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Q9NDJ2 (DOM_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length3198 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9

Subunit structure

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. Ref.5

Subcellular location

Nucleus Ref.1.

Tissue specificity

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). Ref.1 Ref.7

Developmental stage

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). Ref.1

Sequence similarities

Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Contains 1 HSA domain.

Contains 1 Myb-like domain.

Sequence caution

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

Ontologies

Keywords
   Biological processCell cycle
Differentiation
Oogenesis
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionChromatin regulator
Developmental protein
Helicase
Hydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from sequence or structural similarity Ref.1. Source: GOC

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin organization

Inferred from mutant phenotype Ref.1. Source: FlyBase

dendrite guidance

Inferred from mutant phenotype PubMed 21284845. Source: FlyBase

dendrite morphogenesis

Inferred from mutant phenotype PubMed 23977298. Source: FlyBase

gene silencing

Inferred from genetic interaction Ref.1. Source: FlyBase

hemopoiesis

Traceable author statement PubMed 14602069PubMed 15199954. Source: FlyBase

histone acetylation

Inferred from direct assay Ref.5. Source: UniProtKB

histone exchange

Inferred from direct assay Ref.5. Source: UniProtKB

instar larval or pupal development

Inferred from mutant phenotype Ref.1. Source: FlyBase

negative regulation of gene expression

Inferred from mutant phenotype Ref.9. Source: FlyBase

negative regulation of hemocyte proliferation

Traceable author statement PubMed 14602069. Source: FlyBase

neurogenesis

Inferred from mutant phenotype PubMed 21549331. Source: FlyBase

oogenesis

Inferred from mutant phenotype Ref.1. Source: FlyBase

positive regulation of Notch signaling pathway

Inferred from genetic interaction Ref.8. Source: FlyBase

positive regulation of gene silencing by miRNA

Inferred from mutant phenotype PubMed 22540035. Source: FlyBase

regulation of alternative mRNA splicing, via spliceosome

Inferred from mutant phenotype PubMed 15492211. Source: FlyBase

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

wing disc pattern formation

Inferred from genetic interaction Ref.8. Source: FlyBase

   Cellular_componentNuA4 histone acetyltransferase complex

Inferred from direct assay Ref.5. Source: UniProtKB

histone acetyltransferase complex

Inferred from physical interaction Ref.5. Source: FlyBase

nucleus

Inferred from direct assay Ref.1Ref.5. Source: FlyBase

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA-dependent ATPase activity

Inferred from sequence or structural similarity Ref.1. Source: FlyBase

helicase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: Q9NDJ2-1)

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 B (identifier: Q9NDJ2-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 31983198Helicase domino
PRO_0000311238

Regions

Domain507 – 57973HSA
Domain926 – 1091166Helicase ATP-binding
Domain1662 – 1812151Helicase C-terminal
Domain2136 – 220570Myb-like
Nucleotide binding939 – 9468ATP By similarity
Coiled coil187 – 21226 Potential
Coiled coil666 – 69631 Potential
Coiled coil741 – 78444 Potential
Coiled coil1951 – 199646 Potential
Compositional bias95 – 995Poly-Gln
Compositional bias101 – 11111Poly-Ala
Compositional bias425 – 4284Poly-Gly
Compositional bias1242 – 12498Poly-Leu
Compositional bias2322 – 3188867Gln-rich

Amino acid modifications

Modified residue6561Phosphoserine Ref.10
Modified residue6641Phosphoserine Ref.10
Modified residue6661Phosphoserine Ref.10
Modified residue7291Phosphothreonine Ref.10
Modified residue7331Phosphoserine Ref.10
Modified residue7361Phosphoserine Ref.10
Modified residue7441Phosphoserine Ref.10
Modified residue8381Phosphothreonine Ref.10

Natural variations

Alternative sequence2009 – 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.
VSP_029443

Experimental info

Sequence conflict15981V → G in AAF82185. Ref.1
Sequence conflict15981V → G in AAK53539. Ref.1
Sequence conflict1611 – 16122SS → LL in AAF82185. Ref.1
Sequence conflict1611 – 16122SS → LL in AAK53539. Ref.1
Sequence conflict16191Q → P in AAF82185. Ref.1
Sequence conflict16191Q → P in AAK53539. Ref.1
Sequence conflict16311P → A in AAF82185. Ref.1
Sequence conflict16311P → A in AAK53539. Ref.1
Sequence conflict21571V → G in AAF82185. Ref.1
Sequence conflict21981R → P in AAF82185. Ref.1
Sequence conflict23401M → MQQQSQQ in AAF82185. Ref.1
Sequence conflict2369 – 23713Missing in AAF82185. Ref.1
Sequence conflict25141T → S in AAF82185. Ref.1
Isoform B:
Sequence conflict21271P → A in AAK53539. Ref.1
Sequence conflict21741K → N in AAK53539. Ref.1
Sequence conflict21801N → T in AAK53539. Ref.1
Sequence conflict22221E → D in AAK53539. Ref.1
Sequence conflict22291E → D in AAK53539. Ref.1
Sequence conflict22871G → E in AAK53539. Ref.1
Sequence conflict24711V → G in AAK53539. Ref.1
Sequence conflict24741A → T in AAK53539. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified November 13, 2007. Version 2.
Checksum: E65C3E86E1E64AB7

FASTA3,198350,239
        10         20         30         40         50         60 
MNEGNSAGGG HEGLSPAPPA VPDRVTPHST EISVAPANST STTVRAAGSV GAALPATRHH 

        70         80         90        100        110        120 
QHIATQVKGI ASSSSKQQKQ LASAQLPVPL SPLPQQQQQT AEATAAAAAP AHSNVSVSSS 

       130        140        150        160        170        180 
TIEASVLPPQ AKRQRLDDNE DRTSAASIVG PAESSNIVSS LLPASVASSS EVGGLSSTAL 

       190        200        210        220        230        240 
QDLNALKKRI LQQKLQILRN LKERHLENVS EYFYLQNGGS MMDYPAWRKK TPTPQFISYS 

       250        260        270        280        290        300 
NANRIDQLIH EDKPSTSAAA AAAQNQKYTT QQTDSVESSL VSGIGTGATK GAPLDGNISN 

       310        320        330        340        350        360 
STVKTNTQSQ VPSKIGSFTE STPAATESNS STTVPGTATS GAATSTSATS AEASGNVLAV 

       370        380        390        400        410        420 
EAEIKIPAVG ATPVAISTKL PAAVVQLTQQ GGTPLLPCNT SAGSTALRRP QGQNNASSGS 

       430        440        450        460        470        480 
AAASGGGGSL TPTPLYTGNG PAALGGSGGL TPGTPTSGSL LSPALGGGSG TPNSAAQEFS 

       490        500        510        520        530        540 
FKAKQEVYVM QRISELQREG LWTERRLPKL QEPSRPKAHW DYLLEEMVWL AADFAQERKW 

       550        560        570        580        590        600 
KKNAAKKCAK MVQKYFQDKA TAAQRAEKAQ ELQLKRVASF IAREVKSFWS NVEKLVEYKH 

       610        620        630        640        650        660 
QTKIEEKRKQ ALDQHLSFIV DQTEKFSQQL VEGMNKSVAD TPSLNSSRLT SPKRESDDDF 

       670        680        690        700        710        720 
RPESGSEDDE ETIAKAEEDA ADVKEEVTAL AKESEMDFDD FLNDLPPGYL ENRDKLMKEE 

       730        740        750        760        770        780 
QSSAIKTETP DDSDDSEFEA KEASDDDENT ISKQEEAEQE IDHKKEIDEL EADNDLSVEQ 

       790        800        810        820        830        840 
LLAKYKSEQP PSPKRRKLAP RDPELDSDDD STAVDSTEES EDAATEDEED LSTVKTDTDM 

       850        860        870        880        890        900 
EEQDEQEDGL KSLMADADAT SGAAGSGSTA GASGNKDDML NDAAALAESL QPKGNTLSST 

       910        920        930        940        950        960 
NVVTPVPFLL KHSLREYQHI GLDWLVTMNE RKLNGILADE MGLGKTIQTI ALLAHLACAK 

       970        980        990       1000       1010       1020 
GNWGPHLIVV PSSVMLNWEM EFKKWCPGFK ILTYYGSQKE RKLKRVGWTK PNAFHVCITS 

      1030       1040       1050       1060       1070       1080 
YKLVVQDQQS FRRKKWKYLI LDEAQNIKNF KSQRWQLLLN FSTERRLLLT GTPLQNDLME 

      1090       1100       1110       1120       1130       1140 
LWSLMHFLMP YVFSSHREFK EWFSNPMTGM IEGNMEYNET LITRLHKVIR PFLLRRLKKE 

      1150       1160       1170       1180       1190       1200 
VEKQMPKKYE HVITCRLSNR QRYLYEDFMS RAKTRETLQT GNLLSVINVL MQLRKVCNHP 

      1210       1220       1230       1240       1250       1260 
NMFEARPTIS PFQMDGITFH TPRLVCDIME YDPFTQINLE TLNLLLLHLE QTMTAYVSHK 

      1270       1280       1290       1300       1310       1320 
SRLLAPPRKL IEDIDTAPLP APRCPNGKYR FHIRVRSAEL AQRIKLNAVK VGASPAMRLE 

      1330       1340       1350       1360       1370       1380 
GSKIMPMRNL LPSGRVLKRV SASINPVNMA LKPVVINSVV TTTSSSTTAS SPTGALSVLS 

      1390       1400       1410       1420       1430       1440 
NSKLLGARSQ INAPTPAKVA KTMQDGKPFF YLTPATNSGA AGARLTLTSK TTASASTTTS 

      1450       1460       1470       1480       1490       1500 
RTTVTASTTS GQQLIRDPIV KDLATHVKST VQKQSIANGK TEPEEETEAE DPYKVQELIQ 

      1510       1520       1530       1540       1550       1560 
MRKEQRLAAL KRMAMINRRR TDATPIYGED CREAIQRCMQ ATRSLKRSTW QTRGYANCCT 

      1570       1580       1590       1600       1610       1620 
AMAHRNGWSL NHLLKSFEER CADLKPVFAN FVIYVPSVCA PRIRRYVQNL SSTHWQHEQR 

      1630       1640       1650       1660       1670       1680 
IENIVDQALR PKLALLHPII SEMTTKFPDP RLIQYDCGKL QTMDRLLRQL KVNGHRVLIF 

      1690       1700       1710       1720       1730       1740 
TQMTKMLDVL EAFLNYHGHI YLRLDGSTRV EQRQILMERF NGDKRIFCFI LSTRSGGVGI 

      1750       1760       1770       1780       1790       1800 
NLTGADTVIF YDSDWNPTMD AQAQDRCHRI GQTRDVHIYR LVSERTIEVN ILKKANQKRM 

      1810       1820       1830       1840       1850       1860 
LSDMAIEGGN FTTTYFKSST IKDLFTMEQS EQDESSQEKS ENKDRIVATT TLSDTPSTVV 

      1870       1880       1890       1900       1910       1920 
ETEKQSLRAF EHALAAAEDE QDVQATKTAK AEVAADLAEF DENIPIATED PNAEGGPQVE 

      1930       1940       1950       1960       1970       1980 
LSKADLEMQN LVKQLSPIER YAMRFVEETG AAWTAEQLRA AEAELEAQKR EWEANRLAAM 

      1990       2000       2010       2020       2030       2040 
HKEEELLKQE TEAEEMLTYS RKDSSNQVWI SRNTMEQMPM WCPPTPPQDN DNDIYIDYSL 

      2050       2060       2070       2080       2090       2100 
SFMYELEPIA ETDLPPVYVR KEHKRSRTDA GYDGSRRPNK MRREDNYVPP RSLFDRPTPQ 

      2110       2120       2130       2140       2150       2160 
LARLRRELKS QRFRGSFKPN MPIPGLKPQL PTKPLTEPEA MAEWCVFEDM AILHVLVNLQ 

      2170       2180       2190       2200       2210       2220 
GLPCSLMLLS PGQTPNWDLV SEMVNFCSKT YRSARQCRWR YETHIQPREE GKVVESPKKQ 

      2230       2240       2250       2260       2270       2280 
KKLKPTLRTE YLKSPLRYLR TTQLYVSDNN ASFYKTMRSR FDSIKTAYLK KAPPPKRQFS 

      2290       2300       2310       2320       2330       2340 
APSLMNPKHM EVLQEFGILN YDQPVSPQNI AAMKANKIRE KQRGQQMSQP PVGVGVVQQM 

      2350       2360       2370       2380       2390       2400 
QQQSQQQQQP APPPLPQQQQ PQQVVQQVQQ QQQQQQQQQQ QQVVQQQLPT VSNVQQTLPV 

      2410       2420       2430       2440       2450       2460 
QQTVELVQQQ PTTTTTVAVP AAGGQLQQLQ IQHLTSSNVS PGQQTAILLH QPQQQLRTHP 

      2470       2480       2490       2500       2510       2520 
GQGGQSNTQQ LVKTIVGTSS SLTAGQLQQL AQQSAVASGG QSSVSVVLTT PVQTLPSVVQ 

      2530       2540       2550       2560       2570       2580 
PQIGSGAQIV SISSQTLPVN SSPQLGSIVQ TQSLPQVVSV STLPTVGTVL TTTANQPQQQ 

      2590       2600       2610       2620       2630       2640 
HQTTAVTTLN TTMLRGQRIV STAAGNTLQQ RTTAGGQSIV SMPNLGQGAS PSQFQTQLRL 

      2650       2660       2670       2680       2690       2700 
AAVPTSPATQ TTQLVTTKGI PVSALQQGGK TTVIPVTQQS GGAHIQLYRQ RSLKVLQTTT 

      2710       2720       2730       2740       2750       2760 
QAVPSGSAGA TGATANLVQA GGTIIQASNM ATHVTSQKVA VSGMPGTSTT VQAGNVVSSV 

      2770       2780       2790       2800       2810       2820 
QMHGQARTQF IKQMAAGKQQ LQRQVVSADG TTTTTAAGDM LLVKRHNILA AQKAQQASGA 

      2830       2840       2850       2860       2870       2880 
LFTTTTGQQQ QQQQQQGQLP VAGQPQQVTQ HQIASLVKAS TAAAASGSSV NAGGVTVSAT 

      2890       2900       2910       2920       2930       2940 
NPTVQAGSVN MTLPQLKPGS QIKVTMPNQM RHLQMQQQLT MPRKISRMTQ LVSASGQPTA 

      2950       2960       2970       2980       2990       3000 
TNIITTTGPQ QQQQGVTVSG GGTLPTVASQ QQQQQHQQKV GGGNSVQAQL LHIQNTKGLS 

      3010       3020       3030       3040       3050       3060 
NSVTMQQIQQ VMRSGQQGTL ATTNLVLGKT SVGRVIPVSV ASQANQRQTI QVVSAASAQA 

      3070       3080       3090       3100       3110       3120 
LAAGNLRTHV AGPSIASTLK VAAPGSAGGQ TTQQTLIAAL QHNQRQNASP VRLQTTAGGN 

      3130       3140       3150       3160       3170       3180 
LLAVVQQQQQ QQHTSIAGPT AGPAEVMTIT QTTTTLPTVG SLQQQQQQQQ QQGGISQPTT 

      3190 
QQVRKLVQKK ILIRSEKE 

« Hide

Isoform B [UniParc].

Checksum: 4A500F08369326EC
Show »

FASTA2,497274,615

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING (ISOFORMS AND B).
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_524833.2. NM_080094.3.
NP_788424.1. NM_176244.2.
UniGeneDm.7802.

3D structure databases

ProteinModelPortalQ9NDJ2.
SMRQ9NDJ2. Positions 889-1204, 1644-1829.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid69802. 20 interactions.
IntActQ9NDJ2. 1 interaction.
STRING7227.FBpp0071529.

Proteomic databases

PaxDbQ9NDJ2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0071603; FBpp0071529; FBgn0020306. [Q9NDJ2-1]
GeneID45655.
KEGGdme:Dmel_CG9696.
UCSCCG9696-RA. d. melanogaster. [Q9NDJ2-1]

Organism-specific databases

CTD45655.
FlyBaseFBgn0020306. dom.

Phylogenomic databases

eggNOGCOG0553.
GeneTreeENSGT00530000063427.
InParanoidQ9NDJ2.
KOK11320.
OMARYETHIQ.
OrthoDBEOG79CXXJ.
PhylomeDBQ9NDJ2.

Gene expression databases

BgeeQ9NDJ2.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR013999. 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]
PfamPF00271. Helicase_C. 1 hit.
PF07529. HSA. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00573. HSA. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 3 hits.
PROSITEPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51204. HSA. 1 hit.
PS50090. MYB_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi45655.
NextBio838265.
PROQ9NDJ2.

Entry information

Entry nameDOM_DROME
AccessionPrimary (citable) accession number: Q9NDJ2
Secondary accession number(s): Q7YZ94 expand/collapse secondary AC list , Q95TN6, Q968U6, Q9I7V8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 13, 2007
Last modified: April 16, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase