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Information on EC 6.1.1.6 - lysine-tRNA ligase and Organism(s) Mus musculus and UniProt Accession Q99MN1

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Mus musculus
UNIPROT: Q99MN1 not found.
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The taxonomic range for the selected organisms is: Mus musculus
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Lysyl-tRNA synthetase
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KARS
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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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lysyl tRNA synthetase
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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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Synthetase, lysyl-transfer ribonucleate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
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Aminoacylation
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-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
L-lysine:tRNALys ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9031-26-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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the enzyme is exposed on the surface of stressed cells, on which it co-localized with calreticulin in lipid rafts
Manually annotated by BRENDA team
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KARS also occurs in the supernatant of stressed cells
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Manually annotated by BRENDA team
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the enzyme is exposed on the surface of stressed cells, on which it co-localized with calreticulin in lipid rafts
Manually annotated by BRENDA team
additional information
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anthracyclin-induced translocation of KARS from the endoplasmic reticulum to the cell surface
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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depletion of KARS with small interfering RNAs suppresses calreticulin exposure on the cell surface induced by anthracyclines or UVC light
physiological function
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KARS mediates translocation of calreticulin from endoplasmic reticulum to the plasma membrane at the cell surface
additional information
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recombinant KARS protein is unable to influence the binding of recombinant CRT to the cell surface. Moreover, recombinant KARS protein is unable to stimulate macrophages in vitro
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SYK_MOUSE
595
0
67840
Swiss-Prot
other Location (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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high molecular mass aminoacyl-tRNA synthetase complex with a coherent structure that can be visualized by electron microscopy
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni+-affinity column
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged LysRS in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme depletion by KARS specific siRNA
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Norcum, M.T.
Isolation and electron microscopic characterization of the high molecular mass aminoacyl-tRNA synthetase complex from murine erythroleukemia cells
J. Biol. Chem.
264
15043-15051
1989
Mus musculus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Kepp, O.; Gdoura, A.; Martins, I.; Panaretakis, T.; Schlemmer, F.; Tesniere, A.; Fimia, G.M.; Ciccosanti, F.; Burgevin, A.; Piacentini, M.; Eggleton, P.; Young, P.J.; Zitvogel, L.; van Endert, P.; Kroemer, G.
Lysyl tRNA synthetase is required for the translocation of calreticulin to the cell surface in immunogenic death
Cell Cycle
9
3072-3077
2010
Mus musculus
Manually annotated by BRENDA team