Affinage

SRPK2

SRSF protein kinase 2 · UniProt P78362

Length
688 aa
Mass
77.5 kDa
Annotated
2026-06-10
30 papers in source corpus 19 papers cited in narrative 19 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

SRPK2 is a serine/arginine protein kinase that phosphorylates RS-domain-containing substrates with a stringent preference for SR dipeptides, coupling signaling inputs to pre-mRNA splicing and broader cellular outcomes (PMID:9472028). Substrate recognition is mediated by a conserved electronegative docking groove that determines whether a substrate is phosphorylated processively, as for SRSF1, or at a single restricted site, as for acinusS (PMID:24444330). Through phosphorylation of SR proteins such as SF2/ASF and SC35, SRPK2 controls the assembly and nuclear distribution of splicing factors and enhances SR protein engagement of U1-70K (PMID:9472028, PMID:9446799, PMID:29153836). Within the spliceosome it phosphorylates the RS domain of PRP28/DDX23 to stabilize its tri-snRNP association and drive B-complex formation (PMID:18425142), and it resolves co-transcriptional R-loops to limit DNA double-strand breaks and genomic instability (PMID:28076779). SRPK2 nuclear translocation is gated by sequential upstream phosphorylation: mTORC1-activated S6K1 phosphorylates Ser-494 to prime CK1-mediated Ser-497 phosphorylation, licensing nuclear import and splicing of lipogenic pre-mRNAs to sustain de novo lipid synthesis (PMID:29153836), while Akt phosphorylation of Thr-492 promotes nuclear entry, cyclin D1 upregulation, and 14-3-3 binding that restrains its activity (PMID:19592491). In neurons SRPK2 is a driver of neurodegenerative pathology: it phosphorylates tau on Ser-214 to suppress microtubule polymerization and axon elongation (PMID:23197718), and phosphorylates delta-secretase (AEP) on Ser-226 to accelerate its activation and cleavage of APP and tau, with phosphomimetic and non-phosphorylatable mutants respectively worsening and attenuating Alzheimer's disease pathology in mouse models (PMID:28826672). SRPK2 is recruited by partner proteins to assemble splicing platforms—exemplified by BRD4-dependent recruitment controlling ACSL3 splicing and ferroptosis susceptibility (PMID:37993451)—and additionally phosphorylates viral RS-motif substrates including hepatitis B virus core protein and EBV BLRF2 (PMID:12134018, PMID:23326445, PMID:38324561).

Mechanistic history

Synthesis pass · year-by-year structured walk · 18 steps
  1. 1998 High

    Established SRPK2 as an SR-protein-specific kinase, defining its core substrate specificity and a role in spliceosome assembly and splicing-factor trafficking.

    Evidence Random peptide selection, in vitro kinase assays, Co-IP, and overexpression imaging of nuclear splicing factors

    PMID:9446799 PMID:9472028

    Open questions at the time
    • Did not define endogenous regulation of SRPK2 activity
    • Physiological splicing targets not yet identified
  2. 2002 High

    Showed SRPK2 phosphorylates the arginine-rich C-terminal domain of HBV core protein at physiological sites, extending its substrate range to viral RS-like motifs.

    Evidence Kinase purification from HuH-7 lysates, mass spectrometry, in vitro phosphorylation with site mapping

    PMID:12134018

    Open questions at the time
    • Functional consequence for viral replication not addressed in this study
  3. 2005 Medium

    Revealed a kinase-independent function of SRPK2 in suppressing HBV pregenomic RNA packaging, separating its catalytic from non-catalytic roles.

    Evidence Wild-type and kinase-dead overexpression in HBV-replicating cells with Southern/Northern blots

    PMID:16122776

    Open questions at the time
    • Molecular basis of kinase-independent suppression unresolved
    • Single lab
  4. 2008 High

    Defined a direct spliceosomal substrate by showing SRPK2 phosphorylates PRP28/DDX23 RS domain to enable tri-snRNP integration into the B complex.

    Evidence RNAi with complementation, immunodepletion, in vitro splicing reconstitution, snRNP Co-IP in HeLa

    PMID:18425142

    Open questions at the time
    • Upstream signals controlling this phosphorylation not defined here
  5. 2009 High

    Identified Akt-mediated Thr-492 phosphorylation as a switch controlling SRPK2 nuclear translocation, cyclin D1 upregulation, and neuronal apoptosis, with 14-3-3 as an inhibitory partner.

    Evidence Site-directed mutagenesis, in vitro kinase assays, reciprocal Co-IP, nuclear fractionation, neuronal death assays

    PMID:19592491

    Open questions at the time
    • Direct splicing targets linking SC35 phosphorylation to p53 inactivation not enumerated
  6. 2010 Medium

    Showed caspase cleavage generates a nuclear N-terminal SRPK2 fragment that promotes apoptosis, and that Akt/14-3-3 protect SRPK2 from cleavage, integrating it into apoptotic control.

    Evidence Cleavage-site mutagenesis, fractionation, nuclear translocation and cell death assays

    PMID:21056976

    Open questions at the time
    • Pro-apoptotic targets of the cleavage fragment unknown
    • Single lab
  7. 2012 High

    Established SRPK2 as a direct tau kinase phosphorylating Ser-214 that impairs microtubule dynamics and axon growth, and as an in vivo driver of cognitive deficits.

    Evidence In vitro kinase assay with site mapping, microtubule and axon assays, in vivo lentiviral knockdown with behavior/LTP in APP/PS1 mice

    PMID:23197718

    Open questions at the time
    • Upstream regulation of neuronal SRPK2 not defined here
  8. 2013 Medium

    Linked stress and genotoxic signaling to SRPK2 by showing oxidative/DNA-damaging agents drive its phosphorylation, nuclear accumulation, and altered splice-site selection.

    Evidence Site-directed mutagenesis identifying a localization-required serine, fractionation, minigene splicing reporters

    PMID:23613995

    Open questions at the time
    • Upstream stress-activated kinase not identified
    • Single lab
  9. 2013 Medium

    Extended viral substrate repertoire by showing SRPK2 phosphorylates the EBV BLRF2 RS motif (Ser-148/150), required for gammaherpesvirus replication.

    Evidence Interaction assays, in vitro kinase assay, S148A/S150A mutagenesis, viral complementation

    PMID:23326445

    Open questions at the time
    • Mechanism by which BLRF2 phosphorylation supports replication unclear
    • Single lab
  10. 2014 Medium

    Defined the structural basis of substrate selection, showing a conserved electronegative docking groove dictates processive versus single-site phosphorylation.

    Evidence In vitro kinase assays, docking-groove mutagenesis, substrate binding and phosphorylation kinetics

    PMID:24444330

    Open questions at the time
    • Structural model of the groove-substrate complex not resolved in this study
    • Single lab
  11. 2017 High

    Placed SRPK2 downstream of mTORC1-S6K1-CK1, showing sequential Ser-494/Ser-497 phosphorylation drives nuclear import and splicing of lipogenic pre-mRNAs to control de novo lipid synthesis.

    Evidence In vitro kinase assays, phospho-site mutagenesis, genome-wide transcriptomics, metabolic lipid labeling, genetic/pharmacological inhibition

    PMID:29153836

    Open questions at the time
    • Full set of lipogenic splicing targets and tissue-specific effects not exhaustively mapped
  12. 2017 High

    Identified delta-secretase (AEP) Ser-226 as an SRPK2 substrate whose phosphorylation accelerates AEP activation and APP/tau cleavage, causally modulating Alzheimer's pathology in vivo.

    Evidence In vitro kinase assay, S226D/S226A mutagenesis, viral injection into 3xTg/5XFAD mice, behavior and histopathology

    PMID:28826672

    Open questions at the time
    • Signals activating SRPK2 toward AEP in disease not defined
  13. 2017 Medium

    Connected SRPK2 to genome stability by showing its phosphorylation of DDX23 during Pol II pausing prevents R-loop accumulation and DNA double-strand breaks.

    Evidence RNAi of SRPK2/DDX23, R-loop and gammaH2AX detection, transcription inhibitor treatments

    PMID:28076779

    Open questions at the time
    • Direct demonstration of R-loop resolution mechanism missing
    • Single lab
  14. 2019 Medium

    Uncovered a non-splicing role: SRPK2 binds CAST1/ERC2 via coiled-coil domains and localizes to synapses, implicating it in presynaptic scaffold assembly.

    Evidence Co-IP with domain-deletion mapping, synaptic fractionation, immunofluorescence in HEK293T/SH-SY5Y

    PMID:31671734

    Open questions at the time
    • Functional consequence for synaptic transmission untested
    • Overexpression-based, single lab
  15. 2019 Medium

    Characterized the solution behavior of SRPK2, showing a monomer-dimer equilibrium and elongated shape conferred by its non-kinase regions.

    Evidence SAXS, analytical SEC, sedimentation velocity AUC on recombinant protein

    PMID:31229549

    Open questions at the time
    • No high-resolution structure
    • Functional relevance of oligomeric state untested
  16. 2022 Medium

    Demonstrated a SRPK2-specific (not SRPK1) requirement for actin dynamics, proliferation, and invasion in melanoma and for tumor progression in vivo.

    Evidence CRISPR-Cas9 knockout, actin polymerization and invasion assays, in vivo melanoma models

    PMID:36212152

    Open questions at the time
    • Molecular link between SRPK2 and actin regulation not defined
    • Single lab
  17. 2023 Medium

    Showed SRPK2 is recruited by BRD4 into a SRSF2 splicing platform controlling ACSL3 splicing, arachidonic acid synthesis, and ferroptosis susceptibility.

    Evidence BRD4 inhibition, SRPK2 knockdown, ACSL3 splicing assays, arachidonic acid and ferroptosis readouts in osteosarcoma in vitro and in vivo

    PMID:37993451

    Open questions at the time
    • Direct BRD4-SRPK2 interaction interface not mapped
    • Single lab
  18. 2024 High

    Resolved how SRPK2 engages HBV capsid, with cryo-EM showing docking-groove binding to unphosphorylated core protein that blocks premature assembly until phosphorylation reactivates it.

    Evidence Cryo-EM of HBV capsid-SRPK2 complex, pull-downs, in vitro capsid assembly assays, docking-groove mutagenesis, SRPK2 KO in HepG2

    PMID:38324561

    Open questions at the time
    • In vivo relevance of assembly inhibition to HBV infection not established

Open questions

Synthesis pass · forward-looking unresolved questions
  • How SRPK2 substrate selectivity, signaling-gated localization, and tissue-specific phenotypes (lipogenesis, neurodegeneration, tumor invasion, viral assembly) are integrated into a unified regulatory logic remains unresolved.
  • No high-resolution structure of a docking-groove-substrate complex
  • Mechanism linking SRPK2 to actin dynamics undefined
  • Comprehensive map of physiological splicing targets across tissues lacking

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 6 GO:0016740 transferase activity 3 GO:0140110 transcription regulator activity 2
Localization
GO:0005634 nucleus 4 GO:0005654 nucleoplasm 2 GO:0005829 cytosol 2
Pathway
R-HSA-8953854 Metabolism of RNA 4 R-HSA-1430728 Metabolism 2 R-HSA-5357801 Programmed Cell Death 2 R-HSA-1640170 Cell Cycle 1 R-HSA-73894 DNA Repair 1
Partners
AKT1BRD4CAST1/ERC2DDX23SRSF1SRSF2U1-70KYWHAB
Complex memberships
U4/U6-U5 tri-snRNP

Evidence

Reading pass · 19 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1998 SRPK2 is an SR protein-specific kinase with a stringent preference for SR dipeptides; phosphorylation of ASF/SF2 by SRPK2 enhances its interaction with U1 70K, and overexpression of SRPK2 induces redistribution of splicing factors in the nucleus, indicating a role in spliceosome assembly and trafficking of splicing factors. Random peptide selection for phosphorylation site preference, in vitro kinase assay, co-immunoprecipitation, overexpression with immunofluorescence microscopy The Journal of cell biology High 9472028
1998 Overexpression of mouse SRPK2 causes disassembly of nuclear speckles containing cotransfected SF2/ASF and endogenous SC35, and SRPK2 phosphorylates SF2/ASF on the same sites as SRPK1 in vitro. In vitro kinase assay with phosphopeptide mapping, overexpression with immunofluorescence of nuclear speckles Biochemical and biophysical research communications Medium 9446799
2002 SRPK1 and SRPK2 are the major cellular kinases that phosphorylate the arginine-rich C-terminal domain of hepatitis B virus core protein on the same serine residues phosphorylated in vivo; both were identified by purification, mass spectrometry, and immunoblot from HuH-7 lysates. Kinase purification from cell lysates, mass spectrometry identification, in vitro phosphorylation assay, immunoblot Journal of virology High 12134018
2005 SRPK1 and SRPK2 suppress HBV replication by reducing pregenomic RNA packaging efficiency without affecting core particle formation; this suppressive effect is independent of their kinase activity toward the core protein, as kinase-dead mutants retain suppressive activity and overexpression does not alter in vivo core protein phosphorylation. Overexpression of wild-type and kinase-dead mutants in HBV-replicating cells, Southern blot for HBV DNA, Northern blot for pgRNA packaging Virology Medium 16122776
2008 SRPK2 associates with the U4/U6-U5 tri-snRNP and phosphorylates the RS domain of human PRP28 (DDX23); this phosphorylation is required for stable PRP28 association with the tri-snRNP and for tri-snRNP integration into the spliceosomal B complex. RNAi knockdown in HeLa cells, immunodepletion/complementation of nuclear extracts, in vitro splicing assays, co-immunoprecipitation with snRNP fractions Nature structural & molecular biology High 18425142
2009 Akt phosphorylates SRPK2 on Thr-492, promoting SRPK2 nuclear translocation, cyclin D1 upregulation, cell cycle reentry, and apoptosis in neurons; SRPK2 phosphorylates SC35, inactivating p53 and contributing to cyclin D1 upregulation; 14-3-3 binding to Akt-phosphorylated SRPK2 inhibits these events. Site-directed mutagenesis, in vitro kinase assay, co-immunoprecipitation, nuclear fractionation, neuronal overexpression/knockdown with cell death readouts The Journal of biological chemistry High 19592491
2010 SRPK2 is cleaved by caspases at Asp-139 and Asp-403 during apoptosis; the N-terminal cleavage product translocates to the nucleus and promotes chromatin condensation and apoptotic cell death; Akt phosphorylation of SRPK2 prevents caspase cleavage, and 14-3-3β binding to Akt-phosphorylated SRPK2 further protects it from degradation. Site-directed mutagenesis of caspase cleavage sites, subcellular fractionation, nuclear translocation assays, cell death assays The Journal of biological chemistry Medium 21056976
2012 SRPK2 directly phosphorylates tau on Ser-214, suppresses tau-dependent microtubule polymerization, and inhibits axonal elongation in neurons; depletion of SRPK2 in dentate gyrus of APP/PS1 mice reduces tau phosphorylation and alleviates cognitive deficits and impaired LTP. In vitro kinase assay with site mapping, microtubule polymerization assay, axon elongation assay, in vivo lentiviral knockdown, behavioral and electrophysiological tests The Journal of neuroscience High 23197718
2013 SRPK2 phosphorylates the RS motif (Ser-148 and Ser-150) of EBV tegument protein BLRF2; mutation of this RS motif abrogates BLRF2's ability to support gammaherpesvirus replication. Binary and co-complex protein interaction assays, in vitro kinase assay, mutagenesis (S148A+S150A), viral replication complementation assay PloS one Medium 23326445
2013 Paraquat treatment induces phosphorylation and nuclear accumulation of SRPK2, leading to increased SR protein phosphorylation and altered splice site selection; site-specific mutagenesis identified a single serine residue required for nuclear localization; genotoxic agents (cisplatin, γ-radiation) also promote SRPK2 phosphorylation and nuclear localization, coupling DNA damage response to alternative splicing via SRPK2. Site-directed mutagenesis, nuclear fractionation, phosphomimetic mutant transfection, minigene splicing reporter assay PloS one Medium 23613995
2014 A conserved electronegative docking groove on SRPK2 (not its non-kinase regions) mediates substrate binding for both SRSF1 and acinusS; SRPK2 phosphorylates SRSF1 processively, but an electronegative region on acinusS restricts SRPK2 phosphorylation to a single specific site despite multiple RS dipeptides being present. In vitro kinase assay, mutagenesis of docking groove, substrate binding assays, phosphorylation kinetics The Biochemical journal Medium 24444330
2017 mTORC1-activated S6K1 phosphorylates SRPK2 at Ser-494, which primes CK1-mediated Ser-497 phosphorylation; these events promote SRPK2 nuclear translocation where it phosphorylates SR proteins and promotes SR protein binding to U1-70K, inducing splicing of lipogenic pre-mRNAs; inhibition leads to intron retention and nonsense-mediated decay of lipogenic genes, blunting de novo lipid synthesis. In vitro kinase assay, site-directed mutagenesis, nuclear fractionation, genome-wide transcriptome analysis, RNA splicing assays, metabolic labeling of lipid synthesis, genetic/pharmacological inhibition Cell High 29153836
2017 SRPK2 phosphorylates delta-secretase (AEP) at Ser-226, accelerating its autocatalytic cleavage and cytoplasmic translocation, leading to enhanced enzymatic activity toward APP and tau; phosphomimetic S226D promotes AD pathology in young 3xTg mice, while non-phosphorylatable S226A decreases APP/tau cleavage and attenuates AD pathology in 5XFAD mice. In vitro kinase assay, site-directed mutagenesis (S226D/S226A), viral injection into mouse models, behavioral testing, histopathological analysis of plaques and tangles Molecular cell High 28826672
2017 SRPK2 phosphorylates DDX23 (PRP28) in response to RNA Pol II pausing during transcription; in the absence of SRPK2 or DDX23, R-loops accumulate leading to DNA double-strand breaks and genomic instability. RNAi knockdown of SRPK2 and DDX23, R-loop detection (immunofluorescence/slot blot), DNA damage assays (γH2AX), transcription inhibitor treatments Cell reports Medium 28076779
2019 SRPK2 forms a complex with CAST1/ERC2 via coiled-coil domains CC1 and CC4, and overexpression of SRPK2 regulates self-assembly of CAST1/ERC2 in heterologous cells; SRPK2 is localized to brain synaptic fractions, suggesting it modulates presynaptic scaffold assembly. Co-immunoprecipitation in HEK293T and SH-SY5Y cells, domain deletion analysis, synaptic fractionation, immunofluorescence Cells Medium 31671734
2019 Full-length SRPK2 exists predominantly as a monomer-dimer equilibrium in solution with an elongated shape; the truncated kinase domain version dimerizes at higher concentrations; the flexible non-kinase regions confer unique structural properties relative to the SRPK family. Small-angle X-ray scattering (SAXS), analytical size exclusion chromatography, sedimentation velocity analytical ultracentrifugation International journal of biological macromolecules Medium 31229549
2022 CRISPR-Cas9 knockout of SRPK2, but not SRPK1, impairs actin polymerization dynamics as well as proliferative and invasive capacity of B16F10 melanoma cells in vitro, and reduces tumor progression in subcutaneous and caudal vein melanoma models in vivo. CRISPR-Cas9 knockout, actin polymerization assay, invasion assay, in vivo tumor progression models Frontiers in genetics Medium 36212152
2024 SRPK2 uses a specific docking groove to interact with and phosphorylate the C-terminal arginine-rich domain of HBV core protein (Cp); direct interaction of SRPK2's docking groove with unphosphorylated Cp inhibits premature viral capsid assembly in vitro, whereas Cp phosphorylation reactivates assembly; cryo-EM structure of HBV capsid-SRPK2 complex shows kinases decorating the capsid surface via Cp C-terminal domain; SRPK2 knockout in HepG2 cells suppresses Cp phosphorylation in cellulo. Cryo-electron microscopy structure determination, pull-down assays, in vitro capsid assembly assay, site-directed mutagenesis of docking groove, SRPK2 knockout in HepG2 cells PLoS pathogens High 38324561
2023 BRD4 recruits SRPK2 to assemble a splicing catalytic platform that controls splicing of ACSL3 pre-mRNA; this BRD4-SRPK2-SRSF2 axis influences arachidonic acid synthesis and susceptibility to erastin-induced ferroptosis in osteosarcoma cells. BRD4 inhibition, SRPK2 knockdown, RNA splicing assays for ACSL3 pre-mRNA, arachidonic acid measurement, ferroptosis assays in vitro and in vivo Cell death & disease Medium 37993451

Source papers

Stage 0 corpus · 30 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1998 SRPK2: a differentially expressed SR protein-specific kinase involved in mediating the interaction and localization of pre-mRNA splicing factors in mammalian cells. The Journal of cell biology 275 9472028
2017 Post-transcriptional Regulation of De Novo Lipogenesis by mTORC1-S6K1-SRPK2 Signaling. Cell 186 29153836
2012 Abnormal expression of the pre-mRNA splicing regulators SRSF1, SRSF2, SRPK1 and SRPK2 in non small cell lung carcinoma. PloS one 128 23071587
2002 Identification of SRPK1 and SRPK2 as the major cellular protein kinases phosphorylating hepatitis B virus core protein. Journal of virology 124 12134018
2008 Phosphorylation of human PRP28 by SRPK2 is required for integration of the U4/U6-U5 tri-snRNP into the spliceosome. Nature structural & molecular biology 114 18425142
2009 Interaction of Akt-phosphorylated SRPK2 with 14-3-3 mediates cell cycle and cell death in neurons. The Journal of biological chemistry 103 19592491
1998 Novel SR-protein-specific kinase, SRPK2, disassembles nuclear speckles. Biochemical and biophysical research communications 102 9446799
2017 Transcription Dynamics Prevent RNA-Mediated Genomic Instability through SRPK2-Dependent DDX23 Phosphorylation. Cell reports 95 28076779
2017 Delta-Secretase Phosphorylation by SRPK2 Enhances Its Enzymatic Activity, Provoking Pathogenesis in Alzheimer's Disease. Molecular cell 55 28826672
2012 SRPK2 phosphorylates tau and mediates the cognitive defects in Alzheimer's disease. The Journal of neuroscience : the official journal of the Society for Neuroscience 50 23197718
2005 Suppression of hepatitis B virus replication by SRPK1 and SRPK2 via a pathway independent of the phosphorylation of the viral core protein. Virology 46 16122776
2016 SRPK2 promotes the growth and migration of the colon cancer cells. Gene 26 27041240
2013 Paraquat modulates alternative pre-mRNA splicing by modifying the intracellular distribution of SRPK2. PloS one 22 23613995
2013 An RS motif within the Epstein-Barr virus BLRF2 tegument protein is phosphorylated by SRPK2 and is important for viral replication. PloS one 20 23326445
2018 Enhanced expression of SRPK2 contributes to aggressive progression and metastasis in prostate cancer. Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie 19 29587239
1999 Localization of serine kinases, SRPK1 (SFRSK1) and SRPK2 (SFRSK2), specific for the SR family of splicing factors in mouse and human chromosomes. Genomics 17 10198174
2023 The BRD4-SRPK2-SRSF2 signal modulates the splicing efficiency of ACSL3 pre-mRNA and influences erastin-induced ferroptosis in osteosarcoma cells. Cell death & disease 15 37993451
2010 The N-terminal fragment from caspase-cleaved serine/arginine protein-specific kinase2 (SRPK2) translocates into the nucleus and promotes apoptosis. The Journal of biological chemistry 13 21056976
2019 Downregulation of SRPK2 promotes cell cycle arrest though E2F1 in non-small cell lung cancer. European journal of histochemistry : EJH 12 31833327
2022 An IGF-1R-mTORC1-SRPK2 signaling Axis contributes to FASN regulation in breast cancer. BMC cancer 10 36096767
2019 Serine-Arginine Protein Kinase SRPK2 Modulates the Assembly of the Active Zone Scaffolding Protein CAST1/ERC2. Cells 10 31671734
2024 LTR retrotransposon-derived LncRNA LINC01446 promotes hepatocellular carcinoma progression and angiogenesis by regulating the SRPK2/SRSF1/VEGF axis. Cancer letters 9 38945203
2020 Cooperation of SRPK2, Numb and p53 in the malignant biology and chemosensitivity of colorectal cancer. Bioscience reports 7 31898732
2019 CRISPR/Cas9-mediated double knockout of SRPK1 and SRPK2 in a nasopharyngeal carcinoma cell line. Cancer reports (Hoboken, N.J.) 7 32671994
2024 SRPK2 Mediates HBV Core Protein Phosphorylation and Capsid Assembly via Docking Interaction. PLoS pathogens 6 38324561
2022 Impaired expression of serine/arginine protein kinase 2 (SRPK2) affects melanoma progression. Frontiers in genetics 6 36212152
2014 Primary structural features of SR-like protein acinusS govern the phosphorylation mechanism by SRPK2. The Biochemical journal 6 24444330
2022 SRPK2 Expression and Beta-Amyloid Accumulation Are Associated With BV2 Microglia Activation. Frontiers in integrative neuroscience 2 35153686
2019 Insights into the full-length SRPK2 structure and its hydrodynamic behavior. International journal of biological macromolecules 2 31229549
2026 Oncogenic Role of SRPK2 in Different Types of Cancer: A Systematic Review. Journal of cellular and molecular medicine 0 42178601

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