+ |
PRKACA | up-regulates
phosphorylation
|
SRSF1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-196397 |
Ser119 |
YGPPSRRsENRVVVS |
Homo sapiens |
|
pmid |
sentence |
22393468 |
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 |
phosphorylation
|
SRSF1 |
0.399 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-179615 |
Ser238 |
SRGSPRYsPRHSRSR |
Homo sapiens |
|
pmid |
sentence |
18658135 |
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 |
+ |
CLK3 | up-regulates activity
phosphorylation
|
SRSF1 |
0.545 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273859 |
|
|
in vitro |
|
pmid |
sentence |
8617202 |
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 |
+ |
SRSF1 | up-regulates
|
Alternative_Splicing_Regulation |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273861 |
|
|
Homo sapiens |
|
pmid |
sentence |
26273603 |
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 |
+ |
CLK1 | up-regulates activity
phosphorylation
|
SRSF1 |
0.695 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273857 |
|
|
in vitro |
|
pmid |
sentence |
8617202 |
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 |
+ |
SRP54 | up-regulates activity
binding
|
SRSF1 |
0.304 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261161 |
|
|
in vitro |
|
pmid |
sentence |
8816452 |
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 |
+ |
CLK2 | up-regulates activity
phosphorylation
|
SRSF1 |
0.302 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273858 |
|
|
in vitro |
|
pmid |
sentence |
8617202 |
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 |
+ |
SRPK1 | up-regulates
phosphorylation
|
SRSF1 |
0.796 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-66465 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
10196197 |
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 |
+ |
CLK4 | up-regulates activity
phosphorylation
|
SRSF1 |
0.365 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273860 |
|
|
in vitro |
|
pmid |
sentence |
8617202 |
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 |