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P51530 (DNA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. DNA replication nuclease DNA2
    EC=3.1.-.-
  2. DNA replication ATP-dependent helicase DNA2
    EC=3.6.4.12
Gene names
Name:DNA2
Synonyms:DNA2L, KIAA0083
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1060 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.5 Ref.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12

Catalytic activity

ATP + H2O = ADP + phosphate. Ref.5

Cofactor

Binds 1 4Fe-4S cluster By similarity.

Subunit structure

Interacts with BLM and WDHD1. Ref.9 Ref.11

Subcellular location

Nucleus. Mitochondrion. Note: Was initially reported to be exclusively mitochondrial (Ref.6). However, it was later shown to localize both in mitochondrion and nucleus (Ref.7). Ref.6 Ref.7

Post-translational modification

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. Ref.8

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13

Sequence similarities

Belongs to the DNA2/NAM7 helicase family.

Sequence caution

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.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
DNA replication
   Cellular componentMitochondrion
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Progressive external ophthalmoplegia
   Ligand4Fe-4S
ATP-binding
DNA-binding
Iron
Iron-sulfur
Metal-binding
Nucleotide-binding
   Molecular functionEndonuclease
Helicase
Hydrolase
Nuclease
   PTMAcetylation
   Technical termComplete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.4Ref.5. Source: GOC

DNA catabolic process, endonucleolytic

Inferred from direct assay Ref.4Ref.5Ref.6Ref.8Ref.12. Source: GOC

DNA double-strand break processing

Inferred from direct assay Ref.9. Source: UniProtKB

DNA duplex unwinding

Inferred from direct assay Ref.5Ref.8. Source: GOC

DNA replication

Inferred from mutant phenotype Ref.11. Source: UniProtKB

DNA replication checkpoint

Inferred from mutant phenotype Ref.11. Source: UniProtKB

DNA replication, Okazaki fragment processing

Inferred from direct assay Ref.12. Source: UniProtKB

DNA replication, removal of RNA primer

Inferred from direct assay Ref.6. Source: UniProtKB

DNA strand elongation involved in DNA replication

Traceable author statement. Source: Reactome

base-excision repair

Inferred from direct assay Ref.6. Source: UniProtKB

mitochondrial DNA repair

Inferred from direct assay Ref.7. Source: UniProtKB

mitochondrial DNA replication

Inferred from direct assay Ref.6Ref.7. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

positive regulation of DNA replication

Inferred from direct assay Ref.6. Source: UniProtKB

telomere maintenance

Traceable author statement. Source: Reactome

telomere maintenance via recombination

Traceable author statement. Source: Reactome

telomere maintenance via semi-conservative replication

Traceable author statement. Source: Reactome

   Cellular_componentmitochondrial nucleoid

Inferred from direct assay Ref.7. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

5'-3' DNA helicase activity

Inferred from direct assay Ref.8. Source: UniProtKB

5'-flap endonuclease activity

Inferred from direct assay Ref.4Ref.5Ref.6Ref.8Ref.12. Source: UniProtKB

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity

Traceable author statement Ref.6. Source: UniProtKB

DNA binding

Inferred from direct assay Ref.8Ref.12. Source: UniProtKB

DNA helicase activity

Inferred from direct assay Ref.5. Source: UniProtKB

helicase activity

Traceable author statement Ref.6. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nuclease activity

Inferred from direct assay Ref.9. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.8Ref.9. Source: UniProtKB

single-stranded DNA-dependent ATPase activity

Inferred from direct assay Ref.4Ref.5. Source: UniProtKB

site-specific endodeoxyribonuclease activity, specific for altered base

Inferred from direct assay Ref.6. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P51530-1)

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.
Isoform 2 (identifier: P51530-2)

The sequence of this isoform differs from the canonical sequence as follows:
     664-687: ILYACGFSVLLTSYTHSAVDNILL → FRRFIQLSSNLQSKKFADQSPLNP
     688-1060: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P51530-3)

The sequence of this isoform differs from the canonical sequence as follows:
     663-900: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: P51530-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1040-1060: IDLPSREHESLCHILGDFQRE → SFFFCIWSHLIAL
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10601060DNA replication ATP-dependent helicase/nuclease DNA2
PRO_0000080712

Regions

Nucleotide binding648 – 6558ATP Potential
Region81 – 519439Nuclease activity By similarity
Region520 – 1060541Helicase activity By similarity

Sites

Metal binding1361Iron-sulfur (4Fe-4S) By similarity
Metal binding3931Iron-sulfur (4Fe-4S) By similarity
Metal binding3961Iron-sulfur (4Fe-4S) By similarity
Metal binding4021Iron-sulfur (4Fe-4S) By similarity

Natural variations

Alternative sequence663 – 900238Missing in isoform 3.
VSP_021869
Alternative sequence664 – 68724ILYAC…DNILL → FRRFIQLSSNLQSKKFADQS PLNP in isoform 2.
VSP_021870
Alternative sequence688 – 1060373Missing in isoform 2.
VSP_021871
Alternative sequence1040 – 106021IDLPS…DFQRE → SFFFCIWSHLIAL in isoform 4.
VSP_044185
Natural variant1981R → 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. Ref.13
VAR_069905
Natural variant2271K → E in PEOA6; the mutant protein has significantly reduced nuclease and helicase activity; consistent with a loss of function mutation. Ref.13
VAR_069906
Natural variant6371V → 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. Ref.13
VAR_069907

Experimental info

Mutagenesis2771D → A: Abolishes ability to resect DNA in present of BLM. Ref.5 Ref.9 Ref.11
Mutagenesis6541K → E: Abolishes ability to unwind DNA, while it does not affect ability to resect DNA. Ref.5 Ref.9 Ref.10 Ref.11
Sequence conflict9861K → N in AAH28188. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 12, 2006. Version 3.
Checksum: 727D4B268FD75C5A

FASTA1,060120,415
        10         20         30         40         50         60 
MEQLNELELL MEKSFWEEAE LPAELFQKKV VASFPRTVLS TGMDNRYLVL AVNTVQNKEG 

        70         80         90        100        110        120 
NCEKRLVITA SQSLENKELC ILRNDWCSVP VEPGDIIHLE GDCTSDTWII DKDFGYLILY 

       130        140        150        160        170        180 
PDMLISGTSI ASSIRCMRRA VLSETFRSSD PATRQMLIGT VLHEVFQKAI NNSFAPEKLQ 

       190        200        210        220        230        240 
ELAFQTIQEI RHLKEMYRLN LSQDEIKQEV EDYLPSFCKW AGDFMHKNTS TDFPQMQLSL 

       250        260        270        280        290        300 
PSDNSKDNST CNIEVVKPMD IEESIWSPRF GLKGKIDVTV GVKIHRGYKT KYKIMPLELK 

       310        320        330        340        350        360 
TGKESNSIEH RSQVVLYTLL SQERRADPEA GLLLYLKTGQ MYPVPANHLD KRELLKLRNQ 

       370        380        390        400        410        420 
MAFSLFHRIS KSATRQKTQL ASLPQIIEEE KTCKYCSQIG NCALYSRAVE QQMDCSSVPI 

       430        440        450        460        470        480 
VMLPKIEEET QHLKQTHLEY FSLWCLMLTL ESQSKDNKKN HQNIWLMPAS EMEKSGSCIG 

       490        500        510        520        530        540 
NLIRMEHVKI VCDGQYLHNF QCKHGAIPVT NLMAGDRVIV SGEERSLFAL SRGYVKEINM 

       550        560        570        580        590        600 
TTVTCLLDRN LSVLPESTLF RLDQEEKNCD IDTPLGNLSK LMENTFVSKK LRDLIIDFRE 

       610        620        630        640        650        660 
PQFISYLSSV LPHDAKDTVA CILKGLNKPQ RQAMKKVLLS KDYTLIVGMP GTGKTTTICT 

       670        680        690        700        710        720 
LVRILYACGF SVLLTSYTHS AVDNILLKLA KFKIGFLRLG QIQKVHPAIQ QFTEQEICRS 

       730        740        750        760        770        780 
KSIKSLALLE ELYNSQLIVA TTCMGINHPI FSRKIFDFCI VDEASQISQP ICLGPLFFSR 

       790        800        810        820        830        840 
RFVLVGDHQQ LPPLVLNREA RALGMSESLF KRLEQNKSAV VQLTVQYRMN SKIMSLSNKL 

       850        860        870        880        890        900 
TYEGKLECGS DKVANAVINL RHFKDVKLEL EFYADYSDNP WLMGVFEPNN PVCFLNTDKV 

       910        920        930        940        950        960 
PAPEQVEKGG VSNVTEAKLI VFLTSIFVKA GCSPSDIGII APYRQQLKII NDLLARSIGM 

       970        980        990       1000       1010       1020 
VEVNTVDKYQ GRDKSIVLVS FVRSNKDGTV GELLKDWRRL NVAITRAKHK LILLGCVPSL 

      1030       1040       1050       1060 
NCYPPLEKLL NHLNSEKLII DLPSREHESL CHILGDFQRE 

« Hide

Isoform 2 [UniParc].

Checksum: 8B6E028A05B190FE
Show »

FASTA68778,498
Isoform 3 [UniParc].

Checksum: BFFA20A722F4430B
Show »

FASTA82293,347
Isoform 4 [UniParc].

Checksum: 76545663BC48445D
Show »

FASTA1,052119,504

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Biochemical analysis of human Dna2."
Masuda-Sasa T., Imamura O., Campbell J.L.
Nucleic Acids Res. 34:1865-1875(2006) [PubMed] [Europe PMC] [Abstract]
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]"Human Dna2 is a nuclear and mitochondrial DNA maintenance protein."
Duxin J.P., Dao B., Martinsson P., Rajala N., Guittat L., Campbell J.L., Spelbrink J.N., Stewart S.A.
Mol. Cell. Biol. 29:4274-4282(2009) [PubMed] [Europe PMC] [Abstract]
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]"Mutations in DNA2 link progressive myopathy to mitochondrial DNA instability."
Ronchi D., Di Fonzo A., Lin W., Bordoni A., Liu C., Fassone E., Pagliarani S., Rizzuti M., Zheng L., Filosto M., Ferro M.T., Ranieri M., Magri F., Peverelli L., Li H., Yuan Y.C., Corti S., Sciacco M. expand/collapse author list , Moggio M., Bresolin N., Shen B., Comi G.P.
Am. J. Hum. Genet. 92:293-300(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PEOA6 HIS-198; GLU-227 AND ILE-637, CHARACTERIZATION OF VARIANTS PEOA6 HHIS-198; GLU-227 AND ILE-637.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS44415.1. [P51530-1]
PIRT50697.
RefSeqNP_001073918.2. NM_001080449.2. [P51530-1]
UniGeneHs.532446.

3D structure databases

ProteinModelPortalP51530.
SMRP51530. Positions 448-1043.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108103. 7 interactions.
STRING9606.ENSP00000382133.

PTM databases

PhosphoSiteP51530.

Proteomic databases

MaxQBP51530.
PaxDbP51530.
PRIDEP51530.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358410; ENSP00000351185; ENSG00000138346. [P51530-1]
ENST00000399179; ENSP00000382132; ENSG00000138346. [P51530-3]
GeneID1763.
KEGGhsa:1763.
UCSCuc031pvh.1. human. [P51530-1]

Organism-specific databases

CTD1763.
GeneCardsGC10M070173.
HGNCHGNC:2939. DNA2.
HPAHPA037487.
MIM601810. gene.
615156. phenotype.
neXtProtNX_P51530.
Orphanet352470. Mitochondrial DNA deletion syndrome with progressive myopathy.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1112.
HOGENOMHOG000168456.
HOVERGENHBG081456.
InParanoidP51530.
KOK10742.
PhylomeDBP51530.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpressP51530.
BgeeP51530.
CleanExHS_DNA2.
GenevestigatorP51530.

Family and domain databases

Gene3D3.40.50.300. 3 hits.
InterProIPR014808. DNA_replication_fac_Dna2_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF08696. Dna2. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
ProtoNetSearch...

Other

GeneWikiDNA2L.
GenomeRNAi1763.
NextBio7187.
PROP51530.
SOURCESearch...

Entry information

Entry nameDNA2_HUMAN
AccessionPrimary (citable) accession number: P51530
Secondary accession number(s): Q2NKM1 expand/collapse secondary AC list , Q5TC49, Q5TC50, Q6P455, Q6PI80, Q7Z6H9, Q8N346
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 12, 2006
Last modified: July 9, 2014
This is version 114 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM