| UniProt functional annotation for Q969S2 | |||
| UniProt code: Q969S2. |
| Organism: | Homo sapiens (Human). | |
| Taxonomy: | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. | |
| Function: | Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Has DNA glycosylase activity towards 5- hydroxyuracil and other oxidized derivatives of cytosine with a preference for mismatched double-stranded DNA (DNA bubbles). Has low or no DNA glycosylase activity towards thymine glycol, 2-hydroxyadenine, hypoxanthine and 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. {ECO:0000269|PubMed:12097317, ECO:0000269|PubMed:14522990, ECO:0000269|PubMed:15175427, ECO:0000269|PubMed:15339932}. | |
| Catalytic activity: | Reaction=(DNA)-(deoxyribonucleoside 5'-phosphate)-(deoxyribose 5'- phosphate)-(deoxyribonucleoside 5'-phosphate) = (DNA)-3'- (deoxyribonucleoside 5'-phosphate)-(2,3-dehydro-2,3-deoxyribose 5'- phosphate) + H(+) + phospho-5'-(DNA); Xref=Rhea:RHEA:66592, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067, ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695, ChEBI:CHEBI:167181; EC=4.2.99.18; Evidence={ECO:0000255|PROSITE- ProRule:PRU00392}; | |
| Activity regulation: | Acetylation of Lys-50 leads to loss of DNA nicking activity. Acetylation of Lys-154 has no effect. | |
| Subunit: | Binds EP300. | |
| Subcellular location: | Nucleus {ECO:0000269|PubMed:12097317}. | |
| Tissue specificity: | Detected in testis, skeletal muscle, heart, brain, placenta, lung, pancreas, kidney and liver. {ECO:0000269|PubMed:12097317}. | |
| Domain: | The zinc-finger domain is important for DNA binding. | |
| Similarity: | Belongs to the FPG family. {ECO:0000255|PROSITE- ProRule:PRU00392}. | |
Annotations taken from UniProtKB at the EBI.