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SRSF protein kinase 1

SRPK1, SR protein kinase 1
This gene encodes a serine/arginine protein kinase specific for the SR (serine/arginine-rich domain) family of splicing factors. The protein localizes to the nucleus and the cytoplasm. It is thought to play a role in regulation of both constitutive and alternative splicing by regulating intracellular localization of splicing factors. Alternative splicing of this gene results in multiple transcript variants. Additional alternatively spliced transcript variants have been described for this gene, but their full length nature have not been determined.[provided by RefSeq, Jul 2010] (from NCBI)
Top mentioned proteins: CAN, SRPK2, vascular endothelial growth factor, Clk, STEP
Papers on SRPK1
Expression of SRPK1 in gliomas and its role in glioma cell lines viability.
Nikolakaki et al., Thessaloníki, Greece. In Tumour Biol, Feb 2016
UNASSIGNED: Among factors regulating the splicing of major importance is serine/arginine protein kinase 1 (SRPK1) that phosphorylates SR splicing factors.
Up-regulation of SRPK1 in non-small cell lung cancer promotes the growth and migration of cancer cells.
Chen et al., Shanghai, China. In Tumour Biol, Jan 2016
UNASSIGNED: Dys-regulation of serine-arginine protein kinase 1 (SRPK1) has been reported in non-small cell lung cancer (NSCLC).
Serine-arginine protein kinase 1 (SRPK1), a determinant of angiogenesis, is upregulated in prostate cancer and correlates with disease stage and invasion.
Oltean et al., Bristol, United Kingdom. In J Clin Pathol, Nov 2015
Preferential splicing of proangiogenic VEGF is determined by serine-arginine protein kinase 1 (SRPK1), which is upregulated in a number of cancers.
Triple-layer dissection of the lung adenocarcinoma transcriptome: regulation at the gene, transcript, and exon levels.
Chen et al., Yü-ching, Taiwan. In Oncotarget, Nov 2015
Genes selected by both detection methods include C16orf59, DAP3, ETV4, GABARAPL1, PPAR, RADIL, RSPO1, SERTM1, SRPK1, ST6GALNAC6, and TNXB.
Serine-arginine protein kinase 1 is associated with hepatocellular carcinoma progression and poor patient survival.
Shen et al., Guangzhou, China. In Tumour Biol, Aug 2015
UNASSIGNED: The pre-mRNA splicing regulator serine-arginine protein kinase 1 (SRPK1) promotes cancer development and various pathophysiological processes.
Increased Serine-Arginine (SR) Protein Phosphorylation Changes Pre-mRNA Splicing in Hypoxia.
Kanopka et al., Vilnius, Lithuania. In J Biol Chem, Aug 2015
We also show that expression of SR protein kinases (CLK1, SRPK1, SRPK2) in hypoxic cells is elevated at mRNA and protein levels.
The crucial role of SRPK1 in TGF-β-induced proliferation and apoptosis in the esophageal squamous cell carcinomas.
Li et al., Jinan, China. In Med Oncol, Jul 2015
In recent years, transforming growth factor-β (TGF-β) and the serine-arginine protein kinase 1 (SRPK1) have been recommended as a key signal mediator that is involved in oncogenesis.
A Multi-Breed Genome-Wide Association Analysis for Canine Hypothyroidism Identifies a Shared Major Risk Locus on CFA12.
Rosengren Pielberg et al., Uppsala, Sweden. In Plos One, 2014
This breed-shared risk haplotype includes three genes (LHFPL5, SRPK1 and SLC26A8) and does not extend to the dog leukocyte antigen (DLA) class II gene cluster located in the vicinity.
Potential Antileukemia Effect and Structural Analyses of SRPK Inhibition by N-(2-(Piperidin-1-yl)-5-(Trifluoromethyl)Phenyl)Isonicotinamide (SRPIN340).
Bressan et al., Viçosa, Brazil. In Plos One, 2014
Previous investigations have described the overexpression of SRPK1 and SRPK2 in leukemia and other cancer types, suggesting that they would be useful targets for developing novel antitumor strategies.
How mRNA is misspliced in acute myelogenous leukemia (AML)?
Wattel et al., In Oncotarget, 2014
Through the repression of the kinase SRPK1, WT1 modifies the splicing of VEGF, which plays important roles in hematopoiesis and angiogenesis.
The Akt-SRPK-SR axis constitutes a major pathway in transducing EGF signaling to regulate alternative splicing in the nucleus.
Fu et al., San Diego, United States. In Mol Cell, 2012
These findings reveal a major signal transduction pathway for regulated splicing and place SRPKs in a central position in the pathway, consistent with their reputed roles in a large number of human cancers.
SRPK1 inhibition in vivo: modulation of VEGF splicing and potential treatment for multiple diseases.
Bates et al., Bristol, United Kingdom. In Biochem Soc Trans, 2012
SRPK1 (serine-arginine protein kinase 1) is a protein kinase that specifically phosphorylates proteins containing serine-arginine-rich domains.
Distribution of SRPK1 in human brain.
Giannakouros et al., Thessaloníki, Greece. In J Chem Neuroanat, 2012
The present immunohistochemical study reveals a region- and neuron-specific localization of SRPK1 in human brain.
WT1 mutants reveal SRPK1 to be a downstream angiogenesis target by altering VEGF splicing.
Ladomery et al., Bristol, United Kingdom. In Cancer Cell, 2012
WT1 bound to the SRPK1 promoter, and repressed expression through a specific WT1 binding site
Applying the brakes to multisite SR protein phosphorylation: substrate-induced effects on the splicing kinase SRPK1.
Adams et al., San Diego, United States. In Biochemistry, 2011
protein kinase SRPK1 phosphorylates ~10 serines in the arginine--serine-rich domain (RS domain) of the SR protein SRSF1 in a C- to N-terminal direction, a modification that directs this essential splicing factor from the cytoplasm to the nucleus
Phosphorylation mechanism and structure of serine-arginine protein kinases.
Adams et al., San Diego, United States. In Febs J, 2011
Human alternative splicing factor [serine/arginine-rich splicing factor 1 (SRSF1)], a prototype for the SR protein family, is regiospecifically phosphorylated by SRPK1, a post-translational modification that controls cytoplasmic-nuclear localization.
Serine-arginine protein kinases: a small protein kinase family with a large cellular presence.
Georgatsou et al., Thessaloníki, Greece. In Febs J, 2011
Fifteen years of research subsequent to the purification and cloning of human SRPK1 as a SR splicing factor-phosphorylating protein have lead to the accumulation of information on the function and regulation of the different members of this family, as well as on the genomic organization of SRPK genes in several organisms.
The ratio of SRPK1/SRPK1a regulates erythroid differentiation in K562 leukaemic cells.
Nikolakaki et al., Thessaloníki, Greece. In Biochim Biophys Acta, 2010
SRPK1a may play an important role in linking ribosomal assembly and/or function to erythroid differentiation in human leukaemic cells
A serine kinase regulates intracellular localization of splicing factors in the cell cycle.
Fu et al., San Diego, United States. In Nature, 1994
We have now identified and cloned a kinase, SRPK1, which is regulated by the cell cycle and is specific for SR proteins; this kinase is related to a Caenorhabditis elegans kinase and to the fission yeast kinase Dsk1 (ref.
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