Literature summary for 6.1.1.6 extracted from

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 (2010), Cell Cycle, 9, 3072-3077.

Search for more literature for 6.1.1.6

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cell surface	the enzyme is exposed on the surface of stressed cells, on which it co-localized with calreticulin in lipid rafts	Mus musculus	9986	-
endoplasmic reticulum	-	Mus musculus	5783	-
extracellular	KARS also occurs in the supernatant of stressed cells	Mus musculus	-	-
additional information	anthracyclin-induced translocation of KARS from the endoplasmic reticulum to the cell surface	Mus musculus	-	-
plasma membrane	the enzyme is exposed on the surface of stressed cells, on which it co-localized with calreticulin in lipid rafts	Mus musculus	5886	-

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
CT-26 cell	-	Mus musculus	-

Synonyms

Synonyms	Comment	Organism
KARS	-	Mus musculus
lysyl tRNA synthetase	-	Mus musculus

Expression

Organism	Comment	Expression
Mus musculus	enzyme depletion by KARS specific siRNA	down

General Information

General Information	Comment	Organism
malfunction	depletion of KARS with small interfering RNAs suppresses calreticulin exposure on the cell surface induced by anthracyclines or UVC light	Mus musculus
additional information	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	Mus musculus
physiological function	KARS mediates translocation of calreticulin from endoplasmic reticulum to the plasma membrane at the cell surface	Mus musculus

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Release 2023.1 (January 2023)