Tuftelin-interacting protein 11 (TFIP11)

Tuftelin-interacting protein 11 (TFIP11) is an **RNA-binding protein** and a component of the spliceosome that primarily promotes the release of the lariat-intron during late-stage pre-mRNA splicing[3][6]. It contains a G-patch domain characteristic of RNA-processing proteins, enabling binding to DEAH-box helicase 15 (DHX15), and is involved in **spliceosome disassembly** by mediating the transition of U2, U5, and U6 snRNP-containing complexes to snRNP-free states, thereby facilitating intron turnover[3][6]. TFIP11 also plays an essential role in the 2'-O-methylation of U6 small nuclear RNA, which is required for proper assembly of the U4/U6.U5 tri-snRNP and splicing fidelity[2]. The protein localizes to nuclear speckles, Cajal bodies, and nucleoli, and its cellular functions are largely RNA-dependent[1][2]. TFIP11 is expressed ubiquitously and, though identified through interaction with tuftelin in teeth, is involved in fundamental RNA processing in multiple tissues, with some evidence linking polymorphisms in the gene to dental caries[3]. TFIP11 is not established as a direct therapeutic target, nor are there known drugs or biomarkers associated with its modulation.

Other names

Tuftelin-interacting protein 11TFIP11STIPHSPC006STIP-1TIP39DKFZP434B194Spp382Septin and tuftelin-interacting protein 1NTR1sip1/tuftelin interacting proteinseptin and tuftelin-interacting protein 1bK445C9.6