Polq
entrez
77782
canonical
uniprot
Q8CGS6
canonical
ensembl
ENSMUSG00000034206
resolver
ensp
ENSMUSP00000059757
resolver
ensp
ENSMUSP00000071396
resolver
genesymbol
Polq
resolver
genesymbol_syn
Chaos1
resolver
uniprot
Q3UTE0
resolver
uniprot
Q80XB7
resolver
uniprot_entry
DPOLQ_MOUSE
resolver
uniprot_entry
Q80XB7_MOUSE
resolver
uniprot_sec
Q3UTE0
resolver
amino_acid_sequence
MSLPRRSRKRRRSSSGSDTFSGDGDSFVSPQLRCGPVLSPPPGLGRGRRLTGTGTNKRRVSDDQIDQLLLANWGLPKAVLEKYHSFGVRKMFEWQAECLLLGHVLEGKNLVYSAPTSAGKTLVAELLILKRVLETRKKALFILPFVSVAKEKKCYLQSLFQEVGLKVDGYMGSTSPTGQFSSLDIAVCTIERANGLVNRLIEENKMDLLGMVVVDELHMLGDSHRGYLLELLLTKICYVTRKSASHQAESASTLSNAVQIVGMSATLPNLQLVASWLNAELYHTDFRPVPLLESIKIGNSIYDSSMKLVREFQPLLQVKGDEDHIVSLCYETIQDNHSVLIFCPSKKWCEKVADIIAREFYNLHHQPEGLVKSSEFPPVILDQKSLLEVMDQLKRSPSGLDSVLKNTVPWGVAFHHAGLTFEERDIIEGAFRQGFIRVLAATSTLSSGVNLPARRVIIRTPIFSGQPLDILTYKQMVGRAGRKGVDTMGESILVCKNSEKSKGIALLQGSLEPVHSCLQRQGEVTASMIRAILEIIVGGVASTSQDMQTYAACTFLAAAIQEGKQGMQRNQDDAQLGAIDACVTWLLENEFIQVAEPGDGTGGKVYHPTHLGSATLSSSLSPTDTLDIFADLQRAMKGFVLENDLHIVYLVTPVFEDWISIDWYRFFCLWEKLPTSMKRVAELVGVEEGFLARCVKGKVVARTERQHRQMAIHKRFFTSLVLLDLISEIPLKDINQKYGCNRGQIQSLQQSAAVYAGMITVFSNRLGWHNMELLLSQFQKRLTFGIQRELCDLIRVSLLNAQRARFLYASGFLTVADLARADSAEVEVALKNSLPFKSARKAVDEEEEAAEERRSMRTIWVTGKGLSAREAAALIVEEAKMILQQDLIEMGVRWDPKSPLSSSTHSRTSTSEVKEHTFKSQTKSSHKRLASMGRNSIRASGSNDKPSPDAERGIDDCSEHADSLCKFQGNFEPQTPSICTARKRTSLGINKEMLRKSLKEGKPSTKEVLQTFSSEKTRKTALSFSSEQVNNTLPSGRDRKYQKKSWGSSPVRDSGMHRGDLQGQTMCTSALCEDSQKSLEEQNAEFRSPGLFAKHLPSCAKEKCKKPSLPLQRQQACSRRSTESCAAVGHPAAGSSPAAARDRRGLAARETEKGNEALTENGGESQLQDTYPVSQYLEYHSEKHTNTCTRQKTLTEGQAGSSYVARDSNDAAPIKCERMKLNSKDRDSNPCRQALGSYTGRTEALQSTAKLGQAGGQCENLLNSSGVQGKTGAHATNRTEHSHASNPAFCDFGDSLDLDTQSEEIIEQMATENTMQGAKAVVIMEEGSAMQNKCHSTPGDQHVPGAANTDHVDSKKVESVKANTEKNINRGAPVSLIFHTQGENGACFKGNEHSVTDSQLNSFLQGFETQEIVKPIIPLAPQMRTPTGVEEESLPETSLNMSDSILFDSFGEDGFGQGQSPDIKANQPLLSEMTPNHFSNPPHPQEDPVMTPTVSEPQGTQQQGVCLSGESIIFSDIDSAQVIEALDNMAAFHVQENCNSVALKTLEPSDSAVLGNECPQGKLVRGDQNEGSPKPKLTETNQDNSFTWSGASFNLSPELQRILDKVSSPRENEKPKMIHVNLSSFEGNSKESHEREEINSDLGTVQRTSVFPSNEVKNRTEGLESKARHGGASSPLPRKESAAADDNGLIPPTPVPASASKVAFPEILGTSVKRQKASSALQPGESCLFGSPSDNQNQDLSQELRDSLKDYDGSVADTSFFLQSQDGLLLTQASCSSESLAIIDVASDQILFQTFVKEWQCQKRFSISLACEKMTSSMSSKTATIGGKLKQVSLPQEATVEDAGFPVRGCDGAVVVGLAVCWGAKDAYYLSLQKEQKQSEISPSLAPPPLDATLTVKERMECLQSCLQKKSDRERSVVTYDFIQTYKVLLLSCGISLEPSYEDPKVACWLLDPDSKEPTLHSIVTSFLPHELALLEGMETGPGIQSLGLNVNTEHSGRYRASVESVLIFNSMNQLNSLLQKENLHDIFCKVEMPSQYCLALLELNGIGFSTAECESQKHVMQAKLDAIETQAYQLAGHSFSFTSADDIAQVLFLELKLPPNGEMKTQGSKKTLGSTRRGNESGRRMRLGRQFSTSKDILNKLKGLHPLPGLILEWRRISNAITKVVFPLQREKHLNPLLRMERIYPVSQSHTATGRITFTEPNIQNVPRDFEIKMPTLVRESPPSQAPKGRFPMAIGQDKKVYGLHPGHRTQMEEKASDRGVPFSVSMRHAFVPFPGGLILAADYSQLELRILAHLSRDCRLIQVLNTGADVFRSIAAEWKMIEPDAVGDDLRQHAKQICYGIIYGMGAKSLGEQMGIKENDAASYIDSFKSRYKGINHFMRDTVKNCRKNGFVETILGRRRYLPGIKDDNPYHKAHAERQAINTTVQGSAADIVKIATVNIQKQLETFRSTFKSHGHRESMLQNDRTGLLPKRKLKGMFCPMRGGFFILQLHDELLYEVAEEDVVQVAQIVKNEMECAIKLSVKLKVKVKIGASWGELKDFDV
uniprot
proteins
ec_number
2.7.7.49
uniprot
proteins
ec_number
2.7.7.7
uniprot
proteins
ec_number
5.6.2.-
uniprot
proteins
function
FUNCTION: Low-fidelity DNA polymerase with a putative helicase activity that promotes microhomology-mediated end-joining (MMEJ), an alternative non-homologous end-joining (NHEJ) machinery required to repair double-strand breaks in DNA during mitosis (PubMed:21883722, PubMed:25275444, PubMed:25642960, PubMed:25642963, PubMed:29079701, PubMed:31537809). MMEJ is an error-prone repair pathway that produces deletions of sequences from the strand being repaired and promotes genomic rearrangements, such as telomere fusions, some of them leading to cellular transformation (PubMed:25275444, PubMed:25642960, PubMed:25642963, PubMed:29079701, PubMed:31537809). MMEJ is required during mitosis to repair persistent double-strand breaks that originate in S-phase (By similarity). Although error-prone, MMEJ protects against chromosomal instability and tumorigenesis (PubMed:30773314). The polymerase acts by binding directly the 2 ends of resected double-strand breaks, allowing microhomologous sequences in the overhangs to form base pairs (By similarity). It then extends each strand from the base-paired region using the opposing overhang as a template (By similarity). Requires partially resected DNA containing 2 to 6 base pairs of microhomology to perform MMEJ (By similarity). The polymerase lacks proofreading activity and is highly promiscuous: unlike most polymerases, promotes extension of ssDNA and partial ssDNA (pssDNA) substrates (By similarity). When the ends of a break do not contain terminal microhomology must identify embedded complementary sequences through a scanning step (By similarity). Promoting dissociation of the replication protein A complex (RPA/RP-A), composed of RPA1, RPA2 and RPA3, from resected double-strand breaks to allow their annealing and subsequent joining by MMEJ (PubMed:29058711). Removal of RPA/RP-A complex proteins prevents RAD51 accumulation at resected ends, thereby inhibiting homology-recombination repair (HR) pathway (PubMed:25642960, PubMed:25642963, PubMed:29058711). Also shows RNA-directed DNA polymerase activity to mediate DNA repair in vitro; however this activity needs additional evidence in vivo (By similarity). May also have lyase activity (By similarity). Involved in somatic hypermutation of immunoglobulin genes, a process that requires the activity of DNA polymerases to ultimately introduce mutations at both A/T and C/G base pairs (PubMed:16172387, PubMed:16222339, PubMed:16890500, PubMed:17449470). However, POLQ does not play a major role in somatic hypermutation (PubMed:18485835). POLQ-mediated end joining activity is involved in random integration of exogenous DNA hampers (PubMed:28687761). {ECO:0000250|UniProtKB:O75417, ECO:0000269|PubMed:16172387, ECO:0000269|PubMed:16222339, ECO:0000269|PubMed:16890500, ECO:0000269|PubMed:17449470, ECO:0000269|PubMed:18485835, ECO:0000269|PubMed:21883722, ECO:0000269|PubMed:25275444, ECO:0000269|PubMed:25642960, ECO:0000269|PubMed:25642963, ECO:0000269|PubMed:28687761, ECO:0000269|PubMed:29058711, ECO:0000269|PubMed:29079701, ECO:0000269|PubMed:30773314, ECO:0000269|PubMed:31537809}.
uniprot
proteins
mass_dalton
280714
uniprot
proteins
mutagenesis
MUTAGEN 120; /note="K->G: Abolished helicase activity."; /evidence="ECO:0000269|PubMed:29058711"; MUTAGEN 120; /note="K->M: Abolishes ATP-binding in the helicase domain without affecting the ability to confer resistance to DNA damage."; /evidence="ECO:0000269|PubMed:25275444"; MUTAGEN 1932; /note="S->P: In chaos1; mice display higher frequencies of spontaneous and radiation- or mitomycin C-induced micronucleated erythrocytes."; /evidence="ECO:0000269|PubMed:15542845"; MUTAGEN 2494..2495; /note="DE->AA: Abolishes DNA polymerase activity and ability to confer resistance to DNA damage."; /evidence="ECO:0000269|PubMed:25275444, ECO:0000269|PubMed:25642960"; MUTAGEN 2494..2495; /note="DE->PR: Abolished DNA polymerase activity."; /evidence="ECO:0000269|PubMed:29058711
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by PLK1; promoting interaction with TOPBP1 and recruitment to DNA damage sites. {ECO:0000250|UniProtKB:O75417}.
uniprot
proteins
protein_family
DNA polymerase type-A family
uniprot
proteins
pubmed
12663541
uniprot
proteins
pubmed
15542845
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16172387
uniprot
proteins
pubmed
16222339
uniprot
proteins
pubmed
16890500
uniprot
proteins
pubmed
17449470
uniprot
proteins
pubmed
18485835
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19630521
uniprot
proteins
pubmed
21883722
uniprot
proteins
pubmed
25275444
uniprot
proteins
pubmed
25642960
uniprot
proteins
pubmed
25642963
uniprot
proteins
pubmed
28687761
uniprot
proteins
pubmed
29058711
uniprot
proteins
pubmed
29079701
uniprot
proteins
pubmed
30773314
uniprot
proteins
pubmed
31537809
uniprot
proteins
sequence_length
2544
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O18475}. Chromosome {ECO:0000250|UniProtKB:O75417}. Note=Enriched in chromatin in response to ultaviolet (UV) light. Binds to chromatin during early G1. Recruited to DNA damage sites, such as double-stranded breaks (DSBs), following interaction with TOPBP1 and RHNO1. {ECO:0000250|UniProtKB:O75417}.
uniprot
proteins