Relation Results

Summary

Name SRSF1
Full Name Serine/arginine-rich splicing factor 1
Synonyms Alternative-splicing factor 1, ASF-1, Splicing factor, arginine/serine-rich 1, pre-mRNA-splicing factor SF2, P33 subunit | ASF, SF2, SF2P33, SFRS1
Primary ID Q07955
Links - -
Type protein
Relations 10
Function Plays a role in preventing exon skipping, ensuring the accuracy of splicing and regulating alternative splicing. Interacts with other spliceosomal com ...
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Type: Score: Layout: SPV 
0.20.3930.7980.70.680.3010.5350.2990.3590.351PRKACASRSF1DYRK1ASRPK1Alternative_Splicing_RegulationCLK1SRP54CLK3CLK2CLK4IRAK2

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▶Modifications Tables

Relations
Regulator
Mechanism
target
score ℹ
+ PRKACAup-regulates img/direct-activation.png phosphorylation SRSF1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-196397 Ser119 YGPPSRRsENRVVVS Homo sapiens
pmid sentence
Here, we show that pka phosphorylates srsf1 on serine 119 in vitro. Phosphorylation of srsf1 on this site enhanced the rna binding capacity of srsf1 in vivo
Publications: 1 Organism: Homo Sapiens
+ DYRK1A img/unknown.png phosphorylation SRSF1 0.393
Identifier Residue Sequence Organism Cell Line
SIGNOR-179615 Ser238 SRGSPRYsPRHSRSR Homo sapiens
pmid sentence
Here, we demonstrate that dyrk1a, a kinase encoded by a gene in the ds critical region, phosphorylates alternative splicing factor (asf) at ser-227, ser-234, and ser-238, driving it into nuclear speckles and preventing it from facilitating tau exon 10 inclusion.
Publications: 1 Organism: Homo Sapiens
Tissue: Brain
+ SRPK1up-regulates img/direct-activation.png phosphorylation SRSF1 0.798
Identifier Residue Sequence Organism Cell Line
SIGNOR-66465 Homo sapiens HeLa Cell
pmid sentence
These results suggest that the formation of complexes between sf2/asf and srpks, which is influenced by the phosphorylation state of sf2/asf, may have regulatory roles in the assembly and localization of this splicing factor.
Publications: 1 Organism: Homo Sapiens
+ SRSF1up-regulates img/indirect-activation.png Alternative_Splicing_Regulation 0.7
Identifier Residue Sequence Organism Cell Line
SIGNOR-273861 Homo sapiens
pmid sentence
In particular, SRSF1 recognizes SREs in its own transcripts, leading to alternative splicing, with some transcript forms being degraded by nonsense-mediated mRNA decay (NMD).
Publications: 1 Organism: Homo Sapiens
+ CLK1up-regulates activity img/direct-activation.png phosphorylation SRSF1 0.68
Identifier Residue Sequence Organism Cell Line
SIGNOR-273857 in vitro
pmid sentence
In vitro, Clk/Sty efficiently phosphorylated the SR family member ASF/SF2 on serine residues located within its serine/arginine-rich region (the RS domain). Overexpression of the active Clk/Sty kinase caused a redistribution of SR proteins within the nucleus. These results suggest that Clk/Sty kinase directly regulates the activity and compartmentalization of SR splicing factors.
Publications: 1 Organism: In Vitro
+ SRP54up-regulates activity img/direct-activation.png binding SRSF1 0.301
Identifier Residue Sequence Organism Cell Line
SIGNOR-261161 in vitro
pmid sentence
We have now demonstrated that p54 interacts not only with SC35 and ASF/SF2 but also with U2AF. Pairwise interactions between p54 and other RS domain-containing spliceosomal proteins in comparison with SC35 and ASF/SF2 as detected by the yeast two-hybrid interaction assay. . It is conceivable that p54 can mediate 59 and 39 splice site interaction by interacting directly with U2AF65 associated with the 39 splice site and at the same time interact with other SR proteins, such as ASF/SF2 and SC35, which in turn interact with U1-70K. In this scenario, p54 is different from SC35 or ASF/SF2 in that it cannot directly interact with the 59 component (U1-70K) but can interact with the protein associated with the 39 splice site (U2AF65).
Publications: 1 Organism: In Vitro
+ CLK3up-regulates activity img/direct-activation.png phosphorylation SRSF1 0.535
Identifier Residue Sequence Organism Cell Line
SIGNOR-273859 in vitro
pmid sentence
In vitro, Clk/Sty efficiently phosphorylated the SR family member ASF/SF2 on serine residues located within its serine/arginine-rich region (the RS domain). Overexpression of the active Clk/Sty kinase caused a redistribution of SR proteins within the nucleus. These results suggest that Clk/Sty kinase directly regulates the activity and compartmentalization of SR splicing factors.
Publications: 1 Organism: In Vitro
+ CLK2up-regulates activity img/direct-activation.png phosphorylation SRSF1 0.299
Identifier Residue Sequence Organism Cell Line
SIGNOR-273858 in vitro
pmid sentence
In vitro, Clk/Sty efficiently phosphorylated the SR family member ASF/SF2 on serine residues located within its serine/arginine-rich region (the RS domain). Overexpression of the active Clk/Sty kinase caused a redistribution of SR proteins within the nucleus. These results suggest that Clk/Sty kinase directly regulates the activity and compartmentalization of SR splicing factors.
Publications: 1 Organism: In Vitro
+ CLK4up-regulates activity img/direct-activation.png phosphorylation SRSF1 0.359
Identifier Residue Sequence Organism Cell Line
SIGNOR-273860 in vitro
pmid sentence
In vitro, Clk/Sty efficiently phosphorylated the SR family member ASF/SF2 on serine residues located within its serine/arginine-rich region (the RS domain). Overexpression of the active Clk/Sty kinase caused a redistribution of SR proteins within the nucleus. These results suggest that Clk/Sty kinase directly regulates the activity and compartmentalization of SR splicing factors.
Publications: 1 Organism: In Vitro
+ IRAK2down-regulates activity img/direct_inhibition.png phosphorylation SRSF1 0.351
Identifier Residue Sequence Organism Cell Line
SIGNOR-278406 Homo sapiens
pmid sentence
IRAK2 phosphorylates SRSF1 and thereby reduces SRSF1 binding to the target mRNAs.
Publications: 1 Organism: Homo Sapiens
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