SRPK1 report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0018105Biological processpeptidyl-serine phosphorylation
GO_0045071Biological processnegative regulation of viral genome replication
GO_0007059Biological processchromosome segregation
GO_0045087Biological processinnate immune response
GO_0050684Biological processregulation of mRNA processing
GO_0045070Biological processpositive regulation of viral genome replication
GO_0035556Biological processintracellular signal transduction
GO_0008380Biological processRNA splicing
GO_0048024Biological processregulation of mRNA splicing, via spliceosome
GO_0035092Biological processsperm DNA condensation
GO_0006468Biological processprotein phosphorylation
GO_0000245Biological processspliceosomal complex assembly
GO_0005886Cellular componentplasma membrane
GO_0016607Cellular componentnuclear speck
GO_0005654Cellular componentnucleoplasm
GO_0016363Cellular componentnuclear matrix
GO_0005783Cellular componentendoplasmic reticulum
GO_0005829Cellular componentcytosol
GO_0005737Cellular componentcytoplasm
GO_0000785Cellular componentchromatin
GO_0005634Cellular componentnucleus
GO_0106310Molecular functionprotein serine kinase activity
GO_0004674Molecular functionprotein serine/threonine kinase activity
GO_0000287Molecular functionmagnesium ion binding
GO_0004672Molecular functionprotein kinase activity
GO_0005524Molecular functionATP binding
GO_0003723Molecular functionRNA binding
GO_0005515Molecular functionprotein binding

IV. Literature review

[source]
Gene nameSRPK1
Protein namenon-specific serine/threonine protein kinase (EC 2.7.11.1)
SRSF protein kinase 1 (EC 2.7.11.1) (SFRS protein kinase 1) (Serine/arginine-rich protein-specific kinase 1) (SR-protein-specific kinase 1)
SRSF protein kinase 1
Synonyms
DescriptionFUNCTION: 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. Isoform 2 phosphorylates SFRS2, ZRSR2, LBR and PRM1. Isoform 2 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. Isoform 2 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. Isoform 1 and isoform 2 can induce splicing of exon 10 in MAPT/TAU. The ratio of isoform 1/isoform 2 plays a decisive role in determining cell fate in K-562 leukaemic cell line: isoform 2 favors proliferation where as isoform 1 favors differentiation. .

AccessionsD6RBF8
ENST00000423325.6 [Q96SB4-4]
H3BLV9
ENST00000361690.7
D6RB98
ENST00000507909.1
ENST00000508473.5
H0Y932
Q96SB4
ENST00000512445.5
ENST00000373825.7 [Q96SB4-2]
D6RDZ3
ENST00000510290.5
D6RBM8
ENST00000507292.1