PROSITE documentation PDOC51070
Stonin homology domain (SHD) profile


Human stonins, like their Drosophila homologue stoned B are supposed to be endocytotic proteins involved in clathrin-mediated endocytosis at synapses. The two human stonins, as well as their Drosophila melanogaster and Caenorhabditis elegans homologues, exhibit a modular structure consisting of an N-terminal proline- and serine-rich domain, a central stonin homology domain (SHD), and a C-terminal domain homologous to the signal-binding domain of the mu subunits of adaptor protein (AP) complexes (mu-homology domain) (see <PDOC51072>). The ~140 amino-acid SHD domain has not been described in other proteins and may thus be unique to members of the stonin family. Its function is not yet known [1,2].

The profile we developed covers the entire SHD domain.

Last update:

January 2005 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

SHD, PS51070; Stonin homology domain (SHD) profile  (MATRIX)


1AuthorsMartina J.A. Bonangelino C.J. Aguilar R.C. Bonifacino J.S.
TitleStonin 2: an adaptor-like protein that interacts with components of the endocytic machinery.
SourceJ. Cell Biol. 153:1111-1120(2001).
PubMed ID11381094

2AuthorsWalther K. Diril M.K. Jung N. Haucke V.
TitleFunctional dissection of the interactions of stonin 2 with the adaptor complex AP-2 and synaptotagmin.
SourceProc. Natl. Acad. Sci. U.S.A. 101:964-969(2004).
PubMed ID14726597

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