Go Annotations as Summary Text (Tabular View) (GO Graph)

GO curators for mouse genes have assigned the following annotations to the gene product of Dvl2. (This text reflects annotations as of Wednesday, August 14, 2013.) MGI curation of this mouse gene is considered complete, including annotations derived from the biomedical literature as of August 27, 2010. If you know of any additional information regarding this mouse gene please let us know. Please supply mouse gene symbol and a PubMed ID.

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Summary from NCBI RefSeq

[Summary is not available for the mouse gene. This summary is for the human ortholog.] This gene encodes a member of the dishevelled (dsh) protein family. The vertebrate dsh proteins have approximately 40% amino acid sequence similarity with Drosophila dsh. This gene encodes a 90-kD protein that undergoes posttranslational phosphorylation to form a 95-kD cytoplasmic protein, which may play a role in the signal transduction pathway mediated by multiple Wnt proteins. The mechanisms of dishevelled function in Wnt signaling are likely to be conserved among metazoans. [provided by RefSeq, Jul 2008]

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Summary text based on GO annotations supported by experimental evidence in mouse

• Researchers have inferred from direct assay, that the gene product of Dvl2
  • participates in the following biological processes:
    • canonical Wnt receptor signaling pathway ^[21]
    • cellular protein localization ^[15]
    • positive regulation of JUN kinase activity ^[23]
    • Wnt receptor signaling pathway ^[8]
  • performs the following molecular functions:
    • protein self-association ^[10]
  • is located in the following cellular components:
    • apical part of cell ^[13]
    • clathrin-coated vesicle ^[14]
    • cytoplasm ^{[2, 15]}
    • cytosol ^[10]
    • plasma membrane ^{[1, 14, 18, 19]}
• The gene product of Dvl2 has been shown to bind to the gene products of Dab2, Dact1, Dvl3, Src, Vangl1, Vangl2. ^{[5, 7, 10, 12, 16, 17, 22]} Researchers have inferred, based on physical interactions, that the gene product of Dvl2
  • performs the following molecular functions:
    • frizzled binding ^[20]
    • identical protein binding ^[10]
    • protein domain specific binding ^[11]
• Researchers have inferred, based on phenotypic analysis of mouse mutants, that the gene product of Dvl2
  • participates in the following biological processes:
    • canonical Wnt receptor signaling pathway ^[3]
    • convergent extension involved in neural plate elongation ^[18]
    • heart development ^{[4, 6]}
    • neural tube closure ^[4]
    • outflow tract morphogenesis ^[6]
    • planar cell polarity pathway involved in neural tube closure ^[18]
    • positive regulation of canonical Wnt receptor signaling pathway ^[10]
    • segment specification ^[4]
  • is located in the following cellular components:
    • nucleus ^[2]
• Researchers have inferred, based on genetic interactions, that the gene product of Dvl2
  • participates in the following biological processes:
    • canonical Wnt receptor signaling pathway based on interactions with Csnk1e, Wnt3a ^{[9, 15]}
    • cochlea morphogenesis based on interactions with Dvl1, Dvl3 ^{[3, 19]}
    • convergent extension involved in neural plate elongation based on interactions with Dvl1, Vangl2 ^[18]
    • convergent extension involved in organogenesis based on interactions with Dvl1 ^[19]
    • heart morphogenesis based on interactions with Dvl3 ^[3]
    • planar cell polarity pathway involved in neural tube closure based on interactions with Dvl1, Vangl2 ^[18]
    • positive regulation of protein tyrosine kinase activity based on interactions with Wnt3a ^[22]
    • segmentation based on interactions with ^[8]
    • Wnt receptor signaling pathway, planar cell polarity pathway based on interactions with Dvl1 ^[19]
  • is located in the following cellular components:
    • plasma membrane based on interactions with Wnt3a ^[15]

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Summary text based on GO annotations supported by experimental evidence in other organisms

• From comparative sequence analysis (see table for details), MGI curators have determined that the gene product of Dvl2:
  • participates in the following biological processes:
    • canonical Wnt receptor signaling pathway
    • canonical Wnt receptor signaling pathway involved in regulation of cell proliferation
    • cell migration in hindbrain
    • non-canonical Wnt receptor signaling pathway
    • positive regulation of JUN kinase activity
    • positive regulation of protein phosphorylation
    • positive regulation of sequence-specific DNA binding transcription factor activity
    • positive regulation of transcription, DNA-dependent
    • regulation of JNK cascade
    • transcription from RNA polymerase II promoter
    • Wnt receptor signaling pathway
    • Wnt receptor signaling pathway, planar cell polarity pathway
  • performs the following molecular functions:
    • frizzled binding
    • identical protein binding
  • is located in the following cellular components:
    • cell cortex
    • cytoplasm

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Summary text based on GO annotations supported by structural data

• Dvl2 encodes a protein or proteins that contain the following InterPro domains: DEP domain, Dishevelled C-terminal, Dishevelled family, Dishevelled protein domain, Dishevelled-2, Dishevelled-related protein, DIX domain, PDZ domain, Winged helix-turn-helix DNA-binding domain, indicating that the gene product:
  • participates in the following biological processes:
    • intracellular signal transduction
    • multicellular organismal development
  • performs the following molecular functions:
    • signal transducer activity
  • is located in the following cellular components:
    • intracellular

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Summary text for additional MGI annotations

• Automated translation to GO terms of SwissProt keywords that describe Dvl2 indicates that it:
  • participates in the following biological processes:
    • multicellular organismal development
  • is located in the following cellular components:
    • cytoplasmic vesicle
    • membrane

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References

1. Babayeva S et al. (2011) Planar cell polarity pathway regulates actin rearrangement, cell shape, motility, and nephrin distribution in podocytes. Am J Physiol Renal Physiol, 300:F549-60. (PubMed:20534871)
2. Bouteille N et al. (2009) Inhibition of the Wnt/beta-catenin pathway by the WWOX tumor suppressor protein. Oncogene, 28:2569-80. (PubMed:19465938)
3. Etheridge SL et al. (2008) Murine dishevelled 3 functions in redundant pathways with dishevelled 1 and 2 in normal cardiac outflow tract, cochlea, and neural tube development. PLoS Genet, 4:e1000259. (PubMed:19008950)
4. Hamblet NS et al. (2002) Dishevelled 2 is essential for cardiac outflow tract development, somite segmentation and neural tube closure. Development, 129:5827-38. (PubMed:12421720)
5. Hocevar BA et al. (2003) Regulation of the Wnt signaling pathway by disabled-2 (Dab2). EMBO J, 22:3084-94. (PubMed:12805222)
6. Kioussi C et al. (2002) Identification of a Wnt/Dvl/beta-Catenin --> Pitx2 Pathway Mediating Cell-Type-Specific Proliferation during Development. Cell, 111:673-85. (PubMed:12464179)
7. Kivimae S et al. (2011) All Dact (Dapper/Frodo) scaffold proteins dimerize and exhibit conserved interactions with Vangl, Dvl, and serine/threonine kinases. BMC Biochem, 12:33. (PubMed:21718540)
8. Klingensmith J et al. (1996) Conservation of dishevelled structure and function between flies and mice: isolation and characterization of Dvl2. Mech Dev, 58:15-26. (PubMed:8887313)
9. Lee JS et al. (1999) Characterization of mouse dishevelled (Dvl) proteins in Wnt/Wingless signaling pathway. J Biol Chem, 274:21464-70. (PubMed:10409711)
10. Liu YT et al. (2011) Molecular basis of Wnt activation via the DIX domain protein Ccd1. J Biol Chem, 286:8597-608. (PubMed:21189423)
11. Luo W et al. (2005) Axin contains three separable domains that confer intramolecular, homodimeric, and heterodimeric interactions involved in distinct functions. J Biol Chem, 280:5054-60. (PubMed:15579909)
12. Ma L et al. (2010) Dishevelled-3 C-terminal His single amino acid repeats are obligate for Wnt5a activation of non-canonical signaling. J Mol Signal, 5:19. (PubMed:21092292)
13. Matsuyama M et al. (2009) Sfrp controls apicobasal polarity and oriented cell division in developing gut epithelium. PLoS Genet, 5:e1000427. (PubMed:19300477)
14. Na J et al. (2007) Dishevelled proteins regulate cell adhesion in mouse blastocyst and serve to monitor changes in Wnt signaling. Dev Biol, 302:40-9. (PubMed:17005174)
15. Schwarz-Romond T et al. (2007) Dynamic recruitment of axin by Dishevelled protein assemblies. J Cell Sci, 120:2402-12. (PubMed:17606995)
16. Suriben R et al. (2009) Posterior malformations in Dact1 mutant mice arise through misregulated Vangl2 at the primitive streak. Nat Genet, 41:977-85. (PubMed:19701191)
17. Torban E et al. (2004) Independent mutations in mouse Vangl2 that cause neural tube defects in looptail mice impair interaction with members of the Dishevelled family. J Biol Chem, 279:52703-13. (PubMed:15456783)
18. Wang J et al. (2006) Dishevelled genes mediate a conserved mammalian PCP pathway to regulate convergent extension during neurulation. Development, 133:1767-78. (PubMed:16571627)
19. Wang J et al. (2005) Regulation of polarized extension and planar cell polarity in the cochlea by the vertebrate PCP pathway. Nat Genet, 37:980-5. (PubMed:16116426)
20. Wheeler DS et al. (2011) Direct interaction between NHERF1 and Frizzled regulates beta-catenin signaling. Oncogene, 30:32-42. (PubMed:20802536)
21. Yamamoto S et al. (2008) Cthrc1 selectively activates the planar cell polarity pathway of Wnt signaling by stabilizing the Wnt-receptor complex. Dev Cell, 15:23-36. (PubMed:18606138)
22. Yokoyama N et al. (2009) Dishevelled-2 docks and activates Src in a Wnt-dependent manner. J Cell Sci, 122:4439-51. (PubMed:19920076)
23. Zhang Y et al. (2000) Dimerization choices control the ability of axin and dishevelled to activate c-Jun N-terminal kinase/stress-activated protein kinase. J Biol Chem, 275:25008-14. (PubMed:10829020)

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Gene Ontology Evidence Code Abbreviations:

EXP Inferred from experiment

IC Inferred by curator

IDA Inferred from direct assay

IEA Inferred from electronic annotation

IGI Inferred from genetic interaction

IMP Inferred from mutant phenotype

IPI Inferred from physical interaction

ISS Inferred from sequence or structural similarity

ISO Inferred from sequence orthology

ISA Inferred from sequence alignment

ISM Inferred from sequence model

NAS Non-traceable author statement

ND No biological data available

RCA Reviewed computational analysis

TAS Traceable author statement

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