node metastases have a higher nuclear expression of Ser207 phosphorylated LysRS (50%) as compared to patients with lymph node metastases (27.8%)
metabolism
lysyl-tRNA synthetase (KRS) is one component of multisynthetase complex that consists of eight aminoacyl-tRNA synthetases and three nonenzymatic factors known as ARS-interacting multifunctional protein
physiological function
enzyme lysyl-transfer RNA synthetase is a bifunctional aminoacyl-transfer RNA synthetase catalyzing transfer RNA aminoacylation in both, cytoplasm and mitochondria
physiological function
in addition to its translational function when associated to the a multi-aminoacyl-tRNA synthetase complex (MSC), LysRS is also recruited in nontranslational roles after dissociation from the MSC. The balance between its MSC-associated and MSC-dissociated states is essential to regulate the functions of LysRS in cellular homeostasis
physiological function
KRS at the plasma membrane is important for cancer metastasis, canonical roles of cytosolic KRS in protein translation. KRS and its downstream effectors promote the metastatic migration. Complex formation among KRS, p67LR, and integrins alpha6 and beta1 upon cell adhesion, KRS/p67LR/integrin alpha6beta1 linkage correlates for ERK1/2 activation, KRS-dependent ERK1/2 activation. KRS has prometastatic roles at the invasive margins of KRS-/+ mouse breast tumor and human colon tumor tissues
physiological function
lysyl-tRNA synthetase (KRS) is a multi-functional enzyme, which, in addition to its primary function of aminoacylation of lysine onto the cognate tRNA, has various noncanonical functions. Enzyme KRS interacts with the laminin receptor (LR/RPSA) and enhances laminin-induced cell migration in cancer metastasis. The anticodon-binding domain of KRS binds directly to the C-terminal region of 37 kDa laminin receptor precursor 37LRP, and inhibitors BC-K-01 and BC-K-YH16899 interfere with KRS37LRP binding. In addition, the anticodon-binding domain of KRS binds to laminin. Furthermore, KRS is a major source of diadenosine tetraphosphate (Ap4A) in immunologically activated mast cells, and via translocation into the nucleus, KRS controls the expression of microphthalmia-associated transcription factor (MITF)-inducible genes in allergic responses
physiological function
lysyl-tRNA synthetase (KRS) is an aminoacyl-tRNA synthetase (ARS) that is essential for protein synthesis during ligation of specific amino acids to their cognate tRNAs
malfunction
-
loss of function mutations in the catalytic domain of the enzyme are found in Charcot-Marie-Tooth disease patients. Mitochondrial enzyme binds to mutant superoxide dismutase 1, forming protein aggregates that damage mitochondrial activity and lead to disease onset in amoytophic lateral sclerosis
malfunction
-
cytosolic KRS is released from MSC and translocates to the cell membrane, where it binds to p67LR. BC-K01 and YH16899 to KRS abolishes the KRS-LR interaction
metabolism
-
Shiga toxins trigger the dissociation and secretion of KRS from the multi-aminoacyl-tRNA synthetase complex (MSC) in toxin-sensitive human macrophage-like D-THP-1 cells to enhance proinflammatory responses
metabolism
-
the pro-metastatic functions of enzyme KRS and their pathophysiological implications, overview. KRS is released from the multi-tRNA synthetase complex (MSC) and translocates to the cell membrane, where it binds to p67LR, resulting in cell migration and metastasis. Since KRS plays a key role in the structural stability of the MSC. dissociation of KRS from the MSC may affect the cellular levels of other synthetase components within the MSC. KRS/p67LR/integrin alpha6beta1 complex formation correlates with transduction of intracellular signaling for ERK1/2 activation and paxillin expression/activation
physiological function
-
silencing of LysRS leads to reduced Ap4P production in immunologically activated cells, which results in a lower level of MITF inducible genes. Specific LysRS Ser207 phosphorylation regulates Ap4P production in immunologically stimulated mast cells
physiological function
-
the enzyme plays an essential role in HIV replication, transcriptional regulation, cytokine-like signaling, and transport of proteins to the cell membrane. The enzyme can induce cancer cell migration through interaction with the 67 kDa laminin receptor. The enzyme facilitates the translocation and surface exposure of calreticulin, activating the CRT pathway which leads to death of stressed cells
physiological function
-
aminoacyl-tRNA synthetases (ARSs) are essential enzymes that conjugate specific amino acids to their cognate tRNAs for protein synthesis. Among human ARSs, cytosolic lysyl-tRNA synthetase (KRS) is often highly expressed in cancer cells and tissues, and facilitates cancer cell migration and invasion through the interaction with the 67 kDa laminin receptor on the plasma membrane. Human KRS interacts with the laminin receptor (LR/RPSA) and enhances cell migration upon laminin stimulation. KRS positively regulates the membrane stability of p67LR, leading to efficient signaling for cell migration during cancer metastasis. Model for the pro-metastatic function of KRS via 67LR and integrin in the plasma membrane. Laminin binds to the integrin resulting in the activation of PI3K and p38 MAPK. Then, p38MAPK phosphorylates the KRS that is bound to the N-terminus of AIMP2 in the MSC. The phosphorylated KRS is released from MSC and translocates to the plasma membrane, where it forms the KRS/p67LR/integrin complex. KRS binding to the p67LR prevents Nedd4-mediated ubiquitination resulting in stabilization of p67LR. The KRS/p67LR/integrin complex also transduces intracellular signaling favorable for cell migration, through ERKs/c-Jun./paxillin expression and paxillin activation, leading to cancer cell dissemination and migration. KRS-mediated regulation of epithelial-mesenchymal transition, overview
physiological function
-
Shiga toxins (Stxs) produced by Shiga toxin-producing Escherichia coli (STEC) strains are major virulence factors that cause fatal systemic complications, such as hemolytic uremic syndrome and disruption of the central nervous system. Enzymatically active Stxs trigger the dissociation of lysyl-tRNA synthetase (KRS) from the multi-aminoacyl-tRNA synthetase complex (MSC) in human macrophage-like differentiated THP-1 cells and its subsequent secretion. The secreted KRS acts to increase the production of proinflammatory cytokines and chemokines. Thus, KRS may be one of the key factors that mediate transduction of inflammatory signals in the STEC-infected host
additional information
human cytoplasmic lysyl-tRNA synthetase (LysRS) is associated within a multi-aminoacyl-tRNA synthetase complex (MSC). Within this complex, the p38 component is the scaffold protein that binds the catalytic domain of LysRS via its N-terminal region, LysRS-p38 interaction analysis, Lys356 and His364 of LysRS interact with the peptide from Pro8 to Arg26 in native p38, overview
additional information
-
human cytoplasmic lysyl-tRNA synthetase (LysRS) is associated within a multi-aminoacyl-tRNA synthetase complex (MSC). Within this complex, the p38 component is the scaffold protein that binds the catalytic domain of LysRS via its N-terminal region, LysRS-p38 interaction analysis, Lys356 and His364 of LysRS interact with the peptide from Pro8 to Arg26 in native p38, overview
additional information
noncanonical roles of membranous lysyl-tRNA synthetase in transducing cell-substrate signaling for invasive dissemination of colon cancer spheroids in 3D collagen I gels
additional information
the enzyme is organized in a multi-synthetase complex (MSC)
additional information
-
the enzyme is organized in a multi-synthetase complex (MSC)
additional information
-
human lysyl-tRNA synthetase is bound to the multi-tRNA synthetase complex, mediated by the p38 scaffold protein, the complex maintains and regulates the aminoacylation and nuclear functions of LysRS. p38 mobilizes LysRS for redirection to the nucleus to interact with the microphthalmia associated transcription factor. Each of the N-terminal 48 residues of p38 binds one LysRS dimer and, in so doing, brings two copies of the LysRS dimer into the multi-tRNA synthetase complex. Structural organization of the LysRS-p38 complex, overview
additional information
-
KRS is normally located in the cytosol as a component of the multi-tRNA synthetase complex (MSC) that consists of nine different ARSs and three auxiliary factors named AIMP1, 2 and 3
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SYK_HUMAN
597
0
68048
Swiss-Prot
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
120000
LysRSalpha2, Superdex-200 gel-filtration, results show clearly a dynamic dimer-tetramer oligomerization for LysRS
240000
LysRSalpha4, Superdex-200 gel-filtration, results show clearly a dynamic dimer-tetramer oligomerization for LysRS
270000
calculated mass, alpha2:alpha2 tetramer. This tetramer is probably functional for aminoacylation, because docking of tRNA molecules to the tetrameric LysRS seems not to cause steric clash
64000
predominantly as the 64 kDa processed form in the mitochondrial fraction, Western blot
69000
unprocessed form (i.e. still containing the N-terminal mitochondrial targeting signal) in the cytosolic fraction, Western blot
62000 - 63000
-
isozyme packaged into virions, proteolytically truncated, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotetramer
it is not understood, how the two dimeric proteins combine to make a presumptive alpha2beta2 heterotetramer
homotetramer
alpha2:alpha2 tetramer. This tetramer is probably functional for aminoacylation, because docking of tRNA molecules to the tetrameric LysRS seems not to cause steric clash
additional information
additional information
identification of protein interfaces within the multi-aminoacyl-tRNA synthetase complex including lysyl-tRNA synthetase and the scaffold protein p38, overview
additional information
-
identification of protein interfaces within the multi-aminoacyl-tRNA synthetase complex including lysyl-tRNA synthetase and the scaffold protein p38, overview
additional information
structure analysis of the flexible N-terminal extension and anticodon-binding domain, NMR analysis, overview
additional information
the enzyme is organized in a multi-synthetase complex (MSC)
additional information
-
the enzyme is organized in a multi-synthetase complex (MSC)
additional information
-
in the complex with p38, LysRs shows an alpha2beta1:beta1alpha2 organization, in which a dimeric p38 scaffold holds two LysRS alpha2 dimers in a parallel configuration, overview. The structure is designed to control both retention and mobilization of LysRS from the multi-tRNA synthetase complex
additional information
-
KRS is normally located in the cytosol as a component of the multitRNA synthetase complex (MSC) that consists of nine different ARSs and three auxiliary factors named AIMP1, 2 and 3. A homodimer of KRS is linked to the N-terminal peptide of AIMP2, and the MSC contains two units of the KRS homodimer-AIMP2 monomer complex. This suggests that KRS exists in the MSC as a tetramer that is present at a relatively higher stoichiometry, compared to other components that are bound to the MSC as monomers or dimers
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
the MAPK-ERK pathway leads to the phosphorylation of LysRS on Ser207 and its release from the MSC in activated mast cells. Phosphorylation of Ser207 can be inhibited by U0126 treatment
phosphoprotein
proteolytic modification
phosphoprotein
-
in response to immunological challenge of mast cells, LysRS is phosphorylated on residue Ser207 in a MAPK-dependent manner, released from the multisynthetase complex, and translocated into the nucleus
phosphoprotein
-
Ser207-phosphorylation inactivates the enzyme translationally, but activates its transcriptional function
phosphoprotein
-
phosphorylated KRS is released from multitRNA synthetase complex (MSC) and transölocates to the plasma membrane
proteolytic modification
-
prior of packing of the enzyme into viral particles, it is truncated independent of viral protease
proteolytic modification
-
the enzyme is N-terminally cleaved during incorporation into HIV particles
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
micrositting drop-vapor diffusion method, both DELTAS70-T584 and full length LysRS
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DELTAS70-T584
truncation at S70-T584 and full length LysRS (M1-V597) expressed, purified, and attempted for crystallization
E525K
naturally occuring mutation within a highly conserved region of the catalytic domain, the mutation is involved in neurological disorders in infants
hKRSDELTA1-24
deletion mutation. Construct shows significant stimulation of lysylation by EF1alpha and binding to EF1alpha
hKRSDELTA24-42
deletion mutation. Construct shows significant stimulation of lysylation by EF1alpha and binding to EF1alpha
R438W
naturally occuring mutation within a highly conserved region of the catalytic domain, the mutation is involved in neurological disorders in infants
DELTA1-65
-
mutant enzyme binds poorly to tRNALys, but does not increase tRNALys packaging into HIV-1 viruses
DELTA452-597
-
mutant enzyme binds to but does not aminoacylate tRNALys, still facilitates an increase in tRNALys packaging into virions
F244A
-
the mutant shows 90% aminoacylation activity compared to the wild type enzyme
F244A/I245A
-
the mutant shows 90% aminoacylation activity compared to the wild type enzyme
I246D
-
the mutant shows 60% aminoacylation activity compared to the wild type enzyme
I246D/R247A
-
the mutant shows 20% aminoacylation activity compared to the wild type enzyme
I250D
-
the mutant shows 40% aminoacylation activity compared to the wild type enzyme
I250D/I251D
-
the mutant shows 20% aminoacylation activity compared to the wild type enzyme
I251D
-
the mutant shows 40% aminoacylation activity compared to the wild type enzyme
I254D
-
the mutant shows 40% aminoacylation activity compared to the wild type enzyme
I254D/R255A
-
the mutant shows 30% aminoacylation activity compared to the wild type enzyme
K249A
-
the mutant shows 90% aminoacylation activity compared to the wild type enzyme
R247A
-
the mutant shows 30% aminoacylation activity compared to the wild type enzyme
R255A
-
the mutant shows 40% aminoacylation activity compared to the wild type enzyme
S270D
-
the mutant shows 800fold enhanced catalytic activity compared to the wild type enzyme, with enhanced diadenosine tetraphosphate synthetic activity, enhanced ATP hydrolysis and lost aminoacylation activity for tRNALys
additional information
additional information
incorporation of the non-natural, photo-cross-linkable amino acid p-benzoyl-L-phenylalanine (Bpa) at 27 discrete positions within the catalytic domain of LysRS. Among the 27 distinct LysRS mutants, only those with Bpa inserted in place of Lys356 or His364 are cross-linked with p38, the scaffold protein of the -aminoacyl-tRNA synthetase complex (MSC)
additional information
-
incorporation of the non-natural, photo-cross-linkable amino acid p-benzoyl-L-phenylalanine (Bpa) at 27 discrete positions within the catalytic domain of LysRS. Among the 27 distinct LysRS mutants, only those with Bpa inserted in place of Lys356 or His364 are cross-linked with p38, the scaffold protein of the -aminoacyl-tRNA synthetase complex (MSC)
additional information
-
in vitro construction of the LysRS-p38 complex, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified to homogeneity by Ni-NTA affinity column and a Q highperformance column, both DELTAS70-T584 and full length LysRS
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, genomic organization, expression of cytoplasmic isozyme in Escherichia coli strain BL21(DE3) as His-tagged enzymes, expression in human osteosarcoma cell line 143B
DNA sequence determination and analysis, genomic organization, expression of mitochondrial isozyme in Escherichia coli strain BL21(DE3) as His-tagged enzymes, expression in human osteosarcoma cell line 143B
expressed in the bacterial strain BL21 (DE3) CodonPlus using the vectors pET20b, both DELTAS70-T584 and full length LysRS
gene KARS, DNA and amino acid sequence determination and analysis, genotyping
recombinant expression of enzyme LysRS in Escherichia coli strain BL21(DE3) that also contains pEVOL-p-benzoyl-L-phenylalanine (Bpa) expressing the orthogonal suppression system, namely Methanococcus jannaschii tRNATyr,CUA, an amber suppressor tRNA derived from Methanococcus jannaschii tRNATyr, and Methanococcus jannaschii TyrRSBpa a mutant of Methanococcus jannaschii tyrosyl-tRNA synthetase that specifically aminoacylates Methanococcus jannaschii tRNATyr,CUA with Bpa
COS7 cells are cotransfected with a plasmid containing HIV-1 proviral DNA and a plasmid containing cDNA coding for either full-length human LysRS or a truncated LysRS variant in which the N-terminal 65 amino acids have been deleted (DELTA1-65 LysRS). N-terminally truncated LysRS, which binds poorly to tRNALys, does not increase tRNALys packaging into viruses, while C-terminally truncated LysRS (DELTA452-597), which binds to but does not aminoacylate tRNALys, still facilitates an increase in tRNALys packaging into virions
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the complex formation among KRS, p67LR, and integrins alpha6 and beta1 upon cell adhesion can be disrupted by YH16899 treatment. SW620 cells with inhibitors U1026 or YH16899 blocks dissemination. Blockade of dissemination of KRS-suppressed cells is relieved by ERK1/2 and/or paxillin expression
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
LysRS s207 phosphorylation plays a role as a prognostic factor in lung cancer after primary surgery
medicine
-
KRS is released from the multi-tRNA synthetase complex (MSC) and translocates to the plasma membrane, where it binds to p67LR, resulting in cell migration and metastasis. Modulation of KRS-67LR interaction by an inhibitor BC-KYH16899 may offer a strategy with which to control metastasis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shiba, K.
Human lysyl-tRNA synthetase accepts nucleotide 73 variants and rescues E. coli double defection mutant
J. Biol. Chem.
272
22809-22816
1997
Homo sapiens
Tolkunova, E.; Park, H.; Xia, J.; King, M.P.; Davidson, E.
The human lysyl-tRNA synthetase gene encodes both the cytoplasmic and mitochondrial enzymes by means of an unusual alternative splicing of the primary transcript
J. Biol. Chem.
275
35063-35069
2000
Homo sapiens (Q15046), Homo sapiens
Javanbakht, H.; Halwani, R.; Cen, S.; Saadatmand, J.; Musier-Forsyth, K.; Gottlinger, H.; Kleiman, L.
The interaction between HIV-1 Gag and human lysyl-tRNA synthetase during viral assembly
J. Biol. Chem.
278
27644-27651
2003
Homo sapiens
Cen, S.; Khorchid, A.; Javanbakht, H.; Gabor, J.; Stello, T.; Shiba, K.; Musier-Forsyth, K.; Kleiman, L.
Incorporation of lysyl-tRNA synthetase into human immunodeficiency virus type 1
J. Virol.
75
5043-5048
2001
Homo sapiens
Stello, T.; Hong, M.; Musier-Forsyth, K.
Efficient aminoacylation of tRNALys,3 by human lysyl-tRNA synthetase is dependent on covalent continuity between the acceptor stem and the anticodon domain
Nucleic Acids Res.
27
4823-4829
1999
Homo sapiens
Lee, Y.N.; Nechushtan, H.; Figov, N.; Razin, E.
The function of lysyl-tRNA synthetase and Ap4A as signaling regulators of MITF activity in FcepsilonRI-activated mast cells
Immunity
20
145-151
2004
Homo sapiens
Guo, F.; Gabor, J.; Cen, S.; Hu, K.; Mouland, A.J.; Kleiman, L.
Inhibition of cellular HIV-1 protease activity by lysyl-tRNA synthetase
J. Biol. Chem.
280
26018-26023
2005
Homo sapiens
Cen, S.; Javanbakht, H.; Niu, M.; Kleiman, L.
Ability of wild-type and mutant lysyl-tRNA synthetase to facilitate tRNA(Lys) incorporation into human immunodeficiency virus type 1
J. Virol.
78
1595-1601
2004
Homo sapiens
Halwani, R.; Cen, S.; Javanbakht, H.; Saadatmand, J.; Kim, S.; Shiba, K.; Kleiman, L.
Cellular distribution of Lysyl-tRNA synthetase and its interaction with Gag during human immunodeficiency virus type 1 assembly
J. Virol.
78
7553-7564
2004
Homo sapiens
Park, S.G.; Kim, H.J.; Min, Y.H.; Choi, E.C.; Shin, Y.K.; Park, B.J.; Lee, S.W.; Kim, S.
Human lysyl-tRNA synthetase is secreted to trigger proinflammatory response
Proc. Natl. Acad. Sci. USA
102
6356-6361
2005
Homo sapiens
Sissler, M.; Helm, M.; Frugier, M.; Giege, R.; Florentz, C.
Aminoacylation properties of pathology-related human mitochondrial tRNA(Lys) variants
RNA
10
841-853
2004
Homo sapiens
Kaminska, M.; Francin, M.; Shalak, V.; Mirande, M.
Role of HIV-1 Vpr-induced apoptosis on the release of mitochondrial lysyl-tRNA synthetase
FEBS Lett.
581
3105-3110
2007
Homo sapiens
Kovaleski, B.J.; Kennedy, R.; Hong, M.K.; Datta, S.A.; Kleiman, L.; Rein, A.; Musier-Forsyth, K.
In vitro characterization of the interaction between HIV-1 Gag and human lysyl-tRNA synthetase
J. Biol. Chem.
281
19449-19456
2006
Homo sapiens
Chou, T.F.; Tikh, I.B.; Horta, B.A.; Ghosh, B.; De Alencastro, R.B.; Wagner, C.R.
Engineered monomeric human histidine triad nucleotide-binding protein 1 hydrolyzes fluorogenic acyl-adenylate and lysyl-tRNA synthetase-generated lysyl-adenylate
J. Biol. Chem.
282
15137-15147
2007
Homo sapiens
Kovaleski, B.J.; Kennedy, R.; Khorchid, A.; Kleiman, L.; Matsuo, H.; Musier-Forsyth, K.
Critical role of helix 4 of HIV-1 capsid C-terminal domain in interactions with human lysyl-tRNA synthetase
J. Biol. Chem.
282
32274-32279
2007
Homo sapiens
Chou, T.F.; Wagner, C.R.
Lysyl-tRNA synthetase-generated lysyl-adenylate is a substrate for histidine triad nucleotide binding proteins
J. Biol. Chem.
282
4719-4727
2007
Escherichia coli, Homo sapiens
Kaminska, M.; Shalak, V.; Francin, M.; Mirande, M.
Viral hijacking of mitochondrial lysyl-tRNA synthetase
J. Virol.
81
68-73
2007
Homo sapiens
Yannay-Cohen, N.; Razin, E.
Translation and transcription: the dual functionality of LysRS in mast cells
Mol. Cell
22
127-132
2006
Homo sapiens
Guzzo, C.M.; Yang, D.C.
Lysyl-tRNA synthetase interacts with EF1alpha, aspartyl-tRNA synthetase and p38 in vitro
Biochem. Biophys. Res. Commun.
365
718-723
2008
Homo sapiens (Q15046), Homo sapiens
Kawamata, H.; Magrane, J.; Kunst, C.; King, M.P.; Manfredi, G.
Lysyl-tRNA synthetase is a target for mutant SOD1 toxicity in mitochondria
J. Biol. Chem.
283
28321-28328
2008
Homo sapiens (Q15046)
Meerschaert, K.; Remue, E.; De Ganck, A.; Staes, A.; Boucherie, C.; Gevaert, K.; Vandekerckhove, J.; Kleiman, L.; Gettemans, J.
The Tandem PDZ Protein Syntenin Interacts with the Aminoacyl tRNA Synthetase Complex in a Lysyl-tRNA Synthetase-Dependent Manner
J. Proteome Res.
7
4962-4973
2008
Homo sapiens (Q15046)
Wei, M.; Yang, Y.; Niu, M.; Desfosse, L.; Kennedy, R.; Musier-Forsyth, K.; Kleiman, L.
Inability of HIV-1 produced in murine cells to selectively incorporate primer tRNALys3
J. Virol.
82
12049-12059
2008
Homo sapiens (Q15046), Homo sapiens, Mus musculus (Q99MN1), Mus musculus
Guo, M.; Ignatov, M.; Musier-Forsyth, K.; Schimmel, P.; Yang, X.L.
Crystal structure of tetrameric form of human lysyl-tRNA synthetase: Implications for multisynthetase complex formation
Proc. Natl. Acad. Sci. USA
105
2331-2336
2008
Homo sapiens (Q15046), Homo sapiens
Saadatmand, J.; Guo, F.; Cen, S.; Niu, M.; Kleiman, L.
Interactions of reverse transcriptase sequences in Pol with Gag and LysRS in the HIV-1 tRNALys3 packaging/annealing complex
Virology
380
109-117
2008
Homo sapiens
Yannay-Cohen, N.; Carmi-Levy, I.; Kay, G.; Yang, C.M.; Han, J.M.; Kemeny, D.M.; Kim, S.; Nechushtan, H.; Razin, E.
LysRS serves as a key signaling molecule in the immune response by regulating gene expression
Mol. Cell
34
603-611
2009
Homo sapiens
Fang, P.; Zhang, H.M.; Shapiro, R.; Marshall, A.G.; Schimmel, P.; Yang, X.L.; Guo, M.
Structural context for mobilization of a human tRNA synthetase from its cytoplasmic complex
Proc. Natl. Acad. Sci. USA
108
8239-8244
2011
Homo sapiens
Dewan, V.; Wei, M.; Kleiman, L.; Musier-Forsyth, K.
Dual role for motif 1 residues of human lysyl-tRNA synthetase in dimerization and packaging into HIV-1
J. Biol. Chem.
287
41955-41962
2012
Homo sapiens
Ofir-Birin, Y.; Fang, P.; Bennett, S.P.; Zhang, H.M.; Wang, J.; Rachmin, I.; Shapiro, R.; Song, J.; Dagan, A.; Pozo, J.; Kim, S.; Marshall, A.G.; Schimmel, P.; Yang, X.L.; Nechushtan, H.; Razin, E.; Guo, M.
Structural switch of lysyl-tRNA synthetase between translation and transcription
Mol. Cell
49
30-42
2013
Homo sapiens
Motzik, A.; Nechushtan, H.; Foo, S.Y.; Razin, E.
Non-canonical roles of lysyl-tRNA synthetase in health and disease
Trends Mol. Med.
19
726-731
2013
Homo sapiens
Kim, B.H.; Jung, W.Y.; Lee, H.; Kang, Y.; Jang, Y.J.; Hong, S.W.; Jeong, H.J.; Yoon, S.O.
Lysyl-tRNA synthetase (KRS) expression in gastric carcinoma and tumor-associated inflammation
Ann. Surg. Oncol.
21
2020-2027
2014
Homo sapiens (Q15046), Homo sapiens
Young, H.J.; Lee, J.W.; Kim, S.
Function of membranous lysyl-tRNA synthetase and its implication for tumorigenesis
Biochim. Biophys. Acta
1864
1707-1713
2016
Homo sapiens
Cho, H.Y.; Ul Mushtaq, A.; Lee, J.Y.; Kim, D.G.; Seok, M.S.; Jang, M.; Han, B.W.; Kim, S.; Jeon, Y.H.
Characterization of the interaction between lysyl-tRNA synthetase and laminin receptor by NMR
FEBS Lett.
588
2851-2858
2014
Homo sapiens (Q15046)
Remion, A.; Khoder-Agha, F.; Cornu, D.; Argentini, M.; Redeker, V.; Mirande, M.
Identification of protein interfaces within the multi-aminoacyl-tRNA synthetase complex the case of lysyl-tRNA synthetase and the scaffold protein p38
FEBS open bio
6
696-706
2016
Homo sapiens (Q15046), Homo sapiens
McMillan, H.J.; Humphreys, P.; Smith, A.; Schwartzentruber, J.; Chakraborty, P.; Bulman, D.E.; Beaulieu, C.L.; Beaulieu, C.L.; Majewski, J.; Boycott, K.M.; Geraghty, M.T.
Congenital visual impairment and progressive microcephaly due to lysyl-transfer ribonucleic acid (RNA) synthetase (KARS) mutations the expanding phenotype of aminoacyl-transfer RNA synthetase mutations in human disease
J. Child Neurol.
30
1037-1043
2015
Homo sapiens (Q15046), Homo sapiens
Lee, M.S.; Kwon, H.; Nguyen, L.T.; Lee, E.Y.; Lee, C.Y.; Choi, S.H.; Kim, M.H.
Shiga toxins trigger the secretion of lysyl-tRNA synthetase to enhance proinflammatory responses
J. Microbiol. Biotechnol.
26
432-439
2016
Homo sapiens, Streptococcus pneumoniae (Q04LI2), Streptococcus pneumoniae D39 / NCTC 7466 (Q04LI2)
Nam, S.H.; Kim, D.; Lee, M.S.; Lee, D.; Kwak, T.K.; Kang, M.; Ryu, J.; Kim, H.J.; Song, H.E.; Choi, J.; Lee, G.H.; Kim, S.Y.; Park, S.H.; Kim, D.G.; Kwon, N.H.; Kim, T.Y.; Thiery, J.P.; Kim, S.; Lee, J.W.
Noncanonical roles of membranous lysyl-tRNA synthetase in transducing cell-substrate signaling for invasive dissemination of colon cancer spheroids in 3D collagen I gels
Oncotarget
6
21655-21674
2015
Homo sapiens (Q15046)
Boulos, S.; Park, M.C.; Zeibak, M.; Foo, S.Y.; Jeon, Y.K.; Kim, Y.T.; Motzik, A.; Tshori, S.; Hamburger, T.; Kim, S.; Nechushtan, H.; Razin, E.
Serine 207 phosphorylated lysyl-tRNA synthetase predicts disease-free survival of non-small-cell lung carcinoma
Oncotarget
8
65186-65198
2017
Homo sapiens (Q15046), Homo sapiens
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