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P51530

- DNA2_HUMAN

UniProt

P51530 - DNA2_HUMAN

Protein

DNA replication ATP-dependent helicase/nuclease DNA2

Gene

DNA2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 3 (12 Dec 2006)
      Previous versions | rss
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    Functioni

    Key enzyme involved in DNA replication and DNA repair in nucleus and mitochondrion. Involved in Okazaki fragments processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. Also involved in 5'-end resection of DNA during double-strand break (DSB) repair: recruited by BLM and mediates the cleavage of 5'-ssDNA, while the 3'-ssDNA cleavage is prevented by the presence of RPA. Also involved in DNA replication checkpoint independently of Okazaki fragments processing. Possesses different enzymatic activities, such as single-stranded DNA (ssDNA)-dependent ATPase, 5'-3' helicase and endonuclease activities. While the ATPase and endonuclease activities are well-defined and play a key role in Okazaki fragments processing and DSB repair, the 5'-3' DNA helicase activity is subject to debate. According to various reports, the helicase activity is weak and its function remains largely unclear. Helicase activity may promote the motion of DNA2 on the flap, helping the nuclease function.8 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.1 Publication

    Cofactori

    Binds 1 4Fe-4S cluster.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi136 – 1361Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi393 – 3931Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi396 – 3961Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi402 – 4021Iron-sulfur (4Fe-4S)By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi648 – 6558ATPSequence Analysis

    GO - Molecular functioni

    1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
    2. 5'-3' DNA helicase activity Source: UniProtKB
    3. 5'-flap endonuclease activity Source: UniProtKB
    4. ATPase activity Source: UniProtKB
    5. ATP binding Source: UniProtKB-KW
    6. DNA binding Source: UniProtKB
    7. DNA helicase activity Source: UniProtKB
    8. helicase activity Source: UniProtKB
    9. metal ion binding Source: UniProtKB-KW
    10. nuclease activity Source: UniProtKB
    11. protein binding Source: UniProtKB
    12. single-stranded DNA-dependent ATPase activity Source: UniProtKB
    13. site-specific endodeoxyribonuclease activity, specific for altered base Source: UniProtKB

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. base-excision repair Source: UniProtKB
    3. DNA catabolic process, endonucleolytic Source: GOC
    4. DNA double-strand break processing Source: UniProtKB
    5. DNA duplex unwinding Source: GOC
    6. DNA replication Source: UniProtKB
    7. DNA replication, Okazaki fragment processing Source: UniProtKB
    8. DNA replication, removal of RNA primer Source: UniProtKB
    9. DNA replication checkpoint Source: UniProtKB
    10. DNA strand elongation involved in DNA replication Source: Reactome
    11. mitochondrial DNA repair Source: UniProtKB
    12. mitochondrial DNA replication Source: UniProtKB
    13. mitotic cell cycle Source: Reactome
    14. positive regulation of DNA replication Source: UniProtKB
    15. telomere maintenance Source: Reactome
    16. telomere maintenance via recombination Source: Reactome
    17. telomere maintenance via semi-conservative replication Source: Reactome

    Keywords - Molecular functioni

    Endonuclease, Helicase, Hydrolase, Nuclease

    Keywords - Biological processi

    DNA damage, DNA repair, DNA replication

    Keywords - Ligandi

    4Fe-4S, ATP-binding, DNA-binding, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_70. Removal of the Flap Intermediate.
    REACT_7999. Removal of the Flap Intermediate from the C-strand.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA replication ATP-dependent helicase/nuclease DNA2
    Short name:
    hDNA2
    Alternative name(s):
    DNA replication ATP-dependent helicase-like homolog
    Including the following 2 domains:
    DNA replication nuclease DNA2 (EC:3.1.-.-)
    DNA replication ATP-dependent helicase DNA2 (EC:3.6.4.12)
    Gene namesi
    Name:DNA2
    Synonyms:DNA2L, KIAA0083
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:2939. DNA2.

    Subcellular locationi

    Nucleus. Mitochondrion
    Note: Was initially reported to be exclusively mitochondrial (PubMed:18995831). However, it was later shown to localize both in mitochondrion and nucleus (PubMed:19487465).2 Publications

    GO - Cellular componenti

    1. mitochondrial nucleoid Source: UniProtKB
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Progressive external ophthalmoplegia with mitochondrial DNA deletions, autosomal dominant, 6 (PEOA6) [MIM:615156]: A disorder characterized by muscle weakness, mainly affecting the lower limbs, external ophthalmoplegia, exercise intolerance, and mitochondrial DNA deletions on muscle biopsy. Symptoms may appear in childhood or adulthood and show slow progression.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti198 – 1981R → H in PEOA6; the mutant protein has a complete loss of nuclease activity and severely impaired helicase activity; consistent with a loss of function mutation. 1 Publication
    VAR_069905
    Natural varianti227 – 2271K → E in PEOA6; the mutant protein has significantly reduced nuclease and helicase activity; consistent with a loss of function mutation. 1 Publication
    VAR_069906
    Natural varianti637 – 6371V → I in PEOA6; the mutant protein has decreased nuclease activity (30% of wild-type) and enhanced helicase activity; consistent with a loss of function mutation. 1 Publication
    VAR_069907

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi277 – 2771D → A: Abolishes ability to resect DNA in present of BLM. 3 Publications
    Mutagenesisi654 – 6541K → E: Abolishes ability to unwind DNA, while it does not affect ability to resect DNA. 4 Publications

    Keywords - Diseasei

    Disease mutation, Progressive external ophthalmoplegia

    Organism-specific databases

    MIMi615156. phenotype.
    Orphaneti352470. Mitochondrial DNA deletion syndrome with progressive myopathy.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10601060DNA replication ATP-dependent helicase/nuclease DNA2PRO_0000080712Add
    BLAST

    Post-translational modificationi

    Acetylated by EP300, leading to stimulate the 5'-3' endonuclease, the 5'-3' helicase and DNA-dependent ATPase activities, possibly by increasing DNA substrate affinity.1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP51530.
    PaxDbiP51530.
    PRIDEiP51530.

    PTM databases

    PhosphoSiteiP51530.

    Expressioni

    Gene expression databases

    ArrayExpressiP51530.
    BgeeiP51530.
    CleanExiHS_DNA2.
    GenevestigatoriP51530.

    Organism-specific databases

    HPAiHPA037487.

    Interactioni

    Subunit structurei

    Interacts with BLM and WDHD1.2 Publications

    Protein-protein interaction databases

    BioGridi108103. 8 interactions.
    STRINGi9606.ENSP00000382133.

    Structurei

    3D structure databases

    ProteinModelPortaliP51530.
    SMRiP51530. Positions 448-1043.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni81 – 519439Nuclease activityBy similarityAdd
    BLAST
    Regioni520 – 1060541Helicase activityBy similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the DNA2/NAM7 helicase family.Curated

    Phylogenomic databases

    eggNOGiCOG1112.
    HOGENOMiHOG000168456.
    HOVERGENiHBG081456.
    InParanoidiP51530.
    KOiK10742.
    PhylomeDBiP51530.

    Family and domain databases

    Gene3Di3.40.50.300. 3 hits.
    InterProiIPR014808. DNA_replication_fac_Dna2_N.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF08696. Dna2. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 2 hits.

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P51530-1) [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

    MEQLNELELL MEKSFWEEAE LPAELFQKKV VASFPRTVLS TGMDNRYLVL     50
    AVNTVQNKEG NCEKRLVITA SQSLENKELC ILRNDWCSVP VEPGDIIHLE 100
    GDCTSDTWII DKDFGYLILY PDMLISGTSI ASSIRCMRRA VLSETFRSSD 150
    PATRQMLIGT VLHEVFQKAI NNSFAPEKLQ ELAFQTIQEI RHLKEMYRLN 200
    LSQDEIKQEV EDYLPSFCKW AGDFMHKNTS TDFPQMQLSL PSDNSKDNST 250
    CNIEVVKPMD IEESIWSPRF GLKGKIDVTV GVKIHRGYKT KYKIMPLELK 300
    TGKESNSIEH RSQVVLYTLL SQERRADPEA GLLLYLKTGQ MYPVPANHLD 350
    KRELLKLRNQ MAFSLFHRIS KSATRQKTQL ASLPQIIEEE KTCKYCSQIG 400
    NCALYSRAVE QQMDCSSVPI VMLPKIEEET QHLKQTHLEY FSLWCLMLTL 450
    ESQSKDNKKN HQNIWLMPAS EMEKSGSCIG NLIRMEHVKI VCDGQYLHNF 500
    QCKHGAIPVT NLMAGDRVIV SGEERSLFAL SRGYVKEINM TTVTCLLDRN 550
    LSVLPESTLF RLDQEEKNCD IDTPLGNLSK LMENTFVSKK LRDLIIDFRE 600
    PQFISYLSSV LPHDAKDTVA CILKGLNKPQ RQAMKKVLLS KDYTLIVGMP 650
    GTGKTTTICT LVRILYACGF SVLLTSYTHS AVDNILLKLA KFKIGFLRLG 700
    QIQKVHPAIQ QFTEQEICRS KSIKSLALLE ELYNSQLIVA TTCMGINHPI 750
    FSRKIFDFCI VDEASQISQP ICLGPLFFSR RFVLVGDHQQ LPPLVLNREA 800
    RALGMSESLF KRLEQNKSAV VQLTVQYRMN SKIMSLSNKL TYEGKLECGS 850
    DKVANAVINL RHFKDVKLEL EFYADYSDNP WLMGVFEPNN PVCFLNTDKV 900
    PAPEQVEKGG VSNVTEAKLI VFLTSIFVKA GCSPSDIGII APYRQQLKII 950
    NDLLARSIGM VEVNTVDKYQ GRDKSIVLVS FVRSNKDGTV GELLKDWRRL 1000
    NVAITRAKHK LILLGCVPSL NCYPPLEKLL NHLNSEKLII DLPSREHESL 1050
    CHILGDFQRE 1060
    Length:1,060
    Mass (Da):120,415
    Last modified:December 12, 2006 - v3
    Checksum:i727D4B268FD75C5A
    GO
    Isoform 2 (identifier: P51530-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         664-687: ILYACGFSVLLTSYTHSAVDNILL → FRRFIQLSSNLQSKKFADQSPLNP
         688-1060: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:687
    Mass (Da):78,498
    Checksum:i8B6E028A05B190FE
    GO
    Isoform 3 (identifier: P51530-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         663-900: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:822
    Mass (Da):93,347
    Checksum:iBFFA20A722F4430B
    GO
    Isoform 4 (identifier: P51530-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1040-1060: IDLPSREHESLCHILGDFQRE → SFFFCIWSHLIAL

    Note: No experimental confirmation available.

    Show »
    Length:1,052
    Mass (Da):119,504
    Checksum:i76545663BC48445D
    GO

    Sequence cautioni

    The sequence AAH28188.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAH63664.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAA07647.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAI17237.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI17238.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti986 – 9861K → N in AAH28188. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti198 – 1981R → H in PEOA6; the mutant protein has a complete loss of nuclease activity and severely impaired helicase activity; consistent with a loss of function mutation. 1 Publication
    VAR_069905
    Natural varianti227 – 2271K → E in PEOA6; the mutant protein has significantly reduced nuclease and helicase activity; consistent with a loss of function mutation. 1 Publication
    VAR_069906
    Natural varianti637 – 6371V → I in PEOA6; the mutant protein has decreased nuclease activity (30% of wild-type) and enhanced helicase activity; consistent with a loss of function mutation. 1 Publication
    VAR_069907

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei663 – 900238Missing in isoform 3. 1 PublicationVSP_021869Add
    BLAST
    Alternative sequencei664 – 68724ILYAC…DNILL → FRRFIQLSSNLQSKKFADQS PLNP in isoform 2. 1 PublicationVSP_021870Add
    BLAST
    Alternative sequencei688 – 1060373Missing in isoform 2. 1 PublicationVSP_021871Add
    BLAST
    Alternative sequencei1040 – 106021IDLPS…DFQRE → SFFFCIWSHLIAL in isoform 4. 1 PublicationVSP_044185Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D42046 mRNA. Translation: BAA07647.1. Different initiation.
    AL136233 Genomic DNA. Translation: CAI17238.1. Sequence problems.
    AL136233 Genomic DNA. Translation: CAI17237.1. Sequence problems.
    BC041115 mRNA. Translation: AAH41115.1.
    BC053574 mRNA. Translation: AAH53574.1.
    BC063664 mRNA. Translation: AAH63664.1. Different initiation.
    BC111740 mRNA. Translation: AAI11741.1.
    BC028188 mRNA. Translation: AAH28188.1. Different initiation.
    CCDSiCCDS44415.1. [P51530-1]
    PIRiT50697.
    RefSeqiNP_001073918.2. NM_001080449.2. [P51530-1]
    UniGeneiHs.532446.

    Genome annotation databases

    EnsembliENST00000358410; ENSP00000351185; ENSG00000138346. [P51530-1]
    ENST00000399179; ENSP00000382132; ENSG00000138346. [P51530-3]
    GeneIDi1763.
    KEGGihsa:1763.
    UCSCiuc031pvh.1. human. [P51530-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D42046 mRNA. Translation: BAA07647.1 . Different initiation.
    AL136233 Genomic DNA. Translation: CAI17238.1 . Sequence problems.
    AL136233 Genomic DNA. Translation: CAI17237.1 . Sequence problems.
    BC041115 mRNA. Translation: AAH41115.1 .
    BC053574 mRNA. Translation: AAH53574.1 .
    BC063664 mRNA. Translation: AAH63664.1 . Different initiation.
    BC111740 mRNA. Translation: AAI11741.1 .
    BC028188 mRNA. Translation: AAH28188.1 . Different initiation.
    CCDSi CCDS44415.1. [P51530-1 ]
    PIRi T50697.
    RefSeqi NP_001073918.2. NM_001080449.2. [P51530-1 ]
    UniGenei Hs.532446.

    3D structure databases

    ProteinModelPortali P51530.
    SMRi P51530. Positions 448-1043.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108103. 8 interactions.
    STRINGi 9606.ENSP00000382133.

    PTM databases

    PhosphoSitei P51530.

    Proteomic databases

    MaxQBi P51530.
    PaxDbi P51530.
    PRIDEi P51530.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000358410 ; ENSP00000351185 ; ENSG00000138346 . [P51530-1 ]
    ENST00000399179 ; ENSP00000382132 ; ENSG00000138346 . [P51530-3 ]
    GeneIDi 1763.
    KEGGi hsa:1763.
    UCSCi uc031pvh.1. human. [P51530-1 ]

    Organism-specific databases

    CTDi 1763.
    GeneCardsi GC10M070173.
    HGNCi HGNC:2939. DNA2.
    HPAi HPA037487.
    MIMi 601810. gene.
    615156. phenotype.
    neXtProti NX_P51530.
    Orphaneti 352470. Mitochondrial DNA deletion syndrome with progressive myopathy.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1112.
    HOGENOMi HOG000168456.
    HOVERGENi HBG081456.
    InParanoidi P51530.
    KOi K10742.
    PhylomeDBi P51530.

    Enzyme and pathway databases

    Reactomei REACT_70. Removal of the Flap Intermediate.
    REACT_7999. Removal of the Flap Intermediate from the C-strand.

    Miscellaneous databases

    GeneWikii DNA2L.
    GenomeRNAii 1763.
    NextBioi 7187.
    PROi P51530.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P51530.
    Bgeei P51530.
    CleanExi HS_DNA2.
    Genevestigatori P51530.

    Family and domain databases

    Gene3Di 3.40.50.300. 3 hits.
    InterProi IPR014808. DNA_replication_fac_Dna2_N.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF08696. Dna2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.
      DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Bone marrow.
    2. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 680-1060 (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 567-1060 (ISOFORM 1).
      Tissue: Colon, Duodenum and Lymph.
    4. "Isolation of human Dna2 endonuclease and characterization of its enzymatic properties."
      Kim J.H., Kim H.D., Ryu G.H., Kim D.H., Hurwitz J., Seo Y.S.
      Nucleic Acids Res. 34:1854-1864(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-277 AND LYS-654.
    6. "Human DNA2 is a mitochondrial nuclease/helicase for efficient processing of DNA replication and repair intermediates."
      Zheng L., Zhou M., Guo Z., Lu H., Qian L., Dai H., Qiu J., Yakubovskaya E., Bogenhagen D.F., Demple B., Shen B.
      Mol. Cell 32:325-336(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    7. Cited for: FUNCTION, SUBCELLULAR LOCATION.
    8. "Acetylation of Dna2 endonuclease/helicase and flap endonuclease 1 by p300 promotes DNA stability by creating long flap intermediates."
      Balakrishnan L., Stewart J., Polaczek P., Campbell J.L., Bambara R.A.
      J. Biol. Chem. 285:4398-4404(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION.
    9. "BLM-DNA2-RPA-MRN and EXO1-BLM-RPA-MRN constitute two DNA end resection machineries for human DNA break repair."
      Nimonkar A.V., Genschel J., Kinoshita E., Polaczek P., Campbell J.L., Wyman C., Modrich P., Kowalczykowski S.C.
      Genes Dev. 25:350-362(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BLM, MUTAGENESIS OF ASP-277 AND LYS-654.
    10. "Characterization of the endonuclease and ATP-dependent flap endo/exonuclease of Dna2."
      Fortini B.K., Pokharel S., Polaczek P., Balakrishnan L., Bambara R.A., Campbell J.L.
      J. Biol. Chem. 286:23763-23770(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DNA-BINDING, MUTAGENESIS OF LYS-654.
    11. "Okazaki fragment processing-independent role for human Dna2 enzyme during DNA replication."
      Duxin J.P., Moore H.R., Sidorova J., Karanja K., Honaker Y., Dao B., Piwnica-Worms H., Campbell J.L., Monnat R.J. Jr., Stewart S.A.
      J. Biol. Chem. 287:21980-21991(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DNA-BINDING, INTERACTION WITH WDHD1, MUTAGENESIS OF ASP-277 AND LYS-654.
    12. "Biochemical analyses indicate that binding and cleavage specificities define the ordered processing of human Okazaki fragments by Dna2 and FEN1."
      Gloor J.W., Balakrishnan L., Campbell J.L., Bambara R.A.
      Nucleic Acids Res. 40:6774-6786(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DNA-BINDING.
    13. Cited for: VARIANTS PEOA6 HIS-198; GLU-227 AND ILE-637, CHARACTERIZATION OF VARIANTS PEOA6 HHIS-198; GLU-227 AND ILE-637.

    Entry informationi

    Entry nameiDNA2_HUMAN
    AccessioniPrimary (citable) accession number: P51530
    Secondary accession number(s): Q2NKM1
    , Q5TC49, Q5TC50, Q6P455, Q6PI80, Q7Z6H9, Q8N346
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: December 12, 2006
    Last modified: October 1, 2014
    This is version 116 of the entry and version 3 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, Multifunctional enzyme, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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