SRPK2 (P78362) - Overview - Molecular Target Synopsis
SRPK2, SRSF protein kinase 2
Enzyme Classification 184.108.40.206
Also Known as SRPK2_HUMAN, SRPK2
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 spliceosomal B complex formation via the phosphorylation of DDX23/PRP28. Can mediate hepatitis B virus (HBV) core protein phosphorylation. 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. Interacts with PKB/AKT1 in a phosphorylation-dependent manner. The phosphorylated form (by PKB/AKT1) interacts with YWHAB and YWHAE. Interaction with YWHAB suppresses its cleavage by caspases and inhibits the release of its N-terminal pro-apoptotic fragment. Interacts with SFN. Associates with U4/U6-U5 tri-small nuclear ribonucleoproteins (U4/U6-U5 tri-snRNPs).
|Protein Length||Ensembl Gene||Ensembl Transcript||Ensembl Protein||Uniprot Isoform|
|688||ENSG00000135250||ENST00000357311, ENST00000489828||ENSP00000349863, ENSP00000419791||P78362-1|
UniProt: SRPK2 is active in the following subcellular-locations: cytoplasm, nucleus.
GO terms: SRPK2 is active in the following subcellular-locations: cytoplasm, cytosol, nucleolus, nucleoplasm, nucleus.