InterPro domain: IPR004015

SKIP (SKI-interacting protein) is an essential spliceosomal component and transcriptional coregulator, which may provide regulatory coupling of transcription initiation and splicing [ 1 ]. SKIP was identified in a yeast 2-hybrid screen, where it was shown to interact with both the cellular and viral forms of SKI through the highly conserved region on SKIP known as the SNW domain [ 2 ]. SKIP is now known to interact with a number of other proteins as well. SKIP potentiates the activity of important transcription factors, such as vitamin D receptor, CBF1 (RBP-Jkappa), Smad2/3, and MyoD. It works with Ski in overcoming pRb-mediated cell cycle arrest, and it is targeted by the viral transactivators EBNA2 and E7 [ 3 ].

This entry represents the SNW domain.

1. Transcriptional coregulator SNW/SKIP: the concealed tie of dissimilar pathways. Cell. Mol. Life Sci. 61, 629-40
2. Ski interacts with the evolutionarily conserved SNW domain of Skip. Nucleic Acids Res. 29, 3469-76
3. A role for SKIP in EBNA2 activation of CBF1-repressed promoters. J. Virol. 74, 1939-47