SRSF6

SRSF6 is involved in mRNA splicing and may play a role in the determination of alternative splicing. The encoded nuclear protein belongs to the splicing factor SR family and has been shown to bind with and modulate another member of the family, SFRS12.

Full Name

Serine And Arginine Rich Splicing Factor 6

Function

Plays a role in constitutive splicing and modulates the selection of alternative splice sites. Plays a role in the alternative splicing of MAPT/Tau exon 10. Binds to alternative exons of TNC pre-mRNA and promotes the expression of alternatively spliced TNC. Plays a role in wound healing and in the regulation of keratinocyte differentiation and proliferation via its role in alternative splicing.

Biological Process

Biological Process alternative mRNA splicing, via spliceosomeManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process mRNA splice site selectionManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process mRNA splicing, via spliceosomeManual Assertion Based On ExperimentIBA:GO_Central
Biological Process negative regulation of cell deathManual Assertion Based On ExperimentIDA:MGI
Biological Process negative regulation of keratinocyte differentiationManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process negative regulation of mRNA splicing, via spliceosomeManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process negative regulation of type B pancreatic cell apoptotic processIEA:Ensembl
Biological Process positive regulation of epithelial cell proliferation involved in lung morphogenesisManual Assertion Based On ExperimentIDA:MGI
Biological Process regulation of alternative mRNA splicing, via spliceosomeManual Assertion Based On ExperimentIDA:MGI
Biological Process regulation of keratinocyte proliferationManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process regulation of wound healingManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process response to insulinIEA:Ensembl

Cellular Location

Nucleus
Nucleus speckle

PTM

Extensively phosphorylated on serine residues in the RS domain. Phosphorylated by DYRK1A, probably in the RS domain. Phosphorylation by DYRK1A modulates alternative splice site selection and inhibits the expression of MAPT/Tau exon 10.