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Q07864

- DPOE1_HUMAN

UniProt

Q07864 - DPOE1_HUMAN

Protein

DNA polymerase epsilon catalytic subunit A

Gene

POLE

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 5 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Participates in DNA repair and in chromosomal DNA replication.

    Catalytic activityi

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

    Cofactori

    Binds 1 4Fe-4S cluster.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi2158 – 21581ZincBy similarity
    Metal bindingi2161 – 21611ZincBy similarity
    Metal bindingi2187 – 21871ZincBy similarity
    Metal bindingi2190 – 21901ZincBy similarity
    Metal bindingi2221 – 22211Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi2224 – 22241Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi2236 – 22361Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi2238 – 22381Iron-sulfur (4Fe-4S)By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri2158 – 219033CysA-typeAdd
    BLAST

    GO - Molecular functioni

    1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
    2. chromatin binding Source: UniProtKB
    3. DNA binding Source: UniProtKB
    4. DNA-directed DNA polymerase activity Source: UniProtKB
    5. nucleotide binding Source: InterPro
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. base-excision repair, gap-filling Source: UniProtKB
    2. DNA repair Source: Reactome
    3. DNA replication Source: UniProtKB
    4. DNA replication initiation Source: Reactome
    5. DNA synthesis involved in DNA repair Source: UniProtKB
    6. G1/S transition of mitotic cell cycle Source: UniProtKB
    7. in utero embryonic development Source: Ensembl
    8. mitotic cell cycle Source: Reactome
    9. nucleotide-excision repair Source: Reactome
    10. nucleotide-excision repair, DNA gap filling Source: UniProtKB
    11. telomere maintenance Source: Reactome
    12. telomere maintenance via recombination Source: Reactome
    13. telomere maintenance via semi-conservative replication Source: Reactome
    14. transcription-coupled nucleotide-excision repair Source: Reactome

    Keywords - Molecular functioni

    DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    DNA damage, DNA repair, DNA replication

    Keywords - Ligandi

    4Fe-4S, DNA-binding, Iron, Iron-sulfur, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_1095. Activation of the pre-replicative complex.
    REACT_1993. Repair synthesis for gap-filling by DNA polymerase in TC-NER.
    REACT_2244. DNA replication initiation.
    REACT_378. Repair synthesis of patch ~27-30 bases long by DNA polymerase.
    REACT_7993. Telomere C-strand synthesis initiation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA polymerase epsilon catalytic subunit A (EC:2.7.7.7)
    Alternative name(s):
    DNA polymerase II subunit A
    Gene namesi
    Name:POLE
    Synonyms:POLE1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:9177. POLE.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. epsilon DNA polymerase complex Source: UniProtKB
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProtKB
    5. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Colorectal cancer 12 (CRCS12) [MIM:615083]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. CRCS12 is characterized by a high-penetrance predisposition to the development of colorectal adenomas and carcinomas, with a variable tendency to develop multiple and large tumors. Onset is usually before age 40 years. The histologic features of the tumors are unremarkable.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti424 – 4241L → V in CRCS12; associated with disease susceptibility. 1 Publication
    VAR_069344
    Facial dysmorphism, immunodeficiency, livedo, and short stature (FILS) [MIM:615139]: A syndrome characterized by mild facial dysmorphism, mainly malar hypoplasia, livedo on the skin since birth, and immunodeficiency resulting in recurrent infections. Growth impairment is observed during early childhood and results in variable short stature in adulthood.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi615083. phenotype.
    615139. phenotype.
    Orphaneti352712. Facial dysmorphism - immunodeficiency - livedo - short stature.
    PharmGKBiPA277.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 22862286DNA polymerase epsilon catalytic subunit APRO_0000046455Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1184 – 11841Phosphoserine1 Publication
    Modified residuei1940 – 19401Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ07864.
    PaxDbiQ07864.
    PRIDEiQ07864.

    PTM databases

    PhosphoSiteiQ07864.

    Expressioni

    Gene expression databases

    ArrayExpressiQ07864.
    BgeeiQ07864.
    CleanExiHS_POLE.
    GenevestigatoriQ07864.

    Organism-specific databases

    HPAiHPA058210.

    Interactioni

    Subunit structurei

    Catalytic and central component of the epsilon DNA polymerase complex consisting of four subunits: POLE, POLE2, POLE3 and POLE4. Interacts with RAD17 and TOPBP1.3 Publications

    Protein-protein interaction databases

    BioGridi111422. 17 interactions.
    DIPiDIP-24243N.
    IntActiQ07864. 9 interactions.
    MINTiMINT-145475.
    STRINGi9606.ENSP00000322570.

    Structurei

    3D structure databases

    ProteinModelPortaliQ07864.
    SMRiQ07864. Positions 218-552, 776-1119.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi2221 – 223818CysB motifAdd
    BLAST

    Domaini

    The DNA polymerase activity domain resides in the N-terminal half of the protein, while the C-terminus is necessary for complexing subunits B and C. The C-terminus may also regulate the catalytic activities of the enzyme.
    The CysB motif binds 1 4Fe-4S cluster and is required for the formation of polymerase complexes.By similarity

    Sequence similaritiesi

    Belongs to the DNA polymerase type-B family.Curated
    Contains 1 CysA-type zinc finger.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri2158 – 219033CysA-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0417.
    HOVERGENiHBG051398.
    InParanoidiQ07864.
    KOiK02324.
    OMAiYETHSDN.
    PhylomeDBiQ07864.
    TreeFamiTF105017.

    Family and domain databases

    Gene3Di3.30.420.10. 1 hit.
    InterProiIPR006172. DNA-dir_DNA_pol_B.
    IPR006133. DNA-dir_DNA_pol_B_exonuc.
    IPR006134. DNA-dir_DNA_pol_B_multi_dom.
    IPR013697. DNA_pol_e_suA_C.
    IPR012337. RNaseH-like_dom.
    [Graphical view]
    PfamiPF00136. DNA_pol_B. 1 hit.
    PF03104. DNA_pol_B_exo1. 1 hit.
    PF08490. DUF1744. 1 hit.
    [Graphical view]
    SMARTiSM00486. POLBc. 1 hit.
    [Graphical view]
    SUPFAMiSSF53098. SSF53098. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Q07864-1 [UniParc]FASTAAdd to Basket

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    MSLRSGGRRR ADPGADGEAS RDDGATSSVS ALKRLERSQW TDKMDLRFGF     50
    ERLKEPGEKT GWLINMHPTE ILDEDKRLGS AVDYYFIQDD GSRFKVALPY 100
    KPYFYIATRK GCEREVSSFL SKKFQGKIAK VETVPKEDLD LPNHLVGLKR 150
    NYIRLSFHTV EDLVKVRKEI SPAVKKNREQ DHASDAYTAL LSSVLQRGGV 200
    ITDEEETSKK IADQLDNIVD MREYDVPYHI RLSIDLKIHV AHWYNVRYRG 250
    NAFPVEITRR DDLVERPDPV VLAFDIETTK LPLKFPDAET DQIMMISYMI 300
    DGQGYLITNR EIVSEDIEDF EFTPKPEYEG PFCVFNEPDE AHLIQRWFEH 350
    VQETKPTIMV TYNGDFFDWP FVEARAAVHG LSMQQEIGFQ KDSQGEYKAP 400
    QCIHMDCLRW VKRDSYLPVG SHNLKAAAKA KLGYDPVELD PEDMCRMATE 450
    QPQTLATYSV SDAVATYYLY MKYVHPFIFA LCTIIPMEPD EVLRKGSGTL 500
    CEALLMVQAF HANIIFPNKQ EQEFNKLTDD GHVLDSETYV GGHVEALESG 550
    VFRSDIPCRF RMNPAAFDFL LQRVEKTLRH ALEEEEKVPV EQVTNFEEVC 600
    DEIKSKLASL KDVPSRIECP LIYHLDVGAM YPNIILTNRL QPSAMVDEAT 650
    CAACDFNKPG ANCQRKMAWQ WRGEFMPASR SEYHRIQHQL ESEKFPPLFP 700
    EGPARAFHEL SREEQAKYEK RRLADYCRKA YKKIHITKVE ERLTTICQRE 750
    NSFYVDTVRA FRDRRYEFKG LHKVWKKKLS AAVEVGDAAE VKRCKNMEVL 800
    YDSLQLAHKC ILNSFYGYVM RKGARWYSME MAGIVCFTGA NIITQARELI 850
    EQIGRPLELD TDGIWCVLPN SFPENFVFKT TNVKKPKVTI SYPGAMLNIM 900
    VKEGFTNDQY QELAEPSSLT YVTRSENSIF FEVDGPYLAM ILPASKEEGK 950
    KLKKRYAVFN EDGSLAELKG FEVKRRGELQ LIKIFQSSVF EAFLKGSTLE 1000
    EVYGSVAKVA DYWLDVLYSK AANMPDSELF ELISENRSMS RKLEDYGEQK 1050
    STSISTAKRL AEFLGDQMVK DAGLSCRYII SRKPEGSPVT ERAIPLAIFQ 1100
    AEPTVRKHFL RKWLKSSSLQ DFDIRAILDW DYYIERLGSA IQKIITIPAA 1150
    LQQVKNPVPR VKHPDWLHKK LLEKNDVYKQ KKISELFTLE GRRQVTMAEA 1200
    SEDSPRPSAP DMEDFGLVKL PHPAAPVTVK RKRVLWESQE ESQDLTPTVP 1250
    WQEILGQPPA LGTSQEEWLV WLRFHKKKWQ LQARQRLARR KRQRLESAEG 1300
    VLRPGAIRDG PATGLGSFLR RTARSILDLP WQIVQISETS QAGLFRLWAL 1350
    VGSDLHCIRL SIPRVFYVNQ RVAKAEEGAS YRKVNRVLPR SNMVYNLYEY 1400
    SVPEDMYQEH INEINAELSA PDIEGVYETQ VPLLFRALVH LGCVCVVNKQ 1450
    LVRHLSGWEA ETFALEHLEM RSLAQFSYLE PGSIRHIYLY HHAQAHKALF 1500
    GIFIPSQRRA SVFVLDTVRS NQMPSLGALY SAEHGLLLEK VGPELLPPPK 1550
    HTFEVRAETD LKTICRAIQR FLLAYKEERR GPTLIAVQSS WELKRLASEI 1600
    PVLEEFPLVP ICVADKINYG VLDWQRHGAR RMIRHYLNLD TCLSQAFEMS 1650
    RYFHIPIGNL PEDISTFGSD LFFARHLQRH NHLLWLSPTA RPDLGGKEAD 1700
    DNCLVMEFDD QATVEINSSG CYSTVCVELD LQNLAVNTIL QSHHVNDMEG 1750
    ADSMGISFDV IQQASLEDMI TGGQAASAPA SYDETALCSN TFRILKSMVV 1800
    GWVKEITQYH NIYADNQVMH FYRWLRSPSS LLHDPALHRT LHNMMKKLFL 1850
    QLIAEFKRLG SSVIYANFNR IILCTKKRRV EDAIAYVEYI TSSIHSKETF 1900
    HSLTISFSRC WEFLLWMDPS NYGGIKGKVS SRIHCGLQDS QKAGGAEDEQ 1950
    ENEDDEEERD GEEEEEAEES NVEDLLENNW NILQFLPQAA SCQNYFLMIV 2000
    SAYIVAVYHC MKDGLRRSAP GSTPVRRRGA SQLSQEAEGA VGALPGMITF 2050
    SQDYVANELT QSFFTITQKI QKKVTGSRNS TELSEMFPVL PGSHLLLNNP 2100
    ALEFIKYVCK VLSLDTNITN QVNKLNRDLL RLVDVGEFSE EAQFRDPCRS 2150
    YVLPEVICRS CNFCRDLDLC KDSSFSEDGA VLPQWLCSNC QAPYDSSAIE 2200
    MTLVEVLQKK LMAFTLQDLV CLKCRGVKET SMPVYCSCAG DFALTIHTQV 2250
    FMEQIGIFRN IAQHYGMSYL LETLEWLLQK NPQLGH 2286
    Length:2,286
    Mass (Da):261,518
    Last modified:October 17, 2006 - v5
    Checksum:iA213AE1EA8437DEC
    GO

    Sequence cautioni

    The sequence AAA15448.1 differs from that shown. Reason:
    The sequence AAA15448.1 differs from that shown. Reason: Frameshift at positions 443 and 448.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2237 – 22371S → T in AAA15448. (PubMed:8486689)Curated
    Sequence conflicti2237 – 22371S → T in AAC19148. (PubMed:8486689)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti31 – 311A → S.
    Corresponds to variant rs34047482 [ dbSNP | Ensembl ].
    VAR_061138
    Natural varianti99 – 991P → L.
    Corresponds to variant rs5744739 [ dbSNP | Ensembl ].
    VAR_028429
    Natural varianti189 – 1891A → T Found in a colorectal sample; somatic mutation. 1 Publication
    VAR_069339
    Natural varianti231 – 2311R → H Found in a colorectal sample; somatic mutation. 1 Publication
    VAR_069340
    Natural varianti252 – 2521A → V.
    Corresponds to variant rs5744751 [ dbSNP | Ensembl ].
    VAR_020276
    Natural varianti260 – 2601R → Q.
    Corresponds to variant rs5744752 [ dbSNP | Ensembl ].
    VAR_028430
    Natural varianti286 – 2861P → H Found in a colorectal sample; somatic mutation. 1 Publication
    VAR_069341
    Natural varianti336 – 3361N → S.
    Corresponds to variant rs5744760 [ dbSNP | Ensembl ].
    VAR_020277
    Natural varianti367 – 3671F → S Found in a colorectal sample; somatic mutation. 1 Publication
    VAR_069342
    Natural varianti411 – 4111V → L Found in a colorectal sample; somatic mutation. 1 Publication
    VAR_069343
    Natural varianti424 – 4241L → V in CRCS12; associated with disease susceptibility. 1 Publication
    VAR_069344
    Natural varianti436 – 4361P → R Found in a colorectal sample; somatic mutation. 1 Publication
    VAR_069345
    Natural varianti459 – 4591S → F Found in a colorectal sample; somatic mutation. 1 Publication
    VAR_069346
    Natural varianti695 – 6951F → I.
    Corresponds to variant rs5744799 [ dbSNP | Ensembl ].
    VAR_020278
    Natural varianti762 – 7621R → W Found in a colorectal sample; somatic mutation. 1 Publication
    VAR_069347
    Natural varianti777 – 7771K → N Found in a colorectal sample; somatic mutation. 1 Publication
    VAR_069348
    Natural varianti1008 – 10081K → N Found in a colorectal sample; somatic mutation. 1 Publication
    VAR_069349
    Natural varianti1255 – 12551L → V Found in a colorectal sample; somatic mutation. 1 Publication
    VAR_069350
    Natural varianti1368 – 13681V → M Found in a colorectal sample; somatic mutation. 1 Publication
    VAR_069351
    Natural varianti1382 – 13821R → C.
    Corresponds to variant rs5744904 [ dbSNP | Ensembl ].
    VAR_028431
    Natural varianti1395 – 13951Y → C.
    Corresponds to variant rs5744933 [ dbSNP | Ensembl ].
    VAR_020279
    Natural varianti1396 – 13961N → S.
    Corresponds to variant rs5744934 [ dbSNP | Ensembl ].
    VAR_020280
    Natural varianti1399 – 13991E → Q.
    Corresponds to variant rs5744935 [ dbSNP | Ensembl ].
    VAR_020281
    Natural varianti1421 – 14211P → S.1 Publication
    VAR_069352
    Natural varianti1577 – 15771E → A.
    Corresponds to variant rs5744948 [ dbSNP | Ensembl ].
    VAR_028432
    Natural varianti1712 – 17121A → V.
    Corresponds to variant rs5744950 [ dbSNP | Ensembl ].
    VAR_028433
    Natural varianti1752 – 17521D → N Found in a colorectal sample; somatic mutation. 1 Publication
    VAR_069353
    Natural varianti1857 – 18571K → R.
    Corresponds to variant rs5744971 [ dbSNP | Ensembl ].
    VAR_028434
    Natural varianti1935 – 19351C → Y.
    Corresponds to variant rs5744991 [ dbSNP | Ensembl ].
    VAR_028435
    Natural varianti2013 – 20131D → N.1 Publication
    VAR_069354
    Natural varianti2040 – 20401A → V.
    Corresponds to variant rs5745021 [ dbSNP | Ensembl ].
    VAR_020282
    Natural varianti2056 – 20561A → T Found in a colorectal sample; somatic mutation. 1 Publication
    VAR_069355
    Natural varianti2140 – 21401E → K.
    Corresponds to variant rs5745066 [ dbSNP | Ensembl ].
    VAR_048881
    Natural varianti2159 – 21591R → C.
    Corresponds to variant rs5745067 [ dbSNP | Ensembl ].
    VAR_048882
    Natural varianti2165 – 21651R → H.
    Corresponds to variant rs5745068 [ dbSNP | Ensembl ].
    VAR_020283
    Natural varianti2213 – 22131A → V Found in a colorectal sample; somatic mutation. 1 Publication
    VAR_069356

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S60080 mRNA. Translation: AAA15448.1. Sequence problems.
    L09561 mRNA. Translation: AAC19148.1.
    U49356 mRNA. Translation: AAA90924.1.
    AY273166 Genomic DNA. Translation: AAP12650.1.
    CCDSiCCDS9278.1.
    PIRiG02434.
    RefSeqiNP_006222.2. NM_006231.3.
    UniGeneiHs.524871.

    Genome annotation databases

    EnsembliENST00000320574; ENSP00000322570; ENSG00000177084.
    GeneIDi5426.
    KEGGihsa:5426.
    UCSCiuc001uks.1. human.

    Polymorphism databases

    DMDMi116241339.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S60080 mRNA. Translation: AAA15448.1 . Sequence problems.
    L09561 mRNA. Translation: AAC19148.1 .
    U49356 mRNA. Translation: AAA90924.1 .
    AY273166 Genomic DNA. Translation: AAP12650.1 .
    CCDSi CCDS9278.1.
    PIRi G02434.
    RefSeqi NP_006222.2. NM_006231.3.
    UniGenei Hs.524871.

    3D structure databases

    ProteinModelPortali Q07864.
    SMRi Q07864. Positions 218-552, 776-1119.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111422. 17 interactions.
    DIPi DIP-24243N.
    IntActi Q07864. 9 interactions.
    MINTi MINT-145475.
    STRINGi 9606.ENSP00000322570.

    Chemistry

    ChEMBLi CHEMBL2363042.

    PTM databases

    PhosphoSitei Q07864.

    Polymorphism databases

    DMDMi 116241339.

    Proteomic databases

    MaxQBi Q07864.
    PaxDbi Q07864.
    PRIDEi Q07864.

    Protocols and materials databases

    DNASUi 5426.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000320574 ; ENSP00000322570 ; ENSG00000177084 .
    GeneIDi 5426.
    KEGGi hsa:5426.
    UCSCi uc001uks.1. human.

    Organism-specific databases

    CTDi 5426.
    GeneCardsi GC12M133200.
    H-InvDB HIX0022184.
    HGNCi HGNC:9177. POLE.
    HPAi HPA058210.
    MIMi 174762. gene.
    615083. phenotype.
    615139. phenotype.
    neXtProti NX_Q07864.
    Orphaneti 352712. Facial dysmorphism - immunodeficiency - livedo - short stature.
    PharmGKBi PA277.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0417.
    HOVERGENi HBG051398.
    InParanoidi Q07864.
    KOi K02324.
    OMAi YETHSDN.
    PhylomeDBi Q07864.
    TreeFami TF105017.

    Enzyme and pathway databases

    Reactomei REACT_1095. Activation of the pre-replicative complex.
    REACT_1993. Repair synthesis for gap-filling by DNA polymerase in TC-NER.
    REACT_2244. DNA replication initiation.
    REACT_378. Repair synthesis of patch ~27-30 bases long by DNA polymerase.
    REACT_7993. Telomere C-strand synthesis initiation.

    Miscellaneous databases

    ChiTaRSi POLE. human.
    GeneWikii POLE_(enzyme).
    GenomeRNAii 5426.
    NextBioi 20993.
    PROi Q07864.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q07864.
    Bgeei Q07864.
    CleanExi HS_POLE.
    Genevestigatori Q07864.

    Family and domain databases

    Gene3Di 3.30.420.10. 1 hit.
    InterProi IPR006172. DNA-dir_DNA_pol_B.
    IPR006133. DNA-dir_DNA_pol_B_exonuc.
    IPR006134. DNA-dir_DNA_pol_B_multi_dom.
    IPR013697. DNA_pol_e_suA_C.
    IPR012337. RNaseH-like_dom.
    [Graphical view ]
    Pfami PF00136. DNA_pol_B. 1 hit.
    PF03104. DNA_pol_B_exo1. 1 hit.
    PF08490. DUF1744. 1 hit.
    [Graphical view ]
    SMARTi SM00486. POLBc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53098. SSF53098. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of the cDNA for the catalytic subunit of human DNA polymerase epsilon."
      Kesti T., Frantti H., Syvaeoja J.E.
      J. Biol. Chem. 268:10238-10245(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 48-51; 876-886 AND 1338-1344.
      Tissue: T-cell.
    2. Syvaeoja J.E.
      Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. Asahara H., Goldsmith J.S., Lee E., Linn S.
      Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. NIEHS SNPs program
      Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-2286.
    5. "Identification and cloning of two histone fold motif-containing subunits of HeLa DNA polymerase epsilon."
      Li Y., Pursell Z.F., Linn S.
      J. Biol. Chem. 275:23247-23252(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN EPSILON DNA POLYMERASE COMPLEX.
      Tissue: Cervix carcinoma.
    6. "BRCT domain-containing protein TopBP1 functions in DNA replication and damage response."
      Maekiniemi M., Hillukkala T., Tuusa J., Reini K., Vaara M., Huang D., Pospiech H., Majuri I., Westerling T., Maekelae T.P., Syvaeoja J.E.
      J. Biol. Chem. 276:30399-30406(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TOPBP1.
    7. "The human checkpoint Rad protein Rad17 is chromatin-associated throughout the cell cycle, localizes to DNA replication sites, and interacts with DNA polymerase epsilon."
      Post S.M., Tomkinson A.E., Lee E.Y.-H.P.
      Nucleic Acids Res. 31:5568-5575(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAD17.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1940, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1184, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Polymerase epsilon1 mutation in a human syndrome with facial dysmorphism, immunodeficiency, livedo, and short stature (FILS syndrome)."
      Pachlopnik Schmid J., Lemoine R., Nehme N., Cormier-Daire V., Revy P., Debeurme F., Debre M., Nitschke P., Bole-Feysot C., Legeai-Mallet L., Lim A., de Villartay J.P., Picard C., Durandy A., Fischer A., de Saint Basile G.
      J. Exp. Med. 209:2323-2330(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN FILS.
    12. Cited for: VARIANT CRCS12 VAL-424, VARIANTS THR-189; HIS-231; HIS-286; SER-367; LEU-411; ARG-436; PHE-459; TRP-762; ASN-777; ASN-1008; VAL-1255; MET-1368; SER-1421; ASN-1752; ASN-2013; THR-2056 AND VAL-2213.

    Entry informationi

    Entry nameiDPOE1_HUMAN
    AccessioniPrimary (citable) accession number: Q07864
    Secondary accession number(s): Q13533, Q86VH9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 147 of the entry and version 5 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

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3