InterPro domain: IPR024933

Septin and tuftelin interacting proteins (STIPs) are G-patch domain proteins that are conserved in metazoans. The mouse protein, known as TFT11 was originally identified as a protein interacting with tuftelin, one of the presumed enamel matrix proteins [ 1 ]. The Drosophila protein STP1 was originally identified as a septin-interacting protein [ 2 ]. In both cases these interactions were identified by a yeast two-hybrid system and their function and direct physical association were not characterised. Subsequent studies show that these proteins are widely expressed and function as splicing factors [ 3 , 4 ]. STIP is essential for embryogenesis in Caenorhabditis elegans [ 5 ].

1. Identification of tuftelin- and amelogenin-interacting proteins using the yeast two-hybrid system. Connect. Tissue Res. 38, 257-67;discussion 295-303
2. Identification of septin-interacting proteins and characterization of the Smt3/SUMO-conjugation system in Drosophila. J. Cell. Sci. 115, 1259-71
3. Structural organization and cellular localization of tuftelin-interacting protein 11 (TFIP11). Cell. Mol. Life Sci. 62, 1038-46
4. Conservation of the protein composition and electron microscopy structure of Drosophila melanogaster and human spliceosomal complexes. Mol. Cell. Biol. 29, 281-301
5. Characterization of STIP, a multi-domain nuclear protein, highly conserved in metazoans, and essential for embryogenesis in Caenorhabditis elegans. Exp. Cell Res. 313, 1460-72