| + |
PAK5 | up-regulates activity 
phosphorylation
|
PAK5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250248 |
His19 |
SGPSNFEhRVHTGFD |
in vitro |
|
| pmid |
sentence |
| 12860998 |
Active form of Cdc42, but not Rac1 and Rho, protein was able to activate the purified GST-Pak5 autophosphorylation and kinase activity. Mutations of Pak5, which disrupted the interaction of Cdc42 and Pak5, also abolished the induction of autophosphorylation. The H19L/H22L mutant of Pak5 was insensitive to the Cdc42-induced autophosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250249 |
His22 |
SNFEHRVhTGFDPQE |
in vitro |
|
| pmid |
sentence |
| 12860998 |
Active form of Cdc42, but not Rac1 and Rho, protein was able to activate the purified GST-Pak5 autophosphorylation and kinase activity. Mutations of Pak5, which disrupted the interaction of Cdc42 and Pak5, also abolished the induction of autophosphorylation. The H19L/H22L mutant of Pak5 was insensitive to the Cdc42-induced autophosphorylation. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PAK5 | down-regulates quantity by destabilization 
phosphorylation
|
DNPEP |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275651 |
Ser119 |
VKRRSRRsQVGFQQV |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 31219614 |
We show that PAK5 interacts with and phosphorylates DNPEP at serine 119. | PAK5 decreases DNPEP abundance via the ubiquitin-proteasome pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK5 | up-regulates activity
phosphorylation
|
GATA1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275655 |
Ser161 |
SSLPVPNsAYGGPDF |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 25726523 |
GATA1 is a new substrate of p21-activated kinase 5 (PAK5), which is phosphorylated on serine 161 and 187 (S161 and S187). GATA1 recruits HDAC3/4 to E-cadherin promoter, which is reduced by GATA1 S161A S187A mutant. These data indicate that phosphorylated GATA1 recruits more HDAC3/4 to promote transcriptional repression of E-cadherin, leading to the EMT of breast cancer cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275656 |
Ser187 |
LNSAAYSsPKLRGTL |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 25726523 |
GATA1 is a new substrate of p21-activated kinase 5 (PAK5), which is phosphorylated on serine 161 and 187 (S161 and S187). GATA1 recruits HDAC3/4 to E-cadherin promoter, which is reduced by GATA1 S161A S187A mutant. These data indicate that phosphorylated GATA1 recruits more HDAC3/4 to promote transcriptional repression of E-cadherin, leading to the EMT of breast cancer cells. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PAK5 | up-regulates activity
phosphorylation
|
PACSIN1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263025 |
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 |
| + |
PAK5 | up-regulates activity
phosphorylation
|
TCF3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275653 |
Ser39 |
NGKGRPAsLAGAQFG |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 26212009 |
The p21-activated kinase 5 (PAK5) is overexpressed in advanced cancer and the transcription factor E47 is a direct repressor of E-cadherin and inducer of epithelial-mesenchymal transition (EMT). |In this study, we found that PAK5-mediated E47 phosphorylation promoted EMT in advanced colon cancer. PAK5 interacted with E47 and phosphorylated E47 on Ser39 under hepatocyte growth factor (HGF) stimulation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK5 | down-regulates activity
phosphorylation
|
BAD |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250247 |
Ser75 |
EIRSRHSsYPAGTED |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 12897128 |
P21-Activated kinase 5 (Pak5) localizes to mitochondria and inhibits apoptosis by phosphorylating BAD. Pak5 phosphorylates BAD Ser-112 |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
PAK5 | up-regulates quantity by stabilization
phosphorylation
|
DDX5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275658 |
Thr69 |
HPDLARRtAQEVETY |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 34936874 |
PAK5 promotes RNA helicase DDX5 sumoylation and miRNA-10b processing in a kinase-dependent manner in breast cancer|The increased expression levels of PAK5 and phospho-DDX5 threonine 69 are associated with metastasis and poor clinical outcomes of patients. PAK5 facilitates the phosphorylation-dependent sumoylation of DDX5 to stabilize DDX5. Both the phosphorylation and sumoylation of DDX5 enhance the formation of a DDX5/Drosha/DGCR8 complex, thus promoting microRNA-10b processing. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK5 | up-regulates activity
phosphorylation
|
RELA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275657 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 29041983 |
PAK5-mediated phosphorylation and nuclear translocation of NF-κB-p65 promotes breast cancer cell proliferation in vitro and in vivo|We characterized that PAK5 could promote the phosphorylation and the nuclear translocation of p65 subunit of nuclear factor-kappaB, and demonstrated that p65 could directly bind to the promoter of Cyclin D1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK5 | up-regulates activity
phosphorylation
|
SYNJ1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263026 |
|
|
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 |
3.0
PAK5
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