Splicing factor 3B subunit 6 (SF3B6)

Splicing factor 3B subunit 6 (SF3B6) is a protein component of the SF3B subcomplex within the major and minor spliceosomes, where it is critical for early steps in intron removal from pre-mRNA. SF3B6 plays a key role in stabilizing interactions between the pre-mRNA branch site and U2 snRNA, enabling precise selection and catalysis during splicing—particularly for introns with poor sequence complementarity. It directly contacts the branch site adenosine for the first catalytic step of splicing, and participates in allosteric regulation of SF3B1 for branch point recognition. SF3B6 possesses a conserved RNA recognition motif but its direct RNA-binding activity may be structurally occluded in the integrated complex. SF3B6 is present in humans and some other eukaryotes but absent in yeast, suggesting a specialized role in higher organisms. There is no direct evidence for SF3B6 as a therapeutic drug target, and no known drugs or biomarkers specifically engage this protein. However, perturbations in spliceosome function are linked to cancer and other diseases, making SF3B6 part of a protein complex relevant to gene regulation and disease biology.

Other names

SAP14SF3B14SF3B14ACGI-110HSPC175HT006SF3B14aP14SAP14aPre-mRNA branch site protein p14Spliceosome-associated protein 14 kDaSplicing factor 3b subunit 614kDapre-mRNA branch site protein p14spliceosome-associated protein 14 kDasplicing factor 3B 14 kDa subunitSF3b 14 kDa subunit

Not applicable; no drugs known to act directly on SF3B6. For the SF3B complex (especially SF3B1), mechanisms include inhibition of spliceosome assembly and alteration of branch site recognition, but this is not directly relevant to SF3B6 as a solo target.