+ |
PAK4 | up-regulates
phosphorylation
|
RAN |
0.312 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-167667 |
Ser135 |
DRKVKAKsIVFHRKK |
Homo sapiens |
|
pmid |
sentence |
20805321 |
We show that ran is a substrate for p21-activated kinase 4 (pak4) and that its phosphorylation on serine-135 increases during mitosis.Altogether, our findings strongly suggest that pak4-mediated phosphorylation of gdp- or gtp-bound ran modulates the assembly of complexes that are required at specific subcellular localizations for ran to carry out its functions during mitotic progression. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PAK4 |
phosphorylation
|
RAN |
0.312 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-167671 |
Ser135 |
DRKVKAKsIVFHRKK |
Homo sapiens |
|
pmid |
sentence |
20805321 |
We show that ran is a substrate for p21-activated kinase 4 (pak4) and that its phosphorylation on serine-135 increases during mitosis. our study suggests that pak4-mediated phosphorylation of gdp- or gtp-bound ran regulates the assembly of ran-dependent complexes on the mitotic spindle |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PAK4 | up-regulates quantity by stabilization
phosphorylation
|
SNAI2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277393 |
Ser158 |
CDAQSRKsFSCKYCD |
in vitro |
|
pmid |
sentence |
29849120 |
PAK4 bound and directly phosphorylated Slug at two previously unknown sites, S158 and S254, which resulted in its stabilization. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277394 |
Ser254 |
SKTFSRMsLLHKHEE |
in vitro |
|
pmid |
sentence |
29849120 |
PAK4 bound and directly phosphorylated Slug at two previously unknown sites, S158 and S254, which resulted in its stabilization. |
|
Publications: |
2 |
Organism: |
In Vitro |
+ |
PAK4 | up-regulates activity
phosphorylation
|
MZF1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277422 |
Ser27 |
VMVKLEDsEEEGEAA |
in vitro |
|
pmid |
sentence |
30622337 |
Here, we link ErbB2 activation to invasion via ErbB2-induced, SUMO-directed phosphorylation of a single serine residue, S27, of the transcription factor myeloid zinc finger-1 (MZF1). Phosphorylation of MZF1-S27 is an early response to ErbB2 activation and results in increased transcriptional activity of MZF1.The phosphorylation of MZF1-S27 is preceded by poly-SUMOylation of K23, which can make S27 accessible to efficient phosphorylation by PAK4. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
PAK4 |
phosphorylation
|
PXN |
0.522 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-164889 |
Ser272 |
ELDELMAsLSDFKIQ |
Homo sapiens |
Prostate Gland Cancer Cell |
pmid |
sentence |
20406887 |
We find that pak4 is localised at focal adhesions, is immunoprecipitated with paxillin and phosphorylates paxillin on serine 272. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PAK4 | up-regulates activity
phosphorylation
|
PACSIN1 |
0.301 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263023 |
Ser346 |
SQAGDRGsVSSYDRG |
in vitro |
|
pmid |
sentence |
22371566 |
We identified two novel Pak5 substrates, Pacsin1 and Synaptojanin1, proteins that directly interact with one another to regulate synaptic vesicle endocytosis and recycling. Pacsin1 and Synaptojanin1 were phosphorylated by Pak5 and the other group II Paks in vitro, and Pak5 phosphorylation promoted Pacsin1-Synaptojanin1 binding both in vitro and in vivo. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
PAK4 | down-regulates quantity
phosphorylation
|
FH |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266315 |
Ser46 |
PNAARMAsQNSFRIE |
Homo sapiens |
Non-small Cell Lung Cancer Cell |
pmid |
sentence |
30683654 |
FH is massively phosphorylated at the Ser 46 by PAK4 in non-small cell lung cancer (NSCLC) cells, and PAK4-phosphorylated FH binds to 14-3-3, resulting in cytosolic detention of FH and prohibition of FH/CSL/p53 complex formation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKD3 | up-regulates activity
phosphorylation
|
PAK4 |
0.255 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275931 |
Ser474 |
KEVPRRKsLVGTPYW |
|
|
pmid |
sentence |
23841590 |
PAK4 activity is regulated by an autoinhibitory domain that is released upon RhoGTPase binding as well as phosphorylation at Ser474 in the activation loop of the kinase domain. In the present study, we add another level of complexity to PAK4 regulation by showing that phosphorylation at Ser99 is required for its targeting to the leading edge. This phosphorylation is mediated by PKD1 (protein kinase D1) |
|
Publications: |
1 |
+ |
PAK4 | up-regulates activity
phosphorylation
|
PAK4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-235867 |
Ser474 |
KEVPRRKsLVGTPYW |
Mus musculus |
NIH-3T3 Cell |
pmid |
sentence |
11668177 |
Here we demonstrate that PAK4 is frequently overexpressed in human tumor cell lines of various tissue origins. We also have identified serine (Ser-474) as the likely autophosphorylation site in the kinase domain of PAK4 in vivo. Mutation of this serine to glutamic acid (S474E) results in constitutive activation of the kinase. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
PAK4 | up-regulates
phosphorylation
|
PAK4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-168301 |
Ser474 |
KEVPRRKsLVGTPYW |
Homo sapiens |
|
pmid |
sentence |
20926745 |
Intracellular localization;enzymatic activity, induced;cell growth, altered; |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKD1 | up-regulates activity
phosphorylation
|
PAK4 |
0.255 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275930 |
Ser474 |
KEVPRRKsLVGTPYW |
|
|
pmid |
sentence |
24840177 |
When PKD3 was knocked-down using isoform-specific shRNA (PKD3-shRNA), PAK4 activity (judged by its phosphorylation status at the activation loop using the pS474-PAK4 antibody) was decreased |
|
Publications: |
1 |
+ |
PAK4 | up-regulates
phosphorylation
|
CTNNB1 |
0.291 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-191557 |
Ser675 |
QDYKKRLsVELTSSL |
Homo sapiens |
|
pmid |
sentence |
22173096 |
Pak4 interacts with and phosphorylates _-catenin on ser675, which promotes the tcf/lef transcriptional activity and stabilizes _-catenin through inhibition of its degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PAK4 | up-regulates
phosphorylation
|
ITGB5 |
0.463 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-165702 |
Ser759 |
REFAKFQsERSRARY |
Homo sapiens |
|
pmid |
sentence |
20507994 |
Pak4 specifically phosphorylated the integrin beta5 subunit at ser-759 and ser-762 within the beta5-sers-motif. Point mutation of these two serine residues abolished the pak4-induced cell migration, indicating a functional role for these phosphorylations in migration. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-165706 |
Ser762 |
AKFQSERsRARYEMA |
Homo sapiens |
|
pmid |
sentence |
20507994 |
Pak4 specifically phosphorylated the integrin beta5 subunit at ser-759 and ser-762 within the beta5-sers-motif. Point mutation of these two serine residues abolished the pak4-induced cell migration, indicating a functional role for these phosphorylations in migration. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
PAK4 | down-regulates quantity by destabilization
phosphorylation
|
NFE2L2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277583 |
Thr369 |
ESSSYGDtLLGLSDS |
Mus musculus |
Hepatocyte |
pmid |
sentence |
35108418 |
PAK4 directly phosphorylated Nrf2 at T369, and it led to its nuclear export and proteasomal degradation, all of which impaired antioxidant responses in hepatocytes. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
PAK4 | up-regulates activity
phosphorylation
|
SYNJ1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263024 |
|
|
in vitro |
|
pmid |
sentence |
22371566 |
We identified two novel Pak5 substrates, Pacsin1 and Synaptojanin1, proteins that directly interact with one another to regulate synaptic vesicle endocytosis and recycling. Pacsin1 and Synaptojanin1 were phosphorylated by Pak5 and the other group II Paks in vitro, and Pak5 phosphorylation promoted Pacsin1-Synaptojanin1 binding both in vitro and in vivo. |
|
Publications: |
1 |
Organism: |
In Vitro |