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Q9NDJ2

- DOM_DROME

UniProt

Q9NDJ2 - DOM_DROME

Protein

Helicase domino

Gene

dom

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 2 (13 Nov 2007)
      Previous versions | rss
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    Functioni

    Mediates the ATP-dependent exchange of unmodified histone H2AV for its phosphorylated and acetylated form H2AVK5acS138ph, leading to transcriptional regulation of selected genes by chromatin remodeling. Involved in Notch signaling. Represses E2F target genes. Required for somatic stem cell self-renewal but not for germline stem cell self-renewal. Involved in oogenesis.6 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi939 – 9468ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA binding Source: UniProtKB-KW
    3. DNA-dependent ATPase activity Source: FlyBase
    4. helicase activity Source: UniProtKB-KW
    5. protein binding Source: FlyBase

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. cell cycle Source: UniProtKB-KW
    3. chromatin organization Source: FlyBase
    4. dendrite guidance Source: FlyBase
    5. dendrite morphogenesis Source: FlyBase
    6. gene silencing Source: FlyBase
    7. hemopoiesis Source: FlyBase
    8. histone acetylation Source: UniProtKB
    9. histone exchange Source: UniProtKB
    10. instar larval or pupal development Source: FlyBase
    11. negative regulation of gene expression Source: FlyBase
    12. negative regulation of hemocyte proliferation Source: FlyBase
    13. neurogenesis Source: FlyBase
    14. oogenesis Source: FlyBase
    15. positive regulation of gene silencing by miRNA Source: FlyBase
    16. positive regulation of Notch signaling pathway Source: FlyBase
    17. regulation of alternative mRNA splicing, via spliceosome Source: FlyBase
    18. regulation of transcription, DNA-templated Source: UniProtKB-KW
    19. transcription, DNA-templated Source: UniProtKB-KW
    20. wing disc pattern formation Source: FlyBase

    Keywords - Molecular functioni

    Chromatin regulator, Developmental protein, Helicase, Hydrolase

    Keywords - Biological processi

    Cell cycle, Differentiation, Oogenesis, Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Helicase domino (EC:3.6.4.-)
    Gene namesi
    Name:dom
    ORF Names:CG9696
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0020306. dom.

    Subcellular locationi

    Nucleus 1 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

    1. histone acetyltransferase complex Source: FlyBase
    2. NuA4 histone acetyltransferase complex Source: UniProtKB
    3. nucleus Source: FlyBase

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 31983198Helicase dominoPRO_0000311238Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei656 – 6561Phosphoserine1 Publication
    Modified residuei664 – 6641Phosphoserine1 Publication
    Modified residuei666 – 6661Phosphoserine1 Publication
    Modified residuei729 – 7291Phosphothreonine1 Publication
    Modified residuei733 – 7331Phosphoserine1 Publication
    Modified residuei736 – 7361Phosphoserine1 Publication
    Modified residuei744 – 7441Phosphoserine1 Publication
    Modified residuei838 – 8381Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9NDJ2.

    Expressioni

    Tissue specificityi

    Isoform B is present at high levels in ovary, in follicle cells, nurse cells and oocyte. Isoform B is also present in germline and somatic stem cells from the germarium. Isoform A is undetectable in adult ovary (at protein level).2 Publications

    Developmental stagei

    Isoform A and isoform B are present in 0-12 hours embryonic extracts. During embryonic development, isoform A expression is restricted to the developing nervous system, whereas isoform B is ubiquitously expressed. During postembryonic development, isoform B is found in brain, imaginal disks, lymph glands and salivary glands and isoform A is found in some brain regions, photoreceptor cells and sensory organ precursors (at protein level).1 Publication

    Gene expression databases

    BgeeiQ9NDJ2.

    Interactioni

    Subunit structurei

    Component of the Tip60 chromatin-remodeling complex which contains Domino, Tip60, Tra1, Brd8, E(Pc), DMAP1, Pontin, Reptin, Ing3, Act87E, BAP55, Mrg15, MrgBP, Gas41 and YL-1.1 Publication

    Protein-protein interaction databases

    BioGridi69802. 20 interactions.
    DIPiDIP-60953N.
    IntActiQ9NDJ2. 1 interaction.
    STRINGi7227.FBpp0071529.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NDJ2.
    SMRiQ9NDJ2. Positions 889-1204, 1644-1829.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini507 – 57973HSAPROSITE-ProRule annotationAdd
    BLAST
    Domaini926 – 1091166Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1662 – 1812151Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini2136 – 220570Myb-likePROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili187 – 21226Sequence AnalysisAdd
    BLAST
    Coiled coili666 – 69631Sequence AnalysisAdd
    BLAST
    Coiled coili741 – 78444Sequence AnalysisAdd
    BLAST
    Coiled coili1951 – 199646Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi95 – 995Poly-Gln
    Compositional biasi101 – 11111Poly-AlaAdd
    BLAST
    Compositional biasi425 – 4284Poly-Gly
    Compositional biasi1242 – 12498Poly-Leu
    Compositional biasi2322 – 3188867Gln-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
    Contains 1 HSA domain.PROSITE-ProRule annotation
    Contains 1 Myb-like domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG0553.
    GeneTreeiENSGT00530000063427.
    InParanoidiQ9NDJ2.
    KOiK11320.
    OMAiRYETHIQ.
    OrthoDBiEOG79CXXJ.
    PhylomeDBiQ9NDJ2.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR013999. HAS_subgr.
    IPR014012. Helicase/SANT-assoc_DNA-bd.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR017877. Myb-like_dom.
    IPR027417. P-loop_NTPase.
    IPR000330. SNF2_N.
    [Graphical view]
    PfamiPF00271. Helicase_C. 1 hit.
    PF07529. HSA. 1 hit.
    PF00176. SNF2_N. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    SM00573. HSA. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 3 hits.
    PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51204. HSA. 1 hit.
    PS50090. MYB_LIKE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform A (identifier: Q9NDJ2-1) [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

    MNEGNSAGGG HEGLSPAPPA VPDRVTPHST EISVAPANST STTVRAAGSV     50
    GAALPATRHH QHIATQVKGI ASSSSKQQKQ LASAQLPVPL SPLPQQQQQT 100
    AEATAAAAAP AHSNVSVSSS TIEASVLPPQ AKRQRLDDNE DRTSAASIVG 150
    PAESSNIVSS LLPASVASSS EVGGLSSTAL QDLNALKKRI LQQKLQILRN 200
    LKERHLENVS EYFYLQNGGS MMDYPAWRKK TPTPQFISYS NANRIDQLIH 250
    EDKPSTSAAA AAAQNQKYTT QQTDSVESSL VSGIGTGATK GAPLDGNISN 300
    STVKTNTQSQ VPSKIGSFTE STPAATESNS STTVPGTATS GAATSTSATS 350
    AEASGNVLAV EAEIKIPAVG ATPVAISTKL PAAVVQLTQQ GGTPLLPCNT 400
    SAGSTALRRP QGQNNASSGS AAASGGGGSL TPTPLYTGNG PAALGGSGGL 450
    TPGTPTSGSL LSPALGGGSG TPNSAAQEFS FKAKQEVYVM QRISELQREG 500
    LWTERRLPKL QEPSRPKAHW DYLLEEMVWL AADFAQERKW KKNAAKKCAK 550
    MVQKYFQDKA TAAQRAEKAQ ELQLKRVASF IAREVKSFWS NVEKLVEYKH 600
    QTKIEEKRKQ ALDQHLSFIV DQTEKFSQQL VEGMNKSVAD TPSLNSSRLT 650
    SPKRESDDDF RPESGSEDDE ETIAKAEEDA ADVKEEVTAL AKESEMDFDD 700
    FLNDLPPGYL ENRDKLMKEE QSSAIKTETP DDSDDSEFEA KEASDDDENT 750
    ISKQEEAEQE IDHKKEIDEL EADNDLSVEQ LLAKYKSEQP PSPKRRKLAP 800
    RDPELDSDDD STAVDSTEES EDAATEDEED LSTVKTDTDM EEQDEQEDGL 850
    KSLMADADAT SGAAGSGSTA GASGNKDDML NDAAALAESL QPKGNTLSST 900
    NVVTPVPFLL KHSLREYQHI GLDWLVTMNE RKLNGILADE MGLGKTIQTI 950
    ALLAHLACAK GNWGPHLIVV PSSVMLNWEM EFKKWCPGFK ILTYYGSQKE 1000
    RKLKRVGWTK PNAFHVCITS YKLVVQDQQS FRRKKWKYLI LDEAQNIKNF 1050
    KSQRWQLLLN FSTERRLLLT GTPLQNDLME LWSLMHFLMP YVFSSHREFK 1100
    EWFSNPMTGM IEGNMEYNET LITRLHKVIR PFLLRRLKKE VEKQMPKKYE 1150
    HVITCRLSNR QRYLYEDFMS RAKTRETLQT GNLLSVINVL MQLRKVCNHP 1200
    NMFEARPTIS PFQMDGITFH TPRLVCDIME YDPFTQINLE TLNLLLLHLE 1250
    QTMTAYVSHK SRLLAPPRKL IEDIDTAPLP APRCPNGKYR FHIRVRSAEL 1300
    AQRIKLNAVK VGASPAMRLE GSKIMPMRNL LPSGRVLKRV SASINPVNMA 1350
    LKPVVINSVV TTTSSSTTAS SPTGALSVLS NSKLLGARSQ INAPTPAKVA 1400
    KTMQDGKPFF YLTPATNSGA AGARLTLTSK TTASASTTTS RTTVTASTTS 1450
    GQQLIRDPIV KDLATHVKST VQKQSIANGK TEPEEETEAE DPYKVQELIQ 1500
    MRKEQRLAAL KRMAMINRRR TDATPIYGED CREAIQRCMQ ATRSLKRSTW 1550
    QTRGYANCCT AMAHRNGWSL NHLLKSFEER CADLKPVFAN FVIYVPSVCA 1600
    PRIRRYVQNL SSTHWQHEQR IENIVDQALR PKLALLHPII SEMTTKFPDP 1650
    RLIQYDCGKL QTMDRLLRQL KVNGHRVLIF TQMTKMLDVL EAFLNYHGHI 1700
    YLRLDGSTRV EQRQILMERF NGDKRIFCFI LSTRSGGVGI NLTGADTVIF 1750
    YDSDWNPTMD AQAQDRCHRI GQTRDVHIYR LVSERTIEVN ILKKANQKRM 1800
    LSDMAIEGGN FTTTYFKSST IKDLFTMEQS EQDESSQEKS ENKDRIVATT 1850
    TLSDTPSTVV ETEKQSLRAF EHALAAAEDE QDVQATKTAK AEVAADLAEF 1900
    DENIPIATED PNAEGGPQVE LSKADLEMQN LVKQLSPIER YAMRFVEETG 1950
    AAWTAEQLRA AEAELEAQKR EWEANRLAAM HKEEELLKQE TEAEEMLTYS 2000
    RKDSSNQVWI SRNTMEQMPM WCPPTPPQDN DNDIYIDYSL SFMYELEPIA 2050
    ETDLPPVYVR KEHKRSRTDA GYDGSRRPNK MRREDNYVPP RSLFDRPTPQ 2100
    LARLRRELKS QRFRGSFKPN MPIPGLKPQL PTKPLTEPEA MAEWCVFEDM 2150
    AILHVLVNLQ GLPCSLMLLS PGQTPNWDLV SEMVNFCSKT YRSARQCRWR 2200
    YETHIQPREE GKVVESPKKQ KKLKPTLRTE YLKSPLRYLR TTQLYVSDNN 2250
    ASFYKTMRSR FDSIKTAYLK KAPPPKRQFS APSLMNPKHM EVLQEFGILN 2300
    YDQPVSPQNI AAMKANKIRE KQRGQQMSQP PVGVGVVQQM QQQSQQQQQP 2350
    APPPLPQQQQ PQQVVQQVQQ QQQQQQQQQQ QQVVQQQLPT VSNVQQTLPV 2400
    QQTVELVQQQ PTTTTTVAVP AAGGQLQQLQ IQHLTSSNVS PGQQTAILLH 2450
    QPQQQLRTHP GQGGQSNTQQ LVKTIVGTSS SLTAGQLQQL AQQSAVASGG 2500
    QSSVSVVLTT PVQTLPSVVQ PQIGSGAQIV SISSQTLPVN SSPQLGSIVQ 2550
    TQSLPQVVSV STLPTVGTVL TTTANQPQQQ HQTTAVTTLN TTMLRGQRIV 2600
    STAAGNTLQQ RTTAGGQSIV SMPNLGQGAS PSQFQTQLRL AAVPTSPATQ 2650
    TTQLVTTKGI PVSALQQGGK TTVIPVTQQS GGAHIQLYRQ RSLKVLQTTT 2700
    QAVPSGSAGA TGATANLVQA GGTIIQASNM ATHVTSQKVA VSGMPGTSTT 2750
    VQAGNVVSSV QMHGQARTQF IKQMAAGKQQ LQRQVVSADG TTTTTAAGDM 2800
    LLVKRHNILA AQKAQQASGA LFTTTTGQQQ QQQQQQGQLP VAGQPQQVTQ 2850
    HQIASLVKAS TAAAASGSSV NAGGVTVSAT NPTVQAGSVN MTLPQLKPGS 2900
    QIKVTMPNQM RHLQMQQQLT MPRKISRMTQ LVSASGQPTA TNIITTTGPQ 2950
    QQQQGVTVSG GGTLPTVASQ QQQQQHQQKV GGGNSVQAQL LHIQNTKGLS 3000
    NSVTMQQIQQ VMRSGQQGTL ATTNLVLGKT SVGRVIPVSV ASQANQRQTI 3050
    QVVSAASAQA LAAGNLRTHV AGPSIASTLK VAAPGSAGGQ TTQQTLIAAL 3100
    QHNQRQNASP VRLQTTAGGN LLAVVQQQQQ QQHTSIAGPT AGPAEVMTIT 3150
    QTTTTLPTVG SLQQQQQQQQ QQGGISQPTT QQVRKLVQKK ILIRSEKE 3198
    Length:3,198
    Mass (Da):350,239
    Last modified:November 13, 2007 - v2
    Checksum:iE65C3E86E1E64AB7
    GO
    Isoform B (identifier: Q9NDJ2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2009-3198: WISRNTMEQM...KKILIRSEKE → NTKTDSNSNK...GNASSSGTAR

    Show »
    Length:2,497
    Mass (Da):274,615
    Checksum:i4A500F08369326EC
    GO

    Sequence cautioni

    The sequence AAL13882.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1598 – 15981V → G in AAF82185. (PubMed:11262242)Curated
    Sequence conflicti1598 – 15981V → G in AAK53539. (PubMed:11262242)Curated
    Sequence conflicti1611 – 16122SS → LL in AAF82185. (PubMed:11262242)Curated
    Sequence conflicti1611 – 16122SS → LL in AAK53539. (PubMed:11262242)Curated
    Sequence conflicti1619 – 16191Q → P in AAF82185. (PubMed:11262242)Curated
    Sequence conflicti1619 – 16191Q → P in AAK53539. (PubMed:11262242)Curated
    Sequence conflicti1631 – 16311P → A in AAF82185. (PubMed:11262242)Curated
    Sequence conflicti1631 – 16311P → A in AAK53539. (PubMed:11262242)Curated
    Sequence conflicti2157 – 21571V → G in AAF82185. (PubMed:11262242)Curated
    Sequence conflicti2198 – 21981R → P in AAF82185. (PubMed:11262242)Curated
    Sequence conflicti2340 – 23401M → MQQQSQQ in AAF82185. (PubMed:11262242)Curated
    Sequence conflicti2369 – 23713Missing in AAF82185. (PubMed:11262242)Curated
    Sequence conflicti2514 – 25141T → S in AAF82185. (PubMed:11262242)Curated
    Isoform B (identifier: Q9NDJ2-2)
    Sequence conflicti2127 – 21271P → A in AAK53539. (PubMed:11262242)Curated
    Sequence conflicti2174 – 21741K → N in AAK53539. (PubMed:11262242)Curated
    Sequence conflicti2180 – 21801N → T in AAK53539. (PubMed:11262242)Curated
    Sequence conflicti2222 – 22221E → D in AAK53539. (PubMed:11262242)Curated
    Sequence conflicti2229 – 22291E → D in AAK53539. (PubMed:11262242)Curated
    Sequence conflicti2287 – 22871G → E in AAK53539. (PubMed:11262242)Curated
    Sequence conflicti2471 – 24711V → G in AAK53539. (PubMed:11262242)Curated
    Sequence conflicti2474 – 24741A → T in AAK53539. (PubMed:11262242)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2009 – 31981190WISRN…RSEKE → NTKTDSNSNKRRLVRENRRN SAQKLSRSVSSHSTGSNNKN SKSATTRGNSQNSLNQTVPV GSGISRVNRTGAGVSSSSRG KSNSTKSTGKGTDAAPQVRR QTRLHSLGAVNMASARTPPT RKTTRTALAASAAASTLEDA SLIVEERPKRQSANIAMSKM MKTPFKQNVPSNISIKTTPP KRGRRDSVAAAATRSKLLER RATIAAPLKHMDDESDQDEE EQEEQESEEDTEGEEANATV DDDEEGEEELASLDEETIQT GSQTNDEEDDDEEEVGEEGM VDIDTEDSEADVKSSSTYGT AADGKPEEAESLDGWDAHDQ VQDTTMTSSTYYNVSEESDT DEHHDSKAEAKEPPQNSDKS DESEAVGHTPRTRSRGTVKI NLWTLDVSPVANALNKSSAN RSLKKAPRTESTPKESQSEP RRKITQPKLPKKEETNNKSN SNIGTLHRWISKSPRVMLRS TPVTAASASSSAAVSGVSGG NASSSGTAR in isoform B. 1 PublicationVSP_029443Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF076776 mRNA. Translation: AAF82185.1.
    AF254373 mRNA. Translation: AAK53539.1.
    AE013599 Genomic DNA. Translation: AAM70871.1.
    AE013599 Genomic DNA. Translation: AAM70872.2.
    AY058653 mRNA. Translation: AAL13882.1. Different initiation.
    RefSeqiNP_524833.2. NM_080094.3. [Q9NDJ2-1]
    NP_788424.1. NM_176244.2. [Q9NDJ2-2]
    UniGeneiDm.7802.

    Genome annotation databases

    EnsemblMetazoaiFBtr0071603; FBpp0071529; FBgn0020306. [Q9NDJ2-1]
    GeneIDi45655.
    KEGGidme:Dmel_CG9696.
    UCSCiCG9696-RA. d. melanogaster. [Q9NDJ2-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF076776 mRNA. Translation: AAF82185.1 .
    AF254373 mRNA. Translation: AAK53539.1 .
    AE013599 Genomic DNA. Translation: AAM70871.1 .
    AE013599 Genomic DNA. Translation: AAM70872.2 .
    AY058653 mRNA. Translation: AAL13882.1 . Different initiation.
    RefSeqi NP_524833.2. NM_080094.3. [Q9NDJ2-1 ]
    NP_788424.1. NM_176244.2. [Q9NDJ2-2 ]
    UniGenei Dm.7802.

    3D structure databases

    ProteinModelPortali Q9NDJ2.
    SMRi Q9NDJ2. Positions 889-1204, 1644-1829.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 69802. 20 interactions.
    DIPi DIP-60953N.
    IntActi Q9NDJ2. 1 interaction.
    STRINGi 7227.FBpp0071529.

    Proteomic databases

    PaxDbi Q9NDJ2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0071603 ; FBpp0071529 ; FBgn0020306 . [Q9NDJ2-1 ]
    GeneIDi 45655.
    KEGGi dme:Dmel_CG9696.
    UCSCi CG9696-RA. d. melanogaster. [Q9NDJ2-1 ]

    Organism-specific databases

    CTDi 45655.
    FlyBasei FBgn0020306. dom.

    Phylogenomic databases

    eggNOGi COG0553.
    GeneTreei ENSGT00530000063427.
    InParanoidi Q9NDJ2.
    KOi K11320.
    OMAi RYETHIQ.
    OrthoDBi EOG79CXXJ.
    PhylomeDBi Q9NDJ2.

    Miscellaneous databases

    GenomeRNAii 45655.
    NextBioi 838265.
    PROi Q9NDJ2.

    Gene expression databases

    Bgeei Q9NDJ2.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR013999. HAS_subgr.
    IPR014012. Helicase/SANT-assoc_DNA-bd.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR017877. Myb-like_dom.
    IPR027417. P-loop_NTPase.
    IPR000330. SNF2_N.
    [Graphical view ]
    Pfami PF00271. Helicase_C. 1 hit.
    PF07529. HSA. 1 hit.
    PF00176. SNF2_N. 1 hit.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    SM00573. HSA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 3 hits.
    PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51204. HSA. 1 hit.
    PS50090. MYB_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The domino gene of Drosophila encodes novel members of the SWI2/SNF2 family of DNA-dependent ATPases, which contribute to the silencing of homeotic genes."
      Ruhf M.-L., Braun A., Papoulas O., Tamkun J.W., Randsholt N., Meister M.
      Development 128:1429-1441(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION.
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING (ISOFORMS AND B).
      Strain: Berkeley.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 782-2046 (ISOFORM A).
      Strain: Berkeley.
      Tissue: Embryo.
    5. "Acetylation by Tip60 is required for selective histone variant exchange at DNA lesions."
      Kusch T., Florens L., Macdonald W.H., Swanson S.K., Glaser R.L., Yates J.R. III, Abmayr S.M., Washburn M.P., Workman J.L.
      Science 306:2084-2087(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE TIP60 COMPLEX.
    6. "Human SRCAP and Drosophila melanogaster DOM are homologs that function in the notch signaling pathway."
      Eissenberg J.C., Wong M., Chrivia J.C.
      Mol. Cell. Biol. 25:6559-6569(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Stem cell self-renewal controlled by chromatin remodeling factors."
      Xi R., Xie T.
      Science 310:1487-1489(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    8. "Nipped-A, the Tra1/TRRAP subunit of the Drosophila SAGA and Tip60 complexes, has multiple roles in Notch signaling during wing development."
      Gause M., Eissenberg J.C., Macrae A.F., Dorsett M., Misulovin Z., Dorsett D.
      Mol. Cell. Biol. 26:2347-2359(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "A genome-wide RNA interference screen identifies putative chromatin regulators essential for E2F repression."
      Lu J., Ruhf M.-L., Perrimon N., Leder P.
      Proc. Natl. Acad. Sci. U.S.A. 104:9381-9386(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Phosphoproteome analysis of Drosophila melanogaster embryos."
      Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
      J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-656; SER-664; SER-666; THR-729; SER-733; SER-736; SER-744 AND THR-838, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiDOM_DROME
    AccessioniPrimary (citable) accession number: Q9NDJ2
    Secondary accession number(s): Q7YZ94
    , Q95TN6, Q968U6, Q9I7V8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: November 13, 2007
    Last modified: October 1, 2014
    This is version 99 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3