Amphiphysin 2 (IPR003023)

Short name: Amphiphysin_2

Overlapping homologous superfamilies


Family relationships


Amphiphysins belong to the expanding BAR (Bin-Amphiphysin-Rvsp) family proteins, all members of which share a highly conserved N-terminal BAR domain, which has predicted coiled-coil structures required for amphiphysin dimerisation and plasma membrane interaction [PMID: 12047553]. Almost all members also share a conserved C-terminal Src homology 3 (SH3) domain, which mediates their interactions with the GTPase dynamin and the inositol-5'-phosphatase synaptojanin 1 in vertebrates and with actin in yeast. The central region of all these proteins is most variable. In mammals, the central region of amphiphysin I and amphiphysin IIa contains a proline-arginine-rich region for endophilin binding and a CLAP domain, for binding to clathrin and AP-2. The interactions mediated by both the central and C-terminal domains are believed to be modulated by protein phosphorylation [PMID: 9720601, PMID: 10559861].

Amphiphysins are proteins that are thought to be involved in clathrin-mediated endocytosis, actin function, and signalling pathways. In vertebrates, amphiphysins may regulate, but are not essential for clathrin-mediated endocytosis of SVs. However, in Drosophila amphiphysin is not involved at all in SV endocytosis but is required for T-tubule structure and excitation-contraction coupling muscles and plays a role in membrane morphogenesis in developing photoreceptors and a variety of other cells [PMID: 12047553].

Amphiphysin 2 was the second amphiphysin family member found in mammals. The gene encoding it has been found to be alternatively spliced. The various products have been named: BIN-1, Sh3P9, BRAMP-2 and ALP-1. They have different distribution patterns, with the largest form (~95 kD) being expressed solely in the brain, where it shares a very similar (if not identical) distribution pattern to amphiphysin 1 [PMID: 9720601].

GO terms

Biological Process

GO:0030100 regulation of endocytosis

Molecular Function

No terms assigned in this category.

Cellular Component

No terms assigned in this category.

Contributing signatures

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