InterPro : IPR024933

Name  Septin and tuftelin interacting protein Short Name  STIP
Type  Family Description  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 []. The Drosophila protein STP1 was originally identified as a septin-interacting protein []. 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 [, ]. STIP is essential for embryogenesis in Caenorhabditis elegans [].
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InterPro protein domain ID --> Contigs

 

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5 Publications

First Author Title Year Journal Volume Pages
Paine CT Identification of tuftelin- and amelogenin-interacting proteins using the yeast two-hybrid system. 1998 Connect Tissue Res 38 257-67;discussion 295-303
Ji Q Characterization of STIP, a multi-domain nuclear protein, highly conserved in metazoans, and essential for embryogenesis in Caenorhabditis elegans. 2007 Exp Cell Res 313 1460-72
Shih HP Identification of septin-interacting proteins and characterization of the Smt3/SUMO-conjugation system in Drosophila. 2002 J Cell Sci 115 1259-71
Wen X Structural organization and cellular localization of tuftelin-interacting protein 11 (TFIP11). 2005 Cell Mol Life Sci 62 1038-46
Herold N Conservation of the protein composition and electron microscopy structure of Drosophila melanogaster and human spliceosomal complexes. 2009 Mol Cell Biol 29 281-301



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)