Segment polarity protein dishevelled homolog DVL-1 - O14640 (DVL1_HUMAN)


Protein Feature View of PDB entries mapped to a UniProtKB sequence  

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). UniProt
Pathway Maps
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Subunit Structure
Interacts with CXXC4. Interacts (via PDZ domain) with NXN (By similarity). Interacts with BRD7 and INVS. Interacts (via PDZ domain) with VANGL1 and VANGL2 (via C-terminus). Interacts with ARRB1; the interaction is enhanced by phosphorylation of DVL1. Interacts with CYLD (By similarity). 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 (By similarity). 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 similarity). Interacts (via PDZ domain) with TMEM88. Interacts with DCDC2. Interacts with FOXK2 (PubMed:25805136). Interacts with PKD1 (via extracellular domain) (PubMed:27214281). Interacts (via PDZ domain) with CCDC88C/DAPLE; competes with CCDC88C for binding to frizzled receptor FZD7 and dissociates from CCDC88C following initiation of non-canonical Wnt signaling when CCDC88C displaces DVL1 from ligand-activated FZD7 (PubMed:26126266, PubMed:14750955). UniProt
The DEP domain mediates interaction with the cell membrane. UniProt
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