Literature summary for 3.5.4.37 extracted from

Valente, L.; Nishikura, K.
RNA binding-independent dimerization of adenosine deaminases acting on RNA and dominant negative effects of nonfunctional subunits on dimer functions (2007), J. Biol. Chem., 282, 16054-16061.

Search for more literature for 3.5.4.37

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Sf9 cells	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
additional information	mutations for ADAR1 and ADAR2 within the double-stranded RNA binding domains, that result in the total loss of all binding for long and short dsRNA. These dsRNA binding-deficient ADARs nevertheless dimerize identically to their wild type counterparts, revealing that ADAR dimerization is not mediated by dsRNA. Two monomers with functional double-stranded RNA binding domains are required by a dimer for dsRNA binding and A to I editing activities	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Subunits

Subunits	Comment	Organism
dimer	ADAR1 and ADAR2 form respective homodimers, and this association is essential for their enzymatic activities. ADAR dimerization independent of their binding to dsRNA	Homo sapiens

Synonyms

Synonyms	Comment	Organism
ADAR1	-	Homo sapiens
ADAR2	-	Homo sapiens

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Release 2023.1 (January 2023)