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The protein encoded by this gene belongs to the TDG/mug DNA glycosylase family. Thymine-DNA glycosylase (TDG) removes thymine moieties from G/T mismatches by hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of DNA and the mispaired thymine. With lower activity, this enzyme also removes thymine from C/T and T/T mispairings.
MBD4 (methyl-CpG-binding domain protein 4) is a glycosylase employed in an initial step of base excision repair. MBD4 protein binds preferentially to fully methylated CpG sites . [ 28 ] These altered bases arise from the frequent hydrolysis of cytosine to uracil (see image) and hydrolysis of 5-methylcytosine to thymine, producing G:U and G:T ...
Spontaneous deamination of 5-methylcytosine results in thymine and ammonia. This is the most common single nucleotide mutation. In DNA, this reaction, if detected prior to passage of the replication fork, can be corrected by the enzyme thymine-DNA glycosylase, which removes the thymine base in a G/T mismatch. This leaves an abasic site that is ...
Human MBD4 protein has 580 amino acids with a methyl-CpG-binding domain at amino acids 82–147 and a C-terminal DNA glycosylase domain at amino acids 426–580. [8] These domains are separated by an intervening region that interacts with UHRF1, an E3 ubiquitin ligase, and USP7, a de-ubiquinating enzyme.
Deficiencies in certain proteins leads to disease; protein names are associated with the disease. XPA, XPB, XPC, XPD, XPE, XPF, and XPG all derive from Ń…eroderma pigmentosum and CSA and CSB represent proteins linked to Cockayne syndrome. Additionally, the proteins ERCC1, RPA, RAD23A, RAD23B, and others also participate in nucleotide excision ...
NEIL1 recognizes oxidized pyrimidines, formamidopyrimidines, thymine residues oxidized at the methyl group, and both stereoisomers of thymine glycol. [7] The best substrates for human NEIL1 appear to be the hydantoin lesions, guanidinohydantoin, and spiroiminodihydantoin that are further oxidation products of 8-oxoG. NEIL1 is also capable of ...
For instance, Rad-9 acts as an activator for many vital proteins that are responsible for the base excision repair process. First, Rad-9 interacts with many DNA glycosylases that are responsible for repairing specific nucleotide lesions, e.g. Human NEIL1 DNA glycosylase, thymine DNA glycosylase, 8-oxoguanine DNA glycosylase (OGG1). [11]
22256 Ensembl ENSG00000076248 ENSMUSG00000029591 UniProt P13051 P97931 RefSeq (mRNA) NM_080911 NM_003362 NM_001040691 NM_011677 RefSeq (protein) NP_003353 NP_550433 NP_001035781 NP_035807 Location (UCSC) Chr 12: 109.1 – 109.11 Mb Chr 5: 114.27 – 114.28 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Uracil-DNA glycosylase (also known as UNG or UDG) is an enzyme. Its most ...