Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

DNA replication ATP-dependent helicase/nuclease DNA2 (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_MOUSE              Reviewed;        1062 AA.
Q6ZQJ5; Q14BM9; Q8BSZ0; Q8R3J3;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
12-DEC-2006, sequence version 2.
22-NOV-2017, entry version 101.
RecName: Full=DNA replication ATP-dependent helicase/nuclease DNA2;
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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Embryonic tail;
PubMed=14621295; DOI=10.1093/dnares/10.4.167;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
III. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:167-180(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 263-1078 (ISOFORM 1).
STRAIN=Czech II; TISSUE=Mammary tumor;
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).
-!- 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 (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- 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:0000250}.
-!- INTERACTION:
P70371:Terf1; NbExp=4; IntAct=EBI-6919222, EBI-6919183;
O35144:Terf2; NbExp=4; IntAct=EBI-6919222, EBI-6919263;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Mitochondrion
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q6ZQJ5-1; Sequence=Displayed;
Name=2;
IsoId=Q6ZQJ5-2; Sequence=VSP_021872, VSP_021873;
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:0000250}.
-!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC97861.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AK129051; BAC97861.1; ALT_INIT; mRNA.
EMBL; AK028381; BAC25919.1; -; mRNA.
EMBL; BC025182; AAH25182.1; -; mRNA.
EMBL; BC115716; AAI15717.1; -; mRNA.
CCDS; CCDS35923.1; -. [Q6ZQJ5-1]
RefSeq; NP_796346.2; NM_177372.3. [Q6ZQJ5-1]
UniGene; Mm.21492; -.
PDB; 5EAN; X-ray; 2.36 A; A=1-1056.
PDB; 5EAW; X-ray; 3.00 A; A/B=1-1056.
PDB; 5EAX; X-ray; 3.05 A; A/B=1-1056.
PDBsum; 5EAN; -.
PDBsum; 5EAW; -.
PDBsum; 5EAX; -.
ProteinModelPortal; Q6ZQJ5; -.
SMR; Q6ZQJ5; -.
IntAct; Q6ZQJ5; 2.
STRING; 10090.ENSMUSP00000115750; -.
iPTMnet; Q6ZQJ5; -.
PhosphoSitePlus; Q6ZQJ5; -.
EPD; Q6ZQJ5; -.
PaxDb; Q6ZQJ5; -.
PeptideAtlas; Q6ZQJ5; -.
PRIDE; Q6ZQJ5; -.
Ensembl; ENSMUST00000092462; ENSMUSP00000090119; ENSMUSG00000036875. [Q6ZQJ5-2]
Ensembl; ENSMUST00000131422; ENSMUSP00000115750; ENSMUSG00000036875. [Q6ZQJ5-1]
GeneID; 327762; -.
KEGG; mmu:327762; -.
UCSC; uc007fji.2; mouse. [Q6ZQJ5-1]
CTD; 1763; -.
MGI; MGI:2443732; Dna2.
eggNOG; KOG1805; Eukaryota.
eggNOG; COG1112; LUCA.
GeneTree; ENSGT00780000122010; -.
HOGENOM; HOG000168456; -.
HOVERGEN; HBG081456; -.
InParanoid; Q6ZQJ5; -.
KO; K10742; -.
OMA; DIEENLW; -.
OrthoDB; EOG091G01N1; -.
PhylomeDB; Q6ZQJ5; -.
TreeFam; TF314903; -.
Reactome; R-MMU-174437; Removal of the Flap Intermediate from the C-strand.
Reactome; R-MMU-5685938; HDR through Single Strand Annealing (SSA).
Reactome; R-MMU-5685942; HDR through Homologous Recombination (HRR).
Reactome; R-MMU-5693554; Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
Reactome; R-MMU-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
Reactome; R-MMU-5693579; Homologous DNA Pairing and Strand Exchange.
Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
Reactome; R-MMU-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-MMU-69166; Removal of the Flap Intermediate.
Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
ChiTaRS; Dna2; mouse.
PRO; PR:Q6ZQJ5; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000036875; -.
CleanEx; MM_DNA2; -.
Genevisible; Q6ZQJ5; MM.
GO; GO:0005760; C:gamma DNA polymerase complex; IEA:Ensembl.
GO; GO:0042645; C:mitochondrial nucleoid; ISO:MGI.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0043139; F:5'-3' DNA helicase activity; ISS:UniProtKB.
GO; GO:0017108; F:5'-flap endonuclease activity; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0003678; F:DNA helicase activity; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004518; F:nuclease activity; ISS:UniProtKB.
GO; GO:0043142; F:single-stranded DNA-dependent ATPase activity; ISS:UniProtKB.
GO; GO:0016890; F:site-specific endodeoxyribonuclease activity, specific for altered base; ISS:UniProtKB.
GO; GO:0006284; P:base-excision repair; ISS:UniProtKB.
GO; GO:0000729; P:DNA double-strand break processing; ISS:UniProtKB.
GO; GO:0006260; P:DNA replication; ISS:UniProtKB.
GO; GO:0000076; P:DNA replication checkpoint; ISS:UniProtKB.
GO; GO:0033567; P:DNA replication, Okazaki fragment processing; ISS:UniProtKB.
GO; GO:0043137; P:DNA replication, removal of RNA primer; ISS:UniProtKB.
GO; GO:0043504; P:mitochondrial DNA repair; ISO:MGI.
GO; GO:0006264; P:mitochondrial DNA replication; ISS:UniProtKB.
GO; GO:1902990; P:mitotic telomere maintenance via semi-conservative replication; IMP:BHF-UCL.
GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IDA:BHF-UCL.
GO; GO:0045740; P:positive regulation of DNA replication; ISS:UniProtKB.
GO; GO:0000723; P:telomere maintenance; IMP:BHF-UCL.
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; DNA damage; DNA repair; DNA replication;
DNA-binding; Endonuclease; Helicase; Hydrolase; Iron; Iron-sulfur;
Metal-binding; Mitochondrion; Multifunctional enzyme; Nuclease;
Nucleotide-binding; Nucleus; Reference proteome.
CHAIN 1 1062 DNA replication ATP-dependent
helicase/nuclease DNA2.
/FTId=PRO_0000263604.
NP_BIND 649 656 ATP. {ECO:0000255}.
REGION 82 520 Nuclease activity. {ECO:0000250}.
REGION 521 1062 Helicase activity. {ECO:0000250}.
METAL 137 137 Iron-sulfur (4Fe-4S). {ECO:0000250}.
METAL 394 394 Iron-sulfur (4Fe-4S). {ECO:0000250}.
METAL 397 397 Iron-sulfur (4Fe-4S). {ECO:0000250}.
METAL 403 403 Iron-sulfur (4Fe-4S). {ECO:0000250}.
VAR_SEQ 932 966 GCSPSDIGVIAPYRQQLRIISDLLARSSVGMVEVN -> AA
PQTLASSPRTDSSCGSSATYWPGLLLGWLRLTQ (in
isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_021872.
VAR_SEQ 967 1062 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_021873.
CONFLICT 285 285 I -> K (in Ref. 2; BAC25919).
{ECO:0000305}.
CONFLICT 375 375 P -> L (in Ref. 3; AAH25182).
{ECO:0000305}.
CONFLICT 400 400 I -> M (in Ref. 3; AAH25182).
{ECO:0000305}.
CONFLICT 486 486 T -> M (in Ref. 3; AAH25182).
{ECO:0000305}.
CONFLICT 543 543 A -> V (in Ref. 3; AAH25182).
{ECO:0000305}.
CONFLICT 881 881 P -> S (in Ref. 3; AAH25182).
{ECO:0000305}.
CONFLICT 957 957 R -> Q (in Ref. 3; AAH25182).
{ECO:0000305}.
CONFLICT 1037 1037 A -> T (in Ref. 3; AAH25182).
{ECO:0000305}.
HELIX 4 9 {ECO:0000244|PDB:5EAN}.
HELIX 23 34 {ECO:0000244|PDB:5EAN}.
HELIX 43 45 {ECO:0000244|PDB:5EAW}.
STRAND 47 57 {ECO:0000244|PDB:5EAN}.
STRAND 59 74 {ECO:0000244|PDB:5EAN}.
STRAND 79 83 {ECO:0000244|PDB:5EAN}.
HELIX 85 89 {ECO:0000244|PDB:5EAN}.
STRAND 97 102 {ECO:0000244|PDB:5EAN}.
STRAND 106 111 {ECO:0000244|PDB:5EAN}.
STRAND 113 115 {ECO:0000244|PDB:5EAN}.
STRAND 117 121 {ECO:0000244|PDB:5EAN}.
HELIX 128 133 {ECO:0000244|PDB:5EAN}.
TURN 134 136 {ECO:0000244|PDB:5EAN}.
HELIX 138 146 {ECO:0000244|PDB:5EAN}.
HELIX 148 150 {ECO:0000244|PDB:5EAX}.
HELIX 155 172 {ECO:0000244|PDB:5EAN}.
HELIX 177 188 {ECO:0000244|PDB:5EAN}.
HELIX 191 200 {ECO:0000244|PDB:5EAN}.
HELIX 204 225 {ECO:0000244|PDB:5EAN}.
HELIX 231 233 {ECO:0000244|PDB:5EAN}.
STRAND 252 268 {ECO:0000244|PDB:5EAN}.
TURN 269 272 {ECO:0000244|PDB:5EAN}.
STRAND 273 287 {ECO:0000244|PDB:5EAN}.
STRAND 290 301 {ECO:0000244|PDB:5EAN}.
HELIX 309 322 {ECO:0000244|PDB:5EAN}.
TURN 323 325 {ECO:0000244|PDB:5EAN}.
STRAND 330 336 {ECO:0000244|PDB:5EAN}.
TURN 337 339 {ECO:0000244|PDB:5EAN}.
STRAND 342 346 {ECO:0000244|PDB:5EAN}.
HELIX 349 367 {ECO:0000244|PDB:5EAN}.
STRAND 370 374 {ECO:0000244|PDB:5EAN}.
STRAND 379 381 {ECO:0000244|PDB:5EAN}.
HELIX 391 395 {ECO:0000244|PDB:5EAN}.
HELIX 400 409 {ECO:0000244|PDB:5EAN}.
HELIX 421 431 {ECO:0000244|PDB:5EAN}.
HELIX 436 453 {ECO:0000244|PDB:5EAN}.
HELIX 456 458 {ECO:0000244|PDB:5EAN}.
HELIX 463 466 {ECO:0000244|PDB:5EAN}.
HELIX 470 474 {ECO:0000244|PDB:5EAN}.
STRAND 475 484 {ECO:0000244|PDB:5EAN}.
STRAND 490 493 {ECO:0000244|PDB:5EAN}.
STRAND 496 502 {ECO:0000244|PDB:5EAN}.
STRAND 504 506 {ECO:0000244|PDB:5EAN}.
STRAND 518 525 {ECO:0000244|PDB:5EAN}.
HELIX 526 528 {ECO:0000244|PDB:5EAN}.
STRAND 532 539 {ECO:0000244|PDB:5EAN}.
STRAND 541 550 {ECO:0000244|PDB:5EAN}.
STRAND 561 565 {ECO:0000244|PDB:5EAN}.
HELIX 570 572 {ECO:0000244|PDB:5EAW}.
HELIX 573 582 {ECO:0000244|PDB:5EAN}.
STRAND 584 586 {ECO:0000244|PDB:5EAN}.
HELIX 587 596 {ECO:0000244|PDB:5EAN}.
HELIX 609 611 {ECO:0000244|PDB:5EAN}.
HELIX 614 616 {ECO:0000244|PDB:5EAN}.
HELIX 617 625 {ECO:0000244|PDB:5EAN}.
HELIX 629 640 {ECO:0000244|PDB:5EAN}.
STRAND 641 649 {ECO:0000244|PDB:5EAN}.
HELIX 655 668 {ECO:0000244|PDB:5EAN}.
STRAND 673 679 {ECO:0000244|PDB:5EAN}.
HELIX 680 692 {ECO:0000244|PDB:5EAN}.
HELIX 703 705 {ECO:0000244|PDB:5EAN}.
TURN 708 710 {ECO:0000244|PDB:5EAN}.
HELIX 711 713 {ECO:0000244|PDB:5EAN}.
HELIX 715 721 {ECO:0000244|PDB:5EAN}.
HELIX 727 734 {ECO:0000244|PDB:5EAN}.
STRAND 738 743 {ECO:0000244|PDB:5EAN}.
HELIX 744 746 {ECO:0000244|PDB:5EAN}.
HELIX 750 753 {ECO:0000244|PDB:5EAN}.
STRAND 757 762 {ECO:0000244|PDB:5EAN}.
HELIX 765 767 {ECO:0000244|PDB:5EAN}.
HELIX 770 773 {ECO:0000244|PDB:5EAN}.
HELIX 775 779 {ECO:0000244|PDB:5EAN}.
STRAND 780 787 {ECO:0000244|PDB:5EAN}.
HELIX 799 803 {ECO:0000244|PDB:5EAN}.
TURN 804 807 {ECO:0000244|PDB:5EAN}.
HELIX 810 814 {ECO:0000244|PDB:5EAN}.
HELIX 818 820 {ECO:0000244|PDB:5EAN}.
STRAND 821 824 {ECO:0000244|PDB:5EAN}.
STRAND 826 830 {ECO:0000244|PDB:5EAN}.
HELIX 832 841 {ECO:0000244|PDB:5EAN}.
STRAND 848 851 {ECO:0000244|PDB:5EAN}.
HELIX 852 856 {ECO:0000244|PDB:5EAN}.
HELIX 864 871 {ECO:0000244|PDB:5EAN}.
TURN 872 874 {ECO:0000244|PDB:5EAN}.
HELIX 881 887 {ECO:0000244|PDB:5EAN}.
STRAND 893 897 {ECO:0000244|PDB:5EAN}.
STRAND 899 901 {ECO:0000244|PDB:5EAN}.
STRAND 906 908 {ECO:0000244|PDB:5EAN}.
STRAND 911 913 {ECO:0000244|PDB:5EAN}.
HELIX 915 930 {ECO:0000244|PDB:5EAN}.
HELIX 935 937 {ECO:0000244|PDB:5EAN}.
STRAND 938 941 {ECO:0000244|PDB:5EAN}.
HELIX 945 957 {ECO:0000244|PDB:5EAN}.
STRAND 963 966 {ECO:0000244|PDB:5EAN}.
HELIX 968 971 {ECO:0000244|PDB:5EAN}.
STRAND 976 982 {ECO:0000244|PDB:5EAN}.
STRAND 988 990 {ECO:0000244|PDB:5EAX}.
HELIX 995 997 {ECO:0000244|PDB:5EAN}.
HELIX 999 1006 {ECO:0000244|PDB:5EAN}.
STRAND 1008 1017 {ECO:0000244|PDB:5EAN}.
HELIX 1019 1022 {ECO:0000244|PDB:5EAN}.
HELIX 1026 1036 {ECO:0000244|PDB:5EAN}.
TURN 1037 1039 {ECO:0000244|PDB:5EAN}.
STRAND 1041 1043 {ECO:0000244|PDB:5EAN}.
HELIX 1050 1053 {ECO:0000244|PDB:5EAN}.
SEQUENCE 1062 AA; 119447 MW; CD009CB89ACA775C CRC64;
MEPLDELDLL LLEEDGGAEA VPRVELLRKK ADALFPETVL SRGVDNRYLV LAVETSQNER
GAEEKRLHVT ASQDREHEVL CILRNGWSSV PVEPGDIVHL EGDCTSEPWI IDDDFGYFIL
YPDMMISGTS VASSIRCLRR AVLSETFRGS DPATRQMLIG TILHEVFQKA ISESFAPERL
QELALQTLRE VRHLKEMYRL NLSQDEILCE VEEYLPSFSK WAEDFMRKGP SSEFPQMQLS
LPSDGSNRSS PCNIEVVKSL DIEESIWSPR FGLKGKIDVT VGVKIHRDCK MKYKVMPLEL
KTGKESNSIE HRSQVVLYTL LSQERREDPE AGWLLYLKTG QMYPVPANHL DKRELLKLRN
WLAASLLHRV SRAAPGEEAR LSALPQIIEE EKTCKYCSQI GNCALYSRAV EEQGDDASIP
EAMLSKIQEE TRHLQLAHLK YFSLWCLMLT LESQSKDNRK THQSIWLTPA SELEESGNCV
GNLVRTEPVS RVCDGQYLHN FQRKNGPMPA TNLMAGDRII LSGEERKLFA LSKGYVKKMN
KAAVTCLLDR NLSTLPATTV FRLDREERHG DISTPLGNLS KLMESTDPSK RLRELIIDFR
EPQFIAYLSS VLPHDAKDTV ANILKGLNKP QRQAMKRVLL SKDYTLIVGM PGTGKTTTIC
ALVRILSACG FSVLLTSYTH SAVDNILLKL AKFKVGFLRL GQSHKVHPDI QKFTEEEICR
SRSIASLAHL EELYNSHPIV ATTCMGINHP IFSRKTFDFC IVDEASQISQ PVCLGPLFFS
RRFVLVGDHQ QLPPLVVNRE ARALGMSESL FKRLERNESA VVQLTVQYRM NRKIMSLSNK
LTYAGKLECG SDRVANAVLA LPNLKDARLS LQLYADYSDS PWLAGVLEPD NPVCFLNTDK
VPAPEQVENG GVSNVTEARL IVFLTSTFIK AGCSPSDIGV IAPYRQQLRI ISDLLARSSV
GMVEVNTVDK YQGRDKSLIL VSFVRSNEDG TLGELLKDWR RLNVALTRAK HKLILLGSVS
SLKRFPPLGT LFDHLNAEQL ILDLPSREHE SLSHILGDCQ RD


Related products :

Catalog number Product name Quantity
EIAAB11501 DNA replication ATP-dependent helicase-like homolog,DNA2,DNA2L,DNA2-like helicase,Homo sapiens,Human,KIAA0083
EIAAB11503 DNA replication ATP-dependent helicase-like homolog,Dna2,Dna2l,DNA2-like helicase,Kiaa0083,Mouse,Mus musculus
DNA2_BOVIN Bovine ELISA Kit FOR DNA replication ATP-dependent helicase per nuclease DNA2 96T
EIAAB11502 Chicken,DNA replication ATP-dependent helicase-like homolog,DNA2,DNA2L,DNA2-like helicase,Gallus gallus,RCJMB04_11a16
DNAH10 DNA2 Gene DNA replication helicase 2 homolog (yeast)
E2660h Human DNA2 DNA Replication Helicase 2 Like Protein 96T
CSB-EL006982HU Human DNA replication helicase 2 homolog (yeast) (DNA2) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL006982MO Mouse DNA replication helicase 2 homolog (yeast) (DNA2) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL006982CH Chicken DNA replication helicase 2 homolog (yeast) (DNA2) ELISA kit, Species Chicken, Sample Type serum, plasma 96T
DNA2L_MOUSE ELISA Kit FOR DNA2-like helicase; organism: Mouse; gene name: Dna2 96T
CSB-EL006982HU Human DNA2-like helicase(DNA2) ELISA kit SpeciesHuman 96T
CSB-EL006982MO Mouse DNA2-like helicase(DNA2) ELISA kit SpeciesMouse 96T
CSB-EL006982CH Chicken DNA2-like helicase(DNA2) ELISA kit SpeciesChicken 96T
CSB-EL006982MO Mouse DNA2-like helicase(DNA2) ELISA kit 96T
CSB-EL006982CH Chicken DNA2-like helicase(DNA2) ELISA kit 96T
CSB-EL006982HU Human DNA2-like helicase(DNA2) ELISA kit 96T
EIAAB10832 ATP-dependent RNA helicase p54,Ddx6,DEAD box protein 6,Hlr2,Mouse,Mus musculus,Oncogene RCK homolog,Probable ATP-dependent RNA helicase DDX6,Rck
18-003-44036 Putative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX16 - EC 3.6.1.-; DEAH-box protein 16; ATP-dependent RNA helicase _3 Polyclonal 0.05 mg Aff Pur
18-003-42773 Probable ATP-dependent RNA helicase DDX6 - EC 3.6.1.-; DEAD box protein 6; ATP-dependent RNA helicase p54; Oncogene RCK Polyclonal 0.1 mg Protein A
25-214 SMARCAD1 belongs to the SNF2_RAD54 helicase family. It contains 2 CUE domains, 1 helicase ATP-binding domain, and 1 helicase C-terminal domain. It is a probable ATP-dependent DNA helicase. 0.05 mg
EIAAB10817 ATP-dependent RNA helicase DDX54,ATP-dependent RNA helicase DP97,DDX54,DEAD box protein 54,DEAD box RNA helicase 97 kDa,Homo sapiens,Human
EIAAB46583 ATP-dependent DNA helicase 2 subunit 2,ATP-dependent DNA helicase II 80 kDa subunit,CTC box-binding factor 85 kDa subunit,CTC85,CTCBF,DNA repair protein XRCC5,G22p2,Ku autoantigen protein p86 homolog,
EIAAB11209 ATP-dependent RNA helicase _46,DBP1,DDX15,DEAH box protein 15,DHX15,Homo sapiens,Human,Putative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX15
EIAAB10823 ATP-dependent 61 kDa nucleolar RNA helicase,D11Ertd619e,Ddx56,DEAD box protein 56,Mouse,Mus musculus,Noh61,Probable ATP-dependent RNA helicase DDX56
EIAAB10831 ATP-dependent RNA helicase p54,DDX6,DEAD box protein 6,HLR2,Homo sapiens,Human,Oncogene RCK,Probable ATP-dependent RNA helicase DDX6,RCK


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur