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Protein

DNA polymerase theta

Gene

POLQ

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

DNA polymerase that promotes microhomology-mediated end-joining (MMEJ), an alternative non-homologous end-joining (NHEJ) machinery triggered in response to double-strand breaks in DNA (PubMed:25642963, PubMed:25643323). 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:25642963, PubMed:25643323). POLQ acts as an inhibitor of homology-recombination repair (HR) pathway by limiting RAD51 accumulation at resected ends (PubMed:25642963). POLQ-mediated MMEJ may be required to promote the survival of cells with a compromised HR repair pathway, thereby preventing genomic havoc by resolving unrepaired lesions (By similarity). The polymerase acts by binding directly the 2 ends of resected double-strand breaks, allowing microhomologous sequences in the overhangs to form base pairs. It then extends each strand from the base-paired region using the opposing overhang as a template. Requires partially resected DNA containing 2 to 6 base pairs of microhomology to perform MMEJ (PubMed:25643323). The polymerase activity is highly promiscuous: unlike most polymerases, promotes extension of ssDNA and partial ssDNA (pssDNA) substrates (PubMed:18503084, PubMed:21050863, PubMed:22135286). Also exhibits low-fidelity DNA synthesis, translesion synthesis and lyase activity, and it is implicated in interstrand-cross-link repair, base excision repair and DNA end-joining (PubMed:14576298, PubMed:18503084, PubMed:19188258, PubMed:24648516). 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 (By similarity).By similarity8 Publications

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).2 Publications

Kineticsi

  1. KM=1.095 µM for dATP:T1 Publication
  2. KM=0.622 µM for dATP: abasic site1 Publication
  3. KM=3.08 µM for dGTP: no template1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi115 – 1228ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    • 5'-deoxyribose-5-phosphate lyase activity Source: UniProtKB
    • ATP binding Source: UniProtKB-KW
    • chromatin binding Source: UniProtKB
    • damaged DNA binding Source: ProtInc
    • DNA-directed DNA polymerase activity Source: UniProtKB
    • single-stranded DNA-dependent ATPase activity Source: UniProtKB

    GO - Biological processi

    • base-excision repair Source: UniProtKB
    • cellular response to DNA damage stimulus Source: UniProtKB
    • DNA biosynthetic process Source: GOC
    • DNA-dependent DNA replication Source: InterPro
    • DNA repair Source: Reactome
    • double-strand break repair Source: UniProtKB
    • double-strand break repair via alternative nonhomologous end joining Source: UniProtKB
    • double-strand break repair via homologous recombination Source: Reactome
    • negative regulation of double-strand break repair via homologous recombination Source: UniProtKB
    • protein homooligomerization Source: UniProtKB
    • somatic hypermutation of immunoglobulin genes Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiR-HSA-5685939. HDR through MMEJ (alt-NHEJ).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA polymerase theta2 PublicationsImported (EC:2.7.7.72 Publications)
    Alternative name(s):
    DNA polymerase eta1 Publication
    Gene namesi
    Name:POLQ2 PublicationsImported
    Synonyms:POLH1 Publication
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:9186. POLQ.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Breast cancer (BC)3 Publications
    The gene represented in this entry may be involved in disease pathogenesis.
    Disease descriptionA common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case.
    See also OMIM:114480

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2540 – 25412DE → AA: Abolishes DNA polymerase activity. 2 Publications

    Organism-specific databases

    MIMi114480. phenotype.
    PharmGKBiPA33506.

    Chemistry

    ChEMBLiCHEMBL6025.

    Polymorphism and mutation databases

    BioMutaiPOLQ.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 25902590DNA polymerase thetaPRO_0000101279Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei990 – 9901N6-acetyllysineCombined sources

    Keywords - PTMi

    Acetylation

    Proteomic databases

    EPDiO75417.
    MaxQBiO75417.
    PaxDbiO75417.
    PRIDEiO75417.

    PTM databases

    iPTMnetiO75417.
    PhosphoSiteiO75417.

    Expressioni

    Tissue specificityi

    Highly expressed in testis.1 Publication

    Gene expression databases

    BgeeiO75417.
    CleanExiHS_POLH.
    HS_POLQ.
    ExpressionAtlasiO75417. baseline and differential.
    GenevisibleiO75417. HS.

    Organism-specific databases

    HPAiHPA048931.
    HPA053359.

    Interactioni

    Subunit structurei

    Homomultimer; forms dimers and multimers (PubMed:25643323). Interacts with RAD51 (PubMed:25642963). Interacts with ORC2 and ORC4 (PubMed:24989122).3 Publications

    Protein-protein interaction databases

    BioGridi115946. 2 interactions.
    DIPiDIP-61500N.
    IntActiO75417. 1 interaction.
    STRINGi9606.ENSP00000264233.

    Structurei

    Secondary structure

    1
    2590
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi71 – 733Combined sources
    Helixi78 – 858Combined sources
    Helixi94 – 1018Combined sources
    Beta strandi102 – 1043Combined sources
    Turni105 – 1084Combined sources
    Beta strandi111 – 1144Combined sources
    Helixi121 – 13515Combined sources
    Beta strandi139 – 1468Combined sources
    Helixi147 – 16115Combined sources
    Helixi162 – 1643Combined sources
    Beta strandi168 – 1714Combined sources
    Helixi181 – 1833Combined sources
    Beta strandi185 – 1906Combined sources
    Helixi191 – 20313Combined sources
    Helixi207 – 2093Combined sources
    Beta strandi210 – 2167Combined sources
    Helixi218 – 2214Combined sources
    Helixi229 – 24315Combined sources
    Helixi245 – 2473Combined sources
    Beta strandi260 – 2667Combined sources
    Helixi271 – 2777Combined sources
    Beta strandi281 – 2844Combined sources
    Beta strandi292 – 2987Combined sources
    Beta strandi301 – 3033Combined sources
    Beta strandi309 – 3124Combined sources
    Helixi326 – 33510Combined sources
    Beta strandi340 – 3434Combined sources
    Helixi347 – 36620Combined sources
    Beta strandi380 – 3834Combined sources
    Helixi384 – 39512Combined sources
    Helixi403 – 4086Combined sources
    Helixi409 – 4113Combined sources
    Beta strandi413 – 4164Combined sources
    Helixi422 – 43312Combined sources
    Beta strandi439 – 4424Combined sources
    Helixi444 – 4474Combined sources
    Beta strandi454 – 4607Combined sources
    Beta strandi462 – 4643Combined sources
    Helixi471 – 4788Combined sources
    Turni484 – 4863Combined sources
    Beta strandi490 – 4967Combined sources
    Beta strandi498 – 5003Combined sources
    Helixi501 – 5099Combined sources
    Helixi529 – 54012Combined sources
    Helixi547 – 55610Combined sources
    Turni559 – 5624Combined sources
    Helixi581 – 59111Combined sources
    Beta strandi594 – 5985Combined sources
    Beta strandi607 – 6115Combined sources
    Helixi613 – 6208Combined sources
    Helixi625 – 63814Combined sources
    Beta strandi645 – 6473Combined sources
    Helixi648 – 6536Combined sources
    Helixi666 – 6749Combined sources
    Helixi678 – 68710Combined sources
    Helixi691 – 6988Combined sources
    Turni708 – 7114Combined sources
    Helixi712 – 72817Combined sources
    Turni729 – 7313Combined sources
    Helixi734 – 7418Combined sources
    Helixi745 – 76824Combined sources
    Helixi772 – 7787Combined sources
    Helixi781 – 7877Combined sources
    Helixi791 – 7944Combined sources
    Helixi796 – 7983Combined sources
    Helixi804 – 8118Combined sources
    Turni812 – 8143Combined sources
    Helixi818 – 8225Combined sources
    Helixi826 – 8349Combined sources
    Beta strandi840 – 8423Combined sources
    Beta strandi856 – 8583Combined sources
    Helixi872 – 88918Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4X0PX-ray3.91A/B/C/D1792-2590[»]
    4X0QX-ray3.90A/B1819-2590[»]
    5A9FX-ray3.20A67-894[»]
    5A9JX-ray3.55A/B/C/D1-894[»]
    5AGAX-ray2.90A67-894[»]
    ProteinModelPortaliO75417.
    SMRiO75417. Positions 67-891, 1824-2590.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini102 – 286185Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini321 – 554234Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni847 – 89448Interaction with RAD511 PublicationAdd
    BLAST
    Regioni2142 – 217736Loop 11 PublicationAdd
    BLAST
    Regioni2257 – 232266Loop 22 PublicationsAdd
    BLAST
    Regioni2491 – 253545Loop 31 PublicationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1655 – 171662Sequence analysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi216 – 2194DEAH box

    Domaini

    The loop 2 region is involved in the binding of the 2 ends of resected double-strand breaks and homomultimerization.1 Publication

    Sequence similaritiesi

    Belongs to the DNA polymerase type-A family.Curated
    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiKOG0950. Eukaryota.
    COG0749. LUCA.
    COG1204. LUCA.
    GeneTreeiENSGT00640000091272.
    HOGENOMiHOG000146444.
    HOVERGENiHBG005525.
    InParanoidiO75417.
    KOiK02349.
    OrthoDBiEOG75QR31.
    PhylomeDBiO75417.
    TreeFamiTF105018.

    Family and domain databases

    Gene3Di3.30.420.10. 1 hit.
    3.40.50.300. 3 hits.
    InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
    IPR019760. DNA-dir_DNA_pol_A_CS.
    IPR001098. DNA-dir_DNA_pol_A_palm_dom.
    IPR002298. DNA_polymerase_A.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR012337. RNaseH-like_dom.
    [Graphical view]
    PfamiPF00270. DEAD. 1 hit.
    PF00476. DNA_pol_A. 1 hit.
    PF00271. Helicase_C. 1 hit.
    [Graphical view]
    PRINTSiPR00868. DNAPOLI.
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    SM00482. POLAc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 3 hits.
    SSF53098. SSF53098. 1 hit.
    PROSITEiPS00447. DNA_POLYMERASE_A. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: O75417-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MNLLRRSGKR RRSESGSDSF SGSGGDSSAS PQFLSGSVLS PPPGLGRCLK
    60 70 80 90 100
    AAAAGECKPT VPDYERDKLL LANWGLPKAV LEKYHSFGVK KMFEWQAECL
    110 120 130 140 150
    LLGQVLEGKN LVYSAPTSAG KTLVAELLIL KRVLEMRKKA LFILPFVSVA
    160 170 180 190 200
    KEKKYYLQSL FQEVGIKVDG YMGSTSPSRH FSSLDIAVCT IERANGLINR
    210 220 230 240 250
    LIEENKMDLL GMVVVDELHM LGDSHRGYLL ELLLTKICYI TRKSASCQAD
    260 270 280 290 300
    LASSLSNAVQ IVGMSATLPN LELVASWLNA ELYHTDFRPV PLLESVKVGN
    310 320 330 340 350
    SIYDSSMKLV REFEPMLQVK GDEDHVVSLC YETICDNHSV LLFCPSKKWC
    360 370 380 390 400
    EKLADIIARE FYNLHHQAEG LVKPSECPPV ILEQKELLEV MDQLRRLPSG
    410 420 430 440 450
    LDSVLQKTVP WGVAFHHAGL TFEERDIIEG AFRQGLIRVL AATSTLSSGV
    460 470 480 490 500
    NLPARRVIIR TPIFGGRPLD ILTYKQMVGR AGRKGVDTVG ESILICKNSE
    510 520 530 540 550
    KSKGIALLQG SLKPVRSCLQ RREGEEVTGS MIRAILEIIV GGVASTSQDM
    560 570 580 590 600
    HTYAACTFLA ASMKEGKQGI QRNQESVQLG AIEACVMWLL ENEFIQSTEA
    610 620 630 640 650
    SDGTEGKVYH PTHLGSATLS SSLSPADTLD IFADLQRAMK GFVLENDLHI
    660 670 680 690 700
    LYLVTPMFED WTTIDWYRFF CLWEKLPTSM KRVAELVGVE EGFLARCVKG
    710 720 730 740 750
    KVVARTERQH RQMAIHKRFF TSLVLLDLIS EVPLREINQK YGCNRGQIQS
    760 770 780 790 800
    LQQSAAVYAG MITVFSNRLG WHNMELLLSQ FQKRLTFGIQ RELCDLVRVS
    810 820 830 840 850
    LLNAQRARVL YASGFHTVAD LARANIVEVE VILKNAVPFK SARKAVDEEE
    860 870 880 890 900
    EAVEERRNMR TIWVTGRKGL TEREAAALIV EEARMILQQD LVEMGVQWNP
    910 920 930 940 950
    CALLHSSTCS LTHSESEVKE HTFISQTKSS YKKLTSKNKS NTIFSDSYIK
    960 970 980 990 1000
    HSPNIVQDLN KSREHTSSFN CNFQNGNQEH QTCSIFRARK RASLDINKEK
    1010 1020 1030 1040 1050
    PGASQNEGKT SDKKVVQTFS QKTKKAPLNF NSEKMSRSFR SWKRRKHLKR
    1060 1070 1080 1090 1100
    SRDSSPLKDS GACRIHLQGQ TLSNPSLCED PFTLDEKKTE FRNSGPFAKN
    1110 1120 1130 1140 1150
    VSLSGKEKDN KTSFPLQIKQ NCSWNITLTN DNFVEHIVTG SQSKNVTCQA
    1160 1170 1180 1190 1200
    TSVVSEKGRG VAVEAEKINE VLIQNGSKNQ NVYMKHHDIH PINQYLRKQS
    1210 1220 1230 1240 1250
    HEQTSTITKQ KNIIERQMPC EAVSSYINRD SNVTINCERI KLNTEENKPS
    1260 1270 1280 1290 1300
    HFQALGDDIS RTVIPSEVLP SAGAFSKSEG QHENFLNISR LQEKTGTYTT
    1310 1320 1330 1340 1350
    NKTKNNHVSD LGLVLCDFED SFYLDTQSEK IIQQMATENA KLGAKDTNLA
    1360 1370 1380 1390 1400
    AGIMQKSLVQ QNSMNSFQKE CHIPFPAEQH PLGATKIDHL DLKTVGTMKQ
    1410 1420 1430 1440 1450
    SSDSHGVDIL TPESPIFHSP ILLEENGLFL KKNEVSVTDS QLNSFLQGYQ
    1460 1470 1480 1490 1500
    TQETVKPVIL LIPQKRTPTG VEGECLPVPE TSLNMSDSLL FDSFSDDYLV
    1510 1520 1530 1540 1550
    KEQLPDMQMK EPLPSEVTSN HFSDSLCLQE DLIKKSNVNE NQDTHQQLTC
    1560 1570 1580 1590 1600
    SNDESIIFSE MDSVQMVEAL DNVDIFPVQE KNHTVVSPRA LELSDPVLDE
    1610 1620 1630 1640 1650
    HHQGDQDGGD QDERAEKSKL TGTRQNHSFI WSGASFDLSP GLQRILDKVS
    1660 1670 1680 1690 1700
    SPLENEKLKS MTINFSSLNR KNTELNEEQE VISNLETKQV QGISFSSNNE
    1710 1720 1730 1740 1750
    VKSKIEMLEN NANHDETSSL LPRKESNIVD DNGLIPPTPI PTSASKLTFP
    1760 1770 1780 1790 1800
    GILETPVNPW KTNNVLQPGE SYLFGSPSDI KNHDLSPGSR NGFKDNSPIS
    1810 1820 1830 1840 1850
    DTSFSLQLSQ DGLQLTPASS SSESLSIIDV ASDQNLFQTF IKEWRCKKRF
    1860 1870 1880 1890 1900
    SISLACEKIR SLTSSKTATI GSRFKQASSP QEIPIRDDGF PIKGCDDTLV
    1910 1920 1930 1940 1950
    VGLAVCWGGR DAYYFSLQKE QKHSEISASL VPPSLDPSLT LKDRMWYLQS
    1960 1970 1980 1990 2000
    CLRKESDKEC SVVIYDFIQS YKILLLSCGI SLEQSYEDPK VACWLLDPDS
    2010 2020 2030 2040 2050
    QEPTLHSIVT SFLPHELPLL EGMETSQGIQ SLGLNAGSEH SGRYRASVES
    2060 2070 2080 2090 2100
    ILIFNSMNQL NSLLQKENLQ DVFRKVEMPS QYCLALLELN GIGFSTAECE
    2110 2120 2130 2140 2150
    SQKHIMQAKL DAIETQAYQL AGHSFSFTSS DDIAEVLFLE LKLPPNREMK
    2160 2170 2180 2190 2200
    NQGSKKTLGS TRRGIDNGRK LRLGRQFSTS KDVLNKLKAL HPLPGLILEW
    2210 2220 2230 2240 2250
    RRITNAITKV VFPLQREKCL NPFLGMERIY PVSQSHTATG RITFTEPNIQ
    2260 2270 2280 2290 2300
    NVPRDFEIKM PTLVGESPPS QAVGKGLLPM GRGKYKKGFS VNPRCQAQME
    2310 2320 2330 2340 2350
    ERAADRGMPF SISMRHAFVP FPGGSILAAD YSQLELRILA HLSHDRRLIQ
    2360 2370 2380 2390 2400
    VLNTGADVFR SIAAEWKMIE PESVGDDLRQ QAKQICYGII YGMGAKSLGE
    2410 2420 2430 2440 2450
    QMGIKENDAA CYIDSFKSRY TGINQFMTET VKNCKRDGFV QTILGRRRYL
    2460 2470 2480 2490 2500
    PGIKDNNPYR KAHAERQAIN TIVQGSAADI VKIATVNIQK QLETFHSTFK
    2510 2520 2530 2540 2550
    SHGHREGMLQ SDQTGLSRKR KLQGMFCPIR GGFFILQLHD ELLYEVAEED
    2560 2570 2580 2590
    VVQVAQIVKN EMESAVKLSV KLKVKVKIGA SWGELKDFDV
    Length:2,590
    Mass (Da):289,619
    Last modified:March 8, 2011 - v2
    Checksum:iF5550BED2DAD8013
    GO
    Isoform 2 (identifier: O75417-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-828: Missing.
         829-840: VEVILKNAVPFK → MNSFLSFPISLC

    Show »
    Length:1,762
    Mass (Da):197,541
    Checksum:iACA2EA21B2B69C15
    GO

    Sequence cautioni

    The sequence AAD05272.1 differs from that shown. Reason: Frameshift at position 1754. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti66 – 661R → I in AAR08421 (PubMed:14576298).Curated
    Sequence conflicti982 – 9821T → R in AAR08421 (PubMed:14576298).Curated
    Sequence conflicti2013 – 20131L → F in AAD05272 (Ref. 4) Curated
    Sequence conflicti2513 – 25131Q → R in AAC33565 (PubMed:10395804).Curated
    Sequence conflicti2513 – 25131Q → R in AAR08421 (PubMed:14576298).Curated
    Sequence conflicti2547 – 25471A → V in AAC33565 (PubMed:10395804).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1056 – 10561P → L.
    Corresponds to variant rs34778629 [ dbSNP | Ensembl ].
    VAR_055707

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 828828Missing in isoform 2. 1 PublicationVSP_040747Add
    BLAST
    Alternative sequencei829 – 84012VEVIL…AVPFK → MNSFLSFPISLC in isoform 2. 1 PublicationVSP_040748Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF052573 mRNA. Translation: AAC33565.1.
    AY338826 mRNA. Translation: AAR08421.2.
    AC069239 Genomic DNA. No translation available.
    AC079841 Genomic DNA. No translation available.
    AF043628 mRNA. Translation: AAD05272.1. Frameshift.
    CCDSiCCDS33833.1. [O75417-1]
    RefSeqiNP_955452.3. NM_199420.3. [O75417-1]
    UniGeneiHs.241517.

    Genome annotation databases

    EnsembliENST00000264233; ENSP00000264233; ENSG00000051341. [O75417-1]
    GeneIDi10721.
    KEGGihsa:10721.
    UCSCiuc003eee.5. human. [O75417-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF052573 mRNA. Translation: AAC33565.1.
    AY338826 mRNA. Translation: AAR08421.2.
    AC069239 Genomic DNA. No translation available.
    AC079841 Genomic DNA. No translation available.
    AF043628 mRNA. Translation: AAD05272.1. Frameshift.
    CCDSiCCDS33833.1. [O75417-1]
    RefSeqiNP_955452.3. NM_199420.3. [O75417-1]
    UniGeneiHs.241517.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4X0PX-ray3.91A/B/C/D1792-2590[»]
    4X0QX-ray3.90A/B1819-2590[»]
    5A9FX-ray3.20A67-894[»]
    5A9JX-ray3.55A/B/C/D1-894[»]
    5AGAX-ray2.90A67-894[»]
    ProteinModelPortaliO75417.
    SMRiO75417. Positions 67-891, 1824-2590.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi115946. 2 interactions.
    DIPiDIP-61500N.
    IntActiO75417. 1 interaction.
    STRINGi9606.ENSP00000264233.

    Chemistry

    ChEMBLiCHEMBL6025.

    PTM databases

    iPTMnetiO75417.
    PhosphoSiteiO75417.

    Polymorphism and mutation databases

    BioMutaiPOLQ.

    Proteomic databases

    EPDiO75417.
    MaxQBiO75417.
    PaxDbiO75417.
    PRIDEiO75417.

    Protocols and materials databases

    DNASUi10721.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000264233; ENSP00000264233; ENSG00000051341. [O75417-1]
    GeneIDi10721.
    KEGGihsa:10721.
    UCSCiuc003eee.5. human. [O75417-1]

    Organism-specific databases

    CTDi10721.
    GeneCardsiPOLQ.
    H-InvDBHIX0030706.
    HGNCiHGNC:9186. POLQ.
    HPAiHPA048931.
    HPA053359.
    MIMi114480. phenotype.
    604419. gene.
    neXtProtiNX_O75417.
    PharmGKBiPA33506.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG0950. Eukaryota.
    COG0749. LUCA.
    COG1204. LUCA.
    GeneTreeiENSGT00640000091272.
    HOGENOMiHOG000146444.
    HOVERGENiHBG005525.
    InParanoidiO75417.
    KOiK02349.
    OrthoDBiEOG75QR31.
    PhylomeDBiO75417.
    TreeFamiTF105018.

    Enzyme and pathway databases

    ReactomeiR-HSA-5685939. HDR through MMEJ (alt-NHEJ).

    Miscellaneous databases

    GeneWikiiPOLQ.
    GenomeRNAii10721.
    NextBioi40701.
    PROiO75417.
    SOURCEiSearch...

    Gene expression databases

    BgeeiO75417.
    CleanExiHS_POLH.
    HS_POLQ.
    ExpressionAtlasiO75417. baseline and differential.
    GenevisibleiO75417. HS.

    Family and domain databases

    Gene3Di3.30.420.10. 1 hit.
    3.40.50.300. 3 hits.
    InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
    IPR019760. DNA-dir_DNA_pol_A_CS.
    IPR001098. DNA-dir_DNA_pol_A_palm_dom.
    IPR002298. DNA_polymerase_A.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR012337. RNaseH-like_dom.
    [Graphical view]
    PfamiPF00270. DEAD. 1 hit.
    PF00476. DNA_pol_A. 1 hit.
    PF00271. Helicase_C. 1 hit.
    [Graphical view]
    PRINTSiPR00868. DNAPOLI.
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    SM00482. POLAc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 3 hits.
    SSF53098. SSF53098. 1 hit.
    PROSITEiPS00447. DNA_POLYMERASE_A. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning and chromosomal mapping of the human DNA polymerase theta (POLQ), the eighth human DNA polymerase."
      Sharief F.S., Vojta P.J., Ropp P.A., Copeland W.C.
      Genomics 59:90-96(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Spleen.
    2. "POLQ (Pol theta), a DNA polymerase and DNA-dependent ATPase in human cells."
      Seki M., Marini F., Wood R.D.
      Nucleic Acids Res. 31:6117-6126(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, CATALYTIC ACTIVITY.
    3. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Catalytic activity of Pol eta, a new human DNA polymerase related to the bacterial DNA polymerase I family and Drosophila Mus308."
      Harris P.V., Kaelin C.B., Burtis K.C.
      Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1435-2590.
    5. "Low-fidelity DNA synthesis by human DNA polymerase theta."
      Arana M.E., Seki M., Wood R.D., Rogozin I.B., Kunkel T.A.
      Nucleic Acids Res. 36:3847-3856(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Human DNA polymerase theta possesses 5'-dRP lyase activity and functions in single-nucleotide base excision repair in vitro."
      Prasad R., Longley M.J., Sharief F.S., Hou E.W., Copeland W.C., Wilson S.H.
      Nucleic Acids Res. 37:1868-1877(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF 2540-ASP-GLU-2541.
    7. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-990, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Overexpression of POLQ confers a poor prognosis in early breast cancer patients."
      Higgins G.S., Harris A.L., Prevo R., Helleday T., McKenna W.G., Buffa F.M.
      Oncotarget 1:175-184(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN BC.
    9. Cited for: INVOLVEMENT IN BC.
    10. "Lesion bypass activity of DNA polymerase theta (POLQ) is an intrinsic property of the pol domain and depends on unique sequence inserts."
      Hogg M., Seki M., Wood R.D., Doublie S., Wallace S.S.
      J. Mol. Biol. 405:642-652(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Promiscuous DNA synthesis by human DNA polymerase theta."
      Hogg M., Sauer-Eriksson A.E., Johansson E.
      Nucleic Acids Res. 40:2611-2622(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    12. "A DNA repair variant in POLQ (c.-1060A > G) is associated to hereditary breast cancer patients: a case-control study."
      Brandalize A.P., Schueler-Faccini L., Hoffmann J.S., Caleffi M., Cazaux C., Ashton-Prolla P.
      BMC Cancer 14:850-850(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN BC.
    13. "A role for DNA polymerase theta in promoting replication through oxidative DNA lesion, thymine glycol, in human cells."
      Yoon J.H., Roy Choudhury J., Park J., Prakash S., Prakash L.
      J. Biol. Chem. 289:13177-13185(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF 2540-ASP-GLU-2541.
    14. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ORC2 AND ORC4.
    15. Cited for: FUNCTION, INTERACTION WITH RAD51, SUBCELLULAR LOCATION.
    16. "Mechanism of microhomology-mediated end-joining promoted by human DNA polymerase theta."
      Kent T., Chandramouly G., McDevitt S.M., Ozdemir A.Y., Pomerantz R.T.
      Nat. Struct. Mol. Biol. 22:230-237(2015) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, DOMAIN.

    Entry informationi

    Entry nameiDPOLQ_HUMAN
    AccessioniPrimary (citable) accession number: O75417
    Secondary accession number(s): O95160, Q6VMB5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: March 8, 2011
    Last modified: April 13, 2016
    This is version 124 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Caution

    Was wrongly named DNA polymerase eta (POLH) somne authors (Ref. 4). This protein corresponds to DNA polymerase theta (POLQ) and should not be confused with DNA polymerase eta (POLH) (AC Q9Y253).Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.