PROSITE documentation PDOC51070Stonin 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.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Martina J.A. Bonangelino C.J. Aguilar R.C. Bonifacino J.S. |
| Title | Stonin 2: an adaptor-like protein that interacts with components of the endocytic machinery. | |
| Source | J. Cell Biol. 153:1111-1120(2001). | |
| PubMed ID | 11381094 |
| 2 | Authors | Walther K. Diril M.K. Jung N. Haucke V. |
| Title | Functional dissection of the interactions of stonin 2 with the adaptor complex AP-2 and synaptotagmin. | |
| Source | Proc. Natl. Acad. Sci. U.S.A. 101:964-969(2004). | |
| PubMed ID | 14726597 | |
| DOI | 10.1073/pnas.0307862100 |
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