Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DNA replication ATP-dependent helicase/nuclease DNA2

Gene

DNA2

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

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

[4Fe-4S] clusterBy similarityNote: 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

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • 5'-3' DNA helicase activity Source: UniProtKB
  • 5'-flap endonuclease activity Source: UniProtKB
  • ATPase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • DNA binding Source: UniProtKB
  • DNA helicase activity Source: UniProtKB
  • helicase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • nuclease activity Source: UniProtKB
  • single-stranded DNA-dependent ATPase activity Source: UniProtKB
  • site-specific endodeoxyribonuclease activity, specific for altered base Source: UniProtKB

GO - Biological processi

  • base-excision repair Source: UniProtKB
  • DNA double-strand break processing Source: UniProtKB
  • DNA duplex unwinding Source: GOC
  • DNA replication Source: UniProtKB
  • DNA replication, Okazaki fragment processing Source: UniProtKB
  • DNA replication, removal of RNA primer Source: UniProtKB
  • DNA replication checkpoint Source: UniProtKB
  • DNA strand elongation involved in DNA replication Source: Reactome
  • mitochondrial DNA repair Source: UniProtKB
  • mitochondrial DNA replication Source: UniProtKB
  • mitotic cell cycle Source: Reactome
  • nucleic acid phosphodiester bond hydrolysis Source: GOC
  • positive regulation of DNA replication Source: UniProtKB
  • telomere maintenance Source: Reactome
  • telomere maintenance via recombination Source: Reactome
  • telomere maintenance via semi-conservative replication Source: Reactome
Complete GO annotation...

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 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:2939. DNA2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial nucleoid Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Nucleus

Pathology & Biotechi

Involvement in diseasei

Progressive external ophthalmoplegia with mitochondrial DNA deletions, autosomal dominant, 6 (PEOA6)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:615156
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
Seckel syndrome 8 (SCKL8)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA rare autosomal recessive disorder characterized by proportionate dwarfism of prenatal onset associated with low birth weight, growth retardation, severe microcephaly with a bird-headed like appearance, and mental retardation.

See also OMIM:615807

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, Dwarfism, Mental retardation, Progressive external ophthalmoplegia

Organism-specific databases

MIMi615156. phenotype.
615807. phenotype.
Orphaneti352470. Mitochondrial DNA deletion syndrome with progressive myopathy.

Polymorphism and mutation databases

BioMutaiDNA2.

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

BgeeiP51530.
CleanExiHS_DNA2.
ExpressionAtlasiP51530. baseline and differential.
GenevisibleiP51530. HS.

Organism-specific databases

HPAiHPA037487.

Interactioni

Subunit structurei

Interacts with BLM and WDHD1.2 Publications

Protein-protein interaction databases

BioGridi108103. 36 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.
GeneTreeiENSGT00780000122010.
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. AlignAdd to basket

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

        10         20         30         40         50
MEQLNELELL MEKSFWEEAE LPAELFQKKV VASFPRTVLS TGMDNRYLVL
60 70 80 90 100
AVNTVQNKEG NCEKRLVITA SQSLENKELC ILRNDWCSVP VEPGDIIHLE
110 120 130 140 150
GDCTSDTWII DKDFGYLILY PDMLISGTSI ASSIRCMRRA VLSETFRSSD
160 170 180 190 200
PATRQMLIGT VLHEVFQKAI NNSFAPEKLQ ELAFQTIQEI RHLKEMYRLN
210 220 230 240 250
LSQDEIKQEV EDYLPSFCKW AGDFMHKNTS TDFPQMQLSL PSDNSKDNST
260 270 280 290 300
CNIEVVKPMD IEESIWSPRF GLKGKIDVTV GVKIHRGYKT KYKIMPLELK
310 320 330 340 350
TGKESNSIEH RSQVVLYTLL SQERRADPEA GLLLYLKTGQ MYPVPANHLD
360 370 380 390 400
KRELLKLRNQ MAFSLFHRIS KSATRQKTQL ASLPQIIEEE KTCKYCSQIG
410 420 430 440 450
NCALYSRAVE QQMDCSSVPI VMLPKIEEET QHLKQTHLEY FSLWCLMLTL
460 470 480 490 500
ESQSKDNKKN HQNIWLMPAS EMEKSGSCIG NLIRMEHVKI VCDGQYLHNF
510 520 530 540 550
QCKHGAIPVT NLMAGDRVIV SGEERSLFAL SRGYVKEINM TTVTCLLDRN
560 570 580 590 600
LSVLPESTLF RLDQEEKNCD IDTPLGNLSK LMENTFVSKK LRDLIIDFRE
610 620 630 640 650
PQFISYLSSV LPHDAKDTVA CILKGLNKPQ RQAMKKVLLS KDYTLIVGMP
660 670 680 690 700
GTGKTTTICT LVRILYACGF SVLLTSYTHS AVDNILLKLA KFKIGFLRLG
710 720 730 740 750
QIQKVHPAIQ QFTEQEICRS KSIKSLALLE ELYNSQLIVA TTCMGINHPI
760 770 780 790 800
FSRKIFDFCI VDEASQISQP ICLGPLFFSR RFVLVGDHQQ LPPLVLNREA
810 820 830 840 850
RALGMSESLF KRLEQNKSAV VQLTVQYRMN SKIMSLSNKL TYEGKLECGS
860 870 880 890 900
DKVANAVINL RHFKDVKLEL EFYADYSDNP WLMGVFEPNN PVCFLNTDKV
910 920 930 940 950
PAPEQVEKGG VSNVTEAKLI VFLTSIFVKA GCSPSDIGII APYRQQLKII
960 970 980 990 1000
NDLLARSIGM VEVNTVDKYQ GRDKSIVLVS FVRSNKDGTV GELLKDWRRL
1010 1020 1030 1040 1050
NVAITRAKHK LILLGCVPSL NCYPPLEKLL NHLNSEKLII DLPSREHESL
1060
CHILGDFQRE
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.Curated
The sequence AAH63664.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAA07647.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAI17237.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI17238.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

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:
EMBLi
GenBanki
DDBJi
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.
CCDSiCCDS44415.2. [P51530-1]
PIRiT50697.
RefSeqiNP_001073918.2. NM_001080449.2. [P51530-1]
UniGeneiHs.532446.

Genome annotation databases

EnsembliENST00000358410; ENSP00000351185; ENSG00000138346. [P51530-1]
ENST00000399179; ENSP00000382132; ENSG00000138346. [P51530-2]
ENST00000399180; ENSP00000382133; ENSG00000138346. [P51530-2]
GeneIDi1763.
KEGGihsa:1763.
UCSCiuc031pvh.1. human. [P51530-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
CCDSiCCDS44415.2. [P51530-1]
PIRiT50697.
RefSeqiNP_001073918.2. NM_001080449.2. [P51530-1]
UniGeneiHs.532446.

3D structure databases

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

Protein-protein interaction databases

BioGridi108103. 36 interactions.
STRINGi9606.ENSP00000382133.

PTM databases

PhosphoSiteiP51530.

Polymorphism and mutation databases

BioMutaiDNA2.

Proteomic databases

MaxQBiP51530.
PaxDbiP51530.
PRIDEiP51530.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000358410; ENSP00000351185; ENSG00000138346. [P51530-1]
ENST00000399179; ENSP00000382132; ENSG00000138346. [P51530-2]
ENST00000399180; ENSP00000382133; ENSG00000138346. [P51530-2]
GeneIDi1763.
KEGGihsa:1763.
UCSCiuc031pvh.1. human. [P51530-1]

Organism-specific databases

CTDi1763.
GeneCardsiGC10M070173.
HGNCiHGNC:2939. DNA2.
HPAiHPA037487.
MIMi601810. gene.
615156. phenotype.
615807. phenotype.
neXtProtiNX_P51530.
Orphaneti352470. Mitochondrial DNA deletion syndrome with progressive myopathy.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1112.
GeneTreeiENSGT00780000122010.
HOGENOMiHOG000168456.
HOVERGENiHBG081456.
InParanoidiP51530.
KOiK10742.
PhylomeDBiP51530.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiDNA2. human.
GeneWikiiDNA2L.
GenomeRNAii1763.
NextBioi7187.
PROiP51530.
SOURCEiSearch...

Gene expression databases

BgeeiP51530.
CleanExiHS_DNA2.
ExpressionAtlasiP51530. baseline and differential.
GenevisibleiP51530. HS.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: INVOLVEMENT IN SCKL8.
  14. 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: June 24, 2015
This is version 124 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

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 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.