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DNA replication ATP-dependent helicase/nuclease DNA2 (hDNA2) (DNA replication ATP-dependent helicase-like homolog) [Includes: DNA replication nuclease DNA2 (EC 3.1.-.-); DNA replication ATP-dependent helicase DNA2 (EC 3.6.4.12)]

 DNA2_HUMAN              Reviewed;        1060 AA.
P51530; Q2NKM1; Q5TC49; Q5TC50; Q6P455; Q6PI80; Q7Z6H9; Q8N346;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
12-DEC-2006, sequence version 3.
22-NOV-2017, entry version 145.
RecName: Full=DNA replication ATP-dependent helicase/nuclease DNA2;
Short=hDNA2;
AltName: Full=DNA replication ATP-dependent helicase-like homolog;
Includes:
RecName: Full=DNA replication nuclease DNA2;
EC=3.1.-.-;
Includes:
RecName: Full=DNA replication ATP-dependent helicase DNA2;
EC=3.6.4.12;
Name=DNA2; Synonyms=DNA2L, KIAA0083;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow;
PubMed=7788527; DOI=10.1093/dnares/2.1.37;
Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S.,
Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
"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.";
DNA Res. 2:37-43(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
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.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 680-1060 (ISOFORM 4), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 567-1060 (ISOFORM 1).
TISSUE=Colon, Duodenum, and Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION.
PubMed=16595799; DOI=10.1093/nar/gkl102;
Kim J.H., Kim H.D., Ryu G.H., Kim D.H., Hurwitz J., Seo Y.S.;
"Isolation of human Dna2 endonuclease and characterization of its
enzymatic properties.";
Nucleic Acids Res. 34:1854-1864(2006).
[5]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-277 AND LYS-654.
PubMed=16595800; DOI=10.1093/nar/gkl070;
Masuda-Sasa T., Imamura O., Campbell J.L.;
"Biochemical analysis of human Dna2.";
Nucleic Acids Res. 34:1865-1875(2006).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18995831; DOI=10.1016/j.molcel.2008.09.024;
Zheng L., Zhou M., Guo Z., Lu H., Qian L., Dai H., Qiu J.,
Yakubovskaya E., Bogenhagen D.F., Demple B., Shen B.;
"Human DNA2 is a mitochondrial nuclease/helicase for efficient
processing of DNA replication and repair intermediates.";
Mol. Cell 32:325-336(2008).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19487465; DOI=10.1128/MCB.01834-08;
Duxin J.P., Dao B., Martinsson P., Rajala N., Guittat L.,
Campbell J.L., Spelbrink J.N., Stewart S.A.;
"Human Dna2 is a nuclear and mitochondrial DNA maintenance protein.";
Mol. Cell. Biol. 29:4274-4282(2009).
[8]
ACETYLATION.
PubMed=20019387; DOI=10.1074/jbc.M109.086397;
Balakrishnan L., Stewart J., Polaczek P., Campbell J.L., Bambara R.A.;
"Acetylation of Dna2 endonuclease/helicase and flap endonuclease 1 by
p300 promotes DNA stability by creating long flap intermediates.";
J. Biol. Chem. 285:4398-4404(2010).
[9]
FUNCTION, INTERACTION WITH BLM, AND MUTAGENESIS OF ASP-277 AND
LYS-654.
PubMed=21325134; DOI=10.1101/gad.2003811;
Nimonkar A.V., Genschel J., Kinoshita E., Polaczek P., Campbell J.L.,
Wyman C., Modrich P., Kowalczykowski S.C.;
"BLM-DNA2-RPA-MRN and EXO1-BLM-RPA-MRN constitute two DNA end
resection machineries for human DNA break repair.";
Genes Dev. 25:350-362(2011).
[10]
FUNCTION, DNA-BINDING, AND MUTAGENESIS OF LYS-654.
PubMed=21572043; DOI=10.1074/jbc.M111.243071;
Fortini B.K., Pokharel S., Polaczek P., Balakrishnan L., Bambara R.A.,
Campbell J.L.;
"Characterization of the endonuclease and ATP-dependent flap
endo/exonuclease of Dna2.";
J. Biol. Chem. 286:23763-23770(2011).
[11]
FUNCTION, DNA-BINDING, INTERACTION WITH WDHD1, AND MUTAGENESIS OF
ASP-277 AND LYS-654.
PubMed=22570476; DOI=10.1074/jbc.M112.359018;
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.;
"Okazaki fragment processing-independent role for human Dna2 enzyme
during DNA replication.";
J. Biol. Chem. 287:21980-21991(2012).
[12]
FUNCTION, AND DNA-BINDING.
PubMed=22570407; DOI=10.1093/nar/gks388;
Gloor J.W., Balakrishnan L., Campbell J.L., Bambara R.A.;
"Biochemical analyses indicate that binding and cleavage specificities
define the ordered processing of human Okazaki fragments by Dna2 and
FEN1.";
Nucleic Acids Res. 40:6774-6786(2012).
[13]
INVOLVEMENT IN SCKL8.
PubMed=24389050; DOI=10.1101/gr.160572.113;
Shaheen R., Faqeih E., Ansari S., Abdel-Salam G., Al-Hassnan Z.N.,
Al-Shidi T., Alomar R., Sogaty S., Alkuraya F.S.;
"Genomic analysis of primordial dwarfism reveals novel disease
genes.";
Genome Res. 24:291-299(2014).
[14]
VARIANTS PEOA6 HIS-198; GLU-227 AND ILE-637, AND CHARACTERIZATION OF
VARIANTS PEOA6 HHIS-198; GLU-227 AND ILE-637.
PubMed=23352259; DOI=10.1016/j.ajhg.2012.12.014;
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., Moggio M., Bresolin N., Shen B., Comi G.P.;
"Mutations in DNA2 link progressive myopathy to mitochondrial DNA
instability.";
Am. J. Hum. Genet. 92:293-300(2013).
-!- 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.
{ECO:0000269|PubMed:16595799, ECO:0000269|PubMed:16595800,
ECO:0000269|PubMed:18995831, ECO:0000269|PubMed:19487465,
ECO:0000269|PubMed:21325134, ECO:0000269|PubMed:21572043,
ECO:0000269|PubMed:22570407, ECO:0000269|PubMed:22570476}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000269|PubMed:16595800}.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000250};
Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
-!- SUBUNIT: Interacts with BLM and WDHD1.
{ECO:0000269|PubMed:21325134, ECO:0000269|PubMed:22570476}.
-!- SUBCELLULAR LOCATION: 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). {ECO:0000269|PubMed:18995831,
ECO:0000269|PubMed:19487465}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=P51530-1; Sequence=Displayed;
Name=2;
IsoId=P51530-2; Sequence=VSP_021870, VSP_021871;
Note=No experimental confirmation available.;
Name=3;
IsoId=P51530-3; Sequence=VSP_021869;
Note=No experimental confirmation available.;
Name=4;
IsoId=P51530-4; Sequence=VSP_044185;
Note=No experimental confirmation available.;
-!- PTM: 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.
{ECO:0000269|PubMed:20019387}.
-!- 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.
{ECO:0000269|PubMed:23352259}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Seckel syndrome 8 (SCKL8) [MIM:615807]: A 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. {ECO:0000269|PubMed:24389050}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH28188.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAH63664.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAA07647.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAI17237.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAI17238.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; D42046; BAA07647.1; ALT_INIT; mRNA.
EMBL; AL136233; CAI17238.1; ALT_SEQ; Genomic_DNA.
EMBL; AL136233; CAI17237.1; ALT_SEQ; Genomic_DNA.
EMBL; BC041115; AAH41115.1; -; mRNA.
EMBL; BC053574; AAH53574.1; -; mRNA.
EMBL; BC063664; AAH63664.1; ALT_INIT; mRNA.
EMBL; BC111740; AAI11741.1; -; mRNA.
EMBL; BC028188; AAH28188.1; ALT_INIT; mRNA.
CCDS; CCDS44415.2; -. [P51530-1]
PIR; T50697; T50697.
RefSeq; NP_001073918.2; NM_001080449.2. [P51530-1]
UniGene; Hs.532446; -.
PDB; 5EAY; X-ray; 1.55 A; E/F/G/H=5-17.
PDBsum; 5EAY; -.
ProteinModelPortal; P51530; -.
SMR; P51530; -.
BioGrid; 108103; 43.
IntAct; P51530; 1.
STRING; 9606.ENSP00000382133; -.
iPTMnet; P51530; -.
PhosphoSitePlus; P51530; -.
BioMuta; DNA2; -.
EPD; P51530; -.
MaxQB; P51530; -.
PaxDb; P51530; -.
PeptideAtlas; P51530; -.
PRIDE; P51530; -.
Ensembl; ENST00000358410; ENSP00000351185; ENSG00000138346. [P51530-1]
Ensembl; ENST00000399179; ENSP00000382132; ENSG00000138346. [P51530-2]
Ensembl; ENST00000399180; ENSP00000382133; ENSG00000138346. [P51530-2]
GeneID; 1763; -.
KEGG; hsa:1763; -.
UCSC; uc057tqx.1; human. [P51530-1]
CTD; 1763; -.
DisGeNET; 1763; -.
EuPathDB; HostDB:ENSG00000138346.14; -.
GeneCards; DNA2; -.
HGNC; HGNC:2939; DNA2.
HPA; HPA037487; -.
HPA; HPA057526; -.
MalaCards; DNA2; -.
MIM; 601810; gene.
MIM; 615156; phenotype.
MIM; 615807; phenotype.
neXtProt; NX_P51530; -.
OpenTargets; ENSG00000138346; -.
Orphanet; 352470; Mitochondrial DNA deletion syndrome with progressive myopathy.
eggNOG; KOG1805; Eukaryota.
eggNOG; COG1112; LUCA.
GeneTree; ENSGT00780000122010; -.
HOGENOM; HOG000168456; -.
HOVERGEN; HBG081456; -.
InParanoid; P51530; -.
KO; K10742; -.
OMA; DIEENLW; -.
OrthoDB; EOG091G01N1; -.
PhylomeDB; P51530; -.
Reactome; R-HSA-174437; Removal of the Flap Intermediate from the C-strand.
Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA).
Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
Reactome; R-HSA-5693554; Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
Reactome; R-HSA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
Reactome; R-HSA-5693579; Homologous DNA Pairing and Strand Exchange.
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-HSA-69166; Removal of the Flap Intermediate.
Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
ChiTaRS; DNA2; human.
GeneWiki; DNA2L; -.
GenomeRNAi; 1763; -.
PRO; PR:P51530; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000138346; -.
CleanEx; HS_DNA2; -.
ExpressionAtlas; P51530; baseline and differential.
Genevisible; P51530; HS.
GO; GO:0042645; C:mitochondrial nucleoid; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0000784; C:nuclear chromosome, telomeric region; ISS:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0043139; F:5'-3' DNA helicase activity; IDA:UniProtKB.
GO; GO:0017108; F:5'-flap endonuclease activity; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; TAS:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0003678; F:DNA helicase activity; IDA:UniProtKB.
GO; GO:0004386; F:helicase activity; TAS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004518; F:nuclease activity; IDA:UniProtKB.
GO; GO:0043142; F:single-stranded DNA-dependent ATPase activity; IDA:UniProtKB.
GO; GO:0016890; F:site-specific endodeoxyribonuclease activity, specific for altered base; IDA:UniProtKB.
GO; GO:0006284; P:base-excision repair; IDA:UniProtKB.
GO; GO:0000729; P:DNA double-strand break processing; IDA:UniProtKB.
GO; GO:0006260; P:DNA replication; IMP:UniProtKB.
GO; GO:0000076; P:DNA replication checkpoint; IMP:UniProtKB.
GO; GO:0033567; P:DNA replication, Okazaki fragment processing; IDA:UniProtKB.
GO; GO:0043137; P:DNA replication, removal of RNA primer; IDA:UniProtKB.
GO; GO:0000731; P:DNA synthesis involved in DNA repair; TAS:Reactome.
GO; GO:0044806; P:G-quadruplex DNA unwinding; TAS:BHF-UCL.
GO; GO:0043504; P:mitochondrial DNA repair; IDA:UniProtKB.
GO; GO:0006264; P:mitochondrial DNA replication; IDA:UniProtKB.
GO; GO:1902990; P:mitotic telomere maintenance via semi-conservative replication; ISS:BHF-UCL.
GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; ISS:BHF-UCL.
GO; GO:0045740; P:positive regulation of DNA replication; IDA:UniProtKB.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0000732; P:strand displacement; TAS:Reactome.
GO; GO:0090656; P:t-circle formation; TAS:BHF-UCL.
GO; GO:0000723; P:telomere maintenance; ISS:BHF-UCL.
GO; GO:0032201; P:telomere maintenance via semi-conservative replication; TAS:Reactome.
InterPro; IPR026851; Dna2.
InterPro; IPR014808; DNA_replication_fac_Dna2_N.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR10887:SF14; PTHR10887:SF14; 1.
Pfam; PF08696; Dna2; 1.
SUPFAM; SSF52540; SSF52540; 2.
1: Evidence at protein level;
3D-structure; 4Fe-4S; Acetylation; Alternative splicing; ATP-binding;
Complete proteome; Disease mutation; DNA damage; DNA repair;
DNA replication; DNA-binding; Dwarfism; Endonuclease; Helicase;
Hydrolase; Iron; Iron-sulfur; Mental retardation; Metal-binding;
Mitochondrion; Multifunctional enzyme; Nuclease; Nucleotide-binding;
Nucleus; Primary mitochondrial disease;
Progressive external ophthalmoplegia; Reference proteome.
CHAIN 1 1060 DNA replication ATP-dependent
helicase/nuclease DNA2.
/FTId=PRO_0000080712.
NP_BIND 648 655 ATP. {ECO:0000255}.
REGION 81 519 Nuclease activity. {ECO:0000250}.
REGION 520 1060 Helicase activity. {ECO:0000250}.
METAL 136 136 Iron-sulfur (4Fe-4S). {ECO:0000250}.
METAL 393 393 Iron-sulfur (4Fe-4S). {ECO:0000250}.
METAL 396 396 Iron-sulfur (4Fe-4S). {ECO:0000250}.
METAL 402 402 Iron-sulfur (4Fe-4S). {ECO:0000250}.
VAR_SEQ 663 900 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_021869.
VAR_SEQ 664 687 ILYACGFSVLLTSYTHSAVDNILL -> FRRFIQLSSNLQS
KKFADQSPLNP (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_021870.
VAR_SEQ 688 1060 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_021871.
VAR_SEQ 1040 1060 IDLPSREHESLCHILGDFQRE -> SFFFCIWSHLIAL
(in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_044185.
VARIANT 198 198 R -> 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). {ECO:0000269|PubMed:23352259}.
/FTId=VAR_069905.
VARIANT 227 227 K -> E (in PEOA6; the mutant protein has
significantly reduced nuclease and
helicase activity; consistent with a loss
of function mutation; dbSNP:rs760412883).
{ECO:0000269|PubMed:23352259}.
/FTId=VAR_069906.
VARIANT 637 637 V -> 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; dbSNP:rs746522359).
{ECO:0000269|PubMed:23352259}.
/FTId=VAR_069907.
MUTAGEN 277 277 D->A: Abolishes ability to resect DNA in
present of BLM.
{ECO:0000269|PubMed:16595800,
ECO:0000269|PubMed:21325134,
ECO:0000269|PubMed:22570476}.
MUTAGEN 654 654 K->E: Abolishes ability to unwind DNA,
while it does not affect ability to
resect DNA. {ECO:0000269|PubMed:16595800,
ECO:0000269|PubMed:21325134,
ECO:0000269|PubMed:21572043,
ECO:0000269|PubMed:22570476}.
CONFLICT 986 986 K -> N (in Ref. 3; AAH28188).
{ECO:0000305}.
HELIX 7 10 {ECO:0000244|PDB:5EAY}.
SEQUENCE 1060 AA; 120415 MW; 727D4B268FD75C5A CRC64;
MEQLNELELL MEKSFWEEAE LPAELFQKKV VASFPRTVLS TGMDNRYLVL AVNTVQNKEG
NCEKRLVITA SQSLENKELC ILRNDWCSVP VEPGDIIHLE GDCTSDTWII DKDFGYLILY
PDMLISGTSI ASSIRCMRRA VLSETFRSSD PATRQMLIGT VLHEVFQKAI NNSFAPEKLQ
ELAFQTIQEI RHLKEMYRLN LSQDEIKQEV EDYLPSFCKW AGDFMHKNTS TDFPQMQLSL
PSDNSKDNST CNIEVVKPMD IEESIWSPRF GLKGKIDVTV GVKIHRGYKT KYKIMPLELK
TGKESNSIEH RSQVVLYTLL SQERRADPEA GLLLYLKTGQ MYPVPANHLD KRELLKLRNQ
MAFSLFHRIS KSATRQKTQL ASLPQIIEEE KTCKYCSQIG NCALYSRAVE QQMDCSSVPI
VMLPKIEEET QHLKQTHLEY FSLWCLMLTL ESQSKDNKKN HQNIWLMPAS EMEKSGSCIG
NLIRMEHVKI VCDGQYLHNF QCKHGAIPVT NLMAGDRVIV SGEERSLFAL SRGYVKEINM
TTVTCLLDRN LSVLPESTLF RLDQEEKNCD IDTPLGNLSK LMENTFVSKK LRDLIIDFRE
PQFISYLSSV LPHDAKDTVA CILKGLNKPQ RQAMKKVLLS KDYTLIVGMP GTGKTTTICT
LVRILYACGF SVLLTSYTHS AVDNILLKLA KFKIGFLRLG QIQKVHPAIQ QFTEQEICRS
KSIKSLALLE ELYNSQLIVA TTCMGINHPI FSRKIFDFCI VDEASQISQP ICLGPLFFSR
RFVLVGDHQQ LPPLVLNREA RALGMSESLF KRLEQNKSAV VQLTVQYRMN SKIMSLSNKL
TYEGKLECGS DKVANAVINL RHFKDVKLEL EFYADYSDNP WLMGVFEPNN PVCFLNTDKV
PAPEQVEKGG VSNVTEAKLI VFLTSIFVKA GCSPSDIGII APYRQQLKII NDLLARSIGM
VEVNTVDKYQ GRDKSIVLVS FVRSNKDGTV GELLKDWRRL NVAITRAKHK LILLGCVPSL
NCYPPLEKLL NHLNSEKLII DLPSREHESL CHILGDFQRE


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