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UniProt functional annotation for P06746 | ||
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| UniProt code: P06746. |
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| Organism: | |
Homo sapiens (Human). |
| Taxonomy: | |
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. |
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| Function: | |
Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. {ECO:0000269|PubMed:11805079, ECO:0000269|PubMed:21362556, ECO:0000269|PubMed:9207062, ECO:0000269|PubMed:9572863}. |
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| Catalytic activity: | |
Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.7; |
| Cofactor: | |
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions per subunit. {ECO:0000250}; |
| Subunit: | |
Monomer. Interacts with APEX1, HUWE1/ARF-BP1, STUB1/CHIP and USP47. Interacts with FAM168A (PubMed:25260657). {ECO:0000269|PubMed:12517346, ECO:0000269|PubMed:21362556, ECO:0000269|PubMed:25260657, ECO:0000269|PubMed:8841119, ECO:0000269|PubMed:8841120, ECO:0000269|PubMed:9207062, ECO:0000269|PubMed:9287163}. |
| Subcellular location: | |
Nucleus. Cytoplasm. Note=Cytoplasmic in normal conditions. Translocates to the nucleus following DNA damage. |
| Domain: | |
Residues 239-252 form a flexible loop which appears to affect the polymerase fidelity. {ECO:0000250}. |
| Ptm: | |
Methylation by PRMT6 stimulates the polymerase activity by enhancing DNA binding and processivity. {ECO:0000269|PubMed:16600869}. |
| Ptm: | |
Ubiquitinated at Lys-41, Lys-61 and Lys-81: monoubiquitinated by HUWE1/ARF-BP1. Monoubiquitinated protein is then the target of STUB1/CHIP, which catalyzes polyubiquitination from monoubiquitin, leading to degradation by the proteasome. USP47 mediates the deubiquitination of monoubiquitinated protein, preventing polyubiquitination by STUB1/CHIP and its subsequent degradation. {ECO:0000269|PubMed:19713937, ECO:0000269|PubMed:21362556}. |
| Similarity: | |
Belongs to the DNA polymerase type-X family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.