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Protein

Segment polarity protein dishevelled

Gene

dsh

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

Functioni

Required to establish coherent arrays of polarized cells and segments in embryos. Plays a role in wingless (wg) signaling, possibly through the reception of the wg signal by target cells and subsequent redistribution of arm protein in response to that signal in embryos. This signal seems to be required to establish planar cell polarity and identity.3 Publications

GO - Molecular functioni

  1. frizzled binding Source: GO_Central
  2. Notch binding Source: FlyBase
  3. phosphatidic acid binding Source: FlyBase
  4. protein domain specific binding Source: FlyBase

GO - Biological processi

  1. axon extension Source: FlyBase
  2. axon guidance Source: FlyBase
  3. border follicle cell migration Source: FlyBase
  4. cell migration Source: FlyBase
  5. compound eye morphogenesis Source: FlyBase
  6. dorsal closure Source: FlyBase
  7. dorsal closure, elongation of leading edge cells Source: FlyBase
  8. epidermis morphogenesis Source: FlyBase
  9. establishment of epithelial cell apical/basal polarity Source: FlyBase
  10. establishment of epithelial cell planar polarity Source: FlyBase
  11. establishment of imaginal disc-derived wing hair orientation Source: FlyBase
  12. establishment of ommatidial planar polarity Source: FlyBase
  13. establishment of planar polarity Source: FlyBase
  14. establishment of thoracic bristle planar orientation Source: FlyBase
  15. establishment of tissue polarity Source: FlyBase
  16. female gonad development Source: FlyBase
  17. filopodium assembly Source: FlyBase
  18. heart development Source: FlyBase
  19. heart formation Source: FlyBase
  20. imaginal disc-derived leg joint morphogenesis Source: FlyBase
  21. imaginal disc-derived wing hair organization Source: FlyBase
  22. imaginal disc-derived wing morphogenesis Source: FlyBase
  23. intracellular signal transduction Source: InterPro
  24. lamellipodium assembly Source: FlyBase
  25. motor neuron axon guidance Source: FlyBase
  26. negative regulation of heart induction by canonical Wnt signaling pathway Source: FlyBase
  27. negative regulation of Notch signaling pathway Source: FlyBase
  28. ommatidial rotation Source: FlyBase
  29. oogenesis Source: FlyBase
  30. ovarian follicle cell development Source: FlyBase
  31. protein localization Source: FlyBase
  32. R3/R4 cell fate commitment Source: FlyBase
  33. regulation of actin filament bundle assembly Source: FlyBase
  34. regulation of compound eye pigmentation Source: FlyBase
  35. regulation of tube length, open tracheal system Source: FlyBase
  36. retinal ganglion cell axon guidance Source: FlyBase
  37. salivary gland morphogenesis Source: FlyBase
  38. segment polarity determination Source: UniProtKB-KW
  39. sensory organ development Source: FlyBase
  40. somatic stem cell maintenance Source: FlyBase
  41. synaptic target inhibition Source: FlyBase
  42. wing and notum subfield formation Source: FlyBase
  43. Wnt signaling pathway Source: FlyBase
  44. Wnt signaling pathway, planar cell polarity pathway Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Segmentation polarity protein

Keywords - Biological processi

Wnt signaling pathway

Enzyme and pathway databases

ReactomeiREACT_277242. Signaling by Hippo.
REACT_299289. degradation of DVL.
REACT_299534. WNT mediated activation of DVL.
REACT_322963. TCF dependent signaling in response to WNT.
REACT_326549. negative regulation of TCF-dependent signaling by DVL-interacting proteins.
REACT_327196. WNT5A-dependent internalization of FZD4.
REACT_333353. Asymmetric localization of PCP proteins.
REACT_337991. PCP/CE pathway.
REACT_343579. disassembly of the destruction complex and recruitment of AXIN to the membrane.
SignaLinkiP51140.

Names & Taxonomyi

Protein namesi
Recommended name:
Segment polarity protein dishevelled
Gene namesi
Name:dsh
ORF Names:CG18361
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0000499. dsh.

Subcellular locationi

Cytoplasm. Nucleus. Membrane; Peripheral membrane protein
Note: Associated with the membrane when hyperphosphorylated.

GO - Cellular componenti

  1. adherens junction Source: FlyBase
  2. cytoplasm Source: FlyBase
  3. cytosol Source: GO_Central
  4. nucleus Source: UniProtKB-SubCell
  5. plasma membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 623623Segment polarity protein dishevelledPRO_0000145740Add
BLAST

Post-translational modificationi

Phosphorylated. Wg signaling generates the hyperphosphorylated active forms.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP51140.

Expressioni

Tissue specificityi

Found in egg chambers of the ovary and ubiquitously throughout embryogenesis and in disks. Expression is not seen in salivary glands, muscles or ventral ganglia but is observed in brain lobes.

Developmental stagei

Expressed at high levels at 0-1 hour and from 5-17 hours. Also expressed at high levels in early pupae.1 Publication

Gene expression databases

BgeeiP51140.

Interactioni

Subunit structurei

Interacts with nkd. This interaction may require zinc.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
cnoQ242793EBI-499383,EBI-868783
dgoQ7JUF25EBI-499383,EBI-1158635
nkdQ9VVV910EBI-499383,EBI-125843
Nkd1Q99MH62EBI-499383,EBI-1538321From a different organism.

Protein-protein interaction databases

BioGridi58490. 81 interactions.
IntActiP51140. 17 interactions.
MINTiMINT-8291181.

Structurei

3D structure databases

ProteinModelPortaliP51140.
SMRiP51140. Positions 10-88, 250-338, 391-478.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 9184DIXPROSITE-ProRule annotationAdd
BLAST
Domaini252 – 32473PDZPROSITE-ProRule annotationAdd
BLAST
Domaini404 – 47875DEPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni166 – 623458Interaction with nkdAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi119 – 14628Poly-GlnAdd
BLAST
Compositional biasi154 – 1596Poly-Gln
Compositional biasi551 – 5577Poly-Ser
Compositional biasi599 – 60810Poly-Gly

Sequence similaritiesi

Belongs to the DSH family.Curated
Contains 1 DEP domain.PROSITE-ProRule annotation
Contains 1 DIX domain.PROSITE-ProRule annotation
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG322275.
GeneTreeiENSGT00390000013552.
InParanoidiP51140.
KOiK02353.
OMAiNCSKNEG.
OrthoDBiEOG7BP82N.
PhylomeDBiP51140.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.30.42.10. 1 hit.
InterProiIPR000591. DEP_dom.
IPR008339. Dishevelled_fam.
IPR003351. Dishevelled_protein_dom.
IPR001158. DIX.
IPR026542. Dsh.
IPR015506. Dsh/Dvl-rel.
IPR001478. PDZ.
IPR029071. Ubiquitin-rel_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10878. PTHR10878. 1 hit.
PTHR10878:SF19. PTHR10878:SF19. 1 hit.
PfamiPF00610. DEP. 1 hit.
PF02377. Dishevelled. 1 hit.
PF00778. DIX. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view]
PRINTSiPR01760. DISHEVELLED.
SMARTiSM00021. DAX. 1 hit.
SM00049. DEP. 1 hit.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50186. DEP. 1 hit.
PS50841. DIX. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P51140-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDADRGGGQE TKVIYHIDDE TTPYLVKIPI PSAQVTLRDF KLVLNKQNNN
60 70 80 90 100
YKYFFKSMDA DFGVVKEEIA DDSTILPCFN GRVVSWLVSA DGTNQSDNCS
110 120 130 140 150
ELPTSECELG MGLTNRKLQQ QQQQHQQQQQ QQQQQHQQQQ QQQQQQVQPV
160 170 180 190 200
QLAQQQQQQV LHHQKMMGNP LLQPPPLTYQ SASVLSSDLD STSLFGTESE
210 220 230 240 250
LTLDRDMTDY SSVQRLQVRK KPQRRKKRAP SMSRTSSYSS ITDSTMSLNI
260 270 280 290 300
ITVSINMEAV NFLGISIVGQ SNRGGDGGIY VGSIMKGGAV ALDGRIEPGD
310 320 330 340 350
MILQVNDVNF ENMTNDEAVR VLREVVQKPG PIKLVVAKCW DPNPKGYFTI
360 370 380 390 400
PRTEPVRPID PGAWVAHTQA LTSHDSIIAD IAEPIKERLD QNNLEEIVKA
410 420 430 440 450
MTKPDSGLEI RDRMWLKITI PNAFIGADAV NWVLENVEDV QDRREARRIV
460 470 480 490 500
SAMLRSNYIK HTVNKLTFSE QCYYVVNEER NPNLLGRGHL HPHQLPHGHG
510 520 530 540 550
GHALSHADTE SITSDIGPLP NPPIYMPYSA TYNPSHGYQP IQYGIAERHI
560 570 580 590 600
SSGSSSSDVL TSKDISASQS DITSVIHQAN QLTIAAHGSN KSSGSSNRGG
610 620
GGGGGGGGNN TNDQDVSVFN YVL
Length:623
Mass (Da):68,917
Last modified:June 20, 2005 - v2
Checksum:i0BA24ED350666CF5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti276 – 2761D → N in AAA20216 (PubMed:8149913).Curated
Sequence conflicti565 – 5651I → T in AAA16535 (PubMed:8288125).Curated
Sequence conflicti619 – 6191F → S in AAA16535 (PubMed:8288125).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U02491 mRNA. Translation: AAA20216.1.
L26974 mRNA. Translation: AAA16535.1.
AE014298 Genomic DNA. Translation: AAF48033.1.
BT023781 mRNA. Translation: AAZ41790.1.
PIRiA49840.
RefSeqiNP_511118.2. NM_078563.3.
UniGeneiDm.2927.

Genome annotation databases

EnsemblMetazoaiFBtr0073454; FBpp0073310; FBgn0000499.
GeneIDi32078.
KEGGidme:Dmel_CG18361.
UCSCiCG18361-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U02491 mRNA. Translation: AAA20216.1.
L26974 mRNA. Translation: AAA16535.1.
AE014298 Genomic DNA. Translation: AAF48033.1.
BT023781 mRNA. Translation: AAZ41790.1.
PIRiA49840.
RefSeqiNP_511118.2. NM_078563.3.
UniGeneiDm.2927.

3D structure databases

ProteinModelPortaliP51140.
SMRiP51140. Positions 10-88, 250-338, 391-478.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi58490. 81 interactions.
IntActiP51140. 17 interactions.
MINTiMINT-8291181.

Proteomic databases

PaxDbiP51140.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0073454; FBpp0073310; FBgn0000499.
GeneIDi32078.
KEGGidme:Dmel_CG18361.
UCSCiCG18361-RA. d. melanogaster.

Organism-specific databases

CTDi32078.
FlyBaseiFBgn0000499. dsh.

Phylogenomic databases

eggNOGiNOG322275.
GeneTreeiENSGT00390000013552.
InParanoidiP51140.
KOiK02353.
OMAiNCSKNEG.
OrthoDBiEOG7BP82N.
PhylomeDBiP51140.

Enzyme and pathway databases

ReactomeiREACT_277242. Signaling by Hippo.
REACT_299289. degradation of DVL.
REACT_299534. WNT mediated activation of DVL.
REACT_322963. TCF dependent signaling in response to WNT.
REACT_326549. negative regulation of TCF-dependent signaling by DVL-interacting proteins.
REACT_327196. WNT5A-dependent internalization of FZD4.
REACT_333353. Asymmetric localization of PCP proteins.
REACT_337991. PCP/CE pathway.
REACT_343579. disassembly of the destruction complex and recruitment of AXIN to the membrane.
SignaLinkiP51140.

Miscellaneous databases

GenomeRNAii32078.
NextBioi776701.
PROiP51140.

Gene expression databases

BgeeiP51140.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.30.42.10. 1 hit.
InterProiIPR000591. DEP_dom.
IPR008339. Dishevelled_fam.
IPR003351. Dishevelled_protein_dom.
IPR001158. DIX.
IPR026542. Dsh.
IPR015506. Dsh/Dvl-rel.
IPR001478. PDZ.
IPR029071. Ubiquitin-rel_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10878. PTHR10878. 1 hit.
PTHR10878:SF19. PTHR10878:SF19. 1 hit.
PfamiPF00610. DEP. 1 hit.
PF02377. Dishevelled. 1 hit.
PF00778. DIX. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view]
PRINTSiPR01760. DISHEVELLED.
SMARTiSM00021. DAX. 1 hit.
SM00049. DEP. 1 hit.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50186. DEP. 1 hit.
PS50841. DIX. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Dishevelled is required during wingless signaling to establish both cell polarity and cell identity."
    Theisen H., Purcell J., Bennett M., Kansagara D., Syed A., Marsh J.L.
    Development 120:347-360(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  2. "The Drosophila segment polarity gene dishevelled encodes a novel protein required for response to the wingless signal."
    Klingensmith J., Nusse R., Perrimon N.
    Genes Dev. 8:118-130(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE.
  3. "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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  6. "The dishevelled protein is modified by wingless signaling in Drosophila."
    Yanagawa S., van Leeuwen F., Wodarz A., Klingensmith J., Nusse R.
    Genes Dev. 9:1087-1097(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
  7. "Naked cuticle targets dishevelled to antagonize Wnt signal transduction."
    Rousset R., Mack J.A., Wharton K.A. Jr., Axelrod J.D., Cadigan K.M., Fish M.P., Nusse R., Scott M.P.
    Genes Dev. 15:658-671(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NKD.
  8. "Zinc-dependent interaction between dishevelled and the Drosophila Wnt antagonist naked cuticle."
    Rousset R., Wharton K.A. Jr., Zimmermann G., Scott M.P.
    J. Biol. Chem. 277:49019-49026(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NKD.
  9. "An unconventional nuclear localization motif is crucial for function of the Drosophila Wnt/wingless antagonist Naked cuticle."
    Waldrop S., Chan C.-C., Cagatay T., Zhang S., Rousset R., Mack J.A., Zeng W., Fish M.P., Zhang M., Amanai M., Wharton K.A. Jr.
    Genetics 174:331-348(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NKD, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiDSH_DROME
AccessioniPrimary (citable) accession number: P51140
Secondary accession number(s): Q494J5, Q9VYZ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 30, 1996
Last sequence update: June 20, 2005
Last modified: March 31, 2015
This is version 142 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

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 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.