SRPK2

SRPK2 (SRSF Protein Kinase 2) is a Protein Coding gene. Among its related pathways are mRNA Splicing - Major Pathway. Gene Ontology (GO) annotations related to this gene include protein kinase activity. An important paralog of this gene is SRPK1.

SRSF Protein Kinase 2

Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing (PubMed:9472028, PubMed:18559500, PubMed:21056976).
Promotes neuronal apoptosis by up-regulating cyclin-D1 (CCND1) expression (PubMed:19592491).
This is done by the phosphorylation of SRSF2, leading to the suppression of p53/TP53 phosphorylation thereby relieving the repressive effect of p53/TP53 on cyclin-D1 (CCND1) expression (PubMed:21205200).
Phosphorylates ACIN1, and redistributes it from the nuclear speckles to the nucleoplasm, resulting in cyclin A1 but not cyclin A2 up-regulation (PubMed:18559500).
Plays an essential role in spliceosomal B complex formation via the phosphorylation of DDX23/PRP28 (PubMed:18425142).
Probably by phosphorylating DDX23, leads to the suppression of incorrect R-loops formed during transcription; R-loops are composed of a DNA:RNA hybrid and the associated non-template single-stranded DNA (PubMed:28076779).
Can mediate hepatitis B virus (HBV) core protein phosphorylation (PubMed:12134018).
Plays a negative role in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein but by reducing the packaging efficiency of the pregenomic RNA (pgRNA) without affecting the formation of the viral core particles (PubMed:16122776).

Biological Process angiogenesisISS:BHF-UCL
Biological Process cell differentiationIEA:UniProtKB-KW
Biological Process innate immune response1 PublicationIC:BHF-UCL
Biological Process intracellular signal transductionManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process negative regulation of viral genome replicationManual Assertion Based On ExperimentIDA:BHF-UCL
Biological Process nuclear speck organizationISS:BHF-UCL
Biological Process peptidyl-serine phosphorylationManual Assertion Based On ExperimentIGI:CACAO
Biological Process positive regulation of cell cycleISS:BHF-UCL
Biological Process positive regulation of cell population proliferationManual Assertion Based On ExperimentIDA:BHF-UCL
Biological Process positive regulation of gene expressionISS:BHF-UCL
Biological Process positive regulation of neuron apoptotic processISS:BHF-UCL
Biological Process positive regulation of viral genome replicationManual Assertion Based On ExperimentIDA:BHF-UCL
Biological Process protein phosphorylationManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process R-loop disassemblyManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process regulation of mRNA processingManual Assertion Based On ExperimentIBA:GO_Central
Biological Process regulation of mRNA splicing, via spliceosomeManual Assertion Based On ExperimentTAS:UniProtKB
Biological Process RNA splicingManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process spliceosomal complex assemblyManual Assertion Based On ExperimentIDA:UniProtKB

Cytoplasm
Nucleus, nucleoplasm
Nucleus speckle
Chromosome
Shuttles between the nucleus and the cytoplasm (PubMed:19592491, PubMed:21157427, PubMed:21056976).
KAT5/TIP60 inhibits its nuclear translocation (PubMed:21157427).
Phosphorylation at Thr-492 by PKB/AKT1 promotes nuclear translocation (PubMed:19592491).
Preferentially localizes across the entire gene coding region (PubMed:28076779).
During transcription, accumulates at chromatin loci where unscheduled R-loops form and colocalizes with paused 'Ser-5'-phosphorlyated POLR2A/RNA polymerase II and helicase DDX23 (PubMed:28076779).

Phosphorylation at Thr-492 by PKB/AKT1 enhances its stimulatory activity in triggering cyclin-D1 (CCND1) expression and promoting apoptosis in neurons, which can be blocked by YWHAB. It also enhances its protein kinase activity toward ACIN1 and SRSF2, promotes its nuclear translocation and prevents its proteolytic cleavage.
Proteolytically cleaved at Asp-139 and Asp-403 by caspase-3 during apoptotic cell death. Cleavage at Asp-139 which is the major site of cleavage, produces a small N-terminal fragment that translocates into nucleus and promotes VP16-induced apoptosis.