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Information on EC 3.5.4.37 - double-stranded RNA adenine deaminase
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3.5.4.37 double-stranded RNA adenine deaminaseIUBMB Comments
This eukaryotic enzyme is involved in RNA editing. It destabilizes double-stranded RNA through conversion of adenosine to inosine. Inositol hexakisphosphate is required for activity .
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Word Map
- 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
The enzyme appears in viruses and cellular organisms
Reaction Schemes
adenine in double-stranded RNA
+
=
hypoxanthine in double-stranded RNA
+
Synonyms
adar1, adar2, dsrad, dadar, adenosine deaminase acting on rna 1, double-stranded rna adenosine deaminase, double-stranded rna-specific adenosine deaminase, ciadar1, dsrna adenosine deaminase, adar2 deaminase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADAR
ADAR1
ADAR2
double-stranded RNA-specific adenosine deaminase 1
hADAR2
ADAR1
-
ADAR1
-
two major isoforms of ADAR1, P150 and P110, named following their molecular weights, are yielded by different RNA splicings. The 150 kDa isoform, translated from exon 1a, is the full length protein that is mainly distributed in the cytosol. The 110 kDa isoform, coded by other alternative first exons and lacking the Z-DNA binding domains, is mainly located in the cell nucleus
ADAR2
-
ADAR2 lacks a part of the N-terminus region of ADAR1, upstream of its RNA binding domain, where ADAR1 contains two repeats of a Z-DNA binding motif
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
adenine in double-stranded RNA + H2O = hypoxanthine in double-stranded RNA + NH3
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
double-stranded RNA(adenine) aminohydrolase
This eukaryotic enzyme is involved in RNA editing. It destabilizes double-stranded RNA through conversion of adenosine to inosine. Inositol hexakisphosphate is required for activity [4].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
8-azaadenine in double-stranded RNA + H2O
8-azahypoxanthine in double-stranded RNA + NH3
-
8-aza substitution at adenosine in various RNA substrates accelerates the rate of deamination at these sites by ADAR2 (2.8-17-fold). The magnitude of this effect depends on the RNA structural context of the reacting nucleotide
-
-
?
adenosine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
although codon editing is important, it represents only a small fraction of the editing events in the transcriptome. Editing sites in non-coding regions of RNA are more prevalent. Introns and untranslated regions of mRNA are the primary non-coding targets, but editing also occurs in small RNAs, such as miRNAs. functions in the regulation of a variety of post-transcriptional processes. Inosine has different base-pairing properties from adenosine, and thus, editing alters RNA structure, coding potential and splicing patterns. Function primarily in proteome diversification, especially in the nervous system. Inosine is recognized as guanosine by the translation and splicing machineries, and thus, ADARs can alter the protein-coding information of an mRNA. In addition, because inosine prefers to pair with cytidine, ADARs destabilize dsRNA by changing AU base-pairs to IU mismatches, or increase its stability by changing AC mismatches to IC base-pairs
-
-
?
N6-methyladenine in double-stranded RNA + H2O
N6-methylhypoxanthine in double-stranded RNA + NH3
-
slow substrate for ADAR2, 2% of the rate compared to that of adenosine
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
-
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
-
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
although codon editing is important, it represents only a small fraction of the editing events in the transcriptome. Editing sites in non-coding regions of RNA are more prevalent. Introns and untranslated regions of mRNA are the primary non-coding targets, but editing also occurs in small RNAs, such as miRNAs. functions in the regulation of a variety of post-transcriptional processes. Inosine has different base-pairing properties from adenosine, and thus, editing alters RNA structure, coding potential and splicing patterns. Function primarily in proteome diversification, especially in the nervous system. Inosine is recognized as guanosine by the translation and splicing machineries, and thus, ADARs can alter the protein-coding information of an mRNA. In addition, because inosine prefers to pair with cytidine, ADARs destabilize dsRNA by changing AU base-pairs to IU mismatches, or increase its stability by changing AC mismatches to IC base-pairs
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
identification of ADAR substrates. RNA hairpins in noncoding regions of Caenorhabditis elegans mRNA are edited
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
-
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
-
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
-
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
-
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
A-to-I editing is a form of nucleotide substitution editing, because I is decoded as guanosine instead of A by ribosomes during translation and by polymerases during RNA-dependent RNA replication. Additionally, A-to-I editing can alter RNA structure stability as I:U mismatches are less stable than A:U base pairs. Both viral and cellular RNAs are edited by ADARs. A-to-I editing is of broad physiologic significance. Among the outcomes of A-to-I editing are biochemical changes that affect how viruses interact with their hosts, changes that can lead to either enhanced or reduced virus growth and persistence depending upon the specific virus
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
ADAR1 has the potential both to change information content through editing of mRNA and to regulate gene expression through interacting with the NF90 family proteins
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
ADAR1 is an editing enzyme that deaminates adenosine to inosine in long double stranded RNA duplexes and specific pre-mRNA transcripts
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
ADAR2 is an editing enzymes that deaminates adenosine to inosine in long double stranded RNA duplexes and specific pre-mRNA transcripts
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
although codon editing is important, it represents only a small fraction of the editing events in the transcriptome. Editing sites in non-coding regions of RNA are more prevalent. Introns and untranslated regions of mRNA are the primary non-coding targets, but editing also occurs in small RNAs, such as miRNAs. The enzyme functions in the regulation of a variety of post-transcriptional processes. Inosine has different base-pairing properties from adenosine, and thus, editing alters RNA structure, coding potential and splicing patterns. Function primarily in proteome diversification, especially in the nervous system. Inosine is recognized as guanosine by the translation and splicing machineries, and thus, ADARs can alter the protein-coding information of an mRNA. In addition, because inosine prefers to pair with cytidine, ADARs destabilize dsRNA by changing AU base-pairs to IU mismatches, or increase its stability by changing AC mismatches to IC base-pairs
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
editing of RNA changes the read-out of information from DNA by altering the nucleotide sequence of a transcript. One type of RNA editing found in all metazoans uses double-stranded RNA (dsRNA) as a substrate and results in the deamination of adenosine to give inosine, which is translated as guanosine
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
the enzyme catalyzes the hydrolytic deamination of adenosine to inosine in completely or partially double-stranded RNA
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
ADAR1 contains a domain (Zalpha) that binds specifically to the left-handed Z-DNA conformation with high affinity. As formation of Z-DNA in vivo occurs 5' to, or behind, a moving RNA polymerase during transcription, recognition of Z-DNA by DRADA1 provides a plausible mechanism by which DRADA1 can be targeted to a nascent RNA so that editing occurs before splicing
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
ADAR1-S edits HDV RNA during replication
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
identification of ADAR substrates. RNA hairpins in noncoding regions of human brain mRNA are edited
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
like ADAR1, ADAR2 has a 5' neighbor preference (A = U > C = G), but, unlike ADAR1, also has a 3' neighbor preference (U = G > C = A). ADAR2 prefers certain trinucleotide sequences (UAU, AAG, UAG, AAU). ADAR1 and ADAR2 have overlapping specificities. Xenopus and human ADAR1 have a highly similar, or identical, deamination specificity
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
RNA editing catalyzed by ADAR1 and ADAR2 involves the site-specific conversion of adenosine to inosine within imperfectly duplexed RNA. ADAR1- and ADAR2-mediated editing occurs within transcripts of glutamate receptors in the brain and in hepatitis delta virus RNA in the liver. The Q/R site within the GluR-B premessage is edited more efficiently by ADAR2 than it is by ADAR1. The converse is true for the 160 site within this same transcript. The base-pairing status of the targeted adenosine can affect the efficiency of editing by both ADAR1 and ADAR2. When the the substrate contains an A:C mismatch at the editing site, editing by both ADARs is enhanced compared to when A:A or A:G mismatches or A:U base pairs occurr at the same site. The deaminase domains plays a dominant role in defining the substrate specificity of the resulting enzyme
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
the specificity of the ADAR1 and ADAR2 deaminases ranges from highly site-selective to non-selective, dependent on the duplex structure of the substrate RNA
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
ADAR1 has a preference for binding simple duplex RNA as compared to highly structured RNA substrates
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
the nucleoside analog 8-azanebularine is introduced into this RNA (and derived constructs) to mechanistically trap the protein-RNA complex without catalytic turnover for EMSA and ribonuclease footprinting analyses. The human ADAR2 deaminase domain requires duplex RNA and is sensitive to 2-deoxy substitution at nucleotides opposite the editing site, the local sequence and 8-azanebularine nucleotide positioning on the duplex. The human ADAR2 deaminase domain protects about 23 nt on the edited strand around the editing site in an asymmetric fashion (about 18 nt on the 5' side and about 5 nt on the 3x02 side)
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
-
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
editing of Blcap, FlnA, and some sites within B1 and B2 SINEs clearly depends on ADAR1
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
ADAR1 specifically or preferentially edits 5HT2CR A and B sites
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
-
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
the enzyme is involved in involved in the editing of mammalian RNAs by the site-specific conversion of adenosine to inosine
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
editing frequency in rADAR2 pre-mRNA. Both sequence and structural elements are required to define adenosine moieties targeted for specific ADAR2-mediated deamination
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
pre-mRNA of glutamate receptor subunit B. ADAR2 selectively edits the R/G site (R/G stem-loop), while ADAR1 edits more promiscuously at several other adenosines in the double-stranded stem. The immediate structure surrounding the editing site is important. A purine opposite to the editing site has a negative effect on both selectivity and efficiency of editing. More distant internal loops in the substrate have minor effects on site selectivity, while efficiency of editing is influenced. Changes in the RNA structure that affected editing do not alter the binding abilities of ADAR2. Binding and catalysis are independent events
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
-
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
dsRNA is deaminated at the same sites whether it exists as a free molecule or is flanked by internal loops. Internal loops delineate helix ends for ADAR1. Since ADAR1 deaminates short RNAs at fewer adenosines than long RNAs, loops decrease the number of deaminations within an RNA by dividing a long RNA into shorter substrates
-
-
?
additional information
?
-
overexpression of p150 ADAR1 has no significant effect on the yield of vesicular stomatitis virus. reduction of p110 and p150 ADAR1 proteins to less than 10% to 15% of parental levels (ADAR1-deficient) has no significant effect on growth of Vesicular Stomatitis Virus in the absence of interferon treatment. The level of phosphorylated protein kinase PKR is increased in ADAR1-deficient cells compared to ADAR1-sufficient cells following IFN treatment, regardless of viral infection. ADAR1 suppresses activation of protein kinase PKR and inhibition of growth of Vesicular Stomatitis Virus in response to interferon treatment
-
-
?
additional information
?
-
human APOBEC1 possesses no antiviral activity
-
-
?
additional information
?
-
-
no product is observed with N6-ethyladenosine or 2,6-diaminopurine ribonucleoside in double-stranded RNA
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
adenosine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
although codon editing is important, it represents only a small fraction of the editing events in the transcriptome. Editing sites in non-coding regions of RNA are more prevalent. Introns and untranslated regions of mRNA are the primary non-coding targets, but editing also occurs in small RNAs, such as miRNAs. functions in the regulation of a variety of post-transcriptional processes. Inosine has different base-pairing properties from adenosine, and thus, editing alters RNA structure, coding potential and splicing patterns. Function primarily in proteome diversification, especially in the nervous system. Inosine is recognized as guanosine by the translation and splicing machineries, and thus, ADARs can alter the protein-coding information of an mRNA. In addition, because inosine prefers to pair with cytidine, ADARs destabilize dsRNA by changing AU base-pairs to IU mismatches, or increase its stability by changing AC mismatches to IC base-pairs
-
-
?
additional information
?
-
overexpression of p150 ADAR1 has no significant effect on the yield of vesicular stomatitis virus. reduction of p110 and p150 ADAR1 proteins to less than 10% to 15% of parental levels (ADAR1-deficient) has no significant effect on growth of Vesicular Stomatitis Virus in the absence of interferon treatment. The level of phosphorylated protein kinase PKR is increased in ADAR1-deficient cells compared to ADAR1-sufficient cells following IFN treatment, regardless of viral infection. ADAR1 suppresses activation of protein kinase PKR and inhibition of growth of Vesicular Stomatitis Virus in response to interferon treatment
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
-
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
although codon editing is important, it represents only a small fraction of the editing events in the transcriptome. Editing sites in non-coding regions of RNA are more prevalent. Introns and untranslated regions of mRNA are the primary non-coding targets, but editing also occurs in small RNAs, such as miRNAs. functions in the regulation of a variety of post-transcriptional processes. Inosine has different base-pairing properties from adenosine, and thus, editing alters RNA structure, coding potential and splicing patterns. Function primarily in proteome diversification, especially in the nervous system. Inosine is recognized as guanosine by the translation and splicing machineries, and thus, ADARs can alter the protein-coding information of an mRNA. In addition, because inosine prefers to pair with cytidine, ADARs destabilize dsRNA by changing AU base-pairs to IU mismatches, or increase its stability by changing AC mismatches to IC base-pairs
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
-
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
-
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
A-to-I editing is a form of nucleotide substitution editing, because I is decoded as guanosine instead of A by ribosomes during translation and by polymerases during RNA-dependent RNA replication. Additionally, A-to-I editing can alter RNA structure stability as I:U mismatches are less stable than A:U base pairs. Both viral and cellular RNAs are edited by ADARs. A-to-I editing is of broad physiologic significance. Among the outcomes of A-to-I editing are biochemical changes that affect how viruses interact with their hosts, changes that can lead to either enhanced or reduced virus growth and persistence depending upon the specific virus
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
ADAR1 has the potential both to change information content through editing of mRNA and to regulate gene expression through interacting with the NF90 family proteins
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
ADAR1 is an editing enzyme that deaminates adenosine to inosine in long double stranded RNA duplexes and specific pre-mRNA transcripts
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
ADAR2 is an editing enzymes that deaminates adenosine to inosine in long double stranded RNA duplexes and specific pre-mRNA transcripts
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
although codon editing is important, it represents only a small fraction of the editing events in the transcriptome. Editing sites in non-coding regions of RNA are more prevalent. Introns and untranslated regions of mRNA are the primary non-coding targets, but editing also occurs in small RNAs, such as miRNAs. The enzyme functions in the regulation of a variety of post-transcriptional processes. Inosine has different base-pairing properties from adenosine, and thus, editing alters RNA structure, coding potential and splicing patterns. Function primarily in proteome diversification, especially in the nervous system. Inosine is recognized as guanosine by the translation and splicing machineries, and thus, ADARs can alter the protein-coding information of an mRNA. In addition, because inosine prefers to pair with cytidine, ADARs destabilize dsRNA by changing AU base-pairs to IU mismatches, or increase its stability by changing AC mismatches to IC base-pairs
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
editing of RNA changes the read-out of information from DNA by altering the nucleotide sequence of a transcript. One type of RNA editing found in all metazoans uses double-stranded RNA (dsRNA) as a substrate and results in the deamination of adenosine to give inosine, which is translated as guanosine
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
the enzyme catalyzes the hydrolytic deamination of adenosine to inosine in completely or partially double-stranded RNA
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
-
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
editing of Blcap, FlnA, and some sites within B1 and B2 SINEs clearly depends on ADAR1
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
-
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
the enzyme is involved in involved in the editing of mammalian RNAs by the site-specific conversion of adenosine to inosine
-
-
?
adenine in double-stranded RNA + H2O
hypoxanthine in double-stranded RNA + NH3
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Inositol hexakisphosphate
is buried within the enzyme core, contributing to the protein fold. Inositol hexakisphosphate is required for activity. Amino acids that coordinate inositol hexakisphosphate in the crystal structure are conserved in some adenosine deaminases that act on tRNA
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no inhibition: DNA (salmon sperm, 0.3 mg/ml), RNA (torula yeast, 0.3 mg/ml), acidic proteins (bovine serum albumin and casein, 2.0 mg/ml), polyglutamic acid (2.0 mg/ml), glutamic acid (2 mM), glutamine (2 mM), glyceraldehyde 6-phosphate (2 mM), CaCl2 (5.0 mM), MgCl2 (5.0 mM), EDTA (10 mM), EGTA (10 mM), ATP (10 mM), GTP (10 mM), 5'-AMP (10 mM), adenosine (10 mM), hypoxanthine (10 mM)
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
spatiotemporal expression patterns for ADAR1 and ADAR2 in mouse forebrain. ADAR1 and ADAR2 are broadly distributed in most regions of the mouse forebrain, including the cerebral cortex, hippocampus, and diencephalon. High expression levels are maintained into adulthood. ADAR1 and ADAR2 are expressed in neurons but not astrocytes. ADAR1 mRNA has its lowest expression in the choroid plexus, cortex and hippocampus, while ADAR2 mRNA is least expressed in the cortex and hippocampus, with increased expression in the thalamus
brenda
spatiotemporal expression patterns for ADAR1 and ADAR2 in mouse forebrain. ADAR1 and ADAR2 are broadly distributed in most regions of the mouse forebrain, including the cerebral cortex, hippocampus, and diencephalon. High expression levels are maintained into adulthood. ADAR1 and ADAR2 are expressed in neurons but not astrocytes. ADAR1 mRNA has its lowest expression in the choroid plexus, cortex and hippocampus, while ADAR2 mRNA is least expressed in the cortex and hippocampus, with increased expression in the thalamus
brenda
dADAR is expressed in the developing nervous system
brenda
-
ubiquitously expressed in most tissues but is most abundant in the brain
brenda
expressed abundantly in post-diapause embryo
brenda
-
ADAR2-editing activity inhibits glioblastoma growth through the modulation of the CDC14B/Skp2/p21/p27 axis
brenda
full-length and N-terminally truncated forms of ADAR1 are simultaneously expressed in HeLa cells owing to the usage of alternative starting methionines
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
two major isoforms of ADAR1, P150 and P110, named following their molecular weights, are yielded by different RNA splicings. The 150 kDa isoform, translated from exon 1a, is the full length protein that is mainly distributed in the cytosol. The 110 kDa isoform, coded by other alternative first exons and lacking the Z-DNA binding domains, is mainly located in the cell nucleus
brenda
full-length and N-terminally truncated forms of ADAR1 are simultaneously expressed in HeLa cells. Because the N-terminus of ADAR1 contains a nuclear export signal, the full-length protein (150000 Da) localizes predominantly in the cytoplasm, whereas the N-terminally truncated forms (110000 Da) are exclusively nuclear and accumulate in the nucleolus. In living cells, editing might be regulated by the intracellular compartmentalization of editing enzymes. ADAR1 shuttles between the nucleolus, the nucleoplasm and the cytoplasm
brenda
-
the ADAR1 p150 protein is found in both the cytoplasm and the nucleus, whereas the p110 protein localizes predominantly if not exclusively to the nucleus
brenda
ADAR2 localizes exclusively to the nucleus and accumulates in the nucleolus. In living cells, editing might be regulated by the intracellular compartmentalization of editing enzymes. ADAR2 shuttles between the nucleolus and the nucleoplasm
brenda
full-length and N-terminally truncated forms of ADAR1 are simultaneously expressed in HeLa cells. Because the N-terminus of ADAR1 contains a nuclear export signal, the full-length protein (150000 Da) localizes predominantly in the cytoplasm, whereas the N-terminally truncated forms (110000 Da) are exclusively nuclear and accumulate in the nucleolus. In living cells, editing might be regulated by the intracellular compartmentalization of editing enzymes. ADAR1 shuttles between the nucleolus, the nucleoplasm and the cytoplasm
brenda
-
the ADAR1 p150 protein is found in both the cytoplasm and the nucleus, whereas the p110 protein localizes predominantly if not exclusively to the nucleus
brenda
-
two major isoforms of ADAR1, P150 and P110, named following their molecular weights, are yielded by different RNA splicings. The 150 kDa isoform, translated from exon 1a, is the full length protein that is mainly distributed in the cytosol. The 110 kDa isoform, coded by other alternative first exons and lacking the Z-DNA binding domains, is mainly located in the cell nucleus
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
ADAR1 knockout embryos die at day 11.5 to 12. ADAR1 is not completely necessary for cell survival because some cells survive without ADAR1. ADAR1 is dispensable in pluripotent cells for their survival and proliferation
malfunction
ADAR1-/- homozygous embryos die at E11.0 to E12.5. Widespread apoptosis is detected in many tissues of ADAR1-/- embryos collected live at E10.5 to E11.5, despite their normal gross appearance
malfunction
homozygosity for two different null alleles of ADAR1 causes a consistent embryonic phenotype appearing early at embryonic day 11 and leading to death between embryonic days 11.5 and 12.5. This phenotype manifests a rapidly disintegrating liver structure, along with severe defects in definitive hematopoiesis, encompassing both erythroid and myeloid/granuloid progenitors as well as spleen colonyforming activity from the aorta-gonad-mesonephros region and fetal liver
malfunction
-
knockdown of ADAR2 expression markedly impairs glucose-stimulated insulin secretion in the rat insulinoma INS-1 cells and primary pancreatic islets and significantly diminishes KCl-stimulated secretion of exogenous human growth hormone or endogenous chromogranin B protein in the rat adrenal pheochromocytoma PC12 cells
malfunction
-
the ADAR2 knockout phenotype can be attributed to the lack of editing of the GluR-B receptor. ADAR1 deficiency results in an embryonic lethal phenotype
malfunction
-
knock-down of ADAR1 increases HIV-1 replication in primary macrophages
malfunction
-
loss of ADAR1 induces endoplasmic reticulum stress and activation of interferon signaling, and alters expression in WNT targets, followed by intestinal inflammation and crypt apoptosis
malfunction
A-to-I underediting at the glutamine (Q)/arginine (R) site of the glutamate receptor subunit B (GluR-B) is associated with the pathogenesis and invasiveness of glioma and is confirmed in the glioma cell lines U87, U251 and A172 compared with that in normal human astrocytes. The expression of ADAR2 mRNA was not significantly altered in the glioma cell lines. Aberrant alternative splicing pattern of ADAR2 downregulates A-to-I editing in glioma
malfunction
dysregulation of A-to-I editing by ADAR1 can have profound consequences, ranging from effects on cell growth and development to autoimmune disorders
malfunction
interferon treatment of Adar1-/-x02cells lacking both the p110 constitutive and p150 interferon-inducible ADAR1 proteins induces formation of stress granules, whereas neither wild-type nor Adar2x02-/-x02 cells display a comparable stress granule response following interferon treatment. Phosphorylation of protein synthesis initiation factor eIF2alpha at Ser51 is increased in interferon-treated Adar1x02-/-x02cells but not in either wild-type or Adar2x02-/- cells following interferon treatment
malfunction
knockdown of ADAR by RNA interference induces formation of pseudo-diapause embryos, which lack resistance to the stresses and exhibit high levels of apoptosis
malfunction
knockdown of ADARa in lung adenocarcinoma cells with amplified ADAR leads to decreased migration and invasion
metabolism
ADAR1 is an essential enzyme for normal development. The interferon-inducible ADAR1p150 is involved in immune responses to both exogenous and endogenous triggers, whereas the functions of the constitutively expressed ADAR1p110 are variable. ADAR1 is involved in the recognition of self versus non-self dsRNA. This provides potential explanations for its links to hematopoiesis, type I interferonopathies, and viral infections. Editing in both coding and noncoding sequences results in diseases ranging from cancers to neurological abnormalities. Furthermore, editing of noncoding sequences, like microRNAs, can regulate protein expression, while editing of Alu sequences can affect translational efficiency and editing of proximal sequences. Identifications of long noncoding RNA and retrotransposons as editing targets expand the effects of A-to-I editing. Besides editing, ADAR1 also interacts with other dsRNA-binding proteins in editing-independent manners
metabolism
ADAR2 is the main enzyme responsible for A-to-I editing in humans
metabolism
role of ADAR1 as a suppressor of dsRNA-triggered innate immune responses
metabolism
the enzyme (ADAR1) regulates the phosphorylation of activation of protein kinase (PKR) and eukaryotic translation initiation factor 2 alpha (eIF2) in both an IFN-dependent and IFN-independent manner, and its inhibitory effect on the IFN production partially contributes to its proviral effect. The enzyme promotes the Zika virus replication by inhibiting the activation of protein kinase PKR
metabolism
the enzyme contributes to resistance to stress in Artemia diapause embryos
metabolism
the enzyme is an essential gene for the survival of a subset of cancer cell lines. ADAR1-dependent cell lines display increased expression of interferon-stimulated genes. Activation of type I interferon signaling in the context of ADAR1 deficiency can induce cell lethality in non-ADAR1-dependent cell lines
physiological function
ADAR1 has the potential both to change information content through editing of mRNA and to regulate gene expression through interacting with the NF90 family proteins
physiological function
ADAR1 is required for cell survival and embryo development by protecting against stress-induced apoptosis
physiological function
ADAR1 plays an essential role in adult hematopoiesis through its RNA editing activity in hematopoietic progenitor cells
physiological function
-
ADAR2-editing activity inhibits glioblastoma growth through the modulation of the CDC14B/Skp2/p21/p27 axis
physiological function
-
editing of RNA changes the read-out of information from DNA by altering the nucleotide sequence of a transcript. One type of RNA editing found in all metazoans uses double-stranded RNA (dsRNA) as a substrate and results in the deamination of adenosine to give inosine, which is translated as guanosine
physiological function
-
the enzyme is implicated in the antiviral immune response
physiological function
-
the enzyme is involved in RNA editing in order to generate many different mRNAs from the same gene, increasing the transcriptome and then the proteome. The most frequent RNA editing mechanism in mammals involves the conversion of specific adenosines into inosines by the ADAR family of enzymes. This editing event can change both the sequence and the secondary structure of RNA molecules, with important consequences on both the final proteins and regulatory RNAs. Alteration in RNA editing has been connected to numerous human pathologies and is important in tumor progression. RNA editing on non-coding RNA can affect the secondary (and consequently the tertiary) structure of the RNAs and then modulate and/or prevent RNA-protein and RNA-RNA interactions. RNA editing on non-coding portions of the transcripts could influence splicing, localization, stability and translation efficiency of the transcripts
physiological function
-
ADAR1 is essential for intestinal homeostasis and stem cell maintenance by suppressing endoplasmic reticulum stress and interferon signaling
physiological function
-
ADAR1 restricts HIV-1 replication post-transcriptionally in macrophages harboring HIV-1 provirus
physiological function
-
ADAR1 significantly promotes equine infectious anemia virus replication and infectivity
physiological function
A-to-I editing of endogenous dsRNA is the essential function of ADAR1, preventing the activation of the cytosolic dsRNA response by endogenous transcripts
physiological function
-
equine ADAR1 (eADAR1) is a positive regulator of equine infectious anemia virus (EIAV). eADAR1 significantly promotes EIAV replication, and the enhancement of viral protein expression is associated with the long terminal repeat (LTR) and Rev response element regions. The RNA binding domain 1 of eADAR1 is essential only for enhancing LTR-mediated gene expression. eADAR1 increases the EIAV infectivity
physiological function
the enzyme (ADAR2) is a radar enzyme that maintains a degree of editing in the miRNA population and balances miRNA expression, maintaining them at physiological, that is, safe, levels. Whenever ADAR2 is impaired (that is, in glioblastoma), miRNA homeostasis is altered and this may contribute to cancer progression. The major effect of ADAR2 is to reduce the expression of a large number of miRNAs, most of which act as onco-miRNAs. ADAR2 can edit miR-222/221 and miR-21 precursors and decrease the expression of the corresponding mature onco-miRNAs in vivo and in vitro, with important effects on cell proliferation and migration
physiological function
-
the enzyme is proposed to contribute to the adaptation of equine infectious anemia virus from horses to donkeys
physiological function
the majority of editing in mouse embryo fibroblasts is carried out by ADAR1. ADAR1 p150 as the major A-to-I editor in mouse embryo fibroblasts, acts as a feedback suppressor of innate immune responses otherwise triggered by self-RNAs possessing regions of double-stranded character
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DSRAD_CAEEL
495
0
55320
Swiss-Prot
other Location (Reliability: 1)
DSRAD_HUMAN
1226
0
136066
Swiss-Prot
other Location (Reliability: 4)
DSRAD_MOUSE
1178
0
130447
Swiss-Prot
other Location (Reliability: 4)
DSRAD_RAT
1175
0
129911
Swiss-Prot
other Location (Reliability: 3)
RED1_HUMAN
741
0
80763
Swiss-Prot
other Location (Reliability: 1)
RED1_MOUSE
711
0
78001
Swiss-Prot
other Location (Reliability: 1)
RED1_RAT
711
0
77925
Swiss-Prot
other Location (Reliability: 1)
A0A812B244_SEPPH
697
1
78308
TrEMBL
Secretory Pathway (Reliability: 1)
A0A7L9DJ52_9ANNE
857
0
94010
TrEMBL
other Location (Reliability: 1)
A0A8M1P8J0_DANRE
1381
0
151401
TrEMBL
Mitochondrion (Reliability: 5)
A0A1D6Y7R2_CHICK
1153
0
126062
TrEMBL
Mitochondrion (Reliability: 4)
A0A8B6FM14_MYTGA
643
0
72042
TrEMBL
other Location (Reliability: 4)
A0A8B6GL72_MYTGA
1155
0
129529
TrEMBL
other Location (Reliability: 1)
A0A6J8APA5_MYTCO
722
0
80603
TrEMBL
other Location (Reliability: 4)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
12000
-
x * 12000, the purified monomeric enzyme form is active, but it is not known if the enzyme functions strictly as a monomer, it may dimerize in the presence of substrate or associate in crude mixture with other cellular constituents, SDS-PAGE
150000
90000
2 * 90000, ADAR2 forms a stable enzymatically active homodimer complex, SDS-PAGE
150000
2 * 150000, ADAR1 forms a stable enzymatically active homodimer complex, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
?
-
x * 12000, the purified monomeric enzyme form is active, but it is not known if the enzyme functions strictly as a monomer, it may dimerize in the presence of substrate or associate in crude mixture with other cellular constituents, SDS-PAGE
dimer
2 * 150000, ADAR1 forms a stable enzymatically active homodimer complex, SDS-PAGE
dimer
2 * 90000, ADAR2 forms a stable enzymatically active homodimer complex, SDS-PAGE
dimer
-
ADAR1 and ADAR2 form respective homodimers, and this association is essential for their enzymatic activities. ADAR dimerization independent of their binding to dsRNA
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the proteolytically defined Z-DNA binding domain Za of adenosine deaminase type 1 is crystallized in complex with the DNA oligomer d(TCGCGCG). The crystals are obtained from a solution containing ammonium sulfate as precipitating agent and belong to the tetragonal space group P4212
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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
-
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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
equine ADAR1 (eADAR1) cDNA is cloned from mRNA extracted from eMDMs and expressed using the adenoviral expression vector pDC315
-
expression in Sf9 cells
large-scale overexpression in Saccharomyces cerevisiae with an N-terminal histidine tag that is cleaved by the tobacco etch virus protease
-
overexpression in Escherichia coli and Pichia pastoris, advantages of using Pichia pastoris for overexpression, large scale expression
-
the Z-DNA binding domain is expressed as a C-terminal glutathione S-transferase fusion in Escherichia coli using a pGEX-5X1 cloning vector
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ADAR1 and ADAR2 are expressed at low levels in the fetal brain, and increase gradually over time. High expression levels were maintained into adulthood
CiADAR1 mRNA expression is rapidly and significantly elevated after dsRNA (poly(I:C)) stimulation
-
isoform ADAR1L is induced by interferon gamma or HIV-1 infection in primary macrophages but not in primary CD4 T cells
-
isoform P110 is constitutively expressed in cells. In early mouse embryos, isoform P110 is expressed on day 10.5, but P150 was not expressed until day 15
-
mRNA expression of CiADAR1 is significantly upregulated and reaches peak at 24 h post grass carp reovirus challenge in vivo and in vitro
-
significantly induced in response to the stresses of salinity and heat-shock
the dADAR expression pattern is determined by in situ hybridization to whole Drosophila embryos of various developmental stages. A low level of nonspecific staining is seen in early stage 13 embryos (end of germ-band retraction), specific staining is seen by late stage 13 after condensation of the ventral nerve cord occurs. Staining then proceedes to intensify within the central nervous system, reaching high levels in the embryonic ventral nerve cord and brain by stage 16
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
medicine
drug development
ADAR1 is a potential therapeutic target in a subset of cancers
drug development
the enzyme (ADAR1) promotes the Zika virus replication by inhibiting the activation of protein kinase PKR. The enzyme can be a potential target of antiviral drugs
medicine
ADAR2 is a promising target for an anti-tumoral strategy, since ADAR2 alone can simultaneously modulate more than one miRNA and cellular pathway altered in cancer cells
medicine
enzyme (ADAR1) expression is an independent predictor of tumor recurrence. Small molecule inhibition of focal adhesion kinase activity may be a potential therapeutic strategy for the treatment of lung adenocarcinoma with high ADAR1 expression
medicine
the levels of RNA editing by ADAR1 can serve as new tools for diagnosis in cancer stem cell-related illnesses. In situations where ADAR1 overexpression contributes to disease progression, as in several cancers, or where ADAR1 interacts with other proteins in editing-independent manners, inhibition of ADAR1 could potentially be another strategy in treatment
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hough, R.F.; Bass, B.L.
Purification of the Xenopus laevis double-stranded RNA adenosine deaminase
J. Biol. Chem.
269
9933-9939
1994
Xenopus laevis
brenda
Schwartz, T.; Shafer, K.; Lowenhaupt, K.; Hanlon, E.; Herbert, A.; Rich, A.
Crystallization and preliminary studies of the DNA-binding domain Za from ADAR1 complexed to left-handed DNA
Acta Crystallogr. Sect. D
55
1362-1364
1999
Homo sapiens
brenda
Wang, Q.
RNA editing catalyzed by ADAR1 and its function in mammalian cells
Biochemistry (Moscow)
76
900-911
2011
Mus musculus
brenda
Lehmann, K.A.; Bass, B.L.
Double-stranded RNA adenosine deaminases ADAR1 and ADAR2 have overlapping specificities
Biochemistry
39
12875-12884
2000
Homo sapiens
brenda
Jacobs, M.M.; Fogg, R.L.; Emeson, R.B.; Stanwood, G.D.
ADAR1 and ADAR2 expression and editing activity during forebrain development
Dev. Neurosci.
31
223-237
2009
Mus musculus (Q99MU3), Mus musculus
brenda
Yang, L.; Zhao, L.; Gan, Z.; He, Z.; Xu, J.; Gao, X.; Wang, X.; Han, W.; Chen, L.; Xu, T.; Li, W.; Liu, Y.
Deficiency in RNA editing enzyme ADAR2 impairs regulated exocytosis
FASEB J.
24
3720-3732
2010
Rattus norvegicus
brenda
Yang, C.; Su, J.; Li, Q.; Zhang, R.; Rao, Y.
Identification and expression profiles of ADAR1 gene, responsible for RNA editing, in responses to dsRNA and GCRV challenge in grass carp (Ctenopharyngodon idella)
Fish Shellfish Immunol.
33
1042-1049
2012
Ctenopharyngodon idella
brenda
Veliz, E.A.; Easterwood, L.M.; Beal, P.A.
Substrate analogues for an RNA-editing adenosine deaminase: mechanistic investigation and inhibitor design
J. Am. Chem. Soc.
125
10867-10876
2003
Homo sapiens
brenda
Cho, D.S.; Yang, W.; Lee, J.T.; Shiekhattar, R.; Murray, J.M.; Nishikura, K.
Requirement of dimerization for RNA editing activity of adenosine deaminases acting on RNA
J. Biol. Chem.
278
17093-17102
2003
Homo sapiens, Homo sapiens (P55265), Mus musculus (Q99MU3), Mus musculus
brenda
Hartner, J.C.; Schmittwolf, C.; Kispert, A.; Mller, A.M.,; Higuchi, M.; Seeburg, P.H.
Liver disintegration in the mouse embryo caused by deficiency in the RNA-editing enzyme ADAR1
J. Biol. Chem.
279
4894-4902
2004
Mus musculus (Q99MU3), Mus musculus
brenda
Dawson, T.R.; Sansam, C.L.; Emeson, R.B.
Structure and sequence determinants required for the RNA editing of ADAR2 substrates
J. Biol. Chem.
279
4941-4951
2004
Rattus norvegicus
brenda
Wang, Q.; Miyakoda, M.; Yang, W.; Khillan, J.; Stachura, D.L.; Weiss, M.J.; Nishikura, K.
Stress-induced apoptosis associated with null mutation of ADAR1 RNA editing deaminase gene
J. Biol. Chem.
279
4952-4961
2003
Mus musculus (Q99MU3)
brenda
Valente, L.; Nishikura, K.
RNA binding-independent dimerization of adenosine deaminases acting on RNA and dominant negative effects of nonfunctional subunits on dimer functions
J. Biol. Chem.
282
16054-16061
2007
Homo sapiens
brenda
Desterro, J.M.; Keegan, L.P.; Lafarga, M.; Berciano, M.T.; O'Connell, M.; Carmo-Fonseca, M.
Dynamic association of RNA-editing enzymes with the nucleolus
J. Cell Sci.
116
1805-1818
2003
Homo sapiens, Homo sapiens (P55265)
brenda
Lehmann, K.A.; Bass, B.L.
The importance of internal loops within RNA substrates of ADAR1
J. Mol. Biol.
291
1-13
1999
Xenopus laevis
brenda
Macbeth, M.R.; Bass, B.L.
Large-scale overexpression and purification of ADARs from Saccharomyces cerevisiae for biophysical and biochemical studies
Methods Enzymol.
424
319-331
2007
Homo sapiens
brenda
O'Connell, M.A.; Gerber, A.; Keegan, L.P.
Purification of native and recombinant double-stranded RNA-specific adenosine deaminases
Methods
15
51-62
1998
Bos taurus, Homo sapiens
brenda
Nie, Y.; Ding, L.; Kao, P.N.; Braun, R.; Yang, J.H.
ADAR1 interacts with NF90 through double-stranded RNA and regulates NF90-mediated gene expression independently of RNA editing
Mol. Cell. Biol.
25
6956-6963
2005
Homo sapiens (P55265)
brenda
Kllman, A.M.; Sahlin, M.; Ohman, M.
ADAR2 A->I editing: site selectivity and editing efficiency are separate events
Nucleic Acids Res.
31
4874-4881
2003
Rattus norvegicus
brenda
Ikeda, T.; Ohsugi, T.; Kimura, T.; Matsushita, S.; Maeda, Y.; Harada, S.; Koito, A.
The antiretroviral potency of APOBEC1 deaminase from small animal species
Nucleic Acids Res.
36
6859-6871
2008
Homo sapiens (P41238)
brenda
Galeano, F.; Rossetti, C.; Tomaselli, S.; Cifaldi, L.; Lezzerini, M.; Pezzullo, M.; Boldrini, R.; Massimi, L.; Di Rocco, C.M.; Locatelli, F.; Gallo, A.
ADAR2-editing activity inhibits glioblastoma growth through the modulation of the CDC14B/Skp2/p21/p27 axis
Oncogene
32
998-1009
2013
Homo sapiens
brenda
XuFeng, R.; Boyer, M.J.; Shen, H.; Li, Y.; Yu, H.; Gao, Y.; Yang, Q.; Wang, Q.; Cheng, T.
ADAR1 is required for hematopoietic progenitor cell survival via RNA editing
Proc. Natl. Acad. Sci. USA
106
17763-17768
2009
Mus musculus (Q99MU3)
brenda
Herbert, A.; Alfken, J.; Kim, Y.G.; Mian, I.S.; Nishikura, K.; Rich, A.
A Z-DNA binding domain present in the human editing enzyme, double-stranded RNA adenosine deaminase
Proc. Natl. Acad. Sci. USA
94
8421-8426
1997
Homo sapiens
brenda
Wong, S.K.; Lazinski, D.W.
Replicating hepatitis delta virus RNA is edited in the nucleus by the small form of ADAR1
Proc. Natl. Acad. Sci. USA
99
15118-15123
2002
Homo sapiens
brenda
Morse, D.P.; Aruscavage, P.J.; Bass, B.L.
RNA hairpins in noncoding regions of human brain and Caenorhabditis elegans mRNA are edited by adenosine deaminases that act on RNA
Proc. Natl. Acad. Sci. USA
99
7906-7911
2002
Caenorhabditis elegans, Homo sapiens
brenda
Gallo, A.; Galardi, S.
A-to-I RNA editing and cancer: from pathology to basic science
RNA Biol.
5
135-139
2008
Homo sapiens
brenda
Riedmann, E.M.; Schopoff, S.; Hartner, J.C.; Jantsch, M.F.
Specificity of ADAR-mediated RNA editing in newly identified targets
RNA
14
1110-1118
2008
Mus musculus
brenda
Palladino, M.J.; Keegan, L.P.; O'Connell, M.A.; Reenan, R.A.
dADAR, a Drosophila double-stranded RNA-specific adenosine deaminase is highly developmentally regulated and is itself a target for RNA editing
RNA
6
1004-1018
2000
Drosophila melanogaster (Q9NII1)
brenda
Wong, S.K.; Sato, S.; Lazinski, D.W.
Substrate recognition by ADAR1 and ADAR2
RNA
7
846-858
2001
Homo sapiens, Homo sapiens (P78563)
brenda
Macbeth, M.R.; Schubert, H.L.; Vandemark, A.P.; Lingam, A.T.; Hill, C.P.; Bass B.L.
Inositol hexakisphosphate is bound in the ADAR2 core and required for RNA editing
Science
309
1534-1539
2005
Homo sapiens (P78563), Homo sapiens
brenda
Hundley, H.A.; Bass, B.L.
ADAR editing in double-stranded UTRs and other noncoding RNA sequences
Trends Biochem. Sci.
35
377-383
2010
Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens
brenda
Li, Z.; Wolff, K.C.; Samuel, C.E.
RNA adenosine deaminase ADAR1 deficiency leads to increased activation of protein kinase PKR and reduced vesicular stomatitis virus growth following interferon treatment
Virology
396
316-322
2009
Homo sapiens (P55265)
brenda
Samuel, C.E.
Adenosine deaminases acting on RNA (ADARs) are both antiviral and proviral
Virology
411
180-193
2011
Homo sapiens
brenda
Qiu, W.; Wang, X.; Buchanan, M.; He, K.; Sharma, R.; Zhang, L.; Wang, Q.; Yu, J.
ADAR1 is essential for intestinal homeostasis and stem cell maintenance
Cell Death Dis.
4
e599
2013
Mus musculus
brenda
Weiden, M.D.; Hoshino, S.; Levy, D.N.; Li, Y.; Kumar, R.; Burke, S.A.; Dawson, R.; Hioe, C.E.; Borkowsky, W.; Rom, W.N.; Hoshino, Y.
Adenosine deaminase acting on RNA-1 (ADAR1) inhibits HIV-1 replication in human alveolar macrophages
PLoS ONE
9
e108476
2014
Homo sapiens
brenda
Tang, Y.D.; Na, L.; Fu, L.H.; Yang, F.; Zhu, C.H.; Tang, L.; Li, Q.; Wang, J.Y.; Li, Z.; Wang, X.F.; Li, C.Y.; Wang, X.; Zhou, J.H.
Double-stranded RNA-specific adenosine deaminase 1 (ADAR1) promotes EIAV replication and infectivity
Virology
476
364-371
2015
Equus caballus
brenda
Tang, Y.D.; Zhang, X.; Na, L.; Wang, X.F.; Fu, L.H.; Zhu, C.H.; Wang, X.; Zhou, J.H.
Double-stranded-RNA-specific adenosine deaminase 1 (ADAR1) is proposed to contribute to the adaptation of equine infectious anemia virus from horses to donkeys
Arch. Virol.
161
2667-2672
2016
Equus asinus asinus
brenda
Song, C.; Sakurai, M.; Shiromoto, Y.; Nishikura, K.
Functions of the RNA editing enzyme ADAR1 and their relevance to human diseases
Genes (Basel)
7
E129
2016
Homo sapiens (P55265), Homo sapiens
brenda
Tomaselli, S.; Galeano, F.; Alon, S.; Raho, S.; Galardi, S.; Polito, V.A.; Presutti, C.; Vincenti, S.; Eisenberg, E.; Locatelli, F.; Gallo, A.
Modulation of microRNA editing, expression and processing by ADAR2 deaminase in glioblastoma
Genome Biol.
16
5
2015
Homo sapiens (P78563), Homo sapiens
brenda
George, C.X.; Ramaswami, G.; Li, J.B.; Samuel, C.E.
Editing of cellular self-RNAs by adenosine deaminase ADAR1 suppresses innate immune stress responses
J. Biol. Chem.
291
6158-6168
2016
Mus musculus (Q99MU3), Mus musculus
brenda
Samuel, C.E.
Adenosine deaminase acting on RNA (ADAR1), a suppressor of double-stranded RNA-triggered innate immune responses
J. Biol. Chem.
294
1710-1720
2019
Homo sapiens (P55265)
brenda
Zhou, S.; Yang, C.; Zhao, F.; Huang, Y.; Lin, Y.; Huang, C.; Ma, X.; Du, J.; Wang, Y.; Long, G.; He, J.; Liu, C.; Zhang, P.
Double-stranded RNA deaminase ADAR1 promotes the Zika virus replication by inhibiting the activation of protein kinase PKR
J. Biol. Chem.
294
18168-18180
2019
Homo sapiens (P55265), Homo sapiens
brenda
Gannon, H.S.; Zou, T.; Kiessling, M.K.; Gao, G.F.; Cai, D.; Choi, P.S.; Ivan, A.P.; Buchumenski, I.; Berger, A.C.; Goldstein, J.T.; Cherniack, A.D.; Vazquez, F.; Tsherniak, A.; Levanon, E.Y.; Hahn, W.C.; Meyerson, M.
Identification of ADAR1 adenosine deaminase dependency in a subset of cancer cells
Nat. Commun.
9
5450
2018
Homo sapiens (P55265)
brenda
Phelps, K.J.; Tran, K.; Eifler, T.; Erickson, A.I.; Fisher, A.J.; Beal, P.A.
Recognition of duplex RNA by the deaminase domain of the RNA editing enzyme ADAR2
Nucleic Acids Res.
43
1123-1132
2015
Homo sapiens (P78563), Homo sapiens
brenda
Wang, X.; Vukovic, L.; Koh, H.R.; Schulten, K.; Myong, S.
Dynamic profiling of double-stranded RNA binding proteins
Nucleic Acids Res.
43
7566-7576
2015
Homo sapiens (P55265), Homo sapiens
brenda
Li, Z.; Tian, Y.; Tian, N.; Zhao, X.; Du, C.; Han, L.; Zhang, H.
Aberrant alternative splicing pattern of ADAR2 downregulates adenosine-to-inosine editing in glioma
Oncol. Rep.
33
2845-2852
2015
Homo sapiens (P78563), Homo sapiens
brenda
Amin, E.M.; Liu, Y.; Deng, S.; Tan, K.S.; Chudgar, N.; Mayo, M.W.; Sanchez-Vega, F.; Adusumilli, P.S.; Schultz, N.; Jones, D.R.
The RNA-editing enzyme ADAR promotes lung adenocarcinoma migration and invasion by stabilizing FAK
Sci. Signal.
10
eaah3941
2017
Homo sapiens (P55265)
brenda
Liddicoat, B.J.; Piskol, R.; Chalk, A.M.; Ramaswami, G.; Higuchi, M.; Hartner, J.C.; Li, J.B.; Seeburg, P.H.; Walkley, C.R.
RNA editing by ADAR1 prevents MDA5 sensing of endogenous dsRNA as nonself
Science
349
1115-1120
2015
Mus musculus (Q99MU3)
brenda
Dai, L.; Liu, X.C.; Ye, S.; Li, H.W.; Chen, D.F.; Yu, X.J.; Huang, X.T.; Zhang, L.; Yang, F.; Yang, J.S.; Yang, W.J.
The RNA-editing deaminase ADAR is involved in stress resistance of Artemia diapause embryos
Stress
19
609-620
2016
Artemia parthenogenetica (A0A3G1FKL8)
brenda
Tang, Y.D.; Na, L.; Fu, L.H.; Yang, F.; Zhu, C.H.; Tang, L.; Li, Q.; Wang, J.Y.; Li, Z.; Wang, X.F.; Li, C.Y.; Wang, X.; Zhou, J.H.
Double-stranded RNA-specific adenosine deaminase 1 (ADAR1) promotes EIAV replication and infectivity
Virology
476
364-371
2015
Equus sp.
brenda
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