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SRPK2 may contribute to the formation of hyperphosphorylated tau and the pathogenesis of Alzheimer disease.
Interaction of Akt (show AKT1 Proteins)-phosphorylated SRPK2 with 14-3-3 (show YWHAQ Proteins) mediates cell cycle and cell death in neurons.
Delta-secretase phosphorylation by SRPK2 plays a critical role in aggravating Alzheimer disease pathogenesis.
In this study, it was found that the expression of SRPK2 was up-regulated in the clinical colon cancer samples. Overexpression of SRPK2 promoted the growth and migration of colon cancer cells, while knocking down the expression of SRPK2 inhibited the growth, migration and tumorigenecity of colon cancer cells.
Our results indicate that phosphorylation of SRPK2 plays a crucial role in the regulation of splicing process in head and neck squamous cell carcinoma (HNSCC), and that splicing kinases can be developed as a new class of therapeutic target in HNSCC.
Data indicate serine/arginine-rich protein (show MANF Proteins) kinases SRPK1 (show SRPK1 Proteins)/2/SRPIN340 complexes by molecular docking and molecular dynamics.
A conserved electronegative docking groove in SRPK2 is responsible for substrate binding.
the BLRF2 RS motif is phosphorylated by SRPK2 and is important for viral replication.
Our results demonstrate that SRPK1 (show SRPK1 Proteins) and SRPK2 are host factors essential for Hepatitis C virus replication.
Short-term exercise resulted in a significant increase of mRNA expression of genes encoding proteins involved in the formation of precatalytic splisosome: SRPK2.
Both SRPK1 and SRPK2 are most likely the cellular protein kinases mediating HBV core protein phosphorylation during viral infection and therefore represent important host cell targets for therapeutic intervention in HBV infection.
negative role of SRPK1 and SRPK2 in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein
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. Promotes neuronal apoptosis by up-regulating cyclin-D1 (CCND1) expression. 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. Phosphorylates ACIN1, and redistributes it from the nuclear speckles to the nucleoplasm, resulting in cyclin A1 but not cyclin A2 up- regulation. Plays an essential role in splicesomal B complex formation via the phosphorylation of DDX23/PRP28.
SFRS protein kinase 2
, SFRS protein kinase 3
, serine/threonine-protein kinase SRPK2-like
, SR-protein-specific kinase 2
, SRSF protein kinase 2
, WW domain binding protein 6
, serine/arginine-rich protein-specific kinase 2
, serine/threonine-protein kinase SRPK2
, SR protein kinase 2
, serine kinase SRPK2
, serine/arginine-rich splicing factor kinase 2
, serine/arginine-rich protein specific kinase 2