Mouse anti-Human/Rat sapiens (Human) SRPK2 Monoclonal Antibody

Function

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:18559500, PubMed:21056976, PubMed:9472028). 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). Phosphorylates the N-terminus of ERC1 (By similarity)

Subcellular Location

Cytoplasm; Nucleus, nucleoplasm; Nucleus speckle; Chromosome

Tissue Specificity

Highly expressed in brain, moderately expressed in heart and skeletal muscle and at low levels in lung, liver, and kidney

Subunit

Associates with U4/U6-U5 tri-small nuclear ribonucleoproteins (U4/U6-U5 tri-snRNPs) (PubMed:18425142). Interacts with PKB/AKT1 in a phosphorylation-dependent manner (PubMed:19592491). The phosphorylated form (by PKB/AKT1) interacts with YWHAB and YWHAE (PubMed:19592491). Interaction with YWHAB suppresses its cleavage by caspases and inhibits the release of its N-terminal pro-apoptotic fragment (PubMed:19592491). Interacts with SFN (PubMed:19592491). Interacts with ACIN1 (PubMed:18559500). Interacts with POLR2A/RNA polymerase II; the interaction occurs during the co-transcriptional formation of inappropriate R-loops (PubMed:28076779). Interacts (via kinase domain) with ERC1 (via N-terminus); the interaction is direct and may be involved in SRPK protein localization (By similarity)

• Wang H.-Y. et al. SRPK2: a differentially expressed SR protein-specific kinase involved in mediating the interaction and localization of pre-mRNA splicing factors in mammalian cells. — J. Cell Biol. (1998)
• Hillier L.W. et al. The DNA sequence of human chromosome 7. — Nature (2003)
• Mural R.J. et al. PubMed: CI-5GBDQ6B103N1E (JUL-)
• The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). — Genome Res. (2004)
• Sha J.H. et al. PubMed: CI-FTMH7I3SEKTSE (JUL-)
• Daub H. et al. Identification of SRPK1 and SRPK2 as the major cellular protein kinases phosphorylating hepatitis B virus core protein. — J. Virol. (2002)
• Brill L.M. et al. Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry. — Anal. Chem. (2004)
• Zheng Y. et al. Suppression of hepatitis B virus replication by SRPK1 and SRPK2 via a pathway independent of the phosphorylation of the viral core protein. — Virology (2005)