ZRSR2

This gene encodes an essential splicing factor. The encoded protein associates with the U2 auxiliary factor heterodimer, which is required for the recognition of a functional 3' splice site in pre-mRNA splicing, and may play a role in network interactions during spliceosome assembly.

zinc finger CCCH-type, RNA binding motif and serine/arginine rich 2

Necessary for the splicing of pre-mRNA. It is required for formation of the earliest ATP-dependent splicing complex and interacts with spliceosomal components bound to both the 5'- and 3'-splice sites during spliceosome assembly. It also is required for ATP-dependent interactions of both U1 and U2 snRNPs with pre-mRNA. Interacts with other spliceosomal components, via the RS domains, to form a bridge between the 5'- and 3'-splice site binding components, U1 snRNP and U2AF. Binds to purine-rich RNA sequences, either 5'-AGSAGAGTA-3' (S=C or G) or 5'-GTTCGAGTA-3'. Can bind to beta-globin mRNA and commit it to the splicing pathway. The phosphorylated form (by SRPK2) is required for cellular apoptosis in response to cisplatin treatment.

Biological Process mitotic cell cycle Source:Ensembl
Biological Process mRNA processing Source:ProtInc1 Publication
Biological Process mRNA splicing, via spliceosome Source:GO_Central1 Publication
Biological Process regulation of alternative mRNA splicing, via spliceosome Source:Ensembl
Biological Process response to vitamin E Source:Ensembl
Biological Process RNA splicing Source:ProtInc1 Publication

Nucleus
Nucleus, nucleoplasm
Nucleus speckle
Note: Phosphorylation by SRPK2 provokes its redistribution from the nuclear speckle to nucleoplasm.

Extensively phosphorylated on serine residues in the RS domain. Phosphorylated by SRPK2 and this causes its redistribution from the nuclear speckle to nucleoplasm and controls cell fate decision in response to cisplatin treatment. KAT5/TIP60 inhibits its phosphorylation by preventing SRPK2 nuclear translocation.
Acetylation on Lys-52 by KAT5/TIP60 promotes its proteasomal degradation. This effect is counterbalanced by HDAC6, which positively controls SRSF2 protein level by deacetylating it and preventing its proteasomal degradation.