POLQ

Protein identityUniProt · HPA

UniProt accession

O75417

Gene

POLQ

Ensembl

ENSG00000051341

Chromosome

3

Canonical length

2590 aa

Protein class

Cancer-related genes, Disease related genes, Enzymes, Metabolic proteins, Potential drug targets, Predicted intracellular proteins

Subcellular location

Nucleoplasm,Golgi apparatus,Cytosol

Quaternary structure

Homotetramer

OverviewNCBI Gene

Enables several functions, including catalytic activity, acting on DNA; identical protein binding activity; and magnesium ion binding activity. Involved in DNA metabolic process; negative regulation of double-strand break repair via homologous recombination; and protein homooligomerization. Located in Golgi apparatus; cytosol; and nucleoplasm. Is active in mitochondrial nucleoid; nucleus; and site of double-strand break. [provided by Alliance of Genome Resources, Jul 2025]

Canonical amino-acid sequenceUniProt

2590 residues, UniProt reviewed canonical sequence.

>O75417|POLQ
     1  MNLLRRSGKR RRSESGSDSF SGSGGDSSAS PQFLSGSVLS PPPGLGRCLK AAAAGECKPT
    61  VPDYERDKLL LANWGLPKAV LEKYHSFGVK KMFEWQAECL LLGQVLEGKN LVYSAPTSAG
   121  KTLVAELLIL KRVLEMRKKA LFILPFVSVA KEKKYYLQSL FQEVGIKVDG YMGSTSPSRH
   181  FSSLDIAVCT IERANGLINR LIEENKMDLL GMVVVDELHM LGDSHRGYLL ELLLTKICYI
   241  TRKSASCQAD LASSLSNAVQ IVGMSATLPN LELVASWLNA ELYHTDFRPV PLLESVKVGN
   301  SIYDSSMKLV REFEPMLQVK GDEDHVVSLC YETICDNHSV LLFCPSKKWC EKLADIIARE
   361  FYNLHHQAEG LVKPSECPPV ILEQKELLEV MDQLRRLPSG LDSVLQKTVP WGVAFHHAGL
   421  TFEERDIIEG AFRQGLIRVL AATSTLSSGV NLPARRVIIR TPIFGGRPLD ILTYKQMVGR
   481  AGRKGVDTVG ESILICKNSE KSKGIALLQG SLKPVRSCLQ RREGEEVTGS MIRAILEIIV
   541  GGVASTSQDM HTYAACTFLA ASMKEGKQGI QRNQESVQLG AIEACVMWLL ENEFIQSTEA
   601  SDGTEGKVYH PTHLGSATLS SSLSPADTLD IFADLQRAMK GFVLENDLHI LYLVTPMFED
   661  WTTIDWYRFF CLWEKLPTSM KRVAELVGVE EGFLARCVKG KVVARTERQH RQMAIHKRFF
   721  TSLVLLDLIS EVPLREINQK YGCNRGQIQS LQQSAAVYAG MITVFSNRLG WHNMELLLSQ
   781  FQKRLTFGIQ RELCDLVRVS LLNAQRARVL YASGFHTVAD LARANIVEVE VILKNAVPFK
   841  SARKAVDEEE EAVEERRNMR TIWVTGRKGL TEREAAALIV EEARMILQQD LVEMGVQWNP
   901  CALLHSSTCS LTHSESEVKE HTFISQTKSS YKKLTSKNKS NTIFSDSYIK HSPNIVQDLN
   961  KSREHTSSFN CNFQNGNQEH QTCSIFRARK RASLDINKEK PGASQNEGKT SDKKVVQTFS
  1021  QKTKKAPLNF NSEKMSRSFR SWKRRKHLKR SRDSSPLKDS GACRIHLQGQ TLSNPSLCED
  1081  PFTLDEKKTE FRNSGPFAKN VSLSGKEKDN KTSFPLQIKQ NCSWNITLTN DNFVEHIVTG
  1141  SQSKNVTCQA TSVVSEKGRG VAVEAEKINE VLIQNGSKNQ NVYMKHHDIH PINQYLRKQS
  1201  HEQTSTITKQ KNIIERQMPC EAVSSYINRD SNVTINCERI KLNTEENKPS HFQALGDDIS
  1261  RTVIPSEVLP SAGAFSKSEG QHENFLNISR LQEKTGTYTT NKTKNNHVSD LGLVLCDFED
  1321  SFYLDTQSEK IIQQMATENA KLGAKDTNLA AGIMQKSLVQ QNSMNSFQKE CHIPFPAEQH
  1381  PLGATKIDHL DLKTVGTMKQ SSDSHGVDIL TPESPIFHSP ILLEENGLFL KKNEVSVTDS
  1441  QLNSFLQGYQ TQETVKPVIL LIPQKRTPTG VEGECLPVPE TSLNMSDSLL FDSFSDDYLV
  1501  KEQLPDMQMK EPLPSEVTSN HFSDSLCLQE DLIKKSNVNE NQDTHQQLTC SNDESIIFSE
  1561  MDSVQMVEAL DNVDIFPVQE KNHTVVSPRA LELSDPVLDE HHQGDQDGGD QDERAEKSKL
  1621  TGTRQNHSFI WSGASFDLSP GLQRILDKVS SPLENEKLKS MTINFSSLNR KNTELNEEQE
  1681  VISNLETKQV QGISFSSNNE VKSKIEMLEN NANHDETSSL LPRKESNIVD DNGLIPPTPI
  1741  PTSASKLTFP GILETPVNPW KTNNVLQPGE SYLFGSPSDI KNHDLSPGSR NGFKDNSPIS
  1801  DTSFSLQLSQ DGLQLTPASS SSESLSIIDV ASDQNLFQTF IKEWRCKKRF SISLACEKIR
  1861  SLTSSKTATI GSRFKQASSP QEIPIRDDGF PIKGCDDTLV VGLAVCWGGR DAYYFSLQKE
  1921  QKHSEISASL VPPSLDPSLT LKDRMWYLQS CLRKESDKEC SVVIYDFIQS YKILLLSCGI
  1981  SLEQSYEDPK VACWLLDPDS QEPTLHSIVT SFLPHELPLL EGMETSQGIQ SLGLNAGSEH
  2041  SGRYRASVES ILIFNSMNQL NSLLQKENLQ DVFRKVEMPS QYCLALLELN GIGFSTAECE
  2101  SQKHIMQAKL DAIETQAYQL AGHSFSFTSS DDIAEVLFLE LKLPPNREMK NQGSKKTLGS
  2161  TRRGIDNGRK LRLGRQFSTS KDVLNKLKAL HPLPGLILEW RRITNAITKV VFPLQREKCL
  2221  NPFLGMERIY PVSQSHTATG RITFTEPNIQ NVPRDFEIKM PTLVGESPPS QAVGKGLLPM
  2281  GRGKYKKGFS VNPRCQAQME ERAADRGMPF SISMRHAFVP FPGGSILAAD YSQLELRILA
  2341  HLSHDRRLIQ VLNTGADVFR SIAAEWKMIE PESVGDDLRQ QAKQICYGII YGMGAKSLGE
  2401  QMGIKENDAA CYIDSFKSRY TGINQFMTET VKNCKRDGFV QTILGRRRYL PGIKDNNPYR
  2461  KAHAERQAIN TIVQGSAADI VKIATVNIQK QLETFHSTFK SHGHREGMLQ SDQTGLSRKR
  2521  KLQGMFCPIR GGFFILQLHD ELLYEVAEED VVQVAQIVKN EMESAVKLSV KLKVKVKIGA
  2581  SWGELKDFDV

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against POLQ can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Intracellular

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.39

Highest tissue expression

5.6 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about POLQ.

Disease | AllUniProt

Conditions POLQ is implicated in, by any mechanism.

• Breast cancer (BC) MIM:114480

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

1.22

gnomAD pLI

0

gnomAD missense Z

0.75

DepMap mean gene effect

-0.28

DepMap dependency class

selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 9% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• base-excision repair
• DNA damage response
• DNA repair
• DNA synthesis involved in DNA repair
• double-strand break repair
• double-strand break repair via alternative nonhomologous end joining
• error-prone translesion synthesis
• negative regulation of double-strand break repair via homologous recombination
• protein homooligomerization
• replication fork processing
• somatic hypermutation of immunoglobulin genes

Molecular functions

• 5'-deoxyribose-5-phosphate lyase activity
• ATP binding
• ATP hydrolysis activity
• chromatin binding
• damaged DNA binding
• DNA helicase activity
• DNA-directed DNA polymerase activity
• identical protein binding
• magnesium ion binding
• RNA-directed DNA polymerase activity
• single-stranded DNA helicase activity

Cellular components

• cytosol
• Golgi apparatus
• mitochondrial nucleoid
• nucleoplasm
• nucleus
• site of DNA damage
• site of double-strand break

Protein domainsUniProt · Pfam · InterPro

• DNA-directed DNA polymerase, family A, palm domain
• Helicase, C-terminal domain-like
• DNA polymerase A
• DEAD/DEAH-box helicase domain
• Ribonuclease H-like superfamily
• Helicase superfamily 1/2, ATP-binding domain
• DNA-directed DNA polymerase, family A, conserved site
• P-loop containing nucleoside triphosphate hydrolase
• Ribonuclease H superfamily
• DNA/RNA polymerase superfamily
• DNA polymerase theta-like, helix-turn-helix domain
• POLQ-like, helical domain
• DEAD/DEAH box helicase
• Helicase conserved C-terminal domain
• DNA polymerase family A
• Helix-turn-helix domain
• DNA_pol_Q helicase like region helical domain
• Domain of unknown function DUF7898
• Domain of unknown function (DUF7898)

KeywordsUniProt

• Acetylation
• ATP-binding
• Chromosome
• DNA damage
• DNA repair
• DNA-directed DNA polymerase
• Helicase
• Hydrolase
• Multifunctional enzyme
• Nucleotide-binding
• Nucleotidyltransferase
• Nucleus
• Phosphoprotein
• Transferase

InteractionsUniProt · HPA

Protein binding partners of POLQ in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• ORC2
• ORC4
• RAD51
• RHNO1
• RBM25