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Information on EC 3.2.2.27 - uracil-DNA glycosylase and Organism(s) Homo sapiens

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EC Tree
     3 Hydrolases
         3.2 Glycosylases
             3.2.2 Hydrolysing N-glycosyl compounds
                3.2.2.27 uracil-DNA glycosylase
IUBMB Comments
Uracil-DNA glycosylases are widespread enzymes that are found in all living organisms. EC 3.2.2.27 and double-stranded uracil-DNA glycosylase (EC 3.2.2.28) form a central part of the DNA-repair machinery since they initiate the DNA base-excision repair pathway by hydrolysing the N-glycosidic bond between uracil and the deoxyribose sugar thereby catalysing the removal of mis-incorporated uracil from DNA.
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Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Hydrolyses single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil
Synonyms
uracil-dna glycosylase, smug1, dna n-glycosylase, ung-1, ul114, uracil dna-glycosylase, uracil-dna n-glycosylase, uracil dna glycosylase 2, mjudg, thd1p, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5-formyluracil-DNA glycosylase
-
DNA N-glycosylase
-
single-strand selective monofunctional uracil-DNA glycosylase
single-strand-selective mono-functional uracil-DNA glycosylase
-
-
single-strand-selective monofunctional uracil DNA glycosylase
-
single-strand-selective monofunctional uracil-DNA glycosylase
single-stranded monofunctional uracil DNA N-glycosylase
-
SMUG1
uracil DNA glycosylase
uracil DNA glycosylase 2
-
-
uracil DNA-glycosylase
-
uracil DNA-glycosylase 2
-
uracil-DNA glycosylase
uracil-DNA glycosylase 2
-
-
uracil-DNA N-glycosylase
uracil-N-glycosylase 2
-
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Hydrolyses single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil
show the reaction diagram
the UDG active center contorts the uracil and deoxyribose while the phosphates 5' and 3' of the uridine are anchored by interactions with a proline-rich loop and a glycine-serine loop, UDG catalytic mechanism with channeling of DNA repair intermediates, overview
-
SYSTEMATIC NAME
IUBMB Comments
uracil-DNA deoxyribohydrolase (uracil-releasing)
Uracil-DNA glycosylases are widespread enzymes that are found in all living organisms. EC 3.2.2.27 and double-stranded uracil-DNA glycosylase (EC 3.2.2.28) form a central part of the DNA-repair machinery since they initiate the DNA base-excision repair pathway by hydrolysing the N-glycosidic bond between uracil and the deoxyribose sugar thereby catalysing the removal of mis-incorporated uracil from DNA.
CAS REGISTRY NUMBER
COMMENTARY hide
59088-21-0
cf. EC 3.2.2.28
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3,N4-ethenocytosine-mismatched single-stranded DNA + H2O
3,N4-ethenocytosine + single-stranded DNA with abasic site
show the reaction diagram
-
-
-
?
5-formyluracil-mismatched double-stranded DNA + H2O
5-formyluracil + double-stranded DNA with abasic site
show the reaction diagram
5-formyluracil-mismatched single-stranded DNA + H2O
5-formyluracil + single-stranded DNA with abasic site
show the reaction diagram
-
-
-
?
5-hydroxymethyluracil-mismatched double-stranded DNA + H2O
5-hydroxymethyluracil + double-stranded DNA with abasic site
show the reaction diagram
5-hydroxymethyluracil-mismatched double-stranded DNA with U-A mismatch + H2O
5-hydroxymethyluracil + double-stranded DNA with abasic site
show the reaction diagram
-
-
-
?
5-hydroxymethyluracil-mismatched double-stranded DNA with U-G mismatch + H2O
5-hydroxymethyluracil + double-stranded DNA with abasic site
show the reaction diagram
-
-
-
?
5-hydroxymethyluracil-mismatched single-stranded DNA + H2O
5-hydroxymethyluracil + single-stranded DNA with abasic site
show the reaction diagram
5-hydroxyuracil-mismatched double-stranded DNA + H2O
5-hydroxyuracil + double-stranded DNA with abasic site
show the reaction diagram
5-hydroxyuracil-mismatched single-stranded DNA + H2O
5-hydroxyuracil + single-stranded DNA with abasic site
show the reaction diagram
dUMP-labeled calf thymus DNA + H2O
uracil + ?
show the reaction diagram
-
-
-
?
fU-containing 10 nucleotide DNA sequence 5'-GGAGAfUCTCC-3' with opposing C, T, A, or G + H2O
?
show the reaction diagram
-
-
-
-
?
M6-FAM-labeled single stranded oligonucleotide + H2O
uracil + ?
show the reaction diagram
T12-AGUA-T12
-
-
?
uracil-containing calf thymus DNA + H2O
uracil + calf thymus DNA with abasic site
show the reaction diagram
-
-
-
?
uracil-containing DNA + H2O
uracil + DNA with abasic site
show the reaction diagram
-
uracil-containing DNA substrates with two uracil sites spaced 10, 40 or 80 bp apart
-
-
?
uracil-containing single stranded DNA + H2O
uracil + single stranded DNA with abasic site
show the reaction diagram
-
duplex single stranded DNAs with sequences 5'-TGCACUUAAGAAUUTC-3'/5'-GAAATTCTTAAGTGCAGTGATAGTCTTCCGTCC-(CH2)7-methylene blue-3' and 5'-GAAATTCTTAAGTGCAGTGATAGTCTTCCGTCC-(CH2)7-methylene blue-3'/5'-TGGGGGTGCACTTAAGAATTTC-3'
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
show the reaction diagram
uracil-mismatched DNA + H2O
uracil + DNA with abasic site
show the reaction diagram
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
show the reaction diagram
uracil-mismatched double-stranded DNA with U-A mismatch + H2O
uracil + double-stranded DNA with abasic site
show the reaction diagram
-
-
-
?
uracil-mismatched double-stranded DNA with U-G mismatch + H2O
uracil + double-stranded DNA with abasic site
show the reaction diagram
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3,N4-ethenocytosine-mismatched single-stranded DNA + H2O
3,N4-ethenocytosine + single-stranded DNA with abasic site
show the reaction diagram
-
-
-
?
5-formyluracil-mismatched double-stranded DNA + H2O
5-formyluracil + double-stranded DNA with abasic site
show the reaction diagram
5-formyluracil-mismatched single-stranded DNA + H2O
5-formyluracil + single-stranded DNA with abasic site
show the reaction diagram
-
-
-
?
5-hydroxymethyluracil-mismatched double-stranded DNA + H2O
5-hydroxymethyluracil + double-stranded DNA with abasic site
show the reaction diagram
-
-
-
?
5-hydroxymethyluracil-mismatched single-stranded DNA + H2O
5-hydroxymethyluracil + single-stranded DNA with abasic site
show the reaction diagram
-
-
-
?
5-hydroxyuracil-mismatched double-stranded DNA + H2O
5-hydroxyuracil + double-stranded DNA with abasic site
show the reaction diagram
-
-
-
?
5-hydroxyuracil-mismatched single-stranded DNA + H2O
5-hydroxyuracil + single-stranded DNA with abasic site
show the reaction diagram
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
show the reaction diagram
uracil-mismatched DNA + H2O
uracil + DNA with abasic site
show the reaction diagram
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
show the reaction diagram
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1'-cyano-2'-deoxyuridine
-
4-methylindole
-
4-methylindole is an adenine isostere incapable of hydrogen bonding, and its pair with Thy is inherently prone to spontaneous opening, structure of hUNGin a complex with DNA containing a Thy:4-methylindole pair, a DNA mimic, overview
DNA containing 1'-cyano-2'-deoxyuridine
CNdU, a UDG inhibitor whose respective nucleotide triphosphate is also a substrate for DNA polymerase
-
Ugi
-
UDG inhibitor protein from Bacillus subtilis
-
UGI inhibitor
-
-
Ugi peptide
-
Ugi protein
-
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
APE1
has a strong stimulatory effect on hSMUG1 against dsU, apparently because of enhanced dissociation of hSMUG1 from AP sites in dsDNA. AP sites inhibit hSMUG1
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0046
5-hydroxymethyluracil-mismatched double-stranded DNA with U-A mismatch
pH 7.5, 30°C, recombinant hSMUG1
-
0.0027
5-hydroxymethyluracil-mismatched double-stranded DNA with U-G mismatch
pH 7.5, 30°C, recombinant hSMUG1
-
0.0038
5-hydroxymethyluracil-mismatched single-stranded DNA
pH 7.5, 30°C, recombinant hSMUG1
-
0.00157 - 0.00277
uracil-containing calf thymus DNA
-
0.0007 - 0.004
uracil-mismatched double-stranded DNA with U-A mismatch
-
0.0000022 - 0.0013
uracil-mismatched double-stranded DNA with U-G mismatch
-
0.00157 - 0.00265
uracil-mismatched single-stranded DNA
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.015
5-hydroxymethyluracil-mismatched double-stranded DNA with U-A mismatch
pH 7.5, 30°C, recombinant hSMUG1
-
0.04
5-hydroxymethyluracil-mismatched double-stranded DNA with U-G mismatch
pH 7.5, 30°C, recombinant hSMUG1
-
0.098
5-hydroxymethyluracil-mismatched single-stranded DNA
pH 7.5, 30°C, recombinant hSMUG1
-
0.0002 - 0.0003
fU-containing 10 nucleotide DNA sequence 5'-GGAGAfUCTCC-3' with opposing C, T, A, or G
-
pH 7.5
-
1.45 - 16.85
uracil-containing calf thymus DNA
-
0.052 - 2.28
uracil-mismatched double-stranded DNA with U-A mismatch
-
0.014 - 5.57
uracil-mismatched double-stranded DNA with U-G mismatch
-
0.29 - 46.1
uracil-mismatched single-stranded DNA
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00065 - 0.06
uracil-containing calf thymus DNA
-
1100 - 6367
uracil-mismatched single-stranded DNA
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0138
1'-cyano-2'-deoxyuridine
-
0.1315
DNA containing 1'-cyano-2'-deoxyuridine
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
primary cells from liver and colon
Manually annotated by BRENDA team
colorectal carcinoma cell line
Manually annotated by BRENDA team
colon adenocarcinoma cell line
Manually annotated by BRENDA team
-
low expression level of UNG2
Manually annotated by BRENDA team
-
a HeLa-derived cell line
Manually annotated by BRENDA team
colon tumor cell line
Manually annotated by BRENDA team
additional information
-
UNG2 is cell-cycle regulated with the highest protein level in early to mid-S-phase, in agreement with its role in the repair of incorporated uracils
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
-
UNG2 is a major determinant of the uracil base excision repair pathway, that undergoes rapid proteasome-dependent degradation following HIV-1 infection
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
UNG_HUMAN
313
0
34645
Swiss-Prot
Mitochondrion (Reliability: 3)
A0A126LB28_HUMAN
255
0
28981
TrEMBL
other Location (Reliability: 2)
B4DRT6_HUMAN
270
0
30434
TrEMBL
other Location (Reliability: 4)
E5KTA5_HUMAN
313
0
34645
TrEMBL
Mitochondrion (Reliability: 3)
Q6FHS8_HUMAN
304
0
33926
TrEMBL
Mitochondrion (Reliability: 5)
E5KTA6_HUMAN
304
0
33924
TrEMBL
Mitochondrion (Reliability: 5)
F5GYA2_HUMAN
258
0
28539
TrEMBL
Mitochondrion (Reliability: 5)
CCNO_HUMAN
350
0
38096
Swiss-Prot
-
SMUG1_HUMAN
270
0
29862
Swiss-Prot
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
UNG2 also undergoes sequential phosphorylations at Ser23, Thr60 and Ser64 during the cell cycle. Monophosphorylation at Ser23 in the G1/early S-phase apparently increases association with RPA and replicating chromatin and markedly increases the catalytic turnover number
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with a bacteriophage encoded natural inhibitor, hanging drop vapor diffusion method, using 0.1 M Tris–HCl pH 7.4, 270 mM Li2SO4, 4% (w/v) PEG 550 MME, 17% (w/v) PEG 4000
mutant D183G/K302R, hanging drop vapor diffusion method, using 0.1 M imidazole/maleate pH 7.8, 50 mM NaCl, 41 mM ammonium sulfate and 18% (w/v) PEG4000
mutant enzyme K302R, hanging drop vapor diffusion method, using 0.1 M imidazole/maleate pH 7.8, 50 mM NaCl, 41 mM ammonium sulfate and 18% (w/v) PEG4000
UDG alone and bound to uncleaved substrate and product, X-ray diffraction structure determination and analysis, molecular modelling
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D183G
D183G/K302R
F98H
site-directed mutagenesis, the mutant shows reduced activity with uracil, 5-hydroxyuracil, 5-hydroxymethyluracil, and 5-formyluracil compared to the wild-type enzyme
F98L
site-directed mutagenesis, the mutant shows reduced activity with uracil, 5-hydroxyuracil, 5-hydroxymethyluracil, and 5-formyluracil compared to the wild-type enzyme
G87A
site-directed mutagenesis, the mutant shows reduced activity with uracil, 5-hydroxyuracil, 5-hydroxymethyluracil, and 5-formyluracil compared to the wild-type enzyme
H239L
site-directed mutagenesis, the mutant shows reduced activity with uracil, 5-hydroxyuracil, 5-hydroxymethyluracil, and 5-formyluracil compared to the wild-type enzyme
H239N
site-directed mutagenesis, the mutant shows reduced activity with uracil, 5-hydroxyuracil, 5-hydroxymethyluracil, and 5-formyluracil compared to the wild-type enzyme
N163D
site-directed mutagenesis, the mutant shows reduced activity with uracil, 5-hydroxyuracil, 5-hydroxymethyluracil, and 5-formyluracil compared to the wild-type enzyme
N85A
site-directed mutagenesis, the mutant shows reduced activity with uracil, 5-hydroxyuracil, 5-hydroxymethyluracil, and 5-formyluracil compared to the wild-type enzyme
Q152L/D154E
a siRNA-insensitive, inactive UNG2 mutant, overexpression in UNG2-depleted MAGI-CCR5 producer cells fails to restore viral infectivity
R276X
mutations at Arg276 transform uracil-DNA glycosylase into a single-stranded DNA-specific uracil-DNA glycosylase. The kcat of the R276 mutants is comparable to wild-type UNG on single-stranded DNA and differentially affected by NaCl, however, kcat on double-stranded DNA substrate is reduced 4-12-fold and decreases sharply at NaCl concentrations as low as 20 mM, the mutant proteins exhibit a 2.6 to 7.7fold reduction in affinity for a doubled-stranded oligonucleotide containing a pseudouracil residue opposite 2-aminopurine compared to the wild-type UNG
W231A/F234G
site-directed mutagenesis, the mutation impairs the association of UNG2 with viral protein Vpr UNG2-depleted MAGI-CCR5 producer cells and viral infectivity
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
HEPES pH 7.5, Tris pH 7.5, and imidazole pH 8.0 are the most stabilizing buffers
HEPES pH 7.5, Tris pH 7.5, and imidazole pH 8.0 are the most stabilizing buffers for the enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Q-Sepharose column chromatography
Q-Sepharose column chromatography and Superdex 75 gel filtration
Q-Sepharose column chromatography, SP Sepharose column chromatography and gel filtration
recombinant GST-tagged enzyme about 500fold, the tag is removed
recombinant GST-tagged SMUG1 from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, the tag is cleaved off by thrombin
recombinant hSMUG1 from Escherichia coli strain BL21(DE3) by protamine sulfate precipitation, hydrophobic interaction and adsorption chromatography, ultrafiltration, ion exchange chromatography, polyU-affinity, and again ion exchange chromatography. Recombinant hUNG2 from Escherichia coli strain BL21 by gel filtration, ion exchange chromatography, and ultrafiltration
recombinant hUNG2 from Escherichia coli strain BL21 by gel filtration, ion exchange chromatography, and ultrafiltration
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis
expressed in Escherichia coli BL21(DE3) pLysS cells
expressed in Escherichia coli NR8052 cells
expression as GST-tagged enzyme
expression of His-Myc-tagged GFP-fusion UNG2 1-25 in DLD1 cells
expression of hSMUG1 in Escherichia coli strain BL21(DE3)
expression of hUNG2 in Escherichia coli strain BL21
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
human UNG gene produces two mRNA and two protein products due to alternative transcription initiation sites
-
overexpression of UNG2 inhibits HIV-1 replication
-
SMUG1 from liver cDNA library, expression of GST-tagged SMUG1 in Escherichia coli strain BL21(DE3)
SMUG1 is encoded within a small region of human chromosome 12, cloning from HeLa S3 cells, expression of GST-tagged SMUG1 in Escherichia coli strain BL21(DE3)
SMUG1, sequence comparison
when expressed in Escherichia coli cells, SMUG1 is unable to repair U:G mismatches induced by AID, inhibits proliferation and cannot reduce mutation rates, unlike UNG2 which alleviates the effects of AID
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
depletion of endogenous UNG2 is proteasome-dependent and requires a direct interaction with HIV Vpr but not with integrase, different capacity between HIV-1 and HIV-2 to inhibit intracellular UNG2 expression
-
protein and mRNA levels rapidly decline in G2/M phase. Micro-RNAs down-regulate enzyme activity, mRNA, and protein levels by directly targeting the conserved seed sites in the 3'-untranslated region
-
UDG expression is upregulated 1.75fold in SUMO-1 overexpressing HepG2 cells, SUMO-1 is involved in protein sumoylation
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
fluorescence method for sensitive detection of uracil-DNA glycosylase using TdT-activated Endonuclease IV-assisted hyperbranched signal amplification. The method exhibits high sensitivity with a limit of detection of 0.090 U/ml for pure uracil-DNA glycosylase and shows a dynamic range from 0.1 to 50 U/ml, and can be applied for accurate detection of uracil-DNA glycosylase in HeLa nuclear extract. The method can be used for discrimination of uracil-DNA glycosylase from other DNA glycosylases
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Masaoka,A.; Matsubara, M.; Hasegawa, R.; Tanaka,T.; Kurisu,S.; Terato,H.; Ohyama,Y.; Karino, N.; Matsuda,A
Ide, H.: Mammalian 5-formyluracil-DNA glycosylase. 2. Role of SMUG1 uracil-DNA glycosylase in repair of 5-formyluracil and other oxidized and deaminated base lesions
Biochemistry
42
5003-5012
2003
Homo sapiens (Q53HV7), Homo sapiens, Rattus norvegicus (Q811Q1)
Manually annotated by BRENDA team
Guo, C.; Zhang, X.; Fink, S.P.; Platzer, P.; Wilson, K.; Willson, J.K.; Wang, Z.; Markowitz, S.D.
Ugene, a newly identified protein that is commonly overexpressed in cancer, and that binds uracil DNA-glycosylase
Cancer Res.
68
6118-6126
2008
Homo sapiens (P22674)
Manually annotated by BRENDA team
Haushalter, K.A
Stukenberg, P.T.; Kirschner, M.W.; Verdine, G.L.: Identification of a new uracil-DNA glycosylase family by expression cloning using synthetic inhibitors
Curr. Biol.
9
174-185
1999
Xenopus laevis, Homo sapiens (Q53HV7), Homo sapiens
Manually annotated by BRENDA team
Chen, C.-Y.; Mosbaugh, D.W.; Bennett, S.E.
Mutations at arginine 276 transform human uracil-DNAglycosylase into a single-stranded DNA-specific uracil-DNA glycosylase
DNA Repair
4
793-805
2005
Homo sapiens (P13051), Homo sapiens
Manually annotated by BRENDA team
Boorstein, R.J.; Cumming, A.; Marenstein, D.R.; Chan, M.K.; Ma, Y.; Neubert, T.A.; Brown, S.M.; Teebor, G.W.
Definitive identification of mammalian 5-hydroxymethyluracil DNA N-glycosylase activity as SMUG1
J. Biol. Chem.
276
41991-41997
2001
Homo sapiens (Q53HV7), Homo sapiens, Bos taurus (Q59T47), Bos taurus
Manually annotated by BRENDA team
Kavli, B.; Sundheim, O.; Akbari, M.; Otterlei, M.; Nilsen, H.; Skorpen, F.; Aas, P.A.; Hagen, L.; Krokan, H.E.; Slupphaug, G.
hUNG2 is the major repair enzyme for removal of uracil from U:A matches, U:G mismatches, and U in single-stranded DNA, with hSMUG1 as a broad specificity backup
J. Biol. Chem.
277
39926-39936
2002
Homo sapiens, Homo sapiens (P22674)
Manually annotated by BRENDA team
Darwanto, A.; Theruvathu, J.A.; Sowers, J.L.; Rogstad, D.K.; Pascal, T.; Goddard III, W.; Sowers, L.C.
Mechanisms of base selection by human single-stranded selective monofunctional uracil-DNA glycosylase
J. Biol. Chem.
284
15835-15846
2009
Homo sapiens (Q53HV7), Homo sapiens
Manually annotated by BRENDA team
Mi, R.; Dong, L.; Kaulgud, T.; Hackett, K.W.; Dominy, B.N.; Cao, W.
Insights from xanthine and uracil DNA glycosylase activities of bacterial and human SMUG1: switching SMUG1 to UDG
J. Mol. Biol.
385
761-778
2009
Geobacter metallireducens (Q39ZI0), Geobacter metallireducens, Homo sapiens (Q53HV7), Homo sapiens, Geobacter metallireducens GS-15 / ATCC 53774 / DSM 7210 (Q39ZI0)
Manually annotated by BRENDA team
Priet, S.; Gros, N.; Navarro, J.-M.; Boretto, J.I.; Canard, B.; Querat, G.; Sire, J.
HIV-1-associated uracil DNA glycosylase activity controls dUTP misincorporation in viral DNA and is essential to the HIV-1 life cycle
Mol. Cell
17
479-490
2005
Homo sapiens (P22674)
Manually annotated by BRENDA team
Pearl, J.H.
Structure and function in the uracil-DNA glycosylase superfamily
Mutat. Res.
460
165-181
2000
Escherichia coli, Homo sapiens, Human alphaherpesvirus 1 (P10186)
Manually annotated by BRENDA team
Parikh, S.S.; Putnam, C.D.; Tainer, J.A.
Lessons learned from structural results on uracil-DNA glycosylase
Mutat. Res.
460
183-199
2000
Homo sapiens
Manually annotated by BRENDA team
Matsubara, M.; Tanaka, T.; Terato, H.; Ohmae, E.; Izumi, S.; Katayanagi, K.; Ide, H.
Mutational analysis of the damage-recognition and catalytic mechanism of human SMUG1 DNA glycosylase
Nucleic Acids Res.
32
5291-5302
2004
Homo sapiens (Q53HV7), Homo sapiens
Manually annotated by BRENDA team
Aziz, M.A.; Schupp, J.E.; Kinsella, T.J.
Modulation of the activity of methyl binding domain protein 4 (MBD4/MED1) while processing iododeoxyuridine generated DNA mispairs
Cancer Biol. Ther.
8
1156-1163
2009
Homo sapiens
Manually annotated by BRENDA team
Ma, K.W.; Au, S.W.; Waye, M.M.
Over-expression of SUMO-1 induces the up-regulation of heterogeneous nuclear ribonucleoprotein A2/B1 isoform B1 (hnRNP A2/B1 isoform B1) and uracil DNA glycosylase (UDG) in HepG2 cells
Cell Biochem. Funct.
27
228-237
2009
Homo sapiens
Manually annotated by BRENDA team
Knaevelsrud, I.; Slupphaug, G.; Leiros, I.; Matsuda, A.; Ruoff, P.; Bjelland, S.
Opposite-base dependent excision of 5-formyluracil from DNA by hSMUG1
Int. J. Radiat. Biol.
85
413-420
2009
Homo sapiens
Manually annotated by BRENDA team
Huang, H.; Stivers, J.T.; Greenberg, M.M.
Competitive inhibition of uracil DNA glycosylase by a modified nucleotide whose triphosphate is a substrate for DNA polymerase
J. Am. Chem. Soc.
131
1344-1345
2009
Escherichia coli, Homo sapiens (P13051)
Manually annotated by BRENDA team
Jones, K.L.; Roche, M.; Gantier, M.P.; Begum, N.A.; Honjo, T.; Caradonna, S.; Williams, B.R.; Mak, J.
X4 and R5 HIV-1 have distinct post-entry requirements for uracil DNA glycosylase during infection of primary cells
J. Biol. Chem.
285
18603-18614
2010
Homo sapiens
Manually annotated by BRENDA team
Zharkov, D.O.; Mechetin, G.V.; Nevinsky, G.A.
Uracil-DNA glycosylase: Structural, thermodynamic and kinetic aspects of lesion search and recognition
Mutat. Res.
685
11-20
2010
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Fenard, D.; Houzet, L.; Bernard, E.; Tupin, A.; Brun, S.; Mougel, M.; Devaux, C.; Chazal, N.; Briant, L.
Uracil DNA glycosylase 2 negatively regulates HIV-1 LTR transcription
Nucleic Acids Res.
37
6008-6018
2009
Homo sapiens
Manually annotated by BRENDA team
Visnes, T.; Doseth, B.; Pettersen, H.; Hagen, L.; Sousa, M.; Akbari, M.; Otterlei, M.; Kavli, B.; Slupphaug, G.; Krokan, H.
Uracil in DNA and its processing by different DNA glycosylases
Philos. Trans. R. Soc. Lond. B Biol. Sci.
364
563-568
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Assefa, N.G.; Niiranen, L.; Johnson, K.A.; Leiros, H.K.; Smalas, A.O.; Willassen, N.P.; Moe, E.
Structural and biophysical analysis of interactions between cod and human uracil-DNA N-glycosylase (UNG) and UNG inhibitor (Ugi)
Acta Crystallogr. Sect. D
70
2093-2100
2014
Homo sapiens (P13051), Homo sapiens, Gadus morhua (Q9I983), Gadus morhua
Manually annotated by BRENDA team
Schonhoft, J.D.; Kosowicz, J.G.; Stivers, J.T.
DNA translocation by human uracil DNA glycosylase: role of DNA phosphate charge
Biochemistry
52
2526-2535
2013
Homo sapiens
Manually annotated by BRENDA team
Tao, J.; Song, P.; Sato, Y.; Nishizawa, S.; Teramae, N.; Tong, A.; Xiang, Y.
A label-free and sensitive fluorescent method for the detection of uracil-DNA glycosylase activity
Chem. Commun. (Camb. )
51
929-932
2015
Homo sapiens
Manually annotated by BRENDA team
Assefa, N.; Niiranen, L.; Willassen, N.; Smals, A.; Moe, E.
Thermal unfolding studies of cold adapted uracil-DNA N-glycosylase (UNG) from Atlantic cod (Gadus morhua). A comparative study with human UNG
Comp. Biochem. Physiol. B
161
60-68
2012
Gadus morhua, Homo sapiens (P13051), Homo sapiens
Manually annotated by BRENDA team
Hegre, S.A.; Saetrom, P.; Aas, P.A.; Pettersen, H.S.; Otterlei, M.; Krokan, H.E.
Multiple microRNAs may regulate the DNA repair enzyme uracil-DNA glycosylase
DNA Repair
12
80-86
2013
Homo sapiens
Manually annotated by BRENDA team
Franco, D.; Sgrignani, J.; Bussi, G.; Magistrato, A.
Structural role of uracil DNA glycosylase for the recognition of uracil in DNA duplexes. Clues from atomistic simulations
J. Chem. Inf. Model.
53
1371-1387
2013
Homo sapiens (P13051)
Manually annotated by BRENDA team
Kitamura, K.; Wang, Z.; Chowdhury, S.; Simadu, M.; Koura, M.; Muramatsu, M.
Uracil DNA glycosylase counteracts APOBEC3G-induced hypermutation of hepatitis B viral genomes: excision repair of covalently closed circular DNA
PLoS Pathog.
9
e1003361
2013
Homo sapiens
Manually annotated by BRENDA team
Weil, A.F.; Ghosh, D.; Zhou, Y.; Seiple, L.; McMahon, M.A.; Spivak, A.M.; Siliciano, R.F.; Stivers, J.T.
Uracil DNA glycosylase initiates degradation of HIV-1 cDNA containing misincorporated dUTP and prevents viral integration
Proc. Natl. Acad. Sci. USA
110
E448-E457
2013
Homo sapiens
Manually annotated by BRENDA team
Wu, Y.; Wang, L.; Zhu, J.; Jiang, W.
A DNA machine-based fluorescence amplification strategy for sensitive detection of uracil-DNA glycosylase activity
Biosens. Bioelectron.
68
654-659
2015
Homo sapiens
Manually annotated by BRENDA team
Ahn, J.K.; Lee, C.Y.; Park, K.S.; Park, H.G.
Abasic site-assisted inhibition of nicking endonuclease activity for the sensitive determination of uracil DNA glycosylase
Biotechnol. J.
13
e1700603
2018
Homo sapiens
Manually annotated by BRENDA team
Assefa, N. G.; Niiranen, L.; Willassen, N. P.; Smalas, A.; Moe, E.
Thermal unfolding studies of cold adapted uracil-DNA N-glycosylase (UNG) from Atlantic cod (Gadus morhua). A comparative study with human UNG
Comp. Biochem. Physiol. B
161
60-68
2012
Gadus morhua, Homo sapiens (P13051), Homo sapiens
Manually annotated by BRENDA team
Esadze, A.; Rodriguez, G.; Weiser, B.P.; Cole, P.A.; Stivers, J.T.
Measurement of nanoscale DNA translocation by uracil DNA glycosylase in human cells
Nucleic Acids Res.
45
12413-12424
2017
Homo sapiens
Manually annotated by BRENDA team
Sarno, A.; Lundbaek, M.; Liabakk, N.B.; Aas, P.A.; Mjelle, R.; Hagen, L.; Sousa, M.M.L.; Krokan, H.E.; Kavli, B.
Uracil-DNA glycosylase UNG1 isoform variant supports class switch recombination and repairs nuclear genomic uracil
Nucleic Acids Res.
47
4569-4585
2019
Mus musculus, Homo sapiens (P13051), Homo sapiens
Manually annotated by BRENDA team
Herate, C.; Vigne, C.; Guenzel, C.A.; Lambele, M.; Rouyez, M.C.; Benichou, S.
Uracil DNA glycosylase interacts with the p32 subunit of the replication protein A complex to modulate HIV-1 reverse transcription for optimal virus dissemination
Retrovirology
13
26
2016
Homo sapiens
Manually annotated by BRENDA team
Ren, R.; Shi, K.; Yang, J.; Yuan, R.; Xiang, Y.
DNA three way junction-mediated recycling amplification for sensitive electrochemical monitoring of uracil-DNA glycosylase activity and inhibition
Sens. Actuators B Chem.
258
783-788
2018
Homo sapiens
-
Manually annotated by BRENDA team
Wang, L.; Zhang, H.; Xie, Y.; Chen, H.; Ren, C.; Chen, X.
Target-mediated hyperbranched amplification for sensitive detection of human alkyladenine DNA glycosylase from HeLa cells
Talanta
194
846-851
2019
Homo sapiens (P13051)
Manually annotated by BRENDA team