P51530 (DNA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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:

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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1060 AA.
Sequence status	Complete.
Protein existence	Evidence 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.10 Ref.11 Ref.12 Ref.13
Catalytic activity	ATP + H2O = ADP + phosphate. Ref.5
Cofactor	Binds 1 4Fe-4S cluster By similarity.
Subunit structure	Interacts with BLM and WDHD1. Ref.10 Ref.12
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.
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 process	DNA damage DNA repair DNA replication
Cellular component	Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing
Ligand	4Fe-4S ATP-binding DNA-binding Iron Iron-sulfur Metal-binding Nucleotide-binding
Molecular function	Endonuclease Helicase Hydrolase Nuclease
PTM	Acetylation
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	DNA double-strand break processing Inferred from direct assay Ref.10. Source: UniProtKB DNA replication checkpoint Inferred from mutant phenotype Ref.12. Source: UniProtKB DNA replication, removal of RNA primer Inferred from direct assay Ref.6. Source: UniProtKB S phase of mitotic cell cycle 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 positive regulation of DNA replication Inferred from direct assay Ref.6. Source: UniProtKB telomere maintenance via recombination Traceable author statement. Source: Reactome telomere maintenance via semi-conservative replication Traceable author statement. Source: Reactome
Cellular_component	mitochondrial nucleoid Inferred from direct assay Ref.7. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	4 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.13. Source: UniProtKB ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from direct assay Ref.8Ref.13. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1060	1060	DNA replication ATP-dependent helicase/nuclease DNA2		PRO_0000080712
Regions
	Nucleotide binding	648 – 655	8	ATP Potential
	Region	81 – 519	439	Nuclease activity By similarity
	Region	520 – 1060	541	Helicase activity By similarity
Sites
	Metal binding	136	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	393	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	396	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	402	1	Iron-sulfur (4Fe-4S) By similarity
Natural variations
	Alternative sequence	663 – 900	238	Missing in isoform 3.		VSP_021869
	Alternative sequence	664 – 687	24	ILYAC…DNILL → FRRFIQLSSNLQSKKFADQS PLNP in isoform 2.		VSP_021870
	Alternative sequence	688 – 1060	373	Missing in isoform 2.		VSP_021871
	Alternative sequence	1040 – 1060	21	IDLPS…DFQRE → SFFFCIWSHLIAL in isoform 4.		VSP_044185
Experimental info
	Mutagenesis	277	1	D → A: Abolishes ability to resect DNA in present of BLM. Ref.5 Ref.10 Ref.12
	Mutagenesis	654	1	K → E: Abolishes ability to unwind DNA, while it does not affect ability to resect DNA. Ref.5 Ref.10 Ref.11 Ref.12
	Sequence conflict	986	1	K → N in AAH28188. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 12, 2006. Version 3. Checksum: 727D4B268FD75C5A	FASTA	1,060	120,415
	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
	Isoform 2 [UniParc]. Checksum: 8B6E028A05B190FE	FASTA	687	78,498
	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 LVRFRRFIQL SSNLQSKKFA DQSPLNP
	Isoform 3 [UniParc]. Checksum: BFFA20A722F4430B	FASTA	822	93,347
	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 LVPAPEQVEK GGVSNVTEAK LIVFLTSIFV KAGCSPSDIG IIAPYRQQLK IINDLLARSI 730 740 750 760 770 780 GMVEVNTVDK YQGRDKSIVL VSFVRSNKDG TVGELLKDWR RLNVAITRAK HKLILLGCVP 790 800 810 820 SLNCYPPLEK LLNHLNSEKL IIDLPSREHE SLCHILGDFQ RE
	Isoform 4 [UniParc]. Checksum: 76545663BC48445D	FASTA	1,052	119,504
	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 NCYPPLEKLL NHLNSEKLIS FFFCIWSHLI AL

References

	« Hide 'large scale' referencesShow '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. , 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]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
+	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.
IPI	IPI00216142. IPI00816670. IPI00816801.
PIR	T50697.
RefSeq	NP_001073918.2. NM_001080449.2.
UniGene	Hs.532446.
3D structure databases
ProteinModelPortal	P51530.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000382133.
PTM databases
PhosphoSite	P51530.
Polymorphism databases
DMDM	119370373.
Proteomic databases
PaxDb	P51530.
PRIDE	P51530.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000358410; ENSP00000351185; ENSG00000138346. ENST00000399179; ENSP00000382132; ENSG00000138346. ENST00000549829; ENSP00000450033; ENSG00000138346.
GeneID	1763.
KEGG	hsa:1763.
UCSC	uc021prt.1. human.
Organism-specific databases
CTD	1763.
GeneCards	GC10M070173.
HGNC	HGNC:2939. DNA2.
HPA	HPA037487.
MIM	601810. gene.
neXtProt	NX_P51530.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1112.
HOGENOM	HOG000168456.
HOVERGEN	HBG081456.
InParanoid	P51530.
KO	K10742.
Enzyme and pathway databases
Reactome	REACT_115566. Cell Cycle. REACT_383. DNA Replication.
Gene expression databases
ArrayExpress	P51530.
Bgee	P51530.
CleanEx	HS_DNA2.
Genevestigator	P51530.
GermOnline	ENSG00000138346. Homo sapiens.
Family and domain databases
InterPro	IPR026851. Dna2. IPR014808. DNA_replication_fac_Dna2_N. [Graphical view]
PANTHER	PTHR10887:SF14. PTHR10887:SF14. 1 hit.
Pfam	PF08696. Dna2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	1763.
NextBio	7187.
SOURCE	Search...

Entry information

Entry name

DNA2_HUMAN

Accession

Primary (citable) accession number: P51530
Secondary accession number(s): Q2NKM1 , Q5TC49, Q5TC50, Q6P455, Q6PI80, Q7Z6H9, Q8N346

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	December 12, 2006
Last modified:	May 1, 2013
This is version 103 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.