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P51142

- DVL2_XENLA

UniProt

P51142 - DVL2_XENLA

Protein

Segment polarity protein dishevelled homolog DVL-2

Gene

dvl2

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Involved in at least 2 independent signaling cascades, controlling cell fate via canonical Wnt signaling and cell polarity via a planar cell polarity (PCP) cascade. Acts synergistically with dal/dapple-like to activate Wnt signaling, stabilizing ctnnb1/beta-catenin and leading to dorsal axis formation. Also prevents degradation of ctnnb1/beta-catenin by displacing gsk3 from a complex with ARP/Axin-related protein. Has an additional role in anterior-posterior (A/P) axis formation, specifying different neuroectodermal cell fates along the A/P axis in a dose-dependent manner by activating several early patterning genes. In the PCP pathway, required at the cell membrane for PCP-mediated neural and mesodermal convergent extension during gastrulation and subsequent neural tube closure, acting to activate jnk. Also involved in blastopore closure and archenteron elongation during early, but not late, gastrulation. Associates with ephrin receptors and ligands and acts as part of a downstream PCP pathway to mediate ephrin-mediated cell repulsion via activation of rhoa. Required for efnb1/ephrin-B1-driven movement of non-retinal progenitor cells into the retina during eye field formation. Patterns the hindbrain. Required for ciliogenesis. Controls the docking of basal bodies to the apical plasma membrane; mediates the activation, but not localization of rhoa at the apical surface of ciliated cells during basal body docking. Furthermore, required for the association of basal bodies with membrane-bound vesicles and the vesicle-trafficking protein exoc4/sec8, and this association is in turn required for basal body docking. Once basal bodies are docked, required for the planar polarization of basal bodies that underlies ciliary beating and the directional fluid flow across ciliated epithelia.17 Publications

    GO - Molecular functioni

    1. ephrin receptor binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. signal transducer activity Source: InterPro
    4. syndecan binding Source: UniProtKB

    GO - Biological processi

    1. activation of Rho GTPase activity Source: UniProtKB
    2. anterior/posterior axis specification Source: UniProtKB
    3. canonical Wnt signaling pathway Source: BHF-UCL
    4. ciliary basal body organization Source: UniProtKB
    5. cilium assembly Source: UniProtKB
    6. convergent extension Source: UniProtKB
    7. convergent extension involved in gastrulation Source: UniProtKB
    8. dorsal/ventral axis specification Source: UniProtKB
    9. ephrin receptor signaling pathway Source: UniProtKB
    10. establishment of planar polarity Source: UniProtKB
    11. establishment or maintenance of cell polarity Source: UniProtKB
    12. gastrulation with mouth forming second Source: UniProtKB
    13. intracellular signal transduction Source: InterPro
    14. neural tube closure Source: UniProtKB
    15. neurogenesis Source: UniProtKB
    16. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    17. protein homooligomerization Source: UniProtKB
    18. protein stabilization Source: UniProtKB
    19. Wnt signaling pathway Source: UniProtKB

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Cilium biogenesis/degradation, Gastrulation, Wnt signaling pathway

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Segment polarity protein dishevelled homolog DVL-2
    Short name:
    Dishevelled-2
    Alternative name(s):
    DSH homolog 2
    Xdsh
    Gene namesi
    Name:dvl2
    Synonyms:dsh
    OrganismiXenopus laevis (African clawed frog)
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Organism-specific databases

    XenbaseiXB-GENE-1017467. dvl2.

    Subcellular locationi

    Cytoplasm. Cytoplasmic vesicle. Cell projectioncilium. Nucleus. Cell membrane; Peripheral membrane protein
    Note: Phosphorylated and recruited from the cytoplasm to the cell membrane by frizzled proteins. Also relocated to the cell membrane by sdc4 and ephb1/ephrin-B1. Concentrated at cell membrane in both ciliated and non-ciliated cells. Enriched at the apical surface of ciliated cells. Localized to the cilium rootlet.

    GO - Cellular componenti

    1. cell cortex Source: MGI
    2. cell surface Source: UniProtKB
    3. ciliary rootlet Source: UniProtKB
    4. cytoplasm Source: UniProtKB
    5. cytoplasmic membrane-bounded vesicle Source: UniProtKB
    6. cytoplasmic vesicle Source: UniProtKB
    7. nucleus Source: UniProtKB
    8. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cilium, Cytoplasm, Cytoplasmic vesicle, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi272 – 2754QSNE → AANA: No effect on interaction with dact1-B/dpr.
    Mutagenesisi317 – 3171N → T: Abolishes interaction with dact1-B/dpr. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 736736Segment polarity protein dishevelled homolog DVL-2PRO_0000145748Add
    BLAST

    Post-translational modificationi

    Phosphorylated. Phosphorylation is controlled by frizzled proteins, correlates with the onset of embryo dorsalizing events and is higher in the dorsal half of early cleavage embryos. Phosphorylated on tyrosine residues in response to association with efnb1/ephrin-B1.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Expressioni

    Tissue specificityi

    Expressed equally in both animal-vegetal and dorsal-ventral directions of the early blastula. Becomes enriched on the dorsal side of the embryo after cortical rotation. Expressed along the anterior margin of eye field of neurulae (stage 16 embryos) and in the anterolateral crescent that borders the eye field. Continues to be expressed in the optic cup at stage 26. Expressed in the central nervous system throughout the early tailbud stage including the entire hindbrain.4 Publications

    Developmental stagei

    Expressed maternally. Most abundant in eggs and expressed at a low level in blastulae, gastrulae, neurulae and tailbud embryonic stages.1 Publication

    Interactioni

    Subunit structurei

    Can form homomultimers. Interacts with prickle1. Interacts (via PDZ domain) with ccdc88c/dal and dact1-B/dpr. Interacts (via DIX domain) with ARP/Axin-related protein and dact1-A/frodo. Interacts with sdc4, possibly via fz7. Interacts directly (via DEP domain) with efnb1/ephrin-B1 and indirectly with the phosphorylated ephrin receptors ephb1 and ephb2, via association with SH domain-containing adapters. May interact with lrrc6.10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    A5J0904EBI-6257503,EBI-7401819
    ctnnd1Q8AXM92EBI-6257503,EBI-6260685
    dact1-bQ8QG922EBI-6257503,EBI-6257549

    Protein-protein interaction databases

    BioGridi100626. 2 interactions.
    IntActiP51142. 5 interactions.
    MINTiMINT-100832.

    Structurei

    Secondary structure

    1
    736
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi252 – 2576
    Helixi259 – 2624
    Beta strandi267 – 2704
    Beta strandi281 – 2877
    Helixi291 – 2955
    Beta strandi303 – 3075
    Helixi317 – 32913
    Beta strandi330 – 3323
    Beta strandi334 – 3396

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1L6OX-ray2.20A/B/C252-340[»]
    2F0AX-ray1.80A/B/C/D252-340[»]
    3FY5X-ray2.40A/B254-343[»]
    ProteinModelPortaliP51142.
    SMRiP51142. Positions 252-340, 412-502.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP51142.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 8282DIXPROSITE-ProRule annotationAdd
    BLAST
    Domaini254 – 32673PDZPROSITE-ProRule annotationAdd
    BLAST
    Domaini428 – 50275DEPPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi99 – 11315Poly-ProAdd
    BLAST
    Compositional biasi222 – 2276Poly-Arg
    Compositional biasi680 – 6878Poly-Pro

    Domaini

    The C-terminal region containing the DEP domain is required for membrane accumulation and phosphorylation. Wnt signaling and axis induction requires the DIX domain. The C-terminus contributes to the localization at the cilia base.3 Publications

    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

    HOVERGENiHBG005542.
    KOiK02353.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    2.30.42.10. 1 hit.
    InterProiIPR000591. DEP_dom.
    IPR008341. Dishevelled_2.
    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:SF8. PTHR10878:SF8. 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.
    PR01762. DISHEVELLED2.
    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.

    P51142-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAETKVIYHL DEEETPYLVK VPVPATDIRL RDFKAALGRG HAKYFFKAMD    50
    QDFGVVKEEI SDDNAKLPCF NDRVVSWLAS SEGSQPDSAP PAPATEVRPE 100
    PPPPVPPPIP PPPAERTSGI GDSRPPSFHP NVSGSTEQLD QDNESVISMR 150
    RDRVRRRESS EQAGVGRGVN GRTERHLSGY ESSSTLLTSE IETSICDSEE 200
    DDTMSRFSSS TEQSSASRLL KRHRRRRKQR PPRLERTSSF SSVTDSTMSL 250
    NIITVTLNME KYNFLGISIV GQSNERGDGG IYIGSIMKGG AVAADGRIEP 300
    GDMLLQVNDI NFENMSNDDA VRVLRDIVHK PGPIVLTVAK CWDPSPQGYF 350
    TLPRNEPIHP IDPAAWVSHS AALSGSFPVY PGSASMSSMT SSTSVTETEL 400
    SHALPPVSLF SLSVHTDLAS VVKVMASPES GLEVRDRMWL KITIPNAFLG 450
    SDVVDWLYHH VEGFQDRREA RKFASNLLKA GFIRHTVNKI TFSEQCYYIF 500
    GDLTGCENYM TNLSLNDNDG SSGASDQDTL APLPLPGASP WPLLPTFSYQ 550
    YQAPHPYSTQ PPAYHELSSY SYGMGSAGSQ HSEGSRSSGS NRSDGGRGMQ 600
    KDDRSGVAGV GGGDSKSGSG SESEYSTRSS IRRVGGGEAG PPSERSTSSR 650
    LPPHHPPSVH SYAAPGVPLS YNPMMLMMMP PPPLPPPGVC PPNSSVPPGA 700
    PPLVRDLASV PPELTATRQS FHMAMGNPSE FFVDVM 736
    Length:736
    Mass (Da):79,787
    Last modified:October 1, 1996 - v1
    Checksum:iAF6C9A1662DD7CEB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U31552 mRNA. Translation: AAB00688.1.
    PIRiI51691.
    RefSeqiNP_001084096.1. NM_001090627.1.
    UniGeneiXl.7670.

    Genome annotation databases

    GeneIDi399301.
    KEGGixla:399301.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U31552 mRNA. Translation: AAB00688.1 .
    PIRi I51691.
    RefSeqi NP_001084096.1. NM_001090627.1.
    UniGenei Xl.7670.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1L6O X-ray 2.20 A/B/C 252-340 [» ]
    2F0A X-ray 1.80 A/B/C/D 252-340 [» ]
    3FY5 X-ray 2.40 A/B 254-343 [» ]
    ProteinModelPortali P51142.
    SMRi P51142. Positions 252-340, 412-502.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 100626. 2 interactions.
    IntActi P51142. 5 interactions.
    MINTi MINT-100832.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 399301.
    KEGGi xla:399301.

    Organism-specific databases

    CTDi 1856.
    Xenbasei XB-GENE-1017467. dvl2.

    Phylogenomic databases

    HOVERGENi HBG005542.
    KOi K02353.

    Miscellaneous databases

    EvolutionaryTracei P51142.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    2.30.42.10. 1 hit.
    InterProi IPR000591. DEP_dom.
    IPR008341. Dishevelled_2.
    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:SF8. PTHR10878:SF8. 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.
    PR01762. DISHEVELLED2.
    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. "Dorsalizing and neuralizing properties of Xdsh, a maternally expressed Xenopus homolog of dishevelled."
      Sokol S.Y., Klingensmith J., Perrimon N., Itoh K.
      Development 121:1637-1647(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Tissue: Oocyte.
    2. Erratum
      Sokol S.Y., Klingensmith J., Perrimon N., Itoh K.
      Development 121:3487-3487(1995) [PubMed] [Europe PMC] [Abstract]
    3. "Analysis of Dishevelled signalling pathways during Xenopus development."
      Sokol S.Y.
      Curr. Biol. 6:1456-1467(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    4. "Graded amounts of Xenopus dishevelled specify discrete anteroposterior cell fates in prospective ectoderm."
      Itoh K., Sokol S.Y.
      Mech. Dev. 61:113-125(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Establishment of the dorsal-ventral axis in Xenopus embryos coincides with the dorsal enrichment of dishevelled that is dependent on cortical rotation."
      Miller J.R., Rowning B.A., Larabell C.A., Yang-Snyder J.A., Bates R.L., Moon R.T.
      J. Cell Biol. 146:427-437(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    6. "Interaction of Frizzled 7 and Dishevelled in Xenopus."
      Medina A., Steinbeisser H.
      Dev. Dyn. 218:671-680(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. "Dishevelled phosphorylation, subcellular localization and multimerization regulate its role in early embryogenesis."
      Rothbaecher U., Laurent M.N., Deardorff M.A., Klein P.S., Cho K.W.Y., Fraser S.E.
      EMBO J. 19:1010-1022(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, SUBCELLULAR LOCATION, PHOSPHORYLATION, DOMAIN.
    8. "Interaction of dishevelled and Xenopus axin-related protein is required for wnt signal transduction."
      Itoh K., Antipova A., Ratcliffe M.J., Sokol S.Y.
      Mol. Cell. Biol. 20:2228-2238(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ARP, SUBCELLULAR LOCATION, DOMAIN.
    9. "Dishevelled controls cell polarity during Xenopus gastrulation."
      Wallingford J.B., Rowning B.A., Vogeli K.M., Rothbaecher U., Fraser S.E., Harland R.M.
      Nature 405:81-85(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    10. "Xenopus Dishevelled signaling regulates both neural and mesodermal convergent extension: parallel forces elongating the body axis."
      Wallingford J.B., Harland R.M.
      Development 128:2581-2592(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Neural tube closure requires Dishevelled-dependent convergent extension of the midline."
      Wallingford J.B., Harland R.M.
      Development 129:5815-5825(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Frodo interacts with Dishevelled to transduce Wnt signals."
      Gloy J., Hikasa H., Sokol S.Y.
      Nat. Cell Biol. 4:351-357(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DACT1-A.
    13. "The prickle-related gene in vertebrates is essential for gastrulation cell movements."
      Takeuchi M., Nakabayashi J., Sakaguchi T., Yamamoto T.S., Takahashi H., Takeda H., Ueno N.
      Curr. Biol. 13:674-679(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRICKLE1.
    14. "Association of Dishevelled with Eph tyrosine kinase receptor and ephrin mediates cell repulsion."
      Tanaka M., Kamo T., Ota S., Sugimura H.
      EMBO J. 22:847-858(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EFNB1; EPHB1 AND EPHB2, TISSUE SPECIFICITY, TYROSINE PHOSPHORYLATION.
    15. "Regional requirements for Dishevelled signaling during Xenopus gastrulation: separable effects on blastopore closure, mesendoderm internalization and archenteron formation."
      Ewald A.J., Peyrot S.M., Tyszka J.M., Fraser S.E., Wallingford J.B.
      Development 131:6195-6209(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "Subcellular localization and signaling properties of dishevelled in developing vertebrate embryos."
      Park T.J., Gray R.S., Sato A., Habas R., Wallingford J.B.
      Curr. Biol. 15:1039-1044(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    17. "Novel Daple-like protein positively regulates both the Wnt/beta-catenin pathway and the Wnt/JNK pathway in Xenopus."
      Kobayashi H., Michiue T., Yukita A., Danno H., Sakurai K., Fukui A., Kikuchi A., Asashima M.
      Mech. Dev. 122:1138-1153(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CCDC88C.
    18. "Identification of the Wnt signaling activator leucine-rich repeat in Flightless interaction protein 2 by a genome-wide functional analysis."
      Liu J., Bang A.G., Kintner C., Orth A.P., Chanda S.K., Ding S., Schultz P.G.
      Proc. Natl. Acad. Sci. U.S.A. 102:1927-1932(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "Dishevelled mediates ephrinB1 signalling in the eye field through the planar cell polarity pathway."
      Lee H.-S., Bong Y.-S., Moore K.B., Soria K., Moody S.A., Daar I.O.
      Nat. Cell Biol. 8:55-63(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EFNB1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    20. "Syndecan-4 regulates non-canonical Wnt signalling and is essential for convergent and extension movements in Xenopus embryos."
      Munoz R., Moreno M., Oliva C., Orbenes C., Larrain J.
      Nat. Cell Biol. 8:492-500(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SDC4, SUBCELLULAR LOCATION.
    21. "Cystic kidney gene seahorse regulates cilia-mediated processes and Wnt pathways."
      Kishimoto N., Cao Y., Park A., Sun Z.
      Dev. Cell 14:954-961(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LRRC6.
    22. "Dishevelled controls apical docking and planar polarization of basal bodies in ciliated epithelial cells."
      Park T.J., Mitchell B.J., Abitua P.B., Kintner C., Wallingford J.B.
      Nat. Genet. 40:871-879(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN.
    23. "Dapper, a Dishevelled-associated antagonist of beta-catenin and JNK signaling, is required for notochord formation."
      Cheyette B.N.R., Waxman J.S., Miller J.R., Takemaru K., Sheldahl L.C., Khlebtsova N., Fox E.P., Earnest T.N., Moon R.T.
      Dev. Cell 2:449-461(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 252-340 IN COMPLEX WITH DACT1-B, FUNCTION, INTERACTION WITH DACT1-B, SUBCELLULAR LOCATION, MUTAGENESIS OF 272-GLN--GLU-275 AND ASN-317.
    24. "Conformational flexibility in the PDZ domain of Dishevelled induced by target binding."
      Friedland N., Hung L.-W., Cheyette B.N.R., Miller J.R., Moon R.T., Earnest T.N.
      Submitted (NOV-2005) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 252-340.

    Entry informationi

    Entry nameiDVL2_XENLA
    AccessioniPrimary (citable) accession number: P51142
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 113 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3