3.5.4.37: double-stranded RNA adenine deaminase
This is an abbreviated version!
For detailed information about double-stranded RNA adenine deaminase, go to the full flat file.
Word Map on EC 3.5.4.37
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3.5.4.37
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inosine
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a-to-i
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deaminases
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deamination
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adenosine-to-inosine
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hereditaria
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rna-editing
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pre-mrnas
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dyschromatosis
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symmetrica
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z-dna
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duplex
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ampa
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left-handed
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unedited
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glur-b
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recoding
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site-selective
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macules
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interferon-inducible
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mda5
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hypopigmented
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ifn-inducible
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dsrbds
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interferon-stimulated
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ca2+-permeable
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5-ht2cr
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dicer
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samhd1
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genodermatosis
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rig-i
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hypermutation
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ifn-stimulated
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pigmentary
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interferonopathy
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autoinflammatory
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medicine
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inosine-containing
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dsrna-binding
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drug development
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protein-rna
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antigenome
- 3.5.4.37
- inosine
-
a-to-i
- deaminases
-
deamination
-
adenosine-to-inosine
-
hereditaria
-
rna-editing
- pre-mrnas
-
dyschromatosis
-
symmetrica
- z-dna
- duplex
- ampa
-
left-handed
-
unedited
-
glur-b
-
recoding
-
site-selective
-
macules
-
interferon-inducible
- mda5
-
hypopigmented
-
ifn-inducible
-
dsrbds
-
interferon-stimulated
-
ca2+-permeable
-
5-ht2cr
- dicer
- samhd1
-
genodermatosis
- rig-i
-
hypermutation
-
ifn-stimulated
-
pigmentary
-
interferonopathy
-
autoinflammatory
- medicine
-
inosine-containing
-
dsrna-binding
- drug development
-
protein-rna
-
antigenome
Reaction
Synonyms
ADAR, ADAR1, ADAR1L, ADAR1S, ADAR2, ADAR2 deaminase, adenosine deaminase acting on RNA 1, adenosine deaminase acting on RNA-1, APOBEC1, bADAR1a, CiADAR1, dADAR, double-stranded RNA adenosine deaminase, double-stranded RNA-specific adenosine deaminase, double-stranded RNA-specific adenosine deaminase 1, double-stranded-RNA-specific adenosine deaminase 1, DRADA1, dsRAD, dsRNA adenosine deaminase, hADAR1, hADAR1a, hADAR2, hADAR2-D
ECTree
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Engineering
Engineering on EC 3.5.4.37 - double-stranded RNA adenine deaminase
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E861A
editing-deficient knock-in mutation. Adar1(E861A/E861A) embryos die at embryonic day 13.5, with activated interferon and double-stranded RNA-sensing pathways
additional information
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exchange of deaminase domains between ADAR1 and ADAR2 shows that this domain plays a dominant role in defining the substrate specificity of the resulting enzyme
additional information
exchange of deaminase domains between ADAR1 and ADAR2 shows that this domain plays a dominant role in defining the substrate specificity of the resulting enzyme
additional information
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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