Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain-containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. Plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. Self-associates to form homooligomers when bound to RNA, oligomerization appears to be limited when binding to proteins. Predominantly located in the nucleus but also located partially in the cytoplasm. The KH domain is required for binding to RNA. Tyrosine phosphorylated by several non-receptor tyrosine kinases including LCK, FYN and JAK3. Acetylated. Positively correlates with ability to bind RNA (By similarity). Methylated by HRMT1L2. Required for nuclear localization (By similarity). Belongs to the KHDRBS family.