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P51141

- DVL1_MOUSE

UniProt

P51141 - DVL1_MOUSE

Protein

Segment polarity protein dishevelled homolog DVL-1

Gene

Dvl1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Participates in Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Plays a role both in canonical and non-canonical Wnt signaling. Plays a role in the signal transduction pathways mediated by multiple Wnt genes. Required for LEF1 activation upon WNT1 and WNT3A signaling. DVL1 and PAK1 form a ternary complex with MUSK which is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ).4 Publications

    GO - Molecular functioni

    1. frizzled binding Source: RefGenome
    2. protein binding Source: IntAct
    3. protein kinase binding Source: RefGenome
    4. Rac GTPase binding Source: RefGenome
    5. signal transducer activity Source: InterPro

    GO - Biological processi

    1. axon extension Source: MGI
    2. axon guidance Source: MGI
    3. axonogenesis Source: MGI
    4. canonical Wnt signaling pathway Source: MGI
    5. cochlea morphogenesis Source: MGI
    6. collateral sprouting Source: MGI
    7. convergent extension involved in neural plate elongation Source: MGI
    8. convergent extension involved in organogenesis Source: MGI
    9. cytoplasmic microtubule organization Source: MGI
    10. dendrite morphogenesis Source: MGI
    11. intracellular signal transduction Source: InterPro
    12. negative regulation of protein binding Source: Ensembl
    13. negative regulation of protein kinase activity Source: Ensembl
    14. negative regulation of protein phosphorylation Source: MGI
    15. neural tube development Source: Ensembl
    16. neuromuscular junction development Source: MGI
    17. neurotransmitter secretion Source: MGI
    18. planar cell polarity pathway involved in neural tube closure Source: MGI
    19. positive regulation of canonical Wnt signaling pathway Source: BHF-UCL
    20. positive regulation of neuron projection development Source: MGI
    21. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
    22. positive regulation of transcription, DNA-templated Source: RefGenome
    23. prepulse inhibition Source: MGI
    24. protein localization to microtubule Source: MGI
    25. protein localization to nucleus Source: Ensembl
    26. receptor clustering Source: MGI
    27. regulation of neurotransmitter levels Source: MGI
    28. regulation of protein phosphorylation Source: MGI
    29. skeletal muscle acetylcholine-gated channel clustering Source: MGI
    30. social behavior Source: MGI
    31. synapse organization Source: MGI
    32. transcription from RNA polymerase II promoter Source: Ensembl
    33. Wnt signaling pathway Source: BHF-UCL
    34. Wnt signaling pathway, planar cell polarity pathway Source: MGI

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Wnt signaling pathway

    Enzyme and pathway databases

    ReactomeiREACT_207044. TCF dependent signaling in response to WNT.
    REACT_216784. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    REACT_225118. WNT mediated activation of DVL.
    REACT_227429. degradation of DVL.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Segment polarity protein dishevelled homolog DVL-1
    Short name:
    Dishevelled-1
    Alternative name(s):
    DSH homolog 1
    Gene namesi
    Name:Dvl1
    Synonyms:Dvl
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:94941. Dvl1.

    Subcellular locationi

    Cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Cytoplasmcytosol 1 Publication. Cytoplasmic vesicle 1 Publication
    Note: Localizes at the cell membrane upon interaction with frizzled family members.

    GO - Cellular componenti

    1. axon Source: MGI
    2. cell cortex Source: RefGenome
    3. clathrin-coated vesicle Source: MGI
    4. cytoplasmic membrane-bounded vesicle Source: MGI
    5. cytosol Source: UniProtKB-SubCell
    6. dendrite Source: RefGenome
    7. growth cone Source: RefGenome
    8. lateral plasma membrane Source: Ensembl
    9. membrane Source: BHF-UCL
    10. microtubule Source: RefGenome
    11. microtubule cytoskeleton Source: MGI
    12. neuronal cell body Source: RefGenome
    13. synapse Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoplasmic vesicle, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mice display abnormalities in social behavior and sensorimotor gating.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi17 – 171Y → D: Loss of oligomerization. 1 Publication
    Mutagenesisi438 – 4381K → M: Strongly reduces activity in Wnt signaling. Abolishes location at the cell membrane. 2 Publications
    Mutagenesisi449 – 4491D → I: Reduces activity in Wnt signaling; when associated with I-452. 1 Publication
    Mutagenesisi452 – 4521D → I: Reduces activity in Wnt signaling; when associated with I-449. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 695695Segment polarity protein dishevelled homolog DVL-1PRO_0000145743Add
    BLAST

    Post-translational modificationi

    Ubiquitinated; undergoes both 'Lys-48'-linked ubiquitination, leading to its subsequent degradation by the ubiquitin-proteasome pathway, and 'Lys-63'-linked ubiquitination. The interaction with INVS is required for ubiquitination By similarity. Deubiquitinated by CYLD, which acts on 'Lys-63'-linked ubiquitin chains.By similarity1 Publication

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    PRIDEiP51141.

    PTM databases

    PhosphoSiteiP51141.

    Expressioni

    Tissue specificityi

    High levels are seen in the brain, testis and kidney, lower levels in the ovary, breast, muscle, liver and small intestine, and very low levels are seen in the spleen and thymus. A moderate level expression is seen in the heart.

    Developmental stagei

    Is expressed throughout the embryonic central nervous system from presomite stages and in neuron-rich areas of the brain throughout postnatal development, as well as in many other tissues.

    Gene expression databases

    ArrayExpressiP51141.
    BgeeiP51141.
    CleanExiMM_DVL1.
    GenevestigatoriP51141.

    Interactioni

    Subunit structurei

    Interacts with CXXC4 By similarity. Interacts (via PDZ domain) with TMEM88 By similarity. Interacts with BRD7 and INVS. Interacts through its PDZ domain with the C-terminal regions of VANGL1, VANGL2 and CCDC88C/DAPLE. Interacts (via PDZ domain) with NXN. Interacts with ARRB1; the interaction is enhanced by phosphorylation of DVL1 By similarity. Interacts with CYLD. Interacts (via PDZ domain) with RYK. Self-associates (via DIX domain) and forms higher homooligomers. Interacts (via PDZ domain) with DACT1 and FZD7, where DACT1 and FZD7 compete for the same binding site. Interacts (via DEP domain) with MUSK; the interaction is direct and mediates the formation a DVL1, MUSK and PAK1 ternary complex involved in AChR clustering.By similarity10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Dact1Q8R4A34EBI-1538407,EBI-3870250
    fzd7-bQ8AVJ93EBI-1538407,EBI-3870271From a different organism.
    Tfdp1Q086393EBI-1538407,EBI-1216575
    Tmem88Q9D0N82EBI-1538407,EBI-6136970
    Vangl1Q80Z962EBI-1538407,EBI-1750708
    Vangl2Q91ZD42EBI-1538407,EBI-1750744

    Protein-protein interaction databases

    BioGridi199342. 18 interactions.
    IntActiP51141. 19 interactions.
    MINTiMINT-261881.

    Structurei

    Secondary structure

    1
    695
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 96
    Beta strandi17 – 237
    Beta strandi25 – 273
    Helixi30 – 356
    Helixi42 – 443
    Beta strandi48 – 536
    Turni54 – 563
    Beta strandi57 – 626
    Beta strandi76 – 805
    Beta strandi249 – 2546
    Beta strandi258 – 2603
    Beta strandi264 – 2674
    Beta strandi272 – 2743
    Beta strandi279 – 2835
    Beta strandi286 – 2883
    Helixi289 – 2924
    Helixi297 – 2993
    Beta strandi301 – 3044
    Turni310 – 3123
    Helixi318 – 3269
    Beta strandi327 – 3293
    Beta strandi333 – 3353
    Beta strandi411 – 4133
    Helixi415 – 4239
    Beta strandi427 – 4293
    Beta strandi434 – 4363
    Beta strandi439 – 4435
    Helixi446 – 45712
    Helixi464 – 47613
    Turni477 – 4793
    Beta strandi483 – 4864
    Beta strandi491 – 4933

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FSHNMR-A395-499[»]
    1MC7NMR-A251-345[»]
    2KAWNMR-A248-337[»]
    3PZ8X-ray2.87A/B/C/D/E/F/G/H3-104[»]
    ProteinModelPortaliP51141.
    SMRiP51141. Positions 3-84, 248-337, 406-499.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP51141.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 8585DIXPROSITE-ProRule annotationAdd
    BLAST
    Domaini251 – 32373PDZPROSITE-ProRule annotationAdd
    BLAST
    Domaini425 – 49975DEPPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi390 – 3934Poly-Ser

    Domaini

    The DIX domain promotes homooligomerization.
    The DEP domain mediates interaction with the cell membrane.

    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.
    HOGENOMiHOG000017084.
    HOVERGENiHBG005542.
    InParanoidiQ3U2D3.
    KOiK02353.
    OMAiYPRYGMS.
    OrthoDBiEOG7BP82N.
    TreeFamiTF318198.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    2.30.42.10. 1 hit.
    InterProiIPR000591. DEP_dom.
    IPR008340. Dishevelled_1.
    IPR024580. Dishevelled_C-dom.
    IPR008339. Dishevelled_fam.
    IPR003351. Dishevelled_protein_dom.
    IPR001158. DIX.
    IPR015506. Dsh/Dvl-rel.
    IPR001478. PDZ.
    IPR029071. Ubiquitin-rel_dom.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PANTHERiPTHR10878. PTHR10878. 1 hit.
    PTHR10878:SF5. PTHR10878:SF5. 1 hit.
    PfamiPF00610. DEP. 1 hit.
    PF02377. Dishevelled. 1 hit.
    PF00778. DIX. 1 hit.
    PF12316. Dsh_C. 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.

    P51141-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAETKIIYHM DEEETPYLVK LPVAPERVTL ADFKNVLSNR PVHAYKFFFK    50
    SMDQDFGVVK EEIFDDNAKL PCFNGRVVSW LVLAEGAHSD AGSQGTDSHT 100
    DLPPPLERTG GIGDSRPPSF HPNVASSRDG MDNETGTESM VSHRRERARR 150
    RNRDEAARTN GHPRGDRRRD LGLPPDSAST VLSSELESSS FIDSDEEDNT 200
    SRLSSSTEQS TSSRLVRKHK CRRRKQRLRQ TDRASSFSSI TDSTMSLNII 250
    TVTLNMERHH FLGISIVGQS NDRGDGGIYI GSIMKGGAVA ADGRIEPGDM 300
    LLQVNDVNFE NMSNDDAVRV LREIVSQTGP ISLTVAKCWD PTPRSYFTIP 350
    RADPVRPIDP AAWLSHTAAL TGALPRYGTS PCSSAITRTS SSSLTSSVPG 400
    APQLEEAPLT VKSDMSAIVR VMQLPDSGLE IRDRMWLKIT IANAVIGADV 450
    VDWLYTHVEG FKERREARKY ASSMLKHGFL RHTVNKITFS EQCYYVFGDL 500
    CSNLASLNLN SGSSGASDQD TLAPLPHPSV PWPLGQGYPY QYPGPPPCFP 550
    PAYQDPGFSC GSGSAGSQQS EGSKSSGSTR SSHRTPGREE RRATGAGGSG 600
    SESDHTVPSG SGSTGWWERP VSQLSRGSSP RSQASAVAPG LPPLHPLTKA 650
    YAVVGGPPGG PPVRELAAVP PELTGSRQSF QKAMGNPCEF FVDIM 695
    Length:695
    Mass (Da):75,359
    Last modified:July 27, 2011 - v2
    Checksum:iFA21ACAC48FF71E0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti121 – 1255HPNVA → Q in AAA74049. (PubMed:9132266)Curated
    Sequence conflicti121 – 1211H → Q in AAA74049. (PubMed:9132266)Curated
    Sequence conflicti211 – 2111T → N in AAA74049. (PubMed:9132266)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U10115 mRNA. Translation: AAA82175.1.
    U28138 Genomic DNA. Translation: AAA74049.1.
    AK155349 mRNA. Translation: BAE33208.1.
    AL670236 Genomic DNA. Translation: CAM18392.1.
    CH466594 Genomic DNA. Translation: EDL15045.1.
    BC138848 mRNA. Translation: AAI38849.1.
    BC138849 mRNA. Translation: AAI38850.1.
    CCDSiCCDS19045.1.
    RefSeqiNP_034221.3. NM_010091.3.
    UniGeneiMm.3400.

    Genome annotation databases

    EnsembliENSMUST00000030948; ENSMUSP00000030948; ENSMUSG00000029071.
    ENSMUST00000168552; ENSMUSP00000133137; ENSMUSG00000029071.
    GeneIDi13542.
    KEGGimmu:13542.
    UCSCiuc008wfc.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U10115 mRNA. Translation: AAA82175.1 .
    U28138 Genomic DNA. Translation: AAA74049.1 .
    AK155349 mRNA. Translation: BAE33208.1 .
    AL670236 Genomic DNA. Translation: CAM18392.1 .
    CH466594 Genomic DNA. Translation: EDL15045.1 .
    BC138848 mRNA. Translation: AAI38849.1 .
    BC138849 mRNA. Translation: AAI38850.1 .
    CCDSi CCDS19045.1.
    RefSeqi NP_034221.3. NM_010091.3.
    UniGenei Mm.3400.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FSH NMR - A 395-499 [» ]
    1MC7 NMR - A 251-345 [» ]
    2KAW NMR - A 248-337 [» ]
    3PZ8 X-ray 2.87 A/B/C/D/E/F/G/H 3-104 [» ]
    ProteinModelPortali P51141.
    SMRi P51141. Positions 3-84, 248-337, 406-499.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199342. 18 interactions.
    IntActi P51141. 19 interactions.
    MINTi MINT-261881.

    PTM databases

    PhosphoSitei P51141.

    Proteomic databases

    PRIDEi P51141.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000030948 ; ENSMUSP00000030948 ; ENSMUSG00000029071 .
    ENSMUST00000168552 ; ENSMUSP00000133137 ; ENSMUSG00000029071 .
    GeneIDi 13542.
    KEGGi mmu:13542.
    UCSCi uc008wfc.1. mouse.

    Organism-specific databases

    CTDi 1855.
    MGIi MGI:94941. Dvl1.

    Phylogenomic databases

    eggNOGi NOG322275.
    GeneTreei ENSGT00390000013552.
    HOGENOMi HOG000017084.
    HOVERGENi HBG005542.
    InParanoidi Q3U2D3.
    KOi K02353.
    OMAi YPRYGMS.
    OrthoDBi EOG7BP82N.
    TreeFami TF318198.

    Enzyme and pathway databases

    Reactomei REACT_207044. TCF dependent signaling in response to WNT.
    REACT_216784. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    REACT_225118. WNT mediated activation of DVL.
    REACT_227429. degradation of DVL.

    Miscellaneous databases

    EvolutionaryTracei P51141.
    NextBioi 284142.
    PROi P51141.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P51141.
    Bgeei P51141.
    CleanExi MM_DVL1.
    Genevestigatori P51141.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    2.30.42.10. 1 hit.
    InterProi IPR000591. DEP_dom.
    IPR008340. Dishevelled_1.
    IPR024580. Dishevelled_C-dom.
    IPR008339. Dishevelled_fam.
    IPR003351. Dishevelled_protein_dom.
    IPR001158. DIX.
    IPR015506. Dsh/Dvl-rel.
    IPR001478. PDZ.
    IPR029071. Ubiquitin-rel_dom.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    PANTHERi PTHR10878. PTHR10878. 1 hit.
    PTHR10878:SF5. PTHR10878:SF5. 1 hit.
    Pfami PF00610. DEP. 1 hit.
    PF02377. Dishevelled. 1 hit.
    PF00778. DIX. 1 hit.
    PF12316. Dsh_C. 1 hit.
    PF00595. PDZ. 1 hit.
    [Graphical view ]
    PRINTSi PR01760. DISHEVELLED.
    SMARTi SM00021. DAX. 1 hit.
    SM00049. DEP. 1 hit.
    SM00228. PDZ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50156. SSF50156. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEi PS50186. DEP. 1 hit.
    PS50841. DIX. 1 hit.
    PS50106. PDZ. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of a mouse homolog of the Drosophila segment polarity gene dishevelled."
      Sussman D.J., Klingensmith J., Salinas P., Adams P.S., Nusse R., Perrimon N.
      Dev. Biol. 166:73-86(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6.
      Tissue: Brain.
    2. "Organization and promoter analysis of the mouse dishevelled-1 gene."
      Lijam N., Sussman D.J.
      Genome Res. 5:116-124(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: BALB/c.
    3. "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].
      Strain: NOD.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
      Tissue: Embryo.
    7. Cited for: DISRUPTION PHENOTYPE.
    8. "Regulation of AChR clustering by Dishevelled interacting with MuSK and PAK1."
      Luo Z.G., Wang Q., Zhou J.Z., Wang J., Luo Z., Liu M., He X., Wynshaw-Boris A., Xiong W.C., Lu B., Mei L.
      Neuron 35:489-505(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NEUROMUSCULAR JUNCTION DEVELOPMENT, INTERACTION WITH MUSK AND PAK1.
    9. "BP75, bromodomain-containing M(r) 75,000 protein, binds dishevelled-1 and enhances Wnt signaling by inactivating glycogen synthase kinase-3 beta."
      Kim S., Lee J., Park J., Chung J.
      Cancer Res. 63:4792-4795(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BRD7.
    10. "Mammalian Ryk is a Wnt coreceptor required for stimulation of neurite outgrowth."
      Lu W., Yamamoto V., Ortega B., Baltimore D.
      Cell 119:97-108(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RYK.
    11. "Characterization of function of three domains in dishevelled-1: DEP domain is responsible for membrane translocation of dishevelled-1."
      Pan W.J., Pang S.Z., Huang T., Guo H.Y., Wu D., Li L.
      Cell Res. 14:324-330(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FZD7, MUTAGENESIS OF LYS-438, DOMAIN.
    12. "Independent mutations in mouse Vangl2 that cause neural tube defects in looptail mice impair interaction with members of the Dishevelled family."
      Torban E., Wang H.-J., Groulx N., Gros P.
      J. Biol. Chem. 279:52703-52713(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VANGL1 AND VANGL2.
    13. "The thioredoxin-related redox-regulating protein nucleoredoxin inhibits Wnt-beta-catenin signalling through dishevelled."
      Funato Y., Michiue T., Asashima M., Miki H.
      Nat. Cell Biol. 8:501-508(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NXN.
    14. "Loss of the tumor suppressor CYLD enhances Wnt/beta-catenin signaling through K63-linked ubiquitination of Dvl."
      Tauriello D.V., Haegebarth A., Kuper I., Edelmann M.J., Henraat M., Canninga-van Dijk M.R., Kessler B.M., Clevers H., Maurice M.M.
      Mol. Cell 37:607-619(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, DEUBIQUITINATION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CYLD.
    15. "Structural basis of the recognition of the dishevelled DEP domain in the Wnt signaling pathway."
      Wong H.C., Mao J., Nguyen J.T., Srinivas S., Zhang W., Liu B., Li L., Wu D., Zheng J.
      Nat. Struct. Biol. 7:1178-1184(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 395-495, FUNCTION, MUTAGENESIS OF LYS-438; ASP-449 AND ASP-452.
    16. "Direct binding of the PDZ domain of Dishevelled to a conserved internal sequence in the C-terminal region of Frizzled."
      Wong H.C., Bourdelas A., Krauss A., Lee H.J., Shao Y., Wu D., Mlodzik M., Shi D.L., Zheng J.
      Mol. Cell 12:1251-1260(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 251-345, INTERACTION WITH DACT1 AND FZD7.
    17. "Sulindac inhibits canonical Wnt signaling by blocking the PDZ domain of the protein Dishevelled."
      Lee H.J., Wang N.X., Shi D.L., Zheng J.J.
      Angew. Chem. Int. Ed. 48:6448-6452(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 248-337 IN COMPLEX WITH SULINDAC, INTERACTION WITH DACT1, FUNCTION.
    18. "Molecular basis of Wnt activation via the DIX-domain protein Ccd1."
      Liu Y.T., Dan Q.J., Wang J., Feng Y., Chen L., Liang J., Li Q., Lin S.C., Wang Z.X., Wu J.W.
      J. Biol. Chem. 286:8597-8608(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS) OF 4-104, MUTAGENESIS OF TYR-17, DOMAIN, SUBUNIT.

    Entry informationi

    Entry nameiDVL1_MOUSE
    AccessioniPrimary (citable) accession number: P51141
    Secondary accession number(s): Q3U2D3, Q60868
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 144 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, 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

    External Data

    Dasty 3