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SRSF protein kinase

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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. Plays a central role in the regulatory network for splicing, controlling the intranuclear distribution of splicing factors in interphase cells and the reorganization of nuclear speckles during mitosis. Can influence additional steps of mRNA maturation, as well as other cellular activities, such as chromatin reorganization in somatic and sperm cells and cell cycle progression. Phosphorylates SFRS2, ZRSR2, LBR and PRM1. Phosphorylates SRSF1 using a directional (C-terminal to N-terminal) and a dual-track mechanism incorporating both processive phosphorylation (in which the kinase stays attached to the substrate after each round of phosphorylation) and distributive phosphorylation steps (in which the kinase and substrate dissociate after each phosphorylation event). The RS domain of SRSF1 binds first to a docking groove in the large lobe of the kinase domain of SRPK1. This induces certain structural changes in SRPK1 and/or RRM2 domain of SRSF1, allowing RRM2 to bind the kinase and initiate phosphorylation. The cycles continue for several phosphorylation steps in a processive manner (steps 1-8) until the last few phosphorylation steps (approximately steps 9-12). During that time, a mechanical stress induces the unfolding of the beta-4 motif in RRM2, which then docks at the docking groove of SRPK1. This also signals RRM2 to begin to dissociate, which facilitates SRSF1 dissociation after phosphorylation is completed. Can mediate hepatitis B virus (HBV) core protein phosphorylation. It 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. Can induce splicing of exon 10 in MAPT/TAU.

Below are the list of possible SRSF protein kinase products. If you cannot find the target and/or product is not available in our catalog, please click here to contact us and request the product or submit your request for custom elisa kit production, custom recombinant protein production or custom antibody production. Custom ELISA Kits, Recombinant Proteins and Antibodies can be designed, manufactured and produced according to the researcher's specifications.
 

SRSF protein kinase 1

 SRSF protein kinase 1 ELISA Kit
 SRSF protein kinase 1 Recombinant
 SRSF protein kinase 1 Antibody
Also known as SRSF protein kinase 1 (SFRS protein kinase 1) (Serine/arginine-rich protein-specific kinase 1) (SR-protein-specific kinase 1).
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 th
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e regulation of splicing. Plays a central role in the regulatory network for splicing, controlling the intranuclear distribution of splicing factors in interphase cells and the reorganization of nuclear speckles during mitosis. Can influence additional steps of mRNA maturation, as well as other cellular activities, such as chromatin reorganization in somatic and sperm cells and cell cycle progression. Phosphorylates SFRS2, ZRSR2, LBR and PRM1. Phosphorylates SRSF1 using a directional (C-terminal to N-terminal) and a dual-track mechanism incorporating both processive phosphorylation (in which the kinase stays attached to the substrate after each round of phosphorylation) and distributive phosphorylation steps (in which the kinase and substrate dissociate after each phosphorylation event). The RS domain of SRSF1 binds first to a docking groove in the large lobe of the kinase domain of SRPK1. This induces certain structural changes in SRPK1 and/or RRM2 domain of SRSF1, allowing RRM2 to bind the kinase and initiate phosphorylation. The cycles continue for several phosphorylation steps in a processive manner (steps 1-8) until the last few phosphorylation steps (approximately steps 9-12). During that time, a mechanical stress induces the unfolding of the beta-4 motif in RRM2, which then docks at the docking groove of SRPK1. This also signals RRM2 to begin to dissociate, which facilitates SRSF1 dissociation after phosphorylation is completed. Can mediate hepatitis B virus (HBV) core protein phosphorylation. It 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. Can induce splicing of exon 10 in MAPT/TAU.
 SRPK1 ELISA Kit
 SRPK1 Recombinant
 SRPK1 Antibody
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SRSF protein kinase 2

 SRSF protein kinase 2 ELISA Kit
 SRSF protein kinase 2 Recombinant
 SRSF protein kinase 2 Antibody
Also known as SRSF protein kinase 2 (SFRS protein kinase 2) (Serine/arginine-rich protein-specific kinase 2) (SR-protein-specific kinase 2).
SRPK2: a CMGC kinase of the SRPK family. Phosphorylates the SR (serine/arginine-rich domain) family of splicing factors. Localizes to the nucleus and the cytoplasm. Thought to play a role in regulation of both constitutive and alternative splicing by regul
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ating intracellular localization of splicing factors. Highly expressed in brain and to a lesser extent other tissues. A second alternatively spliced transcript variant has been described, but its full length nature has not been determined.

Protein type: CMGC group; EC 2.7.11.1; Kinase, protein; Protein kinase, CMGC; Protein kinase, Ser/Thr (non-receptor); SRPK family

Cellular Component: cytoplasm; nucleolus; nucleoplasm; nucleus

Molecular Function: ATP binding; magnesium ion binding; protein serine/threonine kinase activity

Biological Process: angiogenesis; negative regulation of viral genome replication; nuclear speck organization and biogenesis; positive regulation of cell cycle; positive regulation of cell proliferation; positive regulation of neuron apoptosis; positive regulation of viral genome replication; protein amino acid phosphorylation; RNA splicing; spliceosome assembly
 Srpk2 ELISA Kit
 Srpk2 Recombinant
 Srpk2 Antibody
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SRSF protein kinase 3

 SRSF protein kinase 3 ELISA Kit
 SRSF protein kinase 3 Recombinant
 SRSF protein kinase 3 Antibody
Also known as SRSF protein kinase 3 (Muscle-specific serine kinase 1) (MSSK-1) (Serine/arginine-rich protein-specific kinase 3) (SR-protein-specific kinase 3) (Serine/threonine-protein kinase 23).
SRPK3: a CMGC protein kinase of the SRPK family. Exclusively expressed in skeletal and heart muscle. Two known splice variant isoforms.

Protein type: CMGC group; EC 2.7.11.1; Kinase, protein; Protein kinase, CMGC; Protein kinase, Ser/Thr (non-receptor); SRPK family

Chromosomal Location of Human Ortholog: Xq28

Molecular Function: protein binding
 SRPK3 ELISA Kit
 SRPK3 Recombinant
 SRPK3 Antibody
 MSSK1 ELISA Kit
 MSSK1 Recombinant
 MSSK1 Antibody
 STK23 ELISA Kit
 STK23 Recombinant
 STK23 Antibody
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