Polb
entrez
29240
canonical
uniprot
P06766
canonical
ensembl
ENSRNOG00000019150
resolver
ensembl
ENSRNOG00055007682
resolver
ensembl
ENSRNOG00060027954
resolver
ensembl
ENSRNOG00065008755
resolver
ensp
ENSRNOP00000026039
resolver
ensp
ENSRNOP00055010253
resolver
ensp
ENSRNOP00060040531
resolver
ensp
ENSRNOP00065010380
resolver
enst
ENSRNOT00000026039
resolver
enst
ENSRNOT00055012865
resolver
enst
ENSRNOT00060048617
resolver
enst
ENSRNOT00065013936
resolver
genesymbol
Polb
resolver
uniprot
Q4G081
resolver
uniprot_entry
DPOLB_RAT
resolver
uniprot_sec
Q4G081
resolver
amino_acid_sequence
MSKRKAPQETLNGGITDMLVELANFEKNVSQAIHKYNAYRKAASVIAKYPHKIKSGAEAKKLPGVGTKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVTGIGPSAARKLVDEGIKTLEDLRKNEDKLNHHQRIGLKYFEDFEKRIPREEMLQMQDIVLNEVKKLDPEYIATVCGSFRRGAESSGDMDVLLTHPNFTSESSKQPKLLHRVVEQLQKVRFITDTLSKGETKFMGVCQLPSENDENEYPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEKGFTINEYTIRPLGVTGVAGEPLPVDSEQDIFDYIQWRYREPKDRSE
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. 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. 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. {ECO:0000250|UniProtKB:P06746}.
uniprot
proteins
mass_dalton
38327
uniprot
proteins
mutagenesis
MUTAGEN 190; /note="D->E,S: Loss of activity."; /evidence="ECO:0000269|PubMed:2036395"; MUTAGEN 191; /note="M->I: No loss of activity."; MUTAGEN 191; /note="M->T: 50% loss of activity."; MUTAGEN 192; /note="D->E,S: Loss of activity."; /evidence="ECO:0000269|PubMed:2036395"; MUTAGEN 246; /note="D->V: Misincorporates T nucleotide opposite G/C template."; /evidence="ECO:0000269|PubMed:14563842
uniprot
proteins
post_translational_modification
PTM: Methylation by PRMT6 stimulates the polymerase activity by enhancing DNA binding and processivity. {ECO:0000250}.; 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). {ECO:0000250}.
uniprot
proteins
protein_family
DNA polymerase type-X family
uniprot
proteins
pubmed
10656829
uniprot
proteins
pubmed
11330999
uniprot
proteins
pubmed
1420147
uniprot
proteins
pubmed
14563842
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
2036395
uniprot
proteins
pubmed
2198936
uniprot
proteins
pubmed
2404980
uniprot
proteins
pubmed
2873575
uniprot
proteins
pubmed
3597402
uniprot
proteins
pubmed
7516581
uniprot
proteins
pubmed
8137427
uniprot
proteins
pubmed
8639559
uniprot
proteins
pubmed
8841120
uniprot
proteins
sequence_length
335
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P06746}. Cytoplasm {ECO:0000250|UniProtKB:P06746}. Note=Cytoplasmic in normal conditions. Translocates to the nucleus following DNA damage. {ECO:0000250|UniProtKB:P06746}.
uniprot
proteins