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Information on EC 3.5.4.38 - single-stranded DNA cytosine deaminase
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3.5.4.38 single-stranded DNA cytosine deaminaseIUBMB Comments
The enzyme exclusively catalyses deamination of cytosine in single-stranded DNA. It preferentially deaminates five-nucleotide bubbles. The optimal target consists of a single-stranded NWRCN motif (W = A or T, R = A or G) . The enzyme initiates antibody diversification processes by deaminating immunoglobulin sequences.
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Word Map
- 3.5.4.38
- apobec3s
-
deamination
-
hypermutation
- deaminases
- immunoglobulin
- uracil
- viruses
-
apolipoprotein
- retroviruses
-
diversification
- ige
- virion
-
polypeptide-like
-
retroviral
-
mrna-editing
-
retrotransposons
-
antiretroviral
-
retroelements
-
vif-deficient
-
anti-hiv-1
-
retrotransposition
-
class-switching
- glycosylase
- lentiviruses
-
uracil-dna
-
line-1
-
proviral
-
vif-mediated
-
aid-dependent
-
cccdna
-
aid-induced
-
abasic
-
c-to-u
-
encapsidation
-
translesion
-
r-loops
-
sivmac
- molecular biology
- samhd1
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
cytosine in single-stranded DNA
+
=
uracil in single-stranded DNA
+
Synonyms
apobec3b, apobec3a, apobec3f, activation-induced deaminase, apobec3h, apobec3c, apobec3d, single-stranded dna cytosine deaminase, apobec3z1, ssdna cytidine deaminase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
activation-induced cytidine deaminase
activation-induced deaminase
AICDA
AID
APOBEC3A
activation-induced deaminase
-
AID
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cytosine in single-stranded DNA + H2O = uracil in single-stranded DNA + NH3
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
single-stranded DNA cytosine aminohydrolase
The enzyme exclusively catalyses deamination of cytosine in single-stranded DNA. It preferentially deaminates five-nucleotide bubbles. The optimal target consists of a single-stranded NWRCN motif (W = A or T, R = A or G) [2]. The enzyme initiates antibody diversification processes by deaminating immunoglobulin sequences.
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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
5-methylcytosine in single-stranded DNA + H2O
?
the enzyme exhibits low activity toward 5-methylcytosine n single-stranded DNA
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
-
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
-
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
-
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
-
-
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
-
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
-
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
activation-induced cytidine deaminase (AID) produces DNA breaks in immunoglobulin genes during antibody diversification. Double-stranded breaks in the switch region mediate class switch recombination, and contribute to gene conversion and somatic hypermutation in the variable regions. Among potential highly transcribed genes in mouse hybridoma cells, the immunoglobulin heavy and light chain genes are important AID targets, with the immunoglobulin mu switch region being preferred compared to other genomic sites
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
activation-induced deaminase is the initiator for somatic hypermutation (SHM) and class switch recombination (CSR). The enzyme targets the highly repetitive switch regions of the immunoglobulin heavy chain locus to induce DNA double-strand breaks (DSBs), which can be rejoined, leading to switch of constant regions of antibody. When targeting to variable region exons of IgH and IgL loci, the enzyme predominantly induces point mutations, termed SHM, resulting in increased affinity of antibody for antigen. While somatic hypermutation and class switch recombination (CSR) enhance antibody diversity, activation-induced deaminase initiated double-strand breaks and mutations may predispose B cells to carcinogenesis
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
AID mediates hypermutation by deaminating single stranded DNA. In vivo, single stranded DNA may arise transiently during transcription
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the enzyme can act on transcribing DNA. It is required for the maturation of antibodies in higher vertebrates, where it promotes somatic hypermutation
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the enzyme deaminates cytidine residues in the DNA of the variable and the switch regions of the immunoglobulin locus. The resulting uracil induces error-prone DNA synthesis in the case of hypermutation or DNA breaks that activate nonhomologous recombination in the case of class-switch recombination
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the enzyme deaminates DNA at transcribed Ig genes. Expressed immunoglobulin genes undergo alterations in sequence and genomic structure in order to optimize antibody function. A single B cell-specific factor, activation-induced deaminase (AID), initiates these changes by deamination of cytosine to uracil. At the Ig loci of B-cells, AID-initiated damage is processed to produce three distinct outcomes: somatic hypermutation, class switch recombination and gene conversion
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the enzyme initiates antibody diversification processes by deaminating immunoglobulin sequences
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
activation-induced cytidine deaminase initiates secondary antibody diversification processes by deaminating cytidines on single-stranded DNA. AID preferentially deaminates cytidines preceded by W(A/T)R(A/G) dinucleotides, a sequence specificity that is evolutionarily conserved from bony fish to humans. AID preferentially deaminates bubble substrates of five to seven nucleotides rather than larger bubbles and preferentially binds to bubble-type rather than to single-stranded DNA substrates, suggesting that the natural targets of AID are either transcription bubbles or stem-loop structures. AID displays high affinity for single-stranded DNA. All substrates used in activity assays contain a single cytidine within the bubble and differ in the dinucleotide immediately upstream of the target cytidine constituting either WRC motifs (hot spots) or non-WRC motifs (cold spots)
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
among potential highly transcribed genes in mouse hybridoma cells, the immunoglobulin heavy and light chain genes are important targets, with the immunoglobulin mu switch region being preferred compared to other genomic sites
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
exclusively catalyses deamination of cytidine in single-stranded DNA. It shows minimal activity on stem-loop structures and preferentially deaminates five-nucleotide bubbles. The optimal target consists of a single-stranded NWRCN motif (W = A or T, R = A or G). WRC preference involves the recognition of a purine in the R position and that the carbonyl or amino side chains of guanosine negatively influence specificity at the W position
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
no detectable activity on double-stranded DNA. The enzyme catalyzes deoxycytidine to deoxyuridine deamination activity on double-stranded DNA substrates containing a small transcription-like single-stranded DNA bubble. Enzyme activity depends on sequence context
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the enzyme deaminates cytidine residues in the DNA of the variable and the switch regions of the immunoglobulin locus. The resulting uracil induces error-prone DNA synthesis in the case of hypermutation or DNA breaks that activate nonhomologous recombination in the case of class-switch recombination. The enzyme deaminates single-stranded but not double-stranded substrates unless it is in a complex with replication protein A (RPA) and the substrate is actively undergoing transcription
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the enzyme preferentially deaminates cytosine to uracil in single-stranded and not double-stranded DNA the enzyme deaminates DNA at transcribed Ig genes
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the purified, tetrameric enzyme can deaminate cytidine residues in single-stranded DNA, but not in RNA. It deaminates only single-stranded DNA. Neither cytidine nor CTP (or dCTP) are good substrates for the enzyme in vitro
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
conformational equilibrium of the APOBEC3B active site loops, skewed toward being closed, controls enzymatic activity by regulating binding to ssDNA substrates
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the APOBEC3 enzymes are a double-edged sword that can catalyze deamination of cytosine in genomic DNA, which results in potential genomic instability due to the many mutagenic fates of uracil. The enzymes must be able to efficiently deaminate transiently available single-stranded DNA during reverse transcription, replication, or transcription. Specific biochemical characteristics promote deamination in each situation to increase enzyme efficiency through processivity, rapid enzyme cycling between substrates, or oligomerization state
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the APOBEC3 enzymes are a double-edged sword that can catalyze deamination of cytosine in genomic DNA, which results in potential genomic instability due to the many mutagenic fates of uracil. The enzymes must be able to efficiently deaminate transiently available single-stranded DNA during reverse transcription, replication, or transcription. Specific biochemical characteristics promote deamination in each situation to increase enzyme efficiency through processivity, rapid enzyme cycling between substrates, or oligomerization state in DNA
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the enzyme restricts the infectivity of viruses, such as HIV-1, by targeting CCC hotspots scattered through minus DNA strands, reverse-transcribed from genomic RNA
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the enzymes must access single-stranded DNA during the dynamic processes of DNA replication or transcription. The ability of an APOBEC3 to cycle between DNA substrates determines whether it is able to efficiently deaminate single-stranded DNA produced by replication and single-stranded DNA bound by replication protein A. APOBEC3 deaminase activity during transcription has a size limitation that inhibits APOBEC3B tetramers
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
deamination activity of methylated cytosine is demonstrated APOBEC3B
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
high deaminase activities on cytosine and methylated cytosine with relatively high selectivity for methylated cytosine
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
relatively low deaminase activity and selectivity for methylated cytosine
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
RNA binding is integral to APOBEC3H function. RNA-mediated dimerization alters the interactions of the enzyme with ssDNA and other RNA molecules
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the enzyme preferentially converts cytidine to uridine at the third position of triplet cytosine (CCC) hotspots. The phosphate backbone is required for C-terminal domain of the enzyme to slide along the DNA strand and to exert the 3'->5' polarity. The higher the salt cncentration, the less prominent is the 3'->5' polarity
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
-
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
-
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
activation-induced cytidine deaminase (AID) initiates Ig class switch recombination and somatic hypermutation by producing U:G mismatches in DNA. These mismatches also have the potential to induce DNA damage including double-stranded breaks and chromosome translocations
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
activation-induced cytidine deaminase (AID) initiates immunoglobulin class switch DNA recombination (CSR) and somatic hypermutation deaminating deoxycytidines in switch and V(D)J region DNA, respectively, to generate deoxyuracils. Processing of deoxyuracils by uracil DNA glycosylase yields abasic sites, which are excised by apurinic/apyrimidinic endonucleases, eventually generating double strand DNA breaks, the obligatory intermediates of class switch DNA recombination
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
activation-induced cytidine deaminase (AID) is a mutator enzyme that initiates somatic mutation and class switch recombination in B lymphocytes by introducing uracil:guanine mismatches into DNA. Repair pathways process these mismatches to produce point mutations in the Ig variable region or double-stranded DNA breaks in the switch region DNA. The enzyme can also produce off-target DNA damage, including mutations in oncogenes
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
activation-induced deaminase is the initiator for somatic hypermutation (SHM) and class switch recombination (CSR). The enzyme targets the highly repetitive switch regions of the immunoglobulin heavy chain locus to induce DNA double-strand breaks (DSBs), which can be rejoined, leading to switch of constant regions of antibody. When targeting to variable region exons of IgH and IgL loci, the enzyme predominantly induces point mutations, termed SHM, resulting in increased affinity of antibody for antigen. While somatic hypermutation and class switch recombination (CSR) enhance antibody diversity, AID initiated double-strand breaks and mutations may predispose B cells to carcinogenesis
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
in response to antigens, B cells undergo two types of genomic alterations to increase antibody diversity. Affinity for antigen can be increased by introduction of point mutations into immunoglobulin heavy (IgH) and immunoglobulin light (IgL) variable regions by somatic hypermutation. Antibody effector functions can be altered by changing the expressed IgH constant region exons through IgH class switch recombination (CSR). Somatic hypermutation and CSR both require the B-cell-specific activation-induced cytidine deaminase protein (AID), which initiates these reactions through its single-stranded DNA-specific cytidine deaminase activity
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the enzyme induces reproducible DNA breaks at many non-Ig loci in activated B cells
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the enzyme initiates class switch recombination and somatic hypermutation of immunoglobulin genes in B lymphocytes. Activation-induced cytidine deaminase also produces off-target DNA damage, including mutations in oncogenes and double-stranded breaks that can serve as substrates for oncogenic chromosomal translocations
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the enzyme initiates Ig heavy chain (IgH) class switch recombination and Ig somatic hypermutation (SHM) by deaminating cytidines within, respectively, IgH switch regions and Ig variable region (V) exons
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the enzyme does neither catalyzes cytidine to uridine editing of apoB mRNA nor binds to AU-rich RNA targets
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
unlike AID-induced double-strand DNA breaks in immunoglobulin genes, genome-wide activation-induced cytidine deaminase-dependent double-strand DNA breaks are not restricted to transcribed regions and frequently occur within repeated sequence elements, including CA repeats, non-CA tandem repeats, and short interspersed element
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
-
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
activation-induced deaminase (AID) is involved in processes leading to antibody diversification: somatic hypermutation, gene conversion, and class-switch recombination
-
-
?
additional information
?
-
enzyme is able to deaminate 5-methylcytosine in DNA
-
-
?
additional information
?
-
activation-induced cytidine deaminase is function in Pleurodeles waltl. The lack of class switch recombination activity in Pleurodeles waltl is therefore not due to a defect in expression or function of activation-induced cytidine deaminase
-
-
?
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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
additional information
?
-
activation-induced cytidine deaminase is function in Pleurodeles waltl. The lack of class switch recombination activity in Pleurodeles waltl is therefore not due to a defect in expression or function of activation-induced cytidine deaminase
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
-
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
-
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
-
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
activation-induced cytidine deaminase (AID) produces DNA breaks in immunoglobulin genes during antibody diversification. Double-stranded breaks in the switch region mediate class switch recombination, and contribute to gene conversion and somatic hypermutation in the variable regions. Among potential highly transcribed genes in mouse hybridoma cells, the immunoglobulin heavy and light chain genes are important AID targets, with the immunoglobulin mu switch region being preferred compared to other genomic sites
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
activation-induced deaminase is the initiator for somatic hypermutation (SHM) and class switch recombination (CSR). The enzyme targets the highly repetitive switch regions of the immunoglobulin heavy chain locus to induce DNA double-strand breaks (DSBs), which can be rejoined, leading to switch of constant regions of antibody. When targeting to variable region exons of IgH and IgL loci, the enzyme predominantly induces point mutations, termed SHM, resulting in increased affinity of antibody for antigen. While somatic hypermutation and class switch recombination (CSR) enhance antibody diversity, activation-induced deaminase initiated double-strand breaks and mutations may predispose B cells to carcinogenesis
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
AID mediates hypermutation by deaminating single stranded DNA. In vivo, single stranded DNA may arise transiently during transcription
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the enzyme can act on transcribing DNA. It is required for the maturation of antibodies in higher vertebrates, where it promotes somatic hypermutation
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the enzyme deaminates cytidine residues in the DNA of the variable and the switch regions of the immunoglobulin locus. The resulting uracil induces error-prone DNA synthesis in the case of hypermutation or DNA breaks that activate nonhomologous recombination in the case of class-switch recombination
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the enzyme deaminates DNA at transcribed Ig genes. Expressed immunoglobulin genes undergo alterations in sequence and genomic structure in order to optimize antibody function. A single B cell-specific factor, activation-induced deaminase (AID), initiates these changes by deamination of cytosine to uracil. At the Ig loci of B-cells, AID-initiated damage is processed to produce three distinct outcomes: somatic hypermutation, class switch recombination and gene conversion
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the enzyme initiates antibody diversification processes by deaminating immunoglobulin sequences
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
conformational equilibrium of the APOBEC3B active site loops, skewed toward being closed, controls enzymatic activity by regulating binding to ssDNA substrates
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the APOBEC3 enzymes are a double-edged sword that can catalyze deamination of cytosine in genomic DNA, which results in potential genomic instability due to the many mutagenic fates of uracil. The enzymes must be able to efficiently deaminate transiently available single-stranded DNA during reverse transcription, replication, or transcription. Specific biochemical characteristics promote deamination in each situation to increase enzyme efficiency through processivity, rapid enzyme cycling between substrates, or oligomerization state
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the APOBEC3 enzymes are a double-edged sword that can catalyze deamination of cytosine in genomic DNA, which results in potential genomic instability due to the many mutagenic fates of uracil. The enzymes must be able to efficiently deaminate transiently available single-stranded DNA during reverse transcription, replication, or transcription. Specific biochemical characteristics promote deamination in each situation to increase enzyme efficiency through processivity, rapid enzyme cycling between substrates, or oligomerization state in DNA
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the enzyme restricts the infectivity of viruses, such as HIV-1, by targeting CCC hotspots scattered through minus DNA strands, reverse-transcribed from genomic RNA
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the enzymes must access single-stranded DNA during the dynamic processes of DNA replication or transcription. The ability of an APOBEC3 to cycle between DNA substrates determines whether it is able to efficiently deaminate single-stranded DNA produced by replication and single-stranded DNA bound by replication protein A. APOBEC3 deaminase activity during transcription has a size limitation that inhibits APOBEC3B tetramers
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
activation-induced cytidine deaminase (AID) initiates Ig class switch recombination and somatic hypermutation by producing U:G mismatches in DNA. These mismatches also have the potential to induce DNA damage including double-stranded breaks and chromosome translocations
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
activation-induced cytidine deaminase (AID) initiates immunoglobulin class switch DNA recombination (CSR) and somatic hypermutation deaminating deoxycytidines in switch and V(D)J region DNA, respectively, to generate deoxyuracils. Processing of deoxyuracils by uracil DNA glycosylase yields abasic sites, which are excised by apurinic/apyrimidinic endonucleases, eventually generating double strand DNA breaks, the obligatory intermediates of class switch DNA recombination
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
activation-induced cytidine deaminase (AID) is a mutator enzyme that initiates somatic mutation and class switch recombination in B lymphocytes by introducing uracil:guanine mismatches into DNA. Repair pathways process these mismatches to produce point mutations in the Ig variable region or double-stranded DNA breaks in the switch region DNA. The enzyme can also produce off-target DNA damage, including mutations in oncogenes
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
activation-induced deaminase is the initiator for somatic hypermutation (SHM) and class switch recombination (CSR). The enzyme targets the highly repetitive switch regions of the immunoglobulin heavy chain locus to induce DNA double-strand breaks (DSBs), which can be rejoined, leading to switch of constant regions of antibody. When targeting to variable region exons of IgH and IgL loci, the enzyme predominantly induces point mutations, termed SHM, resulting in increased affinity of antibody for antigen. While somatic hypermutation and class switch recombination (CSR) enhance antibody diversity, AID initiated double-strand breaks and mutations may predispose B cells to carcinogenesis
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
in response to antigens, B cells undergo two types of genomic alterations to increase antibody diversity. Affinity for antigen can be increased by introduction of point mutations into immunoglobulin heavy (IgH) and immunoglobulin light (IgL) variable regions by somatic hypermutation. Antibody effector functions can be altered by changing the expressed IgH constant region exons through IgH class switch recombination (CSR). Somatic hypermutation and CSR both require the B-cell-specific activation-induced cytidine deaminase protein (AID), which initiates these reactions through its single-stranded DNA-specific cytidine deaminase activity
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the enzyme induces reproducible DNA breaks at many non-Ig loci in activated B cells
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the enzyme initiates class switch recombination and somatic hypermutation of immunoglobulin genes in B lymphocytes. Activation-induced cytidine deaminase also produces off-target DNA damage, including mutations in oncogenes and double-stranded breaks that can serve as substrates for oncogenic chromosomal translocations
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the enzyme initiates Ig heavy chain (IgH) class switch recombination and Ig somatic hypermutation (SHM) by deaminating cytidines within, respectively, IgH switch regions and Ig variable region (V) exons
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
activation-induced deaminase (AID) is involved in processes leading to antibody diversification: somatic hypermutation, gene conversion, and class-switch recombination
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zinc
coordination of a secondary zinc ion enhances deamination activity up to 160%ing is pinpointed to loop-3 which harbors a catalytically essential and spatially conserved asparagine at its N-terminus
additional information
the enzyme requires a tightly bound metal ion for its action
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
RNA
RNA binding is integral to APOBEC3H function. RNA-mediated dimerization alters the interactions of the enzyme with ssDNA and other RNA molecules
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Km of glutathione S-transferase-AID for the hot-spot transcription bubble substrate HS1bub7 is between 10 and 15 nM. It is not possible to estimate the Km for the cold-spot bubble (i.e., CS1bub7) since the substrate saturation kinetics is not observed. However, as the velocity continues to increase beyond the highest substrate concentration tested, the Km is likely to be severalfold higher for CS1bub7 than for HS1bub7
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22 - 37
the enzyme works with varying efficiencies from room temperature to 37°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
688963, 719247, 719341, 719342, 719404, 719582, 720139, 720140, 720301, 720452, 720569, 720885, 720890
UniProt
brenda
-
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
APOBEC3G is preferentially expressed in mesenchymal gliomas
brenda
additional information
the enzyme is specifically expresssed in germinal center B-cells
brenda
-
AID expression occurs first in pro-B cells and increases on further development, peak AID expression is in immature and T1 B cells from bone marrow, is lower in splenic T1 B cells, and decreases precipitously in the splenic transitional 2 and mature B-cell compartments
brenda
predominantly expressed in the spleen. The enzyme is expressed early during embryonic development of Pleurodeles waltl
brenda
additional information
-
AID cDNA is undetectable in totipotent hematopoietic progenitors, and in cells committed to the T lymphocyte or myeloid lineages
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
activation-induced deaminase is present in a complex containing the regulatory subunit Ialpha and, possibly, the catalytic subunit of protein kinase A in the cytoplasm of B cells, suggesting that protein kinase A itself may contribute in part to the localization of AID in this compartment
brenda
the enzyme predominantly localizes in the cytoplasm and diffuses or is actively transported into the nucleus
brenda
the enzyme undergoes constant nucleocytoplasmic shuttling, with a net balance toward export, thus resulting in a main cytoplasmic localization
brenda
the enzyme predominantly localizes in the cytoplasm and diffuses or is actively transported into the nucleus
brenda
the enzyme undergoes constant nucleocytoplasmic shuttling, with a net balance toward export, thus resulting in a main cytoplasmic localization. The enzyme is polyubiquitinated in the nucleus
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
deficiency in activation-induced deaminase is responsible for a human immunodeficiency
malfunction
when aberrantly expressed in lung or breast tissue, APOBEC3H can contribute to cancer mutagenesis
metabolism
activation-induced deaminase initiated double-strand breaks and mutations may predispose B cells to carcinogenesis
metabolism
APOBEC3B-catalyzed DNA cytosine deamination causes mutations in cancer
metabolism
the APOBEC3 family has many roles, such as restricting endogenous and exogenous retrovirus replication and retrotransposon insertion events and reducing DNA-induced inflammation
metabolism
the enzyme can contribute to cancer through deamination of cytosine to form promutagenic uracil in genomic DNA
metabolism
the enzyme generates cytidine to deoxyuridine mutations in single-stranded DNA, and is capable of restricting replication of HIV-1 by generating mutations in viral genome
physiological function
activation-induced cytidine deaminase (AID) initiates Ig class switch recombination and somatic hypermutation by producing U:G mismatches in DNA. These mismatches also have the potential to induce DNA damage including double-stranded breaks and chromosome translocations
physiological function
activation-induced cytidine deaminase (AID) initiates immunoglobulin class switch DNA recombination (CSR) and somatic hypermutation deaminating deoxycytidines in switch and V(D)J region DNA,respectively, to generate deoxyuracils. Processing of deoxyuracils by uracil DNA glycosylase yields abasic sites, which are excised by apurinic/apyrimidinic endonucleases, eventually generating double strand DNA breaks, the obligatory intermediates of class switch DNA recombination
physiological function
activation-induced cytidine deaminase (AID) is a mutator enzyme that initiates somatic mutation and class switch recombination in B lymphocytes by introducing uracil:guanine mismatches into DNA. Repair pathways process these mismatches to produce point mutations in the Ig variable region or double-stranded DNA breaks in the switch region DNA. The enzyme can also produce off-target DNA damage, including mutations in oncogenes
physiological function
activation-induced cytidine deaminase (AID) produces DNA breaks in immunoglobulin genes during antibody diversification. Double-stranded breaks (DSB) in the switch region mediate class switch recombination, and contribute to gene conversion and somatic hypermutation in the variable regions
physiological function
activation-induced deaminase (AID) is involved in processes leading to antibody diversification: somatic hypermutation, gene conversion, and class-switch recombination
physiological function
AID mediates hypermutation by deaminating single stranded DNA. In vivo, single stranded DNA may arise transiently during transcription
physiological function
expressed immunoglobulin genes undergo alterations in sequence and genomic structure in order to optimize antibody function. The B cell-specific activation-induced deaminase (AID), initiates these changes by deamination of cytosine to uracil. At the Ig loci of B-cells, AID-initiated damage is processed to produce three distinct outcomes: somatic hypermutation, class switch recombination and gene conversion
physiological function
in response to antigens, B cells undergo two types of genomic alterations to increase antibody diversity. Affinity for antigen can be increased by introduction of point mutations into immunoglobulin heavy (IgH) and immunoglobulin light (IgL) variable regions by somatic hypermutation. Antibody effector functions can be altered by changing the expressed IgH constant region exons through IgH class switch recombination (CSR). Somatic hypermutation and CSR both require the B-cell-specific activation-induced cytidine deaminase protein (AID), which initiates these reactions through its single-stranded DNA-specific cytidine deaminase activity
physiological function
the enzyme induces reproducible DNA breaks at many non-Ig loci in activated B cells
physiological function
the enzyme initiates antibody diversification processes by deaminating immunoglobulin sequences
physiological function
the enzyme initiates class switch recombination and somatic hypermutation of immunoglobulin genes in B lymphocytes. Activation-induced cytidine deaminase also produces off-target DNA damage, including mutations in oncogenes and double-stranded breaks that can serve as substrates for oncogenic chromosomal translocations
physiological function
the enzyme is involved in immunoglobulin affinity maturation, gene conversion and class switch recombination. This protein is therefore a major actor in the creation of the antibody repertoire
physiological function
the enzyme is required for the maturation of antibodies in higher vertebrates, where it promotes somatic hypermutation
physiological function
AICDA-/- induced pluripotent stem cells fail to achieve the naive pluripotent state and remain primed for differentiation because of a failure to suppress fibroblast growth factor FGF/extracellular signal-regulated kinases ERK signaling. The mutant cells display marked genomic hypermethylation, but suppression of FGF/ERK signaling by AICDA is independent of deaminase activity
physiological function
APOBEC3A, a is a C>U RNA-editing enzyme that modifies the monocyte/macrophage transcriptome. Transcripts of hundreds of genes undergo sitespecific C>U RNA editing in macrophages during M1 polarization and in monocytes in response to hypoxia and interferons. Amino acid residues of APOBEC3A that are required for its DNA deamination and anti-retrotransposition activities also affect its RNA deamination activity
physiological function
APOBEC3G causes site-specific C-to-U editing of mRNAs from over 600 genes. The edited cytidines are often flanked by inverted repeats, but are largely distinct from those deaminated by isoform APOBEC3A. Both the N-terminal and C-terminal doman are required for the NA editing function
physiological function
APOBEC3Z1 induces double strand DNA breaks and apoptosis upon expression in HeLa cells
physiological function
both heterogeneous nuclear ribonucleoproteins hnRNP K and L exhibit RNA-dependent interactions with AID and are required for antibody class switch recombination. Depletion of hnRNP K reduces somatic hypermutation, and hnRNP K is required for AID-induced DNA breaks
physiological function
the enzyme has important roles in innate immunity but is also a major endogenous source of mutations in cancer
physiological function
the enzyme inhibits replication of retroelements and HIV-1 in CD4+ T cells
physiological function
the enzyme initiates somatic hypermutation and class-switch recombination by deaminating C -> U during transcription of Ig-variable and Ig-switch region DNA, which is essential to produce high-affinity antibodies
Show AA Sequence and Transmembrane Helices (179 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
184000
tetrameric enzyme form, APOBEC3B predominantly forms tetramers and a small proportion existed as dimers, gel filtration
26000
92000
dimeric enzyme form, APOBEC3B predominantly forms tetramers and a small proportion existed as dimers, gel filtration
additional information
activation-induced cytidine deaminase mRNA is not alternatively spliced in Pleurodeles waltl
26000
x * 26000, enzyme containing vector-encoded detection and purification tags, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
tetramer
?
x * 26000, enzyme containing vector-encoded detection and purification tags, SDS-PAGE
dimer
2 * 46000, SDS-PAGE, APOBEC3B predominantly forms tetramers and a small proportion existed as dimers
monomer
non-phosphorylated activation-induced deaminase, is catalytically active as a monomer on single stranded DNA in vitro, including single-stranded DNA found in loops similar to those transiently formed in the immunoglobulin switch regions during transcription
tetramer
4 * 46000, SDS-PAGE, APOBEC3B predominantly forms tetramers and a small proportion existed as dimers
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
ubiquitination
the enzyme is polyubiquitinated in the nucleus. Ubiquitin-mediated nuclear degradation of the enzyme is part of a multilayer control that contributes to the regulation of enzyme function during hypermutation and class switch recombination
phosphoprotein
phosphorylation of S38 is essential for activation-induced deaminase interaction with replication protein A (RPA). The residue S38 is a target for phosphorylation by protein kinase A. Phosphorylation of AID significantly increases its deaminase activity on duplexDNA, although the phosphorylated enzyme still retains its preference for single-stranded substrates
phosphoprotein
protein kinase A phosphorylates activation-induced cytidine deaminase and regulates its activity in GC B cells. Phosphorylation targets specifically Thr27 and Ser38
phosphoprotein
515% of the enzyme expressed in activated B cells is phosphorylated at Ser38. The modified form contributes disproportionately to hypermutation. This form of activation-induced cytidine deaminase is enriched in the chromatin fraction in activated B cells
phosphoprotein
activation-induced cytidine deaminase that is phosphorylated on serine residue 38 interacts with replication protein A, a ssDNA binding protein, to promote deamination of transcribed double-stranded DNA in vitro. The Ser38 phosphorylation site is required for normal class switch recombination and Ig somatic hypermutation in mice
phosphoprotein
in addition to Ser38, the enzyme is also phosphorylated at position Thr140. Mutation of either Ser38 or Thr140 to Ala does not impact catalytic activity, but interfers with class switching and somatic hypermutation in vivo. Ser38 is equally important for both processes, Thr140 phosphorylation preferentially affects somatic mutation
phosphoprotein
phosphorylation at serine 38 and threonine 140 increases activity. Activation-induced cytidine deaminase activity and its oncogenic potential can be downregulated by phosphorylation of Ser3. This process is controlled by serine/threonine protein phosphatase 2A
phosphoprotein
protein kinase A phosphorylates the Ser38. This phosphorylation event activates the enzyme to enable interaction with replication protein A, thereby augmenting the ability of activation-induced cytidine deaminase to effect class switch recombination in vivo
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion technique at 4°C, crystal structure of enzyme variant AIDv(DELTA15), at 2.8 A resolution
generation of a panel of free or DNA-bound AID models based on eight recently resolved APOBEC isoform structures. The majority of AID:DNA complexes would be inactive due to substrate binding such that a cytidine is not positioned for deamination. Most AID conformations exhibit fully or partially occluded catalytic pockets
generation of a panel of free or DNA-bound AID models based on eight resolved APOBEC structures. The majority of AID:DNA complexes would be inactive due to substrate binding such that a cytidine is not positioned for deamination. Most AID conformations exhibit fully or partially occluded catalytic pockets
hanging drop vapor diffusion method, APOBEC3B catalytic domain crystal structures including a dCMP-bound form
modeling of structure. Residue Arg211 in loop 1 is the gatekeeper coordinating DNA. ssDNA binds to the C-terminal domain in a U-shape, and loop 1 undergoes major conformational changes to open up the active site for DNA binding. Residue D314 defines substrate specificity for thymidine over cytidine at -1 position. An auto-inhibited conformation in the C-terminal domain restricts access and binding of DNA to the active site
sitting drop vapor diffusion method at 4°C, crystal structure of the catalytic domain of HIV-1 restriction factor APOBEC3G in complex with ssDNA at 1.86 A resolution
sitting drop vapor-diffusion method, crystal structure of the C-terminal catalytic domain of the enzyme (APOBEC3F) in complex with a 10 nucleotide ssDNA composed of a poly-thymine sequence
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E58Q/C87A/C90A
the mutant enzyme does not bind to single-stranded DNA at all, though it retains some binding to RNA
E72D
mutant is moderately impaired in a ssDNA deamination assay but capable of RNA deamination
G56N
mutation at the N-terminus end of loop-3 does not bestow deamination activity
H248S/H250S
increase in the concentration of zinc does not increase deamination activity
K352A/K355A/K358A
the product formation of the mutant enzyme can not reach saturation even when the maximum protein concentration is obtained
Y333A
the product formation of the mutant enzyme can not reach saturation even when the maximum protein concentration is obtained
S38A
S3A
purified recombinant mutant enzyme S3A and wild-type have similar deamination activities on an ssDNA substrate in vitro. AID-/- B cells expressing AIDS3A show a consistently higher percentage of class-switched IgG1-expressing B cells than control enzyme. Mutating S3 to A does not alter catalysis but does result in increased AID activity in class switch recombination
S3D
AID-/- B cells expressing AID-S3D show a consistently higher percentage of class-switched IgG1-expressing B cells than control enzyme. Mutating S3 to A does not alter catalysis but does result in increased AID activity in class switch recombination
T140A
mutation does not impact catalytic activity, but interfers with class switching and somatic hypermutation in vivo
additional information
S38A
mutant form of activation-induced cytidine deaminase that retains similar catalytic activity on ssDNA as wild-type enzyme. The AIDS38A mutant protein is significantly compromised in its ability to mediate somatic hypermutation SHM. B cells homozygous for the AIDS38A mutation show substantially impaired class switch recombination and Ig somatic hypermutation, correlating with inability of AIDS38A to interact with endogenous replication protein A. Mice haploinsufficient for AIDS38A have more severely impaired class switch recombination when compared with mice haploinsufficient for AIDWT, with class switch recombination levels reduced to nearly background levels. These results unequivocally demonstrate that integrity of the AID S38 phosphorylation site is required for normal class switch recombination and Ig somatic hypermutation in mice and support a role for AID phosphorylation at S38 and replication protein A interaction in regulating class switch recombination and Ig somatic hypermutation
S38A
mutation does not impact catalytic activity, but interfers with class switching and somatic hypermutation in vivo
S38A
the kinetics of single-stranded DNA deaminase activity for wild-type and S38A mutant enzyme are comparable
S38A
the mutant enzyme shows dimished somatic hypermutation activity on artificial and physiological DNA targets
additional information
construction of segment swaps between activation-induced deaminase (AID) and APOBEC3G and determination of their mutational sequence specificity
additional information
-
construction of segment swaps between activation-induced deaminase (AID) and APOBEC3G and determination of their mutational sequence specificity
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme displays a different stability depending on the specific cell compartment in which it is located. In a Burkitts lymphoma cell line the half-life of activation-induced cytidine deaminase is markedly reduced in the nucleus. This destabilization is accompanied by a polyubiquitination that is revealed in the presence of proteasome inhibitors. The same compartment-specific degradation is observed in activated mouse B cells, and also in a nonB cell line
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
construction of stable transformants (mouse hybridoma cells) expressing human activation-induced cytidine deaminase
expression in Escherichia coli
expression in Escherichia coli as a glutathione S-transferase fusion protein
expression in Escherichia coli. Human activation-induced cytidine deaminase purified from Escherichia coli is active without prior treatment with a ribonuclease and deaminates cytosines in plasmid DNA in vitro
expression of 3H9 VDJ knock-in alleles in genomic DNA of immature/T1, mature follicular B cells, and thymocytes from 3H9 and 3H9.Aicda-/- mice, quantitative expression analysis by PCR and immunofluorescence
-
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is increased by epidermal growth factor, tumor necrosis factor alpha, or sodium butyrate
expression of activation-induced cytidine deaminase mRNA is induced in splenic B cells that are activated in vitro or by immunizations with sheep red blood cells. In situ hybridization of immunized spleen sections reveals the restricted expression of AID mRNA in developing germinal centers in which modulation of immunoglobulin gene information through somatic hypermutation and class switch recombination takes place
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
APOBEC3G mediated checkpoint activation through checkpoint kinase 2 (Chk2) is one of the critical regulatory mechanisms that underlies the preferential DNA damage checkpoint response and radioresistance of Glioma Initiating Cells. Thus, anti-APOBEC3G therapy may synergize with radiotherapy and other current treatments to overcome the therapeutic resistance of gliomas. APOBEC3G represents a potential molecular target for novel therapeutics that will improve the treatment outcome of glioma patients
molecular biology
-
a target-AID base editor, designed to recruit cytidine deaminase (CDA) to the target DNA locus via the CRISPR/Cas9 system, can directly induce C to T mutation without double-strand breaks and donor DNA. This system is adopted in Yarrowia lipolytica for multiplex gene disruption. Target-specific gRNA(s) and a fusion protein consisting of a nickase Cas9, CDA1, and uracil DNA glycosylase inhibitor are expressed from a single plasmid to disrupt target genes by introducing a stop codon via C to T mutation within the mutational window. Using this Target-AID system, single gene disruption and simultaneous double gene disruption are achieved with the efficiencies up to 94% and 31%, respectively
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Larijani, M.;Petrov, A.P.; Kolenchenko, O.; Berru, M.; Krylov, S.N.; Martin, A.
AID associates with single-stranded DNA with high affinity and a long complex half-life in a sequence-independent manner
Mol. Cell. Biol.
27
20-30
2007
Homo sapiens (Q9GZX7)
brenda
Vallur, A.C.; Yabuki, M.; Larson, E.D.; Maizels, N.
AID in antibody perfection
Cell. Mol. Life Sci.
64
555-565
2007
Homo sapiens (Q9GZX7)
brenda
Brar, S.S.; Sacho, E.J.; Tessmer, I.; Croteau, D.L.; Erie, D.A.; Diaz, M.
Activation-induced deaminase, AID, is catalytically active as a monomer on single-stranded DNA
DNA Repair
7
77-87
2007
Homo sapiens (Q9GZX7)
brenda
Carpenter, M.A.; Rajagurubandara, E.; Wijesinghe, P.; Bhagwat, A.S.
Determinants of sequence-specificity within human AID and APOBEC3G
DNA Repair
9
579-587
2010
Homo sapiens (Q9GZX7), Homo sapiens
brenda
Lee, S.A.; Parsa, J.Y.; Martin, A.; Baker, M.D.
Activation-induced cytidine deaminase induces DNA break repair events more frequently in the Ig switch region than other sites in the mammalian genome
Eur. J. Immunol.
37
3529-3539
2007
Homo sapiens (Q9GZX7)
brenda
Wang, J.H.
The role of activation-induced deaminase in antibody diversification and genomic instability
Immunol. Res.
55
287-297
2013
Homo sapiens (Q9GZX7), Mus musculus (Q9WVE0)
brenda
Muramatsu, M.; Sankaranand, V.S.; Anant, S.; Sugai, M.; Kinoshita, K.; Davidson, N.O.; Honjo, T.
Specific expression of activation-induced cytidine deaminase (AID), a novel member of the RNA-editing deaminase family in germinal center B cells
J. Biol. Chem.
274
18470-18476
1999
Mus musculus (Q9WVE0), Mus musculus
brenda
Li, G.; Pone, E.J.; Tran, D.C.; Patel, P.J.; Dao, L.; Xu, Z.; Casali, P.
Iron inhibits activation-induced cytidine deaminase enzymatic activity and modulates immunoglobulin class switch DNA recombination
J. Biol. Chem.
287
21520-21529
2012
Mus musculus (Q9WVE0)
brenda
Dickerson, S.K.; Market, E.; Besmer, E.; Papavasiliou, F.N.
AID mediates hypermutation by deaminating single stranded DNA
J. Exp. Med.
197
1291-1296
2003
Homo sapiens (Q9GZX7)
brenda
Aoufouchi, S.; Faili, A.; Zober, C.; D'Orlando, O.; Weller, S.; Weill, J.C.; Reynaud, C.A.
Proteasomal degradation restricts the nuclear lifespan of AID
J. Exp. Med.
205
1357-1368
2008
Homo sapiens (Q9GZX7)
brenda
McBride, K.M.; Gazumyan, A.; Woo, E.M.; Schwickert, T.A.; Chait, B.T.; Nussenzweig, M.C.
Regulation of class switch recombination and somatic mutation by AID phosphorylation
J. Exp. Med.
205
2585-2594
2008
Mus musculus (Q9WVE0)
brenda
Miyazaki, Y.; Inoue, H.; Kikuchi, K.; Ochiai, K.; Kusama, K.
Activation-induced cytidine deaminase mRNA expression in oral squamous cell carcinoma-derived cell lines is upregulated by inflammatory cytokines
J. Oral Sci.
54
71-75
2012
Homo sapiens (Q9GZX7)
brenda
Larijani, M.; Martin, A.
Single-stranded DNA structure and positional context of the target cytidine determine the enzymatic efficiency of AID
Mol. Cell. Biol.
27
8038-8048
2007
Homo sapiens (Q9GZX7)
brenda
Gazumyan, A.; Timachova, K.; Yuen, G.; Siden, E.; Di Virgilio, M.; Woo, E.M.; Chait, B.T.; San-Martin, B.R.; Nussenzweig, M.C.; McBride, K.M.
Amino-terminal phosphorylation of activation-induced cytidine deaminase suppresses c-myc/IgH translocation
Mol. Cell. Biol.
31
442-449
2011
Mus musculus (Q9WVE0)
brenda
Staszewski, O.; Baker, R.E.; Ucher, A.J.; Martier, R.; Stavnezer, J.; Guikema, J.E.
Activation-induced cytidine deaminase induces reproducible DNA breaks at many non-Ig loci in activated B cells
Mol. Cell.
41
232-242
2011
Mus musculus (Q9WVE0)
brenda
Bascove, M.; Frippiat, J.P.
Molecular characterization of Pleurodeles waltl activation-induced cytidine deaminase
Mol. Immunol.
47
1640-1649
2010
Pleurodeles waltl (D5GRW1)
brenda
Basu, U.; Chaudhuri, J.; Alpert, C.; Dutt, S.; Ranganath, S.; Li, G.; Schrum, J.P.; Manis, J.P.; Alt, F.W.
The AID antibody diversification enzyme is regulated by protein kinase A phosphorylation
Nature
438
508-511
2005
Mus musculus (Q9WVE0)
brenda
Sohail, A.; Klapacz, J.; Samaranayake, M.; Ullah, A.; Bhagwat, A.S.
Human activation-induced cytidine deaminase causes transcription-dependent, strand-biased C to U deaminations
Nucleic Acids Res.
31
2990-2994
2003
Homo sapiens (Q9GZX7)
brenda
Bransteitter, R.; Pham, P.; Scharff, M.D.; Goodman, M.F.
Activation-induced cytidine deaminase deaminates deoxycytidine on single-stranded DNA but requires the action of RNase
Proc. Natl. Acad. Sci. USA
100
4102-4107
2003
Homo sapiens (Q9GZX7)
brenda
Yang, G.; Obiakor, H.; Sinha, R.K.; Newman, B.A.; Hood, B.L.; Conrads, T.P.; Veenstra, T.D.; Mage, R.G.
Activation-induced deaminase cloning, localization, and protein extraction from young VH-mutant rabbit appendix
Proc. Natl. Acad. Sci. USA
102
17083-17088
2005
Oryctolagus cuniculus (Q3BAF8), Oryctolagus cuniculus
brenda
Pasqualucci, L.; Kitaura, Y.; Gu, H.; Dalla-Favera, R.
PKA-mediated phosphorylation regulates the function of activation-induced deaminase (AID) in B cells
Proc. Natl. Acad. Sci. USA
103
395-400
2005
Homo sapiens (Q9GZX7)
brenda
McBride, K.M.; Gazumyan, A.; Woo, E.M.; Barreto, V.M.; Robbiani, D.F.; Chait, B.T.; Nussenzweig, M.C.
Regulation of hypermutation by activation-induced cytidine deaminase phosphorylation
Proc. Natl. Acad. Sci. USA
103
8798-8803
2006
Mus musculus (Q9WVE0)
brenda
Cheng, H.L.; Vuong, B.Q.; Basu, U.; Franklin, A.; Schwer, B.; Astarita, J.; Phan, R.T.; Datta, A.; Manis, J.; Alt, F.W.; Chaudhuri, J.
Integrity of the AID serine-38 phosphorylation site is critical for class switch recombination and somatic hypermutation in mice
Proc. Natl. Acad. Sci. USA
106
2717-2122
2009
Mus musculus (Q9WVE0)
brenda
Meyers, G.; Ng, Y.S.; Bannock, J.M.; Lavoie, A.; Walter, J.E.; Notarangelo, L.D.; Kilic, S.S.; Aksu, G.; Debre, M.; Rieux-Laucat, F.; Conley, M.E.; Cunningham-Rundles, C.; Durandy, A.; Meffre, E.
Activation-induced cytidine deaminase (AID) is required for B-cell tolerance in humans
Proc. Natl. Acad. Sci. USA
108
11554-11559
2011
Homo sapiens
brenda
Kuraoka, M.; Holl, T.M.; Liao, D.; Womble, M.; Cain, D.W.; Reynolds, A.E.; Kelsoe, G.
Activation-induced cytidine deaminase mediates central tolerance in B cells
Proc. Natl. Acad. Sci. USA
108
11560-11565
2011
Mus musculus
brenda
Verma, S.; Goldammer, T.; Aitken, R.
Cloning and expression of activation induced cytidine deaminase from Bos taurus
Vet. Immunol. Immunopathol.
134
151-159
2010
Bos taurus (Q2PT36)
brenda
Bae, S.J.; Park, B.G.; Kim, B.G.; Hahn, J.S.
Multiplex gene disruption by targeted base editing of Yarrowia lipolytica genome using cytidine deaminase combined with the CRISPR/Cas9 system
Biotechnol. J.
2019
e1900238
2019
Petromyzon marinus
brenda
Hou, S.; Silvas, T.V.; Leidner, F.; Nalivaika, E.A.; Matsuo, H.; Kurt Yilmaz, N.; Schiffer, C.A.
Structural analysis of the active site and DNA binding of human cytidine deaminase APOBEC3B
J. Chem. Theory Comput.
15
637-647
2019
Homo sapiens (Q9UH17), Homo sapiens
brenda
Sharma, S.; Patnaik, S.K.; Taggart, R.T.; Kannisto, E.D.; Enriquez, S.M.; Gollnick, P.; Baysal, B.E.
APOBEC3A cytidine deaminase induces RNA editing in monocytes and macrophages
Nat. Commun.
6
6881
2015
Homo sapiens (P31941)
brenda
Hu, W.; Begum, N.A.; Mondal, S.; Stanlie, A.; Honjo, T.
Identification of DNA cleavage- and recombination-specific hnRNP cofactors for activation-induced cytidine deaminase
Proc. Natl. Acad. Sci. USA
112
5791-5796
2015
Homo sapiens (Q9GZX7)
brenda
Marx, A.; Galilee, M.; Alian, A.
Zinc enhancement of cytidine deaminase activity highlights a potential allosteric role of loop-3 in regulating APOBEC3 enzymes
Sci. Rep.
5
18191
2015
Homo sapiens (P31941), Homo sapiens (Q9HC16)
brenda
Sharma, S.; Patnaik, S.K.; Taggart, R.T.; Baysal, B.E.
The double-domain cytidine deaminase APOBEC3G is a cellular site-specific RNA editing enzyme
Sci. Rep.
6
39100
2016
Homo sapiens (Q9HC16)
brenda
Li, X.; Caval, V.; Wain-Hobson, S.; Vartanian, J.P.
Elephant APOBEC3A cytidine deaminase induces massive double-stranded DNA breaks and apoptosis
Sci. Rep.
9
728
2019
Loxodonta africana (A0A4Y5QRZ7)
brenda
Kumar, R.; Evans, T.
Activation-induced cytidine deaminase regulates fibroblast growth factor/extracellular signal-regulated kinases signaling to achieve the naive pluripotent state during reprogramming
Stem Cells
37
1003-1017
2019
Mus musculus (Q9WVE0)
brenda
King, J.J.; Manuel, C.A.; Barrett, C.V.; Raber, S.; Lucas, H.; Sutter, P.; Larijani, M.
Catalytic pocket inaccessibility of activation-induced cytidine deaminase is a safeguard against excessive mutagenic activity
Structure
23
615-627
2015
Homo sapiens, Homo sapiens (P31941)
brenda
Adolph, M.B.; Love, R.P.; Chelico, L.
Biochemical basis of APOBEC3 deoxycytidine deaminase activity on diverse DNA substrates
ACS Infect. Dis.
4
224-238
2018
Homo sapiens (P31941), Homo sapiens (Q6NTF7), Homo sapiens (Q8IUX4), Homo sapiens (Q96AK3), Homo sapiens (Q9HC16), Homo sapiens (Q9NRW3), Homo sapiens (Q9UH17)
brenda
Pham, P.; Afif, S.A.; Shimoda, M.; Maeda, K.; Sakaguchi, N.; Pedersen, L.C.; Goodman, M.F.
Structural analysis of the activation-induced deoxycytidine deaminase required in immunoglobulin diversification
DNA Repair
43
48-56
2016
Escherichia coli O157:H7 (P0AEY0)
brenda
Shi, K.; Carpenter, M.A.; Kurahashi, K.; Harris, R.S.; Aihara, H.
Crystal structure of the DNA deaminase APOBEC3B catalytic domain
J. Biol. Chem.
290
28120-28130
2015
Homo sapiens (Q9UH17)
brenda
Ito, F.; Fu, Y.; Kao, S.A.; Yang, H.; Chen, X.S.
Family-wide comparative analysis of cytidine and methylcytidine deamination by eleven human APOBEC proteins
J. Mol. Biol.
429
1787-1799
2017
Homo sapiens (P31941), Homo sapiens (Q6NTF7), Homo sapiens (Q8IUX4), Homo sapiens (Q96AK3), Homo sapiens (Q9HC16), Homo sapiens (Q9NRW3), Homo sapiens (Q9UH17), Homo sapiens
brenda
Feng, Y.; Wong, L.; Morse, M.; Rouzina, I.; Williams, M.C.; Chelico, L.
RNA-mediated dimerization of the human deoxycytidine deaminase APOBEC3H influences enzyme activity and interaction with nucleic acids
J. Mol. Biol.
430
4891-4907
2018
Homo sapiens (Q6NTF7), Homo sapiens
brenda
Fang, Y.; Xiao, X.; Li, S.X.; Wolfe, A.; Chen, X.S.
Molecular interactions of a DNA modifying enzyme APOBEC3F catalytic domain with a single-stranded DNA
J. Mol. Biol.
430
87-101
2018
Homo sapiens (Q8IUX4)
brenda
Maiti, A.; Myint, W.; Kanai, T.; Delviks-Frankenberry, K.; Sierra Rodriguez, C.; Pathak, V.K.; Schiffer, C.A.; Matsuo, H.
Crystal structure of the catalytic domain of HIV-1 restriction factor APOBEC3G in complex with sDNA
Nat. Commun.
9
2460
2018
Homo sapiens (Q9HC16)
brenda
Adolph, M.B.; Love, R.P.; Feng, Y.; Chelico, L.
Enzyme cycling contributes to efficient induction of genome mutagenesis by the cytidine deaminase APOBEC3B
Nucleic Acids Res.
45
11925-11940
2017
Homo sapiens (Q9UH17)
brenda
Wang, Y.; Wu, S.; Zheng, S.; Wang, S.; Wali, A.; Ezhilarasan, R.; Sulman, E.P.; Koul, D.; Alfred Yung, W.K.
APOBEC3G acts as a therapeutic target in mesenchymal gliomas by sensitizing cells to radiation-induced cell death
Oncotarget
8
54285-54296
2017
Homo sapiens (Q9HC16)
brenda
Kamba, K.; Nagata, T.; Katahira, M.
Catalytic analysis of APOBEC3G involving real-time NMR spectroscopy reveals nucleic acid determinants for deamination
PLoS ONE
10
e0124142
2015
Homo sapiens (Q9HC16)
brenda
Shi, K.; Demir, O.e.; Carpenter, M.A.; Wagner, J.; Kurahashi, K.; Harris, R.S.; Amaro, R.E.; Aihara, H.
Conformational switch regulates the DNA cytosine deaminase activity of human APOBEC3B
Sci. Rep.
7
17415
2017
Homo sapiens (Q9UH17), Homo sapiens
brenda
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Release 2023.1 (January 2023)
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