DNA-3-methyladenine glycosylase
Details
- Name
- DNA-3-methyladenine glycosylase
- Synonyms
- 3-alkyladenine DNA glycosylase
- 3-methyladenine DNA glycosidase
- 3.2.2.21
- AAG
- ADPG
- ANPG
- MID1
- N-methylpurine-DNA glycosylase
- Gene Name
- MPG
- Organism
- Humans
- Amino acid sequence
>lcl|BSEQ0049624|DNA-3-methyladenine glycosylase MVTPALQMKKPKQFCRRMGQKKQRPARAGQPHSSSDAAQAPAEQPHSSSDAAQAPCPRER CLGPPTTPGPYRSIYFSSPKGHLTRLGLEFFDQPAVPLARAFLGQVLVRRLPNGTELRGR IVETEAYLGPEDEAAHSRGGRQTPRNRGMFMKPGTLYVYIIYGMYFCMNISSQGDGACVL LRALEPLEGLETMRQLRSTLRKGTASRVLKDRELCSGPSKLCQALAINKSFDQRDLAQDE AVWLERGPLEPSEPAVVAAARVGVGHAGEWARKPLRFYVRGSPWVSVVDRVAEQDTQA
- Number of residues
- 298
- Molecular Weight
- 32868.365
- Theoretical pI
- Not Available
- GO Classification
- Functionsalkylbase DNA N-glycosylase activity / damaged DNA binding / DNA N-glycosylase activity / DNA-3-methyladenine glycosylase activity / DNA-3-methylguanine glycosylase activity / DNA-7-methyladenine glycosylase activity / DNA-7-methylguanine glycosylase activityProcessesbase-excision repair / depurination / DNA dealkylation involved in DNA repairComponentsmitochondrial nucleoid / nucleoplasm
- General Function
- Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, and 7-methylguanine from the damaged DNA polymer formed by alkylation lesions.
- Specific Function
- Alkylbase dna n-glycosylase activity
- Pfam Domain Function
- Pur_DNA_glyco (PF02245)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0049625|DNA-3-methyladenine glycosylase (MPG) ATGGTCACCCCCGCTTTGCAGATGAAGAAACCAAAGCAGTTTTGCCGACGGATGGGGCAA AAGAAGCAGCGACCAGCTAGAGCAGGGCAGCCACACAGCTCGTCCGACGCAGCCCAGGCA CCTGCAGAGCAGCCACACAGCTCGTCCGATGCAGCCCAGGCACCTTGCCCCAGGGAGCGC TGCTTGGGACCGCCCACCACTCCGGGCCCATACCGCAGCATCTATTTCTCAAGCCCAAAG GGCCACCTTACCCGACTGGGGTTGGAGTTCTTCGACCAGCCGGCAGTCCCCCTGGCCCGG GCATTTCTGGGACAGGTCCTAGTCCGGCGACTTCCTAATGGCACAGAACTCCGAGGCCGC ATCGTGGAGACCGAGGCATACCTGGGGCCAGAGGATGAAGCCGCCCACTCAAGGGGTGGC CGGCAGACCCCCCGCAACCGAGGCATGTTCATGAAGCCGGGGACCCTGTACGTGTACATC ATTTACGGCATGTACTTCTGCATGAACATCTCCAGCCAGGGGGACGGGGCTTGCGTCTTG CTGCGAGCACTGGAGCCCCTGGAAGGTCTGGAGACCATGCGTCAGCTTCGCAGCACCCTC CGGAAAGGCACCGCCAGCCGTGTCCTCAAGGACCGCGAGCTCTGCAGTGGCCCCTCCAAG CTGTGCCAGGCCCTGGCCATCAACAAGAGCTTTGACCAGAGGGACCTGGCACAGGATGAA GCTGTATGGCTGGAGCGTGGTCCCCTGGAGCCCAGTGAGCCGGCTGTAGTGGCAGCAGCC CGGGTGGGCGTCGGCCATGCAGGGGAGTGGGCCCGGAAACCCCTCCGCTTCTATGTCCGG GGCAGCCCCTGGGTCAGTGTGGTCGACAGAGTGGCTGAGCAGGACACACAGGCCTGA
- Chromosome Location
- 16
- Locus
- 16p13.3
- External Identifiers
Resource Link UniProtKB ID P29372 UniProtKB Entry Name 3MG_HUMAN HGNC ID HGNC:7211 - General References
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- Chakravarti D, Ibeanu GC, Tano K, Mitra S: Cloning and expression in Escherichia coli of a human cDNA encoding the DNA repair protein N-methylpurine-DNA glycosylase. J Biol Chem. 1991 Aug 25;266(24):15710-5. [Article]
- O'Connor TR, Laval J: Human cDNA expressing a functional DNA glycosylase excising 3-methyladenine and 7-methylguanine. Biochem Biophys Res Commun. 1991 May 15;176(3):1170-7. [Article]
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- van Loon B, Samson LD: Alkyladenine DNA glycosylase (AAG) localizes to mitochondria and interacts with mitochondrial single-stranded binding protein (mtSSB). DNA Repair (Amst). 2013 Mar 1;12(3):177-87. doi: 10.1016/j.dnarep.2012.11.009. Epub 2013 Jan 3. [Article]
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- Lau AY, Scharer OD, Samson L, Verdine GL, Ellenberger T: Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: mechanisms for nucleotide flipping and base excision. Cell. 1998 Oct 16;95(2):249-58. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB00515 Cisplatin approved unknown Details DB01593 Zinc approved, investigational unknown Details DB14487 Zinc acetate approved, investigational unknown Details DB14533 Zinc chloride approved, investigational unknown cofactor Details DB14548 Zinc sulfate, unspecified form approved, experimental unknown cofactor Details