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Protein

DNA replication ATP-dependent helicase/nuclease DNA2

Gene

Dna2

Organism
Mus musculus (Mouse)
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 (By similarity).By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.

Cofactori

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi137 – 1371Iron-sulfur (4Fe-4S)By similarity
Metal bindingi394 – 3941Iron-sulfur (4Fe-4S)By similarity
Metal bindingi397 – 3971Iron-sulfur (4Fe-4S)By similarity
Metal bindingi403 – 4031Iron-sulfur (4Fe-4S)By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi649 – 6568ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

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

ReactomeiR-MMU-174437. Removal of the Flap Intermediate from the C-strand.
R-MMU-5685938. HDR through Single Strand Annealing (SSA).
R-MMU-5685942. HDR through Homologous Recombination (HRR).
R-MMU-5693554. Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
R-MMU-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates.
R-MMU-5693579. Homologous DNA Pairing and Strand Exchange.
R-MMU-5693607. Processing of DNA double-strand break ends.
R-MMU-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-MMU-6804756. Regulation of TP53 Activity through Phosphorylation.
R-MMU-69166. Removal of the Flap Intermediate.
R-MMU-69473. G2/M DNA damage checkpoint.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA replication ATP-dependent helicase/nuclease DNA2
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:2443732. Dna2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10621062DNA replication ATP-dependent helicase/nuclease DNA2PRO_0000263604Add
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.By similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ6ZQJ5.
MaxQBiQ6ZQJ5.
PaxDbiQ6ZQJ5.
PeptideAtlasiQ6ZQJ5.
PRIDEiQ6ZQJ5.

PTM databases

iPTMnetiQ6ZQJ5.

Expressioni

Gene expression databases

BgeeiQ6ZQJ5.
CleanExiMM_DNA2.
GenevisibleiQ6ZQJ5. MM.

Interactioni

Subunit structurei

Interacts with BLM and WDHD1.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Terf1P703714EBI-6919222,EBI-6919183
Terf2O351444EBI-6919222,EBI-6919263

Protein-protein interaction databases

IntActiQ6ZQJ5. 2 interactions.
STRINGi10090.ENSMUSP00000115750.

Structurei

Secondary structure

1
1062
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 96Combined sources
Helixi23 – 3412Combined sources
Helixi43 – 453Combined sources
Beta strandi47 – 5711Combined sources
Beta strandi59 – 7416Combined sources
Beta strandi79 – 835Combined sources
Helixi85 – 895Combined sources
Beta strandi97 – 1026Combined sources
Beta strandi106 – 1116Combined sources
Beta strandi113 – 1153Combined sources
Beta strandi117 – 1215Combined sources
Helixi128 – 1336Combined sources
Turni134 – 1363Combined sources
Helixi138 – 1469Combined sources
Helixi148 – 1503Combined sources
Helixi155 – 17218Combined sources
Helixi177 – 18812Combined sources
Helixi191 – 20010Combined sources
Helixi204 – 22522Combined sources
Helixi231 – 2333Combined sources
Beta strandi252 – 26817Combined sources
Turni269 – 2724Combined sources
Beta strandi273 – 28715Combined sources
Beta strandi290 – 30112Combined sources
Helixi309 – 32214Combined sources
Turni323 – 3253Combined sources
Beta strandi330 – 3367Combined sources
Turni337 – 3393Combined sources
Beta strandi342 – 3465Combined sources
Helixi349 – 36719Combined sources
Beta strandi370 – 3745Combined sources
Beta strandi379 – 3813Combined sources
Helixi391 – 3955Combined sources
Helixi400 – 40910Combined sources
Helixi421 – 43111Combined sources
Helixi436 – 45318Combined sources
Helixi456 – 4583Combined sources
Helixi463 – 4664Combined sources
Helixi470 – 4745Combined sources
Beta strandi475 – 48410Combined sources
Beta strandi490 – 4934Combined sources
Beta strandi496 – 5027Combined sources
Beta strandi504 – 5063Combined sources
Beta strandi518 – 5258Combined sources
Helixi526 – 5283Combined sources
Beta strandi532 – 5398Combined sources
Beta strandi541 – 55010Combined sources
Beta strandi561 – 5655Combined sources
Helixi570 – 5723Combined sources
Helixi573 – 58210Combined sources
Beta strandi584 – 5863Combined sources
Helixi587 – 59610Combined sources
Helixi609 – 6113Combined sources
Helixi614 – 6163Combined sources
Helixi617 – 6259Combined sources
Helixi629 – 64012Combined sources
Beta strandi641 – 6499Combined sources
Helixi655 – 66814Combined sources
Beta strandi673 – 6797Combined sources
Helixi680 – 69213Combined sources
Helixi703 – 7053Combined sources
Turni708 – 7103Combined sources
Helixi711 – 7133Combined sources
Helixi715 – 7217Combined sources
Helixi727 – 7348Combined sources
Beta strandi738 – 7436Combined sources
Helixi744 – 7463Combined sources
Helixi750 – 7534Combined sources
Beta strandi757 – 7626Combined sources
Helixi765 – 7673Combined sources
Helixi770 – 7734Combined sources
Helixi775 – 7795Combined sources
Beta strandi780 – 7878Combined sources
Helixi799 – 8035Combined sources
Turni804 – 8074Combined sources
Helixi810 – 8145Combined sources
Helixi818 – 8203Combined sources
Beta strandi821 – 8244Combined sources
Beta strandi826 – 8305Combined sources
Helixi832 – 84110Combined sources
Beta strandi848 – 8514Combined sources
Helixi852 – 8565Combined sources
Helixi864 – 8718Combined sources
Turni872 – 8743Combined sources
Helixi881 – 8877Combined sources
Beta strandi893 – 8975Combined sources
Beta strandi899 – 9013Combined sources
Beta strandi906 – 9083Combined sources
Beta strandi911 – 9133Combined sources
Helixi915 – 93016Combined sources
Helixi935 – 9373Combined sources
Beta strandi938 – 9414Combined sources
Helixi945 – 95713Combined sources
Beta strandi963 – 9664Combined sources
Helixi968 – 9714Combined sources
Beta strandi976 – 9827Combined sources
Beta strandi988 – 9903Combined sources
Helixi995 – 9973Combined sources
Helixi999 – 10068Combined sources
Beta strandi1008 – 101710Combined sources
Helixi1019 – 10224Combined sources
Helixi1026 – 103611Combined sources
Turni1037 – 10393Combined sources
Beta strandi1041 – 10433Combined sources
Helixi1050 – 10534Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5EANX-ray2.36A1-1056[»]
5EAWX-ray3.00A/B1-1056[»]
5EAXX-ray3.05A/B1-1056[»]
ProteinModelPortaliQ6ZQJ5.
SMRiQ6ZQJ5. Positions 449-1035.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni82 – 520439Nuclease activityBy similarityAdd
BLAST
Regioni521 – 1062542Helicase activityBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the DNA2/NAM7 helicase family.Curated

Phylogenomic databases

eggNOGiKOG1805. Eukaryota.
COG1112. LUCA.
GeneTreeiENSGT00780000122010.
HOGENOMiHOG000168456.
HOVERGENiHBG081456.
InParanoidiQ6ZQJ5.
KOiK10742.
OMAiEHESLCH.
OrthoDBiEOG7K6PT8.
PhylomeDBiQ6ZQJ5.
TreeFamiTF314903.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR026851. Dna2.
IPR014808. DNA_replication_fac_Dna2_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10887:SF14. PTHR10887:SF14. 2 hits.
PfamiPF08696. Dna2. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6ZQJ5-1) [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
MEPLDELDLL LLEEDGGAEA VPRVELLRKK ADALFPETVL SRGVDNRYLV
60 70 80 90 100
LAVETSQNER GAEEKRLHVT ASQDREHEVL CILRNGWSSV PVEPGDIVHL
110 120 130 140 150
EGDCTSEPWI IDDDFGYFIL YPDMMISGTS VASSIRCLRR AVLSETFRGS
160 170 180 190 200
DPATRQMLIG TILHEVFQKA ISESFAPERL QELALQTLRE VRHLKEMYRL
210 220 230 240 250
NLSQDEILCE VEEYLPSFSK WAEDFMRKGP SSEFPQMQLS LPSDGSNRSS
260 270 280 290 300
PCNIEVVKSL DIEESIWSPR FGLKGKIDVT VGVKIHRDCK MKYKVMPLEL
310 320 330 340 350
KTGKESNSIE HRSQVVLYTL LSQERREDPE AGWLLYLKTG QMYPVPANHL
360 370 380 390 400
DKRELLKLRN WLAASLLHRV SRAAPGEEAR LSALPQIIEE EKTCKYCSQI
410 420 430 440 450
GNCALYSRAV EEQGDDASIP EAMLSKIQEE TRHLQLAHLK YFSLWCLMLT
460 470 480 490 500
LESQSKDNRK THQSIWLTPA SELEESGNCV GNLVRTEPVS RVCDGQYLHN
510 520 530 540 550
FQRKNGPMPA TNLMAGDRII LSGEERKLFA LSKGYVKKMN KAAVTCLLDR
560 570 580 590 600
NLSTLPATTV FRLDREERHG DISTPLGNLS KLMESTDPSK RLRELIIDFR
610 620 630 640 650
EPQFIAYLSS VLPHDAKDTV ANILKGLNKP QRQAMKRVLL SKDYTLIVGM
660 670 680 690 700
PGTGKTTTIC ALVRILSACG FSVLLTSYTH SAVDNILLKL AKFKVGFLRL
710 720 730 740 750
GQSHKVHPDI QKFTEEEICR SRSIASLAHL EELYNSHPIV ATTCMGINHP
760 770 780 790 800
IFSRKTFDFC IVDEASQISQ PVCLGPLFFS RRFVLVGDHQ QLPPLVVNRE
810 820 830 840 850
ARALGMSESL FKRLERNESA VVQLTVQYRM NRKIMSLSNK LTYAGKLECG
860 870 880 890 900
SDRVANAVLA LPNLKDARLS LQLYADYSDS PWLAGVLEPD NPVCFLNTDK
910 920 930 940 950
VPAPEQVENG GVSNVTEARL IVFLTSTFIK AGCSPSDIGV IAPYRQQLRI
960 970 980 990 1000
ISDLLARSSV GMVEVNTVDK YQGRDKSLIL VSFVRSNEDG TLGELLKDWR
1010 1020 1030 1040 1050
RLNVALTRAK HKLILLGSVS SLKRFPPLGT LFDHLNAEQL ILDLPSREHE
1060
SLSHILGDCQ RD
Length:1,062
Mass (Da):119,447
Last modified:December 12, 2006 - v2
Checksum:iCD009CB89ACA775C
GO
Isoform 2 (identifier: Q6ZQJ5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     932-966: GCSPSDIGVIAPYRQQLRIISDLLARSSVGMVEVN → AAPQTLASSPRTDSSCGSSATYWPGLLLGWLRLTQ
     967-1062: Missing.

Note: No experimental confirmation available.
Show »
Length:966
Mass (Da):108,508
Checksum:iC3C38997DFB65AE9
GO

Sequence cautioni

The sequence BAC97861.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti285 – 2851I → K in BAC25919 (PubMed:16141072).Curated
Sequence conflicti375 – 3751P → L in AAH25182 (PubMed:15489334).Curated
Sequence conflicti400 – 4001I → M in AAH25182 (PubMed:15489334).Curated
Sequence conflicti486 – 4861T → M in AAH25182 (PubMed:15489334).Curated
Sequence conflicti543 – 5431A → V in AAH25182 (PubMed:15489334).Curated
Sequence conflicti881 – 8811P → S in AAH25182 (PubMed:15489334).Curated
Sequence conflicti957 – 9571R → Q in AAH25182 (PubMed:15489334).Curated
Sequence conflicti1037 – 10371A → T in AAH25182 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei932 – 96635GCSPS…MVEVN → AAPQTLASSPRTDSSCGSSA TYWPGLLLGWLRLTQ in isoform 2. 1 PublicationVSP_021872Add
BLAST
Alternative sequencei967 – 106296Missing in isoform 2. 1 PublicationVSP_021873Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129051 mRNA. Translation: BAC97861.1. Different initiation.
AK028381 mRNA. Translation: BAC25919.1.
BC025182 mRNA. Translation: AAH25182.1.
BC115716 mRNA. Translation: AAI15717.1.
CCDSiCCDS35923.1. [Q6ZQJ5-1]
RefSeqiNP_796346.2. NM_177372.3. [Q6ZQJ5-1]
UniGeneiMm.21492.

Genome annotation databases

EnsembliENSMUST00000092462; ENSMUSP00000090119; ENSMUSG00000036875. [Q6ZQJ5-2]
ENSMUST00000131422; ENSMUSP00000115750; ENSMUSG00000036875. [Q6ZQJ5-1]
GeneIDi327762.
KEGGimmu:327762.
UCSCiuc007fji.2. mouse. [Q6ZQJ5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129051 mRNA. Translation: BAC97861.1. Different initiation.
AK028381 mRNA. Translation: BAC25919.1.
BC025182 mRNA. Translation: AAH25182.1.
BC115716 mRNA. Translation: AAI15717.1.
CCDSiCCDS35923.1. [Q6ZQJ5-1]
RefSeqiNP_796346.2. NM_177372.3. [Q6ZQJ5-1]
UniGeneiMm.21492.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5EANX-ray2.36A1-1056[»]
5EAWX-ray3.00A/B1-1056[»]
5EAXX-ray3.05A/B1-1056[»]
ProteinModelPortaliQ6ZQJ5.
SMRiQ6ZQJ5. Positions 449-1035.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ6ZQJ5. 2 interactions.
STRINGi10090.ENSMUSP00000115750.

PTM databases

iPTMnetiQ6ZQJ5.

Proteomic databases

EPDiQ6ZQJ5.
MaxQBiQ6ZQJ5.
PaxDbiQ6ZQJ5.
PeptideAtlasiQ6ZQJ5.
PRIDEiQ6ZQJ5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000092462; ENSMUSP00000090119; ENSMUSG00000036875. [Q6ZQJ5-2]
ENSMUST00000131422; ENSMUSP00000115750; ENSMUSG00000036875. [Q6ZQJ5-1]
GeneIDi327762.
KEGGimmu:327762.
UCSCiuc007fji.2. mouse. [Q6ZQJ5-1]

Organism-specific databases

CTDi1763.
MGIiMGI:2443732. Dna2.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG1805. Eukaryota.
COG1112. LUCA.
GeneTreeiENSGT00780000122010.
HOGENOMiHOG000168456.
HOVERGENiHBG081456.
InParanoidiQ6ZQJ5.
KOiK10742.
OMAiEHESLCH.
OrthoDBiEOG7K6PT8.
PhylomeDBiQ6ZQJ5.
TreeFamiTF314903.

Enzyme and pathway databases

ReactomeiR-MMU-174437. Removal of the Flap Intermediate from the C-strand.
R-MMU-5685938. HDR through Single Strand Annealing (SSA).
R-MMU-5685942. HDR through Homologous Recombination (HRR).
R-MMU-5693554. Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
R-MMU-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates.
R-MMU-5693579. Homologous DNA Pairing and Strand Exchange.
R-MMU-5693607. Processing of DNA double-strand break ends.
R-MMU-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-MMU-6804756. Regulation of TP53 Activity through Phosphorylation.
R-MMU-69166. Removal of the Flap Intermediate.
R-MMU-69473. G2/M DNA damage checkpoint.

Miscellaneous databases

ChiTaRSiDna2. mouse.
PROiQ6ZQJ5.
SOURCEiSearch...

Gene expression databases

BgeeiQ6ZQJ5.
CleanExiMM_DNA2.
GenevisibleiQ6ZQJ5. MM.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR026851. Dna2.
IPR014808. DNA_replication_fac_Dna2_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10887:SF14. PTHR10887:SF14. 2 hits.
PfamiPF08696. Dna2. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "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."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Embryonic tail.
  2. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
  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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 263-1078 (ISOFORM 1).
    Strain: Czech II.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiDNA2_MOUSE
AccessioniPrimary (citable) accession number: Q6ZQJ5
Secondary accession number(s): Q14BM9, Q8BSZ0, Q8R3J3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 12, 2006
Last modified: July 6, 2016
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.