+ |
AKT2 | down-regulates
phosphorylation
|
KHSRP |
0.351 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-151220 |
Ser193 |
GLPERSVsLTGAPES |
Rattus norvegicus |
|
pmid |
sentence |
17177604 |
AKT phosphorylates the mRNA decay-promoting factor KSRP at a unique serine residue, induces its association with the multifunctional protein 14-3-3, and prevents KSRP interaction with the exoribonucleolytic complex exosome. This impairs KSRPs ability to promote rapid mRNA decay. |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
Pathways: | P38 Signaling and Myogenesis |
+ |
AKT | down-regulates activity
phosphorylation
|
KHSRP |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-151216 |
Ser193 |
GLPERSVsLTGAPES |
Homo sapiens |
|
pmid |
sentence |
17177604 |
Beta-catenin transcript can be stabilized by either wnt or pi3k-akt signaling activation. Akt phosphorylates ksrp at a unique serine residue akt phosphorylates the mrna decay-promoting factor ksrp at a unique serine residue, induces its association with the multifunctional protein 14-3-3, and prevents ksrp interaction with the exoribonucleolytic complex exosome. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AKT1 | down-regulates activity
phosphorylation
|
KHSRP |
0.692 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252497 |
Ser193 |
GLPERSVsLTGAPES |
Homo sapiens |
|
pmid |
sentence |
17177604 |
Beta-catenin transcript can be stabilized by either wnt or pi3k-akt signaling activation. Akt phosphorylates ksrp at a unique serine residue akt phosphorylates the mrna decay-promoting factor ksrp at a unique serine residue, induces its association with the multifunctional protein 14-3-3, and prevents ksrp interaction with the exoribonucleolytic complex exosome. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | P38 Signaling and Myogenesis |
+ |
ATM | up-regulates
phosphorylation
|
KHSRP |
0.435 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-172123 |
Ser274 |
MILIQDGsQNTNVDK |
Homo sapiens |
|
pmid |
sentence |
21329876 |
The atm kinase directly binds to and phosphorylates ksrp, leading to enhanced interaction between ksrp and pri-mirnas and increased ksrp activity in mirna processing |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-172127 |
Ser670 |
GPGAPPGsQPDYSAA |
Homo sapiens |
|
pmid |
sentence |
21329876 |
The atm kinase directly binds to and phosphorylates ksrp, leading to enhanced interaction between ksrp and pri-mirnas and increased ksrp activity in mirna processing |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
MAPK14 | down-regulates activity
phosphorylation
|
KHSRP |
0.555 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-235856 |
Thr692 |
QAAYYGQtPGPGGPQ |
Mus musculus |
C2C12 Cell |
pmid |
sentence |
16364914 |
KSRP, an important factor for AU-rich element (ARE)-directed mRNA decay, undergoes p38-dependent phosphorylation during muscle differentiation. KSRP phosphorylated by p38 displays compromised binding to ARE-containing transcripts and fails to promote their rapid decay, although it retains the ability to interact with the mRNA degradation machinery |
|
Publications: |
1 |
Organism: |
Mus Musculus |
Pathways: | P38 Signaling and Myogenesis |
+ |
14-3-3 | down-regulates
binding
|
KHSRP |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-151212 |
|
|
Homo sapiens |
|
pmid |
sentence |
17177604 |
Akt phosphorylates ksrp at a unique serine residue, creating a functional binding site for the molecular chaperone 14-3-3. As a consequence, akt activation impairs ksrp ability to interact with the exoribonucleolytic complex exosome and, in turn, to promote rapid mrna decay. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
KHSRP | down-regulates
binding
|
DVL3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-23800 |
|
|
Homo sapiens |
Neutrophil, Monocyte |
pmid |
sentence |
2848118 |
Ksrp was shown to interact with the c-terminus of dvl3. We show that ksrp negatively regulates wnt/beta-catenin signaling at the level of post-transcriptional ctnnb1 (beta-catenin) mrna stability. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PTBP2 | up-regulates activity
binding
|
KHSRP |
0.476 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261268 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
11003644 |
Splicing of the c-src N1 exon in neuronal cells depends in part on an intronic cluster of RNA regulatory elements called the downstream control sequence (DCS). |nPTB binds more stably to the DCS RNA than PTB does but is a weaker repressor of splicing in vitro. nPTB also greatly enhances the binding of two other proteins, hnRNP H and KSRP, to the DCS RNA. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PCSK7 | down-regulates
phosphorylation
|
KHSRP |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-143167 |
|
|
Homo sapiens |
Myoblast |
pmid |
sentence |
16364914 |
Ksrp phosphorylated by p38 displays compromised binding to are-containing transcripts and fails to promote their rapid decay,although it retains the ability to interact with the mrna degradation machinery. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Muscle |
+ |
KHSRP | down-regulates quantity by destabilization
post transcriptional regulation
|
CDKN1A |
0.255 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-235859 |
|
|
Mus musculus |
C2C12 Cell |
pmid |
sentence |
16364914 |
Importantly, KSRP knockdown in C2C12 GM cells (Figure 2D) stabilized endogenous my- ogenin and p21 transcripts (Figure 2E). Furthermore, stable knockdown of KSRP, using shRNA, induced the accumulation of p21 mRNA in C2C12 GM while it did not affect the expression of late myogenic markers (MHC and muscle-creatine kinase [MCK]) |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
KHSRP | up-regulates quantity by expression
post transcriptional regulation
|
SRC |
0.275 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261274 |
|
|
in vitro |
|
pmid |
sentence |
9858532 |
We show here that this component of the DCS complex is hnRNP H and that, like hnRNP F and KSRP, hnRNP H is needed for src N1 splicing in vitro. |
|
Publications: |
1 |
Organism: |
In Vitro |