PRIMPOL
entrez
201973
canonical
uniprot
Q96LW4
canonical
ensembl
ENSG00000164306
resolver
ensp
ENSP00000313816
resolver
ensp
ENSP00000420860
resolver
ensp
ENSP00000421913
resolver
ensp
ENSP00000425316
resolver
ensp
ENSP00000538835
resolver
ensp
ENSP00000538836
resolver
ensp
ENSP00000538842
resolver
ensp
ENSP00000538847
resolver
ensp
ENSP00000636729
resolver
ensp
ENSP00000751849
resolver
enst
ENST00000515774
resolver
genesymbol
PRIMPOL
resolver
genesymbol_syn
CCDC111
resolver
hgnc
HGNC:26575
resolver
uniprot
A0A0A0MTC0
resolver
uniprot
A0A5S6SZ32
resolver
uniprot
D3DP55
resolver
uniprot
D6RDM1
resolver
uniprot
Q5HYJ9
resolver
uniprot_entry
A0A5S6SZ32_HUMAN
resolver
uniprot_entry
PRIPO_HUMAN
resolver
uniprot_sec
A0A0A0MTC0
resolver
uniprot_sec
D3DP55
resolver
uniprot_sec
D6RDM1
resolver
uniprot_sec
Q5HYJ9
resolver
amino_acid_sequence
MNRKWEAKLKQIEERASHYERKPLSSVYRPRLSKPEEPPSIWRLFHRQAQAFNFVKSCKEDVHVFALECKVGDGQRIYLVTTYAEFWFYYKSRKNLLHCYEVIPENAVCKLYFDLEFNKPANPGADGKKMVALLIEYVCKALQELYGVNCSAEDVLNLDSSTDEKFSRHLIFQLHDVAFKDNIHVGNFLRKILQPALDLLGSEDDDSAPETTGHGFPHFSEAPARQGFSFNKMFTEKATEESWTSNSKKLERLGSAEQSSPDLSFLVVKNNMGEKHLFVDLGVYTRNRNFRLYKSSKIGKRVALEVTEDNKFFPIQSKDVSDEYQYFLSSLVSNVRFSDTLRILTCEPSQNKQKGVGYFNSIGTSVETIEGFQCSPYPEVDHFVLSLVNKDGIKGGIRRWNYFFPEELLVYDICKYRWCENIGRAHKSNNIMILVDLKNEVWYQKCHDPVCKAENFKSDCFPLPAEVCLLFLFKEEEEFTTDEADETRSNETQNPHKPSPSRLSTGASADAVWDNGIDDAYFLEATEDAELAEAAENSLLSYNSEVDEIPDELIIEVLQE
uniprot
proteins
disease_involvement
DISEASE: Myopia 22, autosomal dominant (MYP22) [MIM:615420]: A refractive error of the eye, in which parallel rays from a distant object come to focus in front of the retina, vision being better for near objects than for far. {ECO:0000269|PubMed:23579484, ECO:0000269|PubMed:25262353}. Note=The disease is caused by variants affecting the gene represented in this entry.
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:24126761, PubMed:24207056, PubMed:24240614, PubMed:24267451, PubMed:24682820, PubMed:25255211, PubMed:25262353, PubMed:25550423, PubMed:25746449, PubMed:27989484, PubMed:28534480, PubMed:29608762, PubMed:30889508, PubMed:31676232). 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 (PubMed:24126761, PubMed:24207056, PubMed:24240614, PubMed:24267451, PubMed:24682820, PubMed:25255211, PubMed:25262353, PubMed:25550423, PubMed:25746449, PubMed:27989484, PubMed:28534480, PubMed:29608762, PubMed:30633872, PubMed:30889508). Shows a high capacity to tolerate DNA damage lesions such as 8oxoG and abasic sites in DNA (PubMed:24126761, PubMed:24207056, PubMed:24240614, PubMed:24267451, PubMed:25746449). 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 (PubMed:24240614, PubMed:26626482, PubMed:28534480, PubMed:30478192). 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 (PubMed:24240614, PubMed:25746449, PubMed:31676232). Also able to incorporate nucleotides opposite DNA lesions such as 8oxoG, like a regular translesion synthesis DNA polymerase (PubMed:24207056, PubMed:25255211, PubMed:25746449). Also required for reinitiating stalled forks after UV damage during nuclear DNA replication (PubMed:24240614). Required for mitochondrial DNA (mtDNA) synthesis and replication, by reinitiating synthesis after UV damage or in the presence of chain-terminating nucleotides (PubMed:24207056). Prevents APOBEC family-mediated DNA mutagenesis by repriming downstream of abasic site to prohibit error-prone translesion synthesis (By similarity). Has non-overlapping function with POLH (PubMed:24240614). In addition to its role in DNA damage response, also required to maintain efficient nuclear and mitochondrial DNA replication in unperturbed cells (PubMed:30715459). {ECO:0000250|UniProtKB:Q6P1E7, ECO:0000269|PubMed:24126761, ECO:0000269|PubMed:24207056, ECO:0000269|PubMed:24240614, ECO:0000269|PubMed:24267451, ECO:0000269|PubMed:24682820, ECO:0000269|PubMed:25255211, ECO:0000269|PubMed:25262353, ECO:0000269|PubMed:25550423, ECO:0000269|PubMed:25746449, ECO:0000269|PubMed:26626482, ECO:0000269|PubMed:27989484, ECO:0000269|PubMed:28534480, ECO:0000269|PubMed:29608762, ECO:0000269|PubMed:30478192, ECO:0000269|PubMed:30633872, ECO:0000269|PubMed:30715459, ECO:0000269|PubMed:30889508, ECO:0000269|PubMed:31676232}.
uniprot
proteins
mass_dalton
64412
uniprot
proteins
mutagenesis
MUTAGEN 89; /note="Y->F: Does not affect DNA primase activity."; /evidence="ECO:0000269|PubMed:25262353"; MUTAGEN 89; /note="Y->S: Reduced DNA primase activity."; /evidence="ECO:0000269|PubMed:25262353"; MUTAGEN 114..116; /note="DLE->ALA: In AxA; abolished DNA primase and polymerase activities."; /evidence="ECO:0000269|PubMed:24207056, ECO:0000269|PubMed:24267451, ECO:0000269|PubMed:24682820, ECO:0000269|PubMed:26626482, ECO:0000269|PubMed:29608762, ECO:0000269|PubMed:30478192, ECO:0000269|PubMed:30889508"; MUTAGEN 114; /note="D->A: Abolishes DNA primase and polymerase activities."; /evidence="ECO:0000269|PubMed:24126761"; MUTAGEN 169; /note="H->N: Abolishes DNA primase and polymerase activities."; /evidence="ECO:0000269|PubMed:24126761"; MUTAGEN 280; /note="D->A: Abolished Mn(2+) DNA primase activity."; /evidence="ECO:0000269|PubMed:30889508"; MUTAGEN 419; /note="C->A: Abolished zinc-binding, leading to altered translesion synthesis; when associated with A-426."; /evidence="ECO:0000269|PubMed:24682820, ECO:0000269|PubMed:26626482, ECO:0000269|PubMed:30478192"; MUTAGEN 419; /note="C->G: In mutant CH; abolished DNA primase activity and impaired ability to restart stalled forks; when associated with Y-426."; /evidence="ECO:0000269|PubMed:24240614"; MUTAGEN 426; /note="H->A: Abolished zinc-binding, leading to altered translesion synthesis; when associated with A-419."; /evidence="ECO:0000269|PubMed:24682820, ECO:0000269|PubMed:26626482, ECO:0000269|PubMed:30478192"; MUTAGEN 426; /note="H->D: Abolishes DNA primase activity, while it increases DNA polymerase activity."; /evidence="ECO:0000269|PubMed:24126761, ECO:0000269|PubMed:24240614"; MUTAGEN 426; /note="H->Y: In mutant CH; abolished DNA primase activity and impaired ability to restart stalled forks; when associated with G-419."; /evidence="ECO:0000269|PubMed:24126761, ECO:0000269|PubMed:24240614"; MUTAGEN 519..522; /note="DAYF->RAYA: Abolished interaction with RPA1, impairing recruitment to chromatin and reducing DNA primase activity; when associated with 551-R--A-554."; /evidence="ECO:0000269|PubMed:28534480"; MUTAGEN 551..554; /note="DELI->RELA: Abolished interaction with RPA1, impairing recruitment to chromatin and reducing DNA primase activity; when associated with 519-R--A-522."; /evidence="ECO:0000269|PubMed:28534480
uniprot
proteins
protein_family
Eukaryotic-type primase small subunit family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23579484
uniprot
proteins
pubmed
24126761
uniprot
proteins
pubmed
24207056
uniprot
proteins
pubmed
24240614
uniprot
proteins
pubmed
24267451
uniprot
proteins
pubmed
24682820
uniprot
proteins
pubmed
25255211
uniprot
proteins
pubmed
25262353
uniprot
proteins
pubmed
25550423
uniprot
proteins
pubmed
25680975
uniprot
proteins
pubmed
25680976
uniprot
proteins
pubmed
25746449
uniprot
proteins
pubmed
26626482
uniprot
proteins
pubmed
26984527
uniprot
proteins
pubmed
27819052
uniprot
proteins
pubmed
27989484
uniprot
proteins
pubmed
28396594
uniprot
proteins
pubmed
28534480
uniprot
proteins
pubmed
29608762
uniprot
proteins
pubmed
30478192
uniprot
proteins
pubmed
30633872
uniprot
proteins
pubmed
30715459
uniprot
proteins
pubmed
30889508
uniprot
proteins
pubmed
31676232
uniprot
proteins
sequence_length
560
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24207056, ECO:0000269|PubMed:24240614}. Mitochondrion matrix {ECO:0000269|PubMed:24207056}. Chromosome {ECO:0000269|PubMed:28534480}. Note=Present in the nucleus, but a larger fraction is localized inside mitochondria (PubMed:24207056). Associates with nuclear chromatin during the G1 and S phases of unperturbed cell cycles (PubMed:24207056). Recruited to stalled replication forks following interaction with RPA1 (PubMed:28534480). {ECO:0000269|PubMed:24207056, ECO:0000269|PubMed:28534480}.
uniprot
proteins