Literature summary for 2.3.2.8 extracted from

Cha-Molstad, H.; Sung, K.S.; Hwang, J.; Kim, K.A.; Yu, J.E.; Yoo, Y.D.; Jang, J.M.; Han, D.H.; Molstad, M.; Kim, J.G.; Lee, Y.J.; Zakrzewska, A.; Kim, S.H.; Kim, S.T.; Kim, S.Y.; Lee, H.G.; Soung, N.K.; Ahn, J.S.; Ciechanover, A.; Kim, B.Y.; Kwon, Y.T.
Amino-terminal arginylation targets endoplasmic reticulum chaperone BiP for autophagy through p62 binding (2015), Nat. Cell Biol., 17, 917-929.

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Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-arginyl-tRNAArg + BiP/GRP78 protein	Mus musculus	-	tRNAArg + L-arginyl-[BiP/GRP78 protein]	-	?
L-arginyl-tRNAArg + calreticulin	Mus musculus	-	tRNAArg + L-arginyl-[calreticulin]	-	?
L-arginyl-tRNAArg + protein	Mus musculus	-	tRNAArg + L-arginyl-[protein]	-	?
L-arginyl-tRNAArg + protein disulfide isomerase	Mus musculus	-	tRNAArg + L-arginyl-[protein disulfide isomerase]	-	?

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
MEF cell	-	Mus musculus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-arginyl-tRNAArg + BiP/GRP78 protein	-	Mus musculus	tRNAArg + L-arginyl-[BiP/GRP78 protein]	-	?
L-arginyl-tRNAArg + calreticulin	-	Mus musculus	tRNAArg + L-arginyl-[calreticulin]	-	?
L-arginyl-tRNAArg + protein	-	Mus musculus	tRNAArg + L-arginyl-[protein]	-	?
L-arginyl-tRNAArg + protein disulfide isomerase	-	Mus musculus	tRNAArg + L-arginyl-[protein disulfide isomerase]	-	?

Synonyms

Synonyms	Comment	Organism
Arg-tRNA transferase	-	Mus musculus
arginyl-tRNA protein transferase	-	Mus musculus
Ate1	-	Mus musculus
R-transferase	-	Mus musculus

General Information

General Information	Comment	Organism
physiological function	N-terminal arginylation by the enzyme is essential for coping with cellular stresses caused by excessive misfolded proteins	Mus musculus

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Release 2023.1 (January 2023)