The PID domain specifically binds to the Asn-Pro-Xaa-Tyr(P) motif found in many tyrosine-phosphorylated proteins.
Signaling adapter of the reelin-mediated signaling pathway, which regulates the migration and differentiation of postmitotic neurons during brain development. Mediates intracellular transduction of Reelin signaling following reelin (RELN)-binding to its receptor: acts by docking proteins through its phosphotyrosine residues and PID domain.
Spinocerebellar ataxia 37
SCA37
A form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA37 is an autosomal dominant form characterized by adult-onset of slowly progressive gait instability, frequent falls, and dysarthria associated with cerebellar atrophy on brain imaging.
None
The disease is caused by variants affecting the gene represented in this entry.
Phosphorylated by FYN on Tyr-198 and Tyr-220 upon reelin induction in embryonic neurons. Also phosphorylated on Ser-524 independently of reelin signaling.
Ubiquitinated by various cullin-5-RING E3 ubiquitin-protein ligase complexes (ECS complexes) following ligand-binding and phosphorylation, leading to its degradation. Ubiquitinated by the ECS(SOCS7) complex in the cortical plate of the developing cerebral cortex following ligand-binding and phosphorylation by FYN, leading to its degradation by the proteasome. Recognized by ZSWIM8 through a disorder targets misorder mechanism that eliminates misfolded DAB1 via ubiquitination and proteasomal degradation (PubMed:35989311).
Mainly expressed in brain.
Disabled homolog 1, DAB1
Proteins
Cardiovascular
63775Da
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