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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)DescriptionActionsGraphical viewLength
    Nucleotide bindingi115 – 122ATPPROSITE-ProRule annotation8

    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-dependent DNA replication Source: InterPro
    • DNA repair Source: ProtInc
    • 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

    BioCyciZFISH:HS00643-MONOMER.
    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)DescriptionActionsGraphical viewLength
    Mutagenesisi2540 – 2541DE → AA: Abolishes DNA polymerase activity. 2 Publications2

    Organism-specific databases

    DisGeNETi10721.
    MIMi114480. phenotype.
    OpenTargetsiENSG00000051341.
    PharmGKBiPA33506.

    Chemistry databases

    ChEMBLiCHEMBL6025.

    Polymorphism and mutation databases

    BioMutaiPOLQ.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001012791 – 2590DNA polymerase thetaAdd BLAST2590

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei990N6-acetyllysineCombined sources1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    EPDiO75417.
    MaxQBiO75417.
    PaxDbiO75417.
    PeptideAtlasiO75417.
    PRIDEiO75417.

    PTM databases

    iPTMnetiO75417.
    PhosphoSitePlusiO75417.

    Expressioni

    Tissue specificityi

    Highly expressed in testis.1 Publication

    Gene expression databases

    BgeeiENSG00000051341.
    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 interactors.
    DIPiDIP-61500N.
    IntActiO75417. 1 interactor.
    STRINGi9606.ENSP00000264233.

    Structurei

    Secondary structure

    12590
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi71 – 73Combined sources3
    Helixi78 – 85Combined sources8
    Helixi94 – 101Combined sources8
    Beta strandi102 – 104Combined sources3
    Turni105 – 108Combined sources4
    Beta strandi111 – 114Combined sources4
    Helixi121 – 135Combined sources15
    Beta strandi139 – 146Combined sources8
    Helixi147 – 161Combined sources15
    Helixi162 – 164Combined sources3
    Beta strandi168 – 171Combined sources4
    Helixi181 – 183Combined sources3
    Beta strandi185 – 190Combined sources6
    Helixi191 – 203Combined sources13
    Helixi207 – 209Combined sources3
    Beta strandi210 – 216Combined sources7
    Helixi218 – 221Combined sources4
    Helixi229 – 243Combined sources15
    Helixi245 – 247Combined sources3
    Beta strandi260 – 266Combined sources7
    Helixi271 – 277Combined sources7
    Beta strandi281 – 284Combined sources4
    Beta strandi292 – 298Combined sources7
    Beta strandi301 – 303Combined sources3
    Beta strandi309 – 312Combined sources4
    Helixi326 – 335Combined sources10
    Beta strandi340 – 343Combined sources4
    Helixi347 – 366Combined sources20
    Beta strandi380 – 383Combined sources4
    Helixi384 – 395Combined sources12
    Helixi403 – 408Combined sources6
    Helixi409 – 411Combined sources3
    Beta strandi413 – 416Combined sources4
    Helixi422 – 433Combined sources12
    Beta strandi439 – 442Combined sources4
    Helixi444 – 447Combined sources4
    Beta strandi454 – 460Combined sources7
    Beta strandi462 – 464Combined sources3
    Helixi471 – 478Combined sources8
    Turni484 – 486Combined sources3
    Beta strandi490 – 496Combined sources7
    Beta strandi498 – 500Combined sources3
    Helixi501 – 509Combined sources9
    Helixi529 – 540Combined sources12
    Helixi547 – 556Combined sources10
    Turni559 – 562Combined sources4
    Helixi581 – 591Combined sources11
    Beta strandi594 – 598Combined sources5
    Beta strandi607 – 611Combined sources5
    Helixi613 – 620Combined sources8
    Helixi625 – 638Combined sources14
    Beta strandi645 – 647Combined sources3
    Helixi648 – 653Combined sources6
    Helixi666 – 674Combined sources9
    Helixi678 – 687Combined sources10
    Helixi691 – 698Combined sources8
    Turni708 – 711Combined sources4
    Helixi712 – 728Combined sources17
    Turni729 – 731Combined sources3
    Helixi734 – 741Combined sources8
    Helixi745 – 768Combined sources24
    Helixi772 – 778Combined sources7
    Helixi781 – 787Combined sources7
    Helixi791 – 794Combined sources4
    Helixi796 – 798Combined sources3
    Helixi804 – 811Combined sources8
    Turni812 – 814Combined sources3
    Helixi818 – 822Combined sources5
    Helixi826 – 834Combined sources9
    Beta strandi840 – 842Combined sources3
    Beta strandi856 – 858Combined sources3
    Helixi872 – 889Combined sources18

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini102 – 286Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST185
    Domaini321 – 554Helicase C-terminalPROSITE-ProRule annotationAdd BLAST234

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni847 – 894Interaction with RAD511 PublicationAdd BLAST48
    Regioni2142 – 2177Loop 11 PublicationAdd BLAST36
    Regioni2257 – 2322Loop 22 PublicationsAdd BLAST66
    Regioni2491 – 2535Loop 31 PublicationAdd BLAST45

    Coiled coil

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Coiled coili1655 – 1716Sequence analysisAdd BLAST62

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi216 – 219DEAH box4

    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.
    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 differs from that shown. Reason: Frameshift at position 1754.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti66R → I in AAR08421 (PubMed:14576298).Curated1
    Sequence conflicti982T → R in AAR08421 (PubMed:14576298).Curated1
    Sequence conflicti2013L → F in AAD05272 (Ref. 4) Curated1
    Sequence conflicti2513Q → R in AAC33565 (PubMed:10395804).Curated1
    Sequence conflicti2513Q → R in AAR08421 (PubMed:14576298).Curated1
    Sequence conflicti2547A → V in AAC33565 (PubMed:10395804).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_0557071056P → L.Corresponds to variant rs34778629dbSNPEnsembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_0407471 – 828Missing in isoform 2. 1 PublicationAdd BLAST828
    Alternative sequenceiVSP_040748829 – 840VEVIL…AVPFK → MNSFLSFPISLC in isoform 2. 1 PublicationAdd BLAST12

    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
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi115946. 2 interactors.
    DIPiDIP-61500N.
    IntActiO75417. 1 interactor.
    STRINGi9606.ENSP00000264233.

    Chemistry databases

    ChEMBLiCHEMBL6025.

    PTM databases

    iPTMnetiO75417.
    PhosphoSitePlusiO75417.

    Polymorphism and mutation databases

    BioMutaiPOLQ.

    Proteomic databases

    EPDiO75417.
    MaxQBiO75417.
    PaxDbiO75417.
    PeptideAtlasiO75417.
    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.
    DisGeNETi10721.
    GeneCardsiPOLQ.
    H-InvDBHIX0030706.
    HGNCiHGNC:9186. POLQ.
    HPAiHPA048931.
    HPA053359.
    MIMi114480. phenotype.
    604419. gene.
    neXtProtiNX_O75417.
    OpenTargetsiENSG00000051341.
    PharmGKBiPA33506.
    GenAtlasiSearch...

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyciZFISH:HS00643-MONOMER.
    ReactomeiR-HSA-5685939. HDR through MMEJ (alt-NHEJ).

    Miscellaneous databases

    GeneWikiiPOLQ.
    GenomeRNAii10721.
    PROiO75417.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000051341.
    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...

    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: November 2, 2016
    This is version 129 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.