Amyloid beta A4 precursor protein-binding family A member 1 (IPR030530)

Short name: Apba1

Overlapping homologous superfamilies


Family relationships



Amyloid beta A4 precursor protein-binding family A member 1, also known as Mint1 or X11alpha, is a neuronal adaptor protein that binds to the intracellular domain of the amyloid precursor protein (APP) [PMID: 12970358]. It belongs to the X11/Mint family of adaptor proteins [PMID: 16764936]. It has been shown to modulate processing of APP and accumulation of Abeta (hallmark pathologies of Alzheimer's disease), making it a potential therapeutic target for Alzheimer's disease [PMID: 20378958]. It may also affect Alzheimer's disease pathogenesis through its interaction with transcription factor FSBP (fibrinogen silencer binding protein), forming a complex that represses glycogen synthase kinase-3beta (GSK3beta) transcription. GSK3beta is a candidate kinase for the phosphorylation of tau in Alzheimer's disease [PMID: 20531236].

X11alpha participates in a brain-specific heterotrimeric complex containing two other PDZ domain proteins, Lin-2/CASK and mLin-7, involved in synaptic vesicle exocytosis and synaptic junctions [PMID: 9753324]. Additional proteins can bind, forming a neuronal multiprotein complex predicted to be involved in receptor localisation [PMID: 9952408].

The X11/Mint family members are multidomain proteins typically composed of a conserved PTB domain and two C-terminal PDZ domains. They are adaptor proteins that possess several functions, such as trafficking and transport, synaptic function and regulation of ion channel [PMID: 16764936]. Two of the family members, X11alpha and X11beta, are expressed primarily in neurones [PMID: 16764936].

GO terms

Biological Process

GO:0007268 chemical synaptic transmission
GO:0065003 protein-containing complex assembly

Molecular Function

GO:0001540 amyloid-beta binding

Cellular Component

GO:0008021 synaptic vesicle

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.