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Protein Page:
DVL3 (human)

Overview
DVL3 a protein in the WNT/planar cell polarity (PCP) signaling pathway. Dvl2-deficient mice indicate that Dvl2 is essential for normal cardiac morphogenesis, somite segmentation and neural tube closure. Transduces the Wnt signal by interacting with the cytoplasmic Axin complex. Dvl and Axin each contain a DIX domains, which mediate their dynamic polymerization. The Dvl-Axin interaction is essential for Wnt signaling. Interacts through its PDZ domain with the C-terminal regions of VANGL1 and VANGL2. Interacts with Dixin and Rac. There is functional redundancy between Dvl1 and Dvl2 in some phenotypes. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis
Chromosomal Location of Human Ortholog: 3q27
Cellular Component: cytosol; nuclear chromatin
Molecular Function: beta-catenin binding; frizzled binding; protease binding; protein binding; protein heterodimerization activity; Rac GTPase binding; receptor binding
Biological Process: positive regulation of GTPase activity; positive regulation of JNK activity; positive regulation of protein amino acid phosphorylation; positive regulation of transcription, DNA-dependent; protein stabilization; Wnt receptor signaling pathway; Wnt receptor signaling pathway through beta-catenin; Wnt receptor signaling pathway, planar cell polarity pathway
Disease: Robinow Syndrome, Autosomal Dominant 3
Reference #:  Q92997 (UniProtKB)
Alt. Names/Synonyms: dishevelled 3 (homologous to Drosophila dsh); dishevelled, dsh homolog 3 (Drosophila); Dishevelled-3; DSH homolog 3; DVL3; KIAA0208; Segment polarity protein dishevelled homolog DVL-3
Gene Symbols: DVL3
Molecular weight: 78,055 Da
Basal Isoelectric point: 6.18  Predict pI for various phosphorylation states
CST Pathways:  Hippo Signaling  |  Microtubule Dynamics  |  mTOR Signaling  |  Translation: eIF4E and p70S6K  |  Wnt/ß-Catenin Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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DVL3

Protein Structure Not Found.


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