ASF also known as SF2 is a member of the SR protein family. It is an essential pre-mRNA splicing factor required for both single and alternative splicing. Phosphorylation on serine residues located within the SR domain directly regulates ASF/SF2 activity and compartmentalization of other SR splicing factors. In addition to interacting with RNA and other splicing factors, such as U1-70K, U2AF and other SR proteins, ASF/SF2 also directly or indirectly interacts with HIV regulatory protein Rev, the C-terminal domain (CTD) of the largest subunit of RNA polymerase II, and numerous transcription factors, thereby suggesting a potential role of ASF/SF2 in coordinating transcription and pre-mRNA splicing.
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SF2 is a protein factor essential for constitutive pre-mRNA splicing in HeLa cell extracts and also activates proximal alternative 5' splice sites in a concentration-dependent manner. This latter property suggests a role for SF2 in preventing exon skipping, ensuring the
SV40 early pre-mRNA is alternatively spliced by utilization of two different 5' splice sites and a shared 3' splice site to produce large T and small t mRNAs. The ratio of small t to large T mRNAs produced in human
We demonstrate that four different proteins from calf thymus are able to restore splicing in the same splicing-deficient extract using several different pre-mRNA substrates. These proteins are members of a conserved family of proteins recognized by a monoclonal antibody that
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