Primpol
entrez
408022
canonical
uniprot
Q6P1E7
canonical
ensembl
ENSMUSG00000038225
resolver
ensp
ENSMUSP00000147574
resolver
ensp
ENSMUSP00000148093
resolver
genesymbol
Primpol
resolver
uniprot
Q8BSR3
resolver
uniprot_entry
PRIPO_MOUSE
resolver
uniprot_sec
Q8BSR3
resolver
amino_acid_sequence
MLRKWEARVKQIEERASHYERKPLSSVYRPRLAKPEEPSSIWKLFHRQNQAFNFVKSCKESVHVFALECKRGNGQRIYLVTSYAQLWFYYKTRKTLLHCYEVIPENAVCKLYFDLEFNKLANPGADGKMMVALLIQHVCKALEEFYNVQCSAEDVFNLDSSTEEKFSRHLIFQLHNVAFKDNRHAGNFVRKILQPALHLIAEDDEAKVPEAVGQDASGFSVTPLKQEISEAREKVGLPKQCDPDLSFLVVKNHMGEKCLFVDLGVYTKNRNFRLYQSSKIGKCVSLEVAEDNRFIPKQSKDISEENQYFLSSLVSNVRFSDTLRVLTCHPSQTKRKRAECFNSTGTSVESIEGFQGSPYPEVDQFVLSLVNKHDIKGGIRRWNYFFPEELLVYDICKYRWCENIGRAHKSNNIMILVDLKNEVWYQKCHDPVCKAQNFKSTCSPLPTEVSLLFLLKDEDFTSGETDDTSTSLTKDSQTPPSCNLSAGGLSAAAWDDEDDALFLEATEDAEFADAADKSLGSMDDIPDELIIEALQNS
uniprot
proteins
ec_number
2.7.7.102
uniprot
proteins
ec_number
2.7.7.7
uniprot
proteins
function
FUNCTION: DNA primase and DNA polymerase required to tolerate replication-stalling lesions by bypassing them (PubMed:26926109, PubMed:29073063). Required to facilitate mitochondrial and nuclear replication fork progression by initiating de novo DNA synthesis using dNTPs and acting as an error-prone DNA polymerase able to bypass certain DNA lesions (By similarity). Shows a high capacity to tolerate DNA damage lesions such as 8oxoG and abasic sites in DNA (By similarity). Provides different translesion synthesis alternatives when DNA replication is stalled: able to synthesize DNA primers downstream of lesions, such as ultraviolet (UV) lesions, R-loops and G-quadruplexes, to allow DNA replication to continue (By similarity). Can also realign primers ahead of 'unreadable lesions' such as abasic sites and 6-4 photoproduct (6-4 pyrimidine-pyrimidinone), thereby skipping the lesion. Repriming avoids fork degradation while leading to accumulation of internal ssDNA gaps behind the forks (By similarity). Also able to incorporate nucleotides opposite DNA lesions such as 8oxoG, like a regular translesion synthesis DNA polymerase (By similarity). Also required for reinitiating stalled forks after UV damage during nuclear DNA replication (By similarity). Required for mitochondrial DNA (mtDNA) synthesis and replication, by reinitiating synthesis after UV damage or in the presence of chain-terminating nucleotides (PubMed:29073063). Prevents APOBEC family-mediated DNA mutagenesis by repriming downstream of abasic site to prohibit error-prone translesion synthesis (PubMed:26926109). Has non-overlapping function with POLH (By similarity). In addition to its role in DNA damage response, also required to maintain efficient nuclear and mitochondrial DNA replication in unperturbed cells (By similarity). {ECO:0000250|UniProtKB:Q96LW4, ECO:0000269|PubMed:26926109, ECO:0000269|PubMed:29073063}.
uniprot
proteins
mass_dalton
61330
uniprot
proteins
protein_family
Eukaryotic-type primase small subunit family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
24207056
uniprot
proteins
pubmed
26926109
uniprot
proteins
pubmed
29073063
uniprot
proteins
sequence_length
537
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96LW4}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q96LW4}. Chromosome {ECO:0000250|UniProtKB:Q96LW4}. Note=Present in the nucleus, but a larger fraction is localized inside mitochondria. Associates with nuclear chromatin during the G1 and S phases of unperturbed cell cycles. Recruited to stalled replication forks following interaction with RPA1. {ECO:0000250|UniProtKB:Q96LW4}.
uniprot
proteins