Splicing factor binding to exonic or intronic sites and acting as either an activator or repressor of exon inclusion (PubMed:22523384). Exhibits a binding preference for CA-rich elements. Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and associated with most nascent transcripts. Associates, together with APEX1, to the negative calcium responsive element (nCaRE) B2 of the APEX2 promoter. As part of a ribonucleoprotein complex composed at least of ZNF827, HNRNPK and the circular RNA circZNF827 that nucleates the complex on chromatin, may negatively regulate the transcription of genes involved in neuronal differentiation (By similarity). Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with HNRNPLL. Interacts with APEX1; the interaction is DNA-dependent. Component of a complex with SETD2 (By similarity). Interacts with ELAVL1 (By similarity). Part of a transcription inhibitory ribonucleoprotein complex composed at least of the circular RNA circZNF827, ZNF827 and HNRNPK (By similarity). Localized in cytoplasmic mRNP granules containing untranslated mRNAs. These granules are not identical with P bodies or stress granules. Detected in hematopoietic cells, including lymphoid progenitor cells. RRM domain 2 has moderate RNA-binding affinity. RRM domains 3 and 4 may facilitate RNA looping when binding to two appropriately separated binding sites within the same target pre-mRNA. Phosphorylation at Ser-541 by CaMK4 enhances interaction with a CaMK4-responsive RNA element (CaRRE1), and prevents inclusion of the stress axis-regulated exon (STREX) of the KCNMA1 potassium channel transcripts upon membrane depolarization. Complete lethality during early embryonic development. Truncated N-terminus.