POLB
entrez
5423
canonical
uniprot
P06746
canonical
ensembl
ENSG00000070501
resolver
ensp
ENSP00000265421
resolver
ensp
ENSP00000657621
resolver
ensp
ENSP00000733757
resolver
enst
ENST00000265421
resolver
genesymbol
POLB
resolver
hgnc
HGNC:9174
resolver
uniprot
B2RC78
resolver
uniprot
B7Z1W5
resolver
uniprot
Q3KP48
resolver
uniprot
Q6FI34
resolver
uniprot_entry
B7Z1W5_HUMAN
resolver
uniprot_entry
DPOLB_HUMAN
resolver
uniprot_sec
B2RC78
resolver
uniprot_sec
Q3KP48
resolver
uniprot_sec
Q6FI34
resolver
amino_acid_sequence
MSKRKAPQETLNGGITDMLTELANFEKNVSQAIHKYNAYRKAASVIAKYPHKIKSGAEAKKLPGVGTKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVSGIGPSAARKFVDEGIKTLEDLRKNEDKLNHHQRIGLKYFGDFEKRIPREEMLQMQDIVLNEVKKVDSEYIATVCGSFRRGAESSGDMDVLLTHPSFTSESTKQPKLLHQVVEQLQKVHFITDTLSKGETKFMGVCQLPSKNDEKEYPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEKGFTINEYTIRPLGVTGVAGEPLPVDSEKDIFDYIQWKYREPKDRSE
uniprot
proteins
ec_number
2.7.7.7
uniprot
proteins
ec_number
4.2.99.-
uniprot
proteins
ec_number
4.2.99.18
uniprot
proteins
function
FUNCTION: Repair polymerase that plays a key role in base-excision repair (PubMed:10556592, PubMed:9207062, PubMed:9572863). During this process, the damaged base is excised by specific DNA glycosylases, the DNA backbone is nicked at the abasic site by an apurinic/apyrimidic (AP) endonuclease, and POLB removes 5'-deoxyribose-phosphate from the preincised AP site acting as a 5'-deoxyribose-phosphate lyase (5'-dRP lyase); through its DNA polymerase activity, it adds one nucleotide to the 3' end of the arising single-nucleotide gap (PubMed:10556592, PubMed:17526740, PubMed:8841119, PubMed:9556598, PubMed:9572863, PubMed:9614142). Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. It is also able to cleave sugar-phosphate bonds 3' to an intact AP site, acting as an AP lyase (PubMed:9614142). {ECO:0000269|PubMed:10556592, ECO:0000269|PubMed:11805079, ECO:0000269|PubMed:17526740, ECO:0000269|PubMed:21362556, ECO:0000269|PubMed:8841119, ECO:0000269|PubMed:9207062, ECO:0000269|PubMed:9556598, ECO:0000269|PubMed:9572863, ECO:0000269|PubMed:9614142}.
uniprot
proteins
mass_dalton
38178
uniprot
proteins
mutagenesis
MUTAGEN 25; /note="F->W: No effect on 5'-dRP lyase activity. Decreased ssDNA binding."; /evidence="ECO:0000269|PubMed:9556598"; MUTAGEN 34; /note="H->G: Decreased 5'-dRP lyase activity. Decreased ssDNA binding."; /evidence="ECO:0000269|PubMed:9556598"; MUTAGEN 35; /note="K->A: Decreased 5'-dRP lyase activity. Decreased ssDNA binding. Loss of 5'-dRP lyase activity; when associated with A-68 and A-72. Decreased ssDNA binding; when associated with A-68 and A-72. No effect on structure shown by circular dichroism."; /evidence="ECO:0000269|PubMed:9556598"; MUTAGEN 35; /note="K->Q: Reduces 5'-dRP lyase activity slightly."; /evidence="ECO:0000269|PubMed:9572863"; MUTAGEN 35; /note="K->R: No effect on 5'-dRP lyase activity."; /evidence="ECO:0000269|PubMed:16172026"; MUTAGEN 39; /note="Y->F: No effect on 5'-dRP lyase activity."; /evidence="ECO:0000269|PubMed:16172026"; MUTAGEN 39; /note="Y->Q: Abolishes DNA polymerase and 5'-dRP lyase activity."; /evidence="ECO:0000269|PubMed:9572863"; MUTAGEN 41; /note="K->R: Abolishes ubiquitination; when associated with R-61 and R-81."; /evidence="ECO:0000269|PubMed:19713937"; MUTAGEN 60; /note="K->A: Decreased 5'-dRP lyase activity. Decreased ssDNA binding."; /evidence="ECO:0000269|PubMed:9556598"; MUTAGEN 61; /note="K->R: Abolishes ubiquitination; when associated with R-41 and R-81."; /evidence="ECO:0000269|PubMed:19713937"; MUTAGEN 68; /note="K->A: No effect on 5'-dRP lyase activity. Decreased ssDNA binding. Loss of 5'-dRP lyase activity; when associated with A-35 and A-72. Decreased ssDNA binding; when associated with A-35 and A-72. No effect on structure shown by circular dichroism."; /evidence="ECO:0000269|PubMed:16172026, ECO:0000269|PubMed:9556598"; MUTAGEN 68; /note="K->Q,R: Slightly reduces 5'-dRP lyase activity."; /evidence="ECO:0000269|PubMed:16172026, ECO:0000269|PubMed:9572863"; MUTAGEN 71; /note="E->Q: No effect on 5'-dRP lyase activity. No effect on structure shown by circular dichroism. No effect on ssDNA binding."; /evidence="ECO:0000269|PubMed:9556598"; MUTAGEN 72; /note="K->A: Severely reduced 5'-dRP lyase activity. Does not affect ssDNA binding. Loss of 5'-dRP lyase activity; when associated with A-35 and A-68. Decreased ssDNA binding; when associated with A-35 and A-68. No effect on structure shown by circular dichroism."; /evidence="ECO:0000269|PubMed:16172026, ECO:0000269|PubMed:9556598"; MUTAGEN 72; /note="K->Q,R: Abolishes 5'-dRP lyase activity. No effect on DNA polymerase activity."; /evidence="ECO:0000269|PubMed:9572863"; MUTAGEN 75; /note="E->A: Slightly decreased 5'-dRP lyase activity. Decreased ssDNA binding. No effect on structure shown by circular dichroism."; /evidence="ECO:0000269|PubMed:9556598"; MUTAGEN 81; /note="K->R: Abolishes ubiquitination; when associated with R-41 and R-61."; /evidence="ECO:0000269|PubMed:19713937"; MUTAGEN 83; /note="R->K: Slight effect. Abolishes methylation by PRMT6 and impairs the polymerase activity; when associated with K-152."; /evidence="ECO:0000269|PubMed:16600869"; MUTAGEN 84; /note="K->A: No effect on structure shown by circular dichroism. No effect on ssDNA binding."; /evidence="ECO:0000269|PubMed:9556598"; MUTAGEN 84; /note="K->R,A: No effect on 5'-dRP lyase activity."; /evidence="ECO:0000269|PubMed:9556598, ECO:0000269|PubMed:9572863"; MUTAGEN 152; /note="R->C: Severely decreased function in base-excision repair. Severely decreased DNA-directed DNA polymerase activity. No effect on 5'-dRP lyase activity. No effect on DNA binding. No effect on structure shown by circular dichroism. No effect on interaction with APEX1, FEN1 and PCNA."; /evidence="ECO:0000269|PubMed:26760506"; MUTAGEN 152; /note="R->K: Slight effect. Abolishes methylation by PRMT6 and impairs the polymerase activity; when associated with K-83."; /evidence="ECO:0000269|PubMed:16600869"; MUTAGEN 285; /note="H->D: Affects DNA-directed DNA polymerase activity; contrary to wild-type enzyme, the mutant efficiently extends mispaired termini in gapped DNA. No effect on secondary structure shown by circular dichroism."; /evidence="ECO:0000269|PubMed:18616290"; MUTAGEN 288; /note="E->K: Changed DNA-directed DNA polymerase activity; in complex with the DNA template and the incoming dNTP, it assumes a close conformation faster than wild-type POLB and exhibits a slower rate of nucleotide release. Results in decreased fidelity on one-base-gapped DNA and increased mutation frequency at A-T base pairs. No effect on secondary structure shown by circular dichroism. No effect on thermal stability."; /evidence="ECO:0000269|PubMed:22650412, ECO:0000269|PubMed:28945359
uniprot
proteins
post_translational_modification
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}.
uniprot
proteins
protein_family
DNA polymerase type-X family
uniprot
proteins
pubmed
10556592
uniprot
proteins
pubmed
10648175
uniprot
proteins
pubmed
11805079
uniprot
proteins
pubmed
12517346
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15075389
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16172026
uniprot
proteins
pubmed
16600869
uniprot
proteins
pubmed
17526740
uniprot
proteins
pubmed
18039710
uniprot
proteins
pubmed
18616290
uniprot
proteins
pubmed
19336415
uniprot
proteins
pubmed
19713937
uniprot
proteins
pubmed
21362556
uniprot
proteins
pubmed
22650412
uniprot
proteins
pubmed
2423078
uniprot
proteins
pubmed
25260657
uniprot
proteins
pubmed
26760506
uniprot
proteins
pubmed
28945359
uniprot
proteins
pubmed
3182828
uniprot
proteins
pubmed
31999437
uniprot
proteins
pubmed
3284575
uniprot
proteins
pubmed
36982964
uniprot
proteins
pubmed
7705833
uniprot
proteins
pubmed
7914364
uniprot
proteins
pubmed
8841119
uniprot
proteins
pubmed
8841120
uniprot
proteins
pubmed
9207062
uniprot
proteins
pubmed
9287163
uniprot
proteins
pubmed
9556598
uniprot
proteins
pubmed
9572863
uniprot
proteins
pubmed
9614142
uniprot
proteins
sequence_length
335
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Cytoplasmic in normal conditions. Translocates to the nucleus following DNA damage.
uniprot
proteins