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Protein

Dosage compensation regulator

Gene

mle

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required in males for dosage compensation of X chromosome linked genes. Mle, msl-1 and msl-3 are colocalized on X chromosome. Each of the msl proteins requires all the other msls for wild-type X-chromosome binding. Probably unwinds double-stranded DNA and RNA in a 3' to 5' direction.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi407 – 4148ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent helicase activity Source: FlyBase
  • ATP-dependent RNA helicase activity Source: GO_Central
  • chromatin binding Source: FlyBase
  • double-stranded RNA binding Source: FlyBase
  • helicase activity Source: FlyBase
  • poly(A) RNA binding Source: GO_Central
  • RNA binding Source: FlyBase
  • RNA helicase activity Source: FlyBase

GO - Biological processi

  • axon extension Source: FlyBase
  • determination of adult lifespan Source: FlyBase
  • dosage compensation Source: FlyBase
  • dosage compensation by hyperactivation of X chromosome Source: FlyBase
  • dosage compensation complex assembly involved in dosage compensation by hyperactivation of X chromosome Source: FlyBase
  • male courtship behavior, veined wing generated song production Source: FlyBase
  • positive regulation of heterochromatin assembly Source: FlyBase
  • positive regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • RNA processing Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-DME-1810476. RIP-mediated NFkB activation via ZBP1.
R-DME-3134963. DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
R-DME-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-DME-72163. mRNA Splicing - Major Pathway.
R-DME-933542. TRAF6 mediated NF-kB activation.

Names & Taxonomyi

Protein namesi
Recommended name:
Dosage compensation regulator (EC:3.6.4.13)
Alternative name(s):
ATP-dependent RNA helicase mle
Protein male-less
Protein maleless
Protein no action potential
Gene namesi
Name:mleImported
Synonyms:napImported
ORF Names:CG11680Imported
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0002774. mle.

Subcellular locationi

  • Nucleus 1 Publication
  • Chromosome 1 Publication

  • Note: Mle is associated with hundreds of discrete sites along the length of the X chromosome in males and not in females, and is associated with 30-40 autosomal sites in both sexes.

GO - Cellular componenti

  • chromatin Source: FlyBase
  • chromosome Source: FlyBase
  • MSL complex Source: FlyBase
  • nuclear chromosome Source: FlyBase
  • nucleus Source: FlyBase
  • polytene chromosome Source: FlyBase
  • X chromosome Source: FlyBase
  • X chromosome located dosage compensation complex, transcription activating Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12931293Dosage compensation regulatorPRO_0000055181Add
BLAST

Proteomic databases

PaxDbiP24785.
PRIDEiP24785.

Expressioni

Developmental stagei

Expressed throughout development; highest in embryos and at equal levels in males and females.1 Publication

Gene expression databases

BgeeiP24785.
ExpressionAtlasiP24785. differential.
GenevisibleiP24785. DM.

Interactioni

Subunit structurei

Interacts with Top2.1 Publication

Protein-protein interaction databases

BioGridi61429. 14 interactions.
IntActiP24785. 6 interactions.
MINTiMINT-768581.
STRINGi7227.FBpp0085367.

Structurei

Secondary structure

1
1293
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni121 – 1233Combined sources
Helixi139 – 1446Combined sources
Helixi147 – 1548Combined sources
Helixi159 – 1613Combined sources
Turni162 – 1643Combined sources
Helixi167 – 18014Combined sources
Beta strandi188 – 1936Combined sources
Helixi195 – 1973Combined sources
Beta strandi199 – 20810Combined sources
Helixi209 – 2113Combined sources
Beta strandi213 – 22311Combined sources
Helixi224 – 24118Combined sources
Helixi269 – 28113Combined sources
Helixi289 – 2913Combined sources
Beta strandi296 – 2983Combined sources
Turni337 – 3404Combined sources
Beta strandi345 – 3506Combined sources
Helixi353 – 37018Combined sources
Helixi372 – 38211Combined sources
Helixi385 – 3895Combined sources
Helixi390 – 39910Combined sources
Beta strandi401 – 4077Combined sources
Helixi413 – 42715Combined sources
Helixi431 – 4333Combined sources
Beta strandi435 – 4428Combined sources
Helixi443 – 45614Combined sources
Beta strandi463 – 4697Combined sources
Beta strandi472 – 4743Combined sources
Beta strandi478 – 4869Combined sources
Helixi487 – 4937Combined sources
Helixi494 – 4963Combined sources
Beta strandi503 – 5086Combined sources
Helixi509 – 5113Combined sources
Helixi514 – 52916Combined sources
Beta strandi534 – 5418Combined sources
Helixi544 – 5507Combined sources
Beta strandi556 – 5594Combined sources
Beta strandi566 – 5694Combined sources
Helixi571 – 5788Combined sources
Helixi584 – 60017Combined sources
Helixi606 – 6083Combined sources
Helixi611 – 6133Combined sources
Helixi621 – 6299Combined sources
Beta strandi632 – 6343Combined sources
Helixi637 – 64913Combined sources
Beta strandi655 – 6595Combined sources
Helixi663 – 67412Combined sources
Turni677 – 6804Combined sources
Turni682 – 6843Combined sources
Beta strandi685 – 6906Combined sources
Helixi696 – 7005Combined sources
Turni701 – 7033Combined sources
Beta strandi711 – 7166Combined sources
Helixi718 – 7203Combined sources
Beta strandi721 – 7233Combined sources
Beta strandi729 – 7346Combined sources
Beta strandi737 – 7448Combined sources
Turni745 – 7484Combined sources
Beta strandi749 – 7568Combined sources
Helixi759 – 7668Combined sources
Beta strandi769 – 7735Combined sources
Beta strandi775 – 7795Combined sources
Helixi783 – 7886Combined sources
Helixi796 – 7994Combined sources
Helixi803 – 8119Combined sources
Helixi817 – 8226Combined sources
Beta strandi824 – 8263Combined sources
Helixi830 – 84213Combined sources
Helixi854 – 8607Combined sources
Beta strandi862 – 8643Combined sources
Helixi866 – 87712Combined sources
Helixi881 – 89010Combined sources
Helixi909 – 9124Combined sources
Helixi913 – 9153Combined sources
Helixi921 – 93717Combined sources
Helixi940 – 95011Combined sources
Helixi954 – 97320Combined sources
Helixi978 – 9814Combined sources
Helixi995 – 100713Combined sources
Turni1008 – 10103Combined sources
Beta strandi1012 – 10176Combined sources
Beta strandi1020 – 10234Combined sources
Helixi1024 – 10263Combined sources
Beta strandi1027 – 10315Combined sources
Beta strandi1049 – 106921Combined sources
Helixi1071 – 10777Combined sources
Beta strandi1082 – 10843Combined sources
Helixi1086 – 10883Combined sources
Beta strandi1090 – 10923Combined sources
Turni1093 – 10953Combined sources
Beta strandi1096 – 11005Combined sources
Helixi1102 – 112423Combined sources
Helixi1126 – 11283Combined sources
Helixi1134 – 114714Combined sources
Turni1149 – 11524Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5AORX-ray2.08A/B1-1293[»]
ProteinModelPortaliP24785.
SMRiP24785. Positions 3-81, 156-249, 325-559, 644-973.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 7069DRBM 1PROSITE-ProRule annotationAdd
BLAST
Domaini169 – 24173DRBM 2PROSITE-ProRule annotationAdd
BLAST
Domaini394 – 560167Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini639 – 813175Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Repeati1202 – 120871
Repeati1209 – 121572
Repeati1216 – 122273
Repeati1223 – 122974
Repeati1230 – 123675
Repeati1237 – 124376
Repeati1244 – 125077
Repeati1251 – 125778
Repeati1258 – 126369

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1202 – 1263629 X 7 AA tandem repeats of G-G-G-Y-G-N-NAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi507 – 5104DEAH box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1173 – 1291119Gly-richAdd
BLAST

Sequence similaritiesi

Contains 2 DRBM (double-stranded RNA-binding) domains.PROSITE-ProRule annotation
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0920. Eukaryota.
COG1643. LUCA.
GeneTreeiENSGT00760000119189.
InParanoidiP24785.
KOiK13184.
OMAiVDDWIRL.
OrthoDBiEOG76471V.
PhylomeDBiP24785.

Family and domain databases

Gene3Di3.30.160.20. 2 hits.
3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR014720. dsRBD_dom.
IPR011709. DUF1605.
IPR007502. Helicase-assoc_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00035. dsrm. 1 hit.
PF04408. HA2. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07717. OB_NTP_bind. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00358. DSRM. 2 hits.
SM00847. HA2. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00690. DEAH_ATP_HELICASE. 1 hit.
PS50137. DS_RBD. 2 hits.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform A (identifier: P24785-1) [UniParc]FASTAAdd to basket

Also known as: 25

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
MDIKSFLYQF CAKSQIEPKF DIRQTGPKNR QRFLCEVRVE PNTYIGVGNS
60 70 80 90 100
TNKKDAEKNA CRDFVNYLVR VGKLNTNDVP ADAGASGGGP RTGLEGAGMA
110 120 130 140 150
GGSGQQKRVF DGQSGPQDLG EAYRPLNHDG GDGGNRYSVI DRIQEQRDMN
160 170 180 190 200
EAEAFDVNAA IHGNWTIENA KERLNIYKQT NNIRDDYKYT PVGPEHARSF
210 220 230 240 250
LAELSIYVPA LNRTVTARES GSNKKSASKS CALSLVRQLF HLNVIEPFSG
260 270 280 290 300
TLKKKKDEQL KPYPVKLSPN LINKIDEVIK GLDLPVVNPR NIKIELDGPP
310 320 330 340 350
IPLIVNLSRI DSSQQDGEKR QESSVIPWAP PQANWNTWHA CNIDEGELAT
360 370 380 390 400
TSIDDLSMDY ERSLRDRRQN DNEYRQFLEF REKLPIAAMR SEILTAINDN
410 420 430 440 450
PVVIIRGNTG CGKTTQIAQY ILDDYICSGQ GGYANIYVTQ PRRISAISVA
460 470 480 490 500
ERVARERCEQ LGDTVGYSVR FESVFPRPYG AILFCTVGVL LRKLEAGLRG
510 520 530 540 550
VSHIIVDEIH ERDVNSDFLL VILRDMVDTY PDLHVILMSA TIDTTKFSKY
560 570 580 590 600
FGICPVLEVP GRAFPVQQFF LEDIIQMTDF VPSAESRRKR KEVEDEEQLL
610 620 630 640 650
SEDKDEAEIN YNKVCEDKYS QKTRNAMAML SESDVSFELL EALLMHIKSK
660 670 680 690 700
NIPGAILVFL PGWNLIFALM KFLQNTNIFG DTSQYQILPC HSQIPRDEQR
710 720 730 740 750
KVFEPVPEGV TKIILSTNIA ETSITIDDIV FVIDICKARM KLFTSHNNLT
760 770 780 790 800
SYATVWASKT NLEQRKGRAG RVRPGFCFTL CSRARFQALE DNLTPEMFRT
810 820 830 840 850
PLHEMALTIK LLRLGSIHHF LSKALEPPPV DAVIEAEVLL REMRCLDAND
860 870 880 890 900
ELTPLGRLLA RLPIEPRLGK MMVLGAVFGC ADLMAIMASY SSTFSEVFSL
910 920 930 940 950
DIGQRRLANH QKALSGTKCS DHVAMIVASQ MWRREKQRGE HMEARFCDWK
960 970 980 990 1000
GLQMSTMNVI WDAKQQLLDL LQQAGFPEEC MISHEVDERI DGDDPVLDVS
1010 1020 1030 1040 1050
LALLCLGLYP NICVHKEKRK VLTTESKAAL LHKTSVNCSN LAVTFPYPFF
1060 1070 1080 1090 1100
VFGEKIRTRA VSCKQLSMVS PLQVILFGSR KIDLAANNIV RVDNWLNFDI
1110 1120 1130 1140 1150
EPELAAKIGA LKPALEDLIT VACDNPSDIL RLEEPYAQLV KVVKDLCVKS
1160 1170 1180 1190 1200
AGDFGLQRES GILPHQSRQF SDGGGPPKRG RFETGRFTNS SFGRRGNGRT
1210 1220 1230 1240 1250
FGGGYGNNGG GYGNNGGGYG NIGGGYGNNA GGYGNNGGYG NNGGGYRNNG
1260 1270 1280 1290
GGYGNNGGGY GNKRGGFGDS FESNRGSGGG FRNGDQGGRW GNF
Length:1,293
Mass (Da):143,661
Last modified:September 27, 2005 - v2
Checksum:i7667679F069BCAF5
GO
Isoform 12 (identifier: P24785-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     199-226: SFLAELSIYVPALNRTVTARESGSNKKS → YVLPFQLSSACISDLTRYGLRPNLKCSP
     227-1293: Missing.

Show »
Length:226
Mass (Da):25,083
Checksum:i32C6CFA40B0F84AF
GO
Isoform B (identifier: P24785-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-357: Missing.

Note: No experimental confirmation available.
Show »
Length:936
Mass (Da):104,129
Checksum:i608D316CAE0E2472
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti590 – 5901R → P in AAC41573 (PubMed:1653648).Curated
Sequence conflicti1263 – 12631K → N in AAC41573 (PubMed:1653648).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1276 – 12761G → V.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 357357Missing in isoform B. 1 PublicationVSP_015690Add
BLAST
Alternative sequencei199 – 22628SFLAE…SNKKS → YVLPFQLSSACISDLTRYGL RPNLKCSP in isoform 12. 1 PublicationVSP_005775Add
BLAST
Alternative sequencei227 – 12931067Missing in isoform 12. 1 PublicationVSP_005776Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74121 mRNA. Translation: AAC41573.1.
AE013599 Genomic DNA. Translation: AAF57297.1.
AE013599 Genomic DNA. Translation: AAM68335.1.
BT003785 mRNA. Translation: AAO41468.1.
BT010267 mRNA. Translation: AAQ23585.1.
PIRiB40025.
RefSeqiNP_476641.1. NM_057293.4. [P24785-1]
NP_724440.1. NM_165451.3. [P24785-3]
UniGeneiDm.2901.

Genome annotation databases

EnsemblMetazoaiFBtr0086031; FBpp0085367; FBgn0002774. [P24785-1]
GeneIDi35523.
KEGGidme:Dmel_CG11680.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74121 mRNA. Translation: AAC41573.1.
AE013599 Genomic DNA. Translation: AAF57297.1.
AE013599 Genomic DNA. Translation: AAM68335.1.
BT003785 mRNA. Translation: AAO41468.1.
BT010267 mRNA. Translation: AAQ23585.1.
PIRiB40025.
RefSeqiNP_476641.1. NM_057293.4. [P24785-1]
NP_724440.1. NM_165451.3. [P24785-3]
UniGeneiDm.2901.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5AORX-ray2.08A/B1-1293[»]
ProteinModelPortaliP24785.
SMRiP24785. Positions 3-81, 156-249, 325-559, 644-973.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61429. 14 interactions.
IntActiP24785. 6 interactions.
MINTiMINT-768581.
STRINGi7227.FBpp0085367.

Proteomic databases

PaxDbiP24785.
PRIDEiP24785.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0086031; FBpp0085367; FBgn0002774. [P24785-1]
GeneIDi35523.
KEGGidme:Dmel_CG11680.

Organism-specific databases

CTDi35523.
FlyBaseiFBgn0002774. mle.

Phylogenomic databases

eggNOGiKOG0920. Eukaryota.
COG1643. LUCA.
GeneTreeiENSGT00760000119189.
InParanoidiP24785.
KOiK13184.
OMAiVDDWIRL.
OrthoDBiEOG76471V.
PhylomeDBiP24785.

Enzyme and pathway databases

ReactomeiR-DME-1810476. RIP-mediated NFkB activation via ZBP1.
R-DME-3134963. DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
R-DME-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-DME-72163. mRNA Splicing - Major Pathway.
R-DME-933542. TRAF6 mediated NF-kB activation.

Miscellaneous databases

GenomeRNAii35523.
PROiP24785.

Gene expression databases

BgeeiP24785.
ExpressionAtlasiP24785. differential.
GenevisibleiP24785. DM.

Family and domain databases

Gene3Di3.30.160.20. 2 hits.
3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR014720. dsRBD_dom.
IPR011709. DUF1605.
IPR007502. Helicase-assoc_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00035. dsrm. 1 hit.
PF04408. HA2. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07717. OB_NTP_bind. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00358. DSRM. 2 hits.
SM00847. HA2. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00690. DEAH_ATP_HELICASE. 1 hit.
PS50137. DS_RBD. 2 hits.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The maleless protein associates with the X chromosome to regulate dosage compensation in Drosophila."
    Kuroda M.I., Kernan M.J., Kreber R., Ganetzky B., Baker B.S.
    Cell 66:935-947(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 12 AND A), FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
    Tissue: Imaginal disk.
  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.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
    Strain: Berkeley.
    Tissue: Embryo.
  5. "Topoisomerase II plays a role in dosage compensation in Drosophila."
    Cugusi S., Ramos E., Ling H., Yokoyama R., Luk K.M., Lucchesi J.C.
    Transcription 4:238-250(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TOP2.

Entry informationi

Entry nameiMLE_DROME
AccessioniPrimary (citable) accession number: P24785
Secondary accession number(s): Q86NQ4, Q9V9J1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: September 27, 2005
Last modified: July 6, 2016
This is version 161 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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