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| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
DNA polymerase beta
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| http://www.biopax.org/relea... |
DPOLB_MOUSE
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| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
2.7.7.7,
4.2.99.-
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| http://www.biopax.org/relea... |
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 (By similarity). CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). COFACTOR: Binds 2 magnesium ions per subunit (By similarity). SUBUNIT: Monomer. Interacts with APEX1, HUWE1/ARF-BP1, STUB1/CHIP and USP47 (By similarity). SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By similarity). Note=Cytoplasmic in normal conditions. Translocates to the nucleus following DNA damage (By similarity). DOMAIN: Residues 239-252 form a flexible loop which appears to affect the polymerase fidelity (By similarity). PTM: Methylation by PRMT6 stimulates the polymerase activity by enhancing DNA binding and processivity (By similarity). 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 (By similarity). SIMILARITY: Belongs to the DNA polymerase type-X family. SEQUENCE CAUTION: Sequence=AAH06681.1; Type=Frameshift; Positions=Several; COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
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