| + |
PAK1 | down-regulates 
phosphorylation
|
ARHGDIA |
0.594 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-126650 |
Ser101 |
LESFKKQsFVLKEGV |
Homo sapiens |
|
| pmid |
sentence |
| 15225553 |
Pak1 binds and phosphorylates rhogdi both in vitro and in vivo at ser101 and ser174. This resulted in dissociation of rac1-rhogdi, but not rhoa-rhogdi, complexes, as determined by in vitro assays of complexation and in vivo by coimmunoprecipitation analysis. We observed that cdc42-induced rac1 activation is inhibited by expression of pak1 autoinhibitory domain. The dissociation of rac1 from rhogdi and its subsequent activation stimulated by pdgf or egf is also attenuated by pak1 autoinhibitory domain, and this is dependent on the ability of rhogdi to be phosphorylated at ser101/174. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-126654 |
Ser174 |
KGMLARGsYSIKSRF |
Homo sapiens |
|
| pmid |
sentence |
| 15225553 |
Pak1 binds and phosphorylates rhogdi both in vitro and in vivo at ser101 and ser174. This resulted in dissociation of rac1-rhogdi, but not rhoa-rhogdi, complexes, as determined by in vitro assays of complexation and in vivo by coimmunoprecipitation analysis. We observed that cdc42-induced rac1 activation is inhibited by expression of pak1 autoinhibitory domain. The dissociation of rac1 from rhogdi and its subsequent activation stimulated by pdgf or egf is also attenuated by pak1 autoinhibitory domain, and this is dependent on the ability of rhogdi to be phosphorylated at ser101/174. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PAK1 |
phosphorylation
|
H3C1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91050 |
Ser11 |
TKQTARKsTGGKAPR |
Homo sapiens |
|
| pmid |
sentence |
| 12151336 |
Histone h3 is a substrate of pak1 both in vitro and in vivo, and it specifically interacted with pak1 but not pak2 or pak3. Site-directed mutagenesis indicated that pak1 phosphorylates histone h3 on ser10. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK1 | down-regulates activity
phosphorylation
|
PREX2 |
0.374 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277181 |
Ser1107 |
DTISNRDsYSDCNSN |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 26438819 |
P21-activated Kinases (PAKs) Mediate the Phosphorylation of PREX2 Protein to Initiate Feedback Inhibition of Rac1 GTPase. PAK-mediated phosphorylation of PREX2 reduced GEF activity toward Rac1 by inhibiting PREX2 binding to PIP3 and Gβγ. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK1 | down-regulates
phosphorylation
|
KIF2C |
0.393 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-199080 |
Ser111 |
KESLRSRsTRMSTVS |
Homo sapiens |
|
| pmid |
sentence |
| 23055517 |
Here we found that mcak is a cognate substrate of pak1 wherein pak1 phosphorylates mcak on serines 192 and 111 both in vivo and in vitro. Furthermore, we found that pak1 phosphorylation of mcak on serines 192 and 111 preferentially regulates its microtubule depolymerization activity and localization to centrosomes |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-199084 |
Ser192 |
VNSVRRKsCLVKEVE |
Homo sapiens |
|
| pmid |
sentence |
| 23055517 |
Here we found that mcak is a cognate substrate of pak1 wherein pak1 phosphorylates mcak on serines 192 and 111 both in vivo and in vitro. Furthermore, we found that pak1 phosphorylation of mcak on serines 192 and 111 preferentially regulates its microtubule depolymerization activity and localization to centrosomes |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PAK1 | down-regulates
phosphorylation
|
PGAM1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91594 |
Ser118 |
QVKIWRRsYDVPPPP |
Homo sapiens |
Neutrophil |
| pmid |
sentence |
| 12189148 |
Activated pak1 inhibits glycolysis by association of its catalytic domain with pgam-b and subsequent phosphorylation of the enzyme on serine residues 23 and 118, thereby abolishing pgam activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91598 |
Ser23 |
WNLENRFsGWYDADL |
Homo sapiens |
Neutrophil |
| pmid |
sentence |
| 12189148 |
Activated pak1 inhibits glycolysis by association of its catalytic domain with pgam-b and subsequent phosphorylation of the enzyme on serine residues 23 and 118, thereby abolishing pgam activity. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PAK1 | up-regulates 
phosphorylation
|
TBCB |
0.459 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-135460 |
Ser128 |
VRSFLKRsKLGRYNE |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 15831477 |
P21-activated kinase 1 regulates microtubule dynamics by phosphorylating tubulin cofactor b. Pak1 directly phosphorylated tcob in vitro and in vivo on serines 65 and 128 and colocalized with tcob on newly polymerized microtubules and on centrosomes. Pak1 phosphorylation is necessary for normal tcob function |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-135464 |
Ser65 |
GVDDKFYsKLDQEDA |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 15831477 |
P21-activated kinase 1 regulates microtubule dynamics by phosphorylating tubulin cofactor b. Pak1 directly phosphorylated tcob in vitro and in vivo on serines 65 and 128 and colocalized with tcob on newly polymerized microtubules and on centrosomes. Pak1 phosphorylation is necessary for normal tcob function |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PAK1 | down-regulates activity
phosphorylation
|
NET1 |
0.251 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263019 |
Ser152 |
PTPAKRRsSALWSEM |
in vitro |
|
| pmid |
sentence |
| 15684429 |
In this work we show that the Rac/Cdc42hs-regulated protein kinase PAK1 down-regulates the activity of the RhoA-specific guanine nucleotide exchange factor NET1. Specifically, PAK1 phosphorylates NET1 on three sites in vitro: serines 152, 153, and 538. Replacement of serines 152 and 153 with glutamate residues down-regulates the activity of NET1 as an exchange factor in vitro and its ability to stimulate actin stress fiber formation in cells. Using a phospho-specific antibody that recognizes NET1 phosphorylated on serine 152, we show that PAK1 phosphorylates NET1 on this site in cells and that Rac1 stimulates serine 152 phosphorylation in a PAK1-dependent manner. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263017 |
Ser152 |
PTPAKRRsSALWSEM |
in vitro |
|
| pmid |
sentence |
| 15684429 |
In this work we show that the Rac/Cdc42hs-regulated protein kinase PAK1 down-regulates the activity of the RhoA-specific guanine nucleotide exchange factor NET1. Specifically, PAK1 phosphorylates NET1 on three sites in vitro: serines 152, 153, and 538. Replacement of serines 152 and 153 with glutamate residues down-regulates the activity of NET1 as an exchange factor in vitro and its ability to stimulate actin stress fiber formation in cells. Using a phospho-specific antibody that recognizes NET1 phosphorylated on serine 152, we show that PAK1 phosphorylates NET1 on this site in cells and that Rac1 stimulates serine 152 phosphorylation in a PAK1-dependent manner. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263018 |
Ser539 |
LTAQRRAsTVSSVTQ |
in vitro |
|
| pmid |
sentence |
| 15684429 |
In this work we show that the Rac/Cdc42hs-regulated protein kinase PAK1 down-regulates the activity of the RhoA-specific guanine nucleotide exchange factor NET1. Specifically, PAK1 phosphorylates NET1 on three sites in vitro: serines 152, 153, and 538. Replacement of serines 152 and 153 with glutamate residues down-regulates the activity of NET1 as an exchange factor in vitro and its ability to stimulate actin stress fiber formation in cells. Using a phospho-specific antibody that recognizes NET1 phosphorylated on serine 152, we show that PAK1 phosphorylates NET1 on this site in cells and that Rac1 stimulates serine 152 phosphorylation in a PAK1-dependent manner. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
PAK1 | down-regulates activity
phosphorylation
|
CTBP1 |
0.411 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-103943 |
Ser158 |
REGTRVQsVEQIREV |
Homo sapiens |
|
| pmid |
sentence |
| 12872159 |
Pak1 phosphorylates ctbp selectively on ser158 within a putative regulatory loop, triggering ctbp cellular redistribution and blocking ctbp ak1 superphosphorylates ctbp and inhibits ctbp dehydrogenase activitycorepressor functions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK1 | down-regulates
phosphorylation
|
STMN1 |
0.382 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-119483 |
Ser16 |
KELEKRAsGQAFELI |
Homo sapiens |
|
| pmid |
sentence |
| 14645234 |
Pak1 phosphorylates op18/stathmin specifically at serine 16 and inactivates its catastrophe promoting activity in biochemical and time lapse microscopy microtubule assembly assays. Furthermore, phosphorylation of either serine 16 or 63 is sufficient to inhibit op18/stathmin in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-79955 |
Ser38 |
SVPEFPLsPPKKKDL |
Homo sapiens |
|
| pmid |
sentence |
| 10913145 |
We find that, in vitro, pak1 phosphorylates op18/stathmin specifically at serine 16 and inactivates its catastrophe promoting activity in biochemical and time lapse microscopy microtubule assembly assays. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183503 |
Ser38 |
SVPEFPLsPPKKKDL |
Homo sapiens |
|
| pmid |
sentence |
| 19162178 |
The hgf-induced wave2 transport, lamellipodia formation, stathmin/op18 phosphorylation at ser38 and binding to kinesin-wave2 complex, but not stathmin/op18 phosphorylation at ser25 and microtubule growth, were abrogated by pak1 inhibitor ipa-3 |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PAK1 | up-regulates
phosphorylation
|
GNAZ |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-48673 |
Ser16 |
EKEAARRsRRIDRHL |
Homo sapiens |
|
| pmid |
sentence |
| 9166747 |
Phosphorylation of either ser(16) by pak1 or ser(27) by pkc decreased the affinity of galpha(z) for gbetagamma;phosphorylation of both residues by pkc caused no further effect. Pak1 thus regulates galpha(z) function by attenuating the inhibitory effects of both gaps and gbetagamma. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney |
| + |
CDK11A | up-regulates activity
phosphorylation
|
PAK1 |
0.393 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273026 |
Ser174 |
TPAVPPVsEDEDDDD |
|
|
| pmid |
sentence |
| 19520772 |
CDK11p58 phosphorylation of PAK1 Ser174 promotes DLC2 binding and roles on cell cycle progression|We show that PAK1 is a substrate of CDK11p58 and can be strongly activated upon phosphorylation. |
|
| Publications: |
1 |
| + |
CDK19 |
phosphorylation
|
PAK1 |
0.338 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-185000 |
Ser174 |
TPAVPPVsEDEDDDD |
Homo sapiens |
|
| pmid |
sentence |
| 19520772 |
Here, we identified p21 activated kinase 1 (pak1) as a new cdk11(p58) substrate and we mapped a new phosphorylation site of ser174 on pak1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CyclinD3/CDK11B | up-regulates activity
phosphorylation
|
PAK1 |
0.395 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273129 |
Ser174 |
TPAVPPVsEDEDDDD |
|
|
| pmid |
sentence |
| 19520772 |
CDK11p58 phosphorylation of PAK1 Ser174 promotes DLC2 binding and roles on cell cycle progression|We show that PAK1 is a substrate of CDK11p58 and can be strongly activated upon phosphorylation. |
|
| Publications: |
1 |
| + |
CyclinD3/CDK11A | up-regulates activity
phosphorylation
|
PAK1 |
0.393 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273124 |
Ser174 |
TPAVPPVsEDEDDDD |
|
|
| pmid |
sentence |
| 19520772 |
CDK11p58 phosphorylation of PAK1 Ser174 promotes DLC2 binding and roles on cell cycle progression|We show that PAK1 is a substrate of CDK11p58 and can be strongly activated upon phosphorylation. |
|
| Publications: |
1 |
| + |
PPP2CB | down-regulates activity
dephosphorylation
|
PAK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248599 |
Ser199 |
PRPEHTKsVYTRSVI |
Rattus norvegicus |
|
| pmid |
sentence |
| 18586681 |
Both sites were dephosphorylated with the same kinetics; the anti-Ser(P)198 antibody was subsequently used as it exhibited lower background staining. Direct comparison of PP2Cα with purified PP1 and PP2A lead us to conclude that at the same molar ratio PP2Cα was the most efficient in dephosphorylating PAK1 (Fig. 1D). In this case we monitored two autophosphorylation sites in the Pak1 N-terminal regulatory region (Ser57 and Ser198/203) using phosphospecific antibodies: both sites showed the same kinetics of inactivation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248598 |
Ser57 |
KKDRFYRsILPGDKT |
Rattus norvegicus |
|
| pmid |
sentence |
| 18586681 |
Both sites were dephosphorylated with the same kinetics; the anti-Ser(P)198 antibody was subsequently used as it exhibited lower background staining. Direct comparison of PP2Cα with purified PP1 and PP2A lead us to conclude that at the same molar ratio PP2Cα was the most efficient in dephosphorylating PAK1 (Fig. 1D). In this case we monitored two autophosphorylation sites in the Pak1 N-terminal regulatory region (Ser57 and Ser198/203) using phosphospecific antibodies: both sites showed the same kinetics of inactivation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248600 |
Thr423 |
PEQSKRStMVGTPYW |
Rattus norvegicus |
|
| pmid |
sentence |
| 18586681 |
Both sites were dephosphorylated with the same kinetics; the anti-Ser(P)198 antibody was subsequently used as it exhibited lower background staining. Direct comparison of PP2Cα with purified PP1 and PP2A lead us to conclude that at the same molar ratio PP2Cα was the most efficient in dephosphorylating PAK1 (Fig. 1D). In this case we monitored two autophosphorylation sites in the Pak1 N-terminal regulatory region (Ser57 and Ser198/203) using phosphospecific antibodies: both sites showed the same kinetics of inactivation. |
|
| Publications: |
3 |
Organism: |
Rattus Norvegicus |
| + |
PPP2CA | down-regulates activity
dephosphorylation
|
PAK1 |
0.365 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248642 |
Ser199 |
PRPEHTKsVYTRSVI |
Rattus norvegicus |
|
| pmid |
sentence |
| 18586681 |
Both sites were dephosphorylated with the same kinetics; the anti-Ser(P)198 antibody was subsequently used as it exhibited lower background staining. Direct comparison of PP2Cα with purified PP1 and PP2A lead us to conclude that at the same molar ratio PP2Cα was the most efficient in dephosphorylating PAK1 (Fig. 1D). In this case we monitored two autophosphorylation sites in the Pak1 N-terminal regulatory region (Ser57 and Ser198/203) using phosphospecific antibodies: both sites showed the same kinetics of inactivation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248641 |
Ser57 |
KKDRFYRsILPGDKT |
Rattus norvegicus |
|
| pmid |
sentence |
| 18586681 |
Both sites were dephosphorylated with the same kinetics; the anti-Ser(P)198 antibody was subsequently used as it exhibited lower background staining. Direct comparison of PP2Cα with purified PP1 and PP2A lead us to conclude that at the same molar ratio PP2Cα was the most efficient in dephosphorylating PAK1 (Fig. 1D). In this case we monitored two autophosphorylation sites in the Pak1 N-terminal regulatory region (Ser57 and Ser198/203) using phosphospecific antibodies: both sites showed the same kinetics of inactivation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248643 |
Thr423 |
PEQSKRStMVGTPYW |
Rattus norvegicus |
|
| pmid |
sentence |
| 18586681 |
Both sites were dephosphorylated with the same kinetics; the anti-Ser(P)198 antibody was subsequently used as it exhibited lower background staining. Direct comparison of PP2Cα with purified PP1 and PP2A lead us to conclude that at the same molar ratio PP2Cα was the most efficient in dephosphorylating PAK1 (Fig. 1D). In this case we monitored two autophosphorylation sites in the Pak1 N-terminal regulatory region (Ser57 and Ser198/203) using phosphospecific antibodies: both sites showed the same kinetics of inactivation. |
|
| Publications: |
3 |
Organism: |
Rattus Norvegicus |
| + |
PPM1A | down-regulates activity
dephosphorylation
|
PAK1 |
0.343 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248492 |
Ser199 |
PRPEHTKsVYTRSVI |
Rattus norvegicus |
|
| pmid |
sentence |
| 18586681 |
Purified PP2Cα protein efficiently dephosphorylated PAK1 in vitro (Fig. 1, D and E). We previously assessed the time course of phospho-PAK1 dephosphorylation assessed using specific antibodies against either Ser(P)198/203 or Thr(P)422 sites in the PAK1 activation loop. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248493 |
Ser57 |
KKDRFYRsILPGDKT |
Rattus norvegicus |
|
| pmid |
sentence |
| 18586681 |
Both sites were dephosphorylated with the same kinetics; the anti-Ser(P)198 antibody was subsequently used as it exhibited lower background staining. Direct comparison of PP2Cα with purified PP1 and PP2A lead us to conclude that at the same molar ratio PP2Cα was the most efficient in dephosphorylating PAK1 (Fig. 1D). In this case we monitored two autophosphorylation sites in the Pak1 N-terminal regulatory region (Ser57 and Ser198/203) using phosphospecific antibodies: both sites showed the same kinetics of inactivation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248491 |
Thr423 |
PEQSKRStMVGTPYW |
Rattus norvegicus |
|
| pmid |
sentence |
| 18586681 |
Purified PP2Cα protein efficiently dephosphorylated PAK1 in vitro (Fig. 1, D and E). We previously assessed the time course of phospho-PAK1 dephosphorylation assessed using specific antibodies against either Ser(P)198/203 or Thr(P)422 sites in the PAK1 activation loop. |
|
| Publications: |
3 |
Organism: |
Rattus Norvegicus |
| + |
PAK1 | up-regulates activity
phosphorylation
|
PAK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250216 |
Ser199 |
PRPEHTKsVYTRSVI |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 9032240 |
Cdc42 and Rac1 cause alpha-PAK autophosphorylation and kinase activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250219 |
Ser57 |
KKDRFYRsILPGDKT |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 9032240 |
Cdc42 and Rac1 cause alpha-PAK autophosphorylation and kinase activation. |
|
| Publications: |
2 |
Organism: |
Chlorocebus Aethiops |
| Pathways: | EGFR Signaling, T cell activation, Toll like receptors |
| + |
PAK1 | up-regulates
phosphorylation
|
ELF3 |
0.468 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-154743 |
Ser207 |
GTGASRSsHSSDSGG |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 17491012 |
Phosphorylation-dependent regulation of stability and transforming potential of ets transcriptional factor ese-1 by p21-activated kinase 1. Pak1 selectively phosphorylates ese-1 at ser(207). Intriguingly, pak1 phosphorylation inactive mutant ese1-s207a is more unstable |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK1 | up-regulates
phosphorylation
|
FLNA |
0.781 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-92065 |
Ser2152 |
TRRRRAPsVANVGSH |
Homo sapiens |
|
| pmid |
sentence |
| 12198493 |
In flna, the pak1-binding site involves tandem repeat 23 in the carboxyl terminus and phosphorylation takes place on serine 2152. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK1 | up-regulates
phosphorylation
|
ILK |
0.419 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-154303 |
Ser246 |
CPRLRIFsHPNVLPV |
Homo sapiens |
|
| pmid |
sentence |
| 17420447 |
We found that pak1 phosphorylates ilk at threonine-173 and serine-246 in vitro and in vivo. together, these results suggest that ilk is a pak1 substrate, undergoes phosphorylation-dependent shuttling between the cell nucleus and cytoplasm, and interacts with gene-regulatory chromatin. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-154307 |
Thr173 |
DTFWKGTtRTRPRNG |
Homo sapiens |
|
| pmid |
sentence |
| 17420447 |
We found that pak1 phosphorylates ilk at threonine-173 and serine-246 in vitro and in vivo. together, these results suggest that ilk is a pak1 substrate, undergoes phosphorylation-dependent shuttling between the cell nucleus and cytoplasm, and interacts with gene-regulatory chromatin. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PAK1 | up-regulates
phosphorylation
|
SNAI1 |
0.408 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-135605 |
Ser246 |
QACARTFsRMSLLHK |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 15833848 |
Pak1 regulates the repressor activity of snail by phosphorylating on ser(246). Pak1 phosphorylation of snail supports snail's accumulation in the nucleus as well as its repressor functions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK1 |
phosphorylation
|
PXN |
0.65 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-146842 |
Ser272 |
ELDELMAsLSDFKIQ |
Homo sapiens |
|
| pmid |
sentence |
| 16717130 |
We show that p21-activated kinase (pak)-induced phosphorylation of serine 273 in paxillin is a critical regulator of this turnover. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK1 | up-regulates
phosphorylation
|
ITGB3BP |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178795 |
Ser28 |
SKITRKKsVITYSPT |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 18521086 |
Serine 28 phosphorylation of nrif3 confers its co-activator function for estrogen receptor-alpha transactivation. p21-activated protein kinase 1 (pak1) phosphorylates eralpha at ser305 and this modification is important in eralpha transactivation function. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK1 | up-regulates activity
phosphorylation
|
MAP2K1 |
0.564 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236002 |
Ser298 |
RTPGRPLsSYGMDSR |
Homo sapiens |
REF-52 Cell |
| pmid |
sentence |
| 12876277 |
We find that adhesion to fibronectin induces pak1-dependent phosphorylation of mek1 on s298 and that this phosphorylation is necessary for efficient activation of mek1 and subsequent mapk activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK1 | up-regulates
phosphorylation
|
ARAF |
0.27 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236342 |
Ser299 |
KNLGYRDsGYYWEVP |
Homo sapiens |
Melanoma Cell |
| pmid |
sentence |
| 15710605 |
Phosphorylation of endogenous a-raf, b-raf and raf-1 on the homologous pak phosphorylation sites (serine 299, serine 445, or serine 338 respectively)we found that the phosphorylation of a-raf on serine 299 was also stimulated by egf, although the duration of phosphorylation on this site was much shorter than for raf-1. Thus, by analogy with raf-1, phosphorylation of this site may play an important role in the a-raf activation mechanism. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EGFR Signaling |
| + |
PAK1 | up-regulates
phosphorylation
|
ESR1 |
0.549 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-94206 |
Ser305 |
IKRSKKNsLALSLTA |
Homo sapiens |
|
| pmid |
sentence |
| 12374744 |
Pak1 directly phosphorylated the activation function-2 domain of the er at the n-terminal residue ser305, and its mutation to ala (s305a) abolished the pak1-mediated phosphorylation and transactivation functions of the er |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Breast |
| + |
PAK1 | up-regulates
phosphorylation
|
RAF1 |
0.585 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-180808 |
Ser338 |
RPRGQRDsSYYWEIE |
Homo sapiens |
|
| pmid |
sentence |
| 18775988 |
P21-activated protein kinases (paks) are serine/threonine protein kinases that phosphorylate raf-1 at ser-338 and ser-339. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-180812 |
Ser339 |
PRGQRDSsYYWEIEA |
Homo sapiens |
|
| pmid |
sentence |
| 18775988 |
P21-activated protein kinases (paks) are serine/threonine protein kinases that phosphorylate raf-1 at ser-338 and ser-339. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PAK1 | down-regulates activity
phosphorylation
|
HACE1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255537 |
Ser385 |
LMKNKRDsTEITSIL |
Homo sapiens |
Uveal Melanoma Cell |
| pmid |
sentence |
| 29362425 |
Using a proteomic approach, we identified serine 385 as a target of group-I PAK kinases […] We have established in vitro that HACE1 is a direct target of PAK1 kinase activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK1 | up-regulates
phosphorylation
|
CTTN |
0.695 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-165216 |
Ser405 |
KTQTPPVsPAPQPTE |
Homo sapiens |
|
| pmid |
sentence |
| 20444238 |
Strikingly, we find that pak1 phosphorylation of cortactin on serine residues 405 and 418 increases its association with n-wasp. Thus, pak1, by controlling the interaction between cortactin and n-wasp, could regulate the polymerization of actin during clathrin-independent endocytosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-169690 |
Ser405 |
KTQTPPVsPAPQPTE |
Homo sapiens |
|
| pmid |
sentence |
| 21079800 |
Strikingly, we find that pak1 phosphorylation of cortactin on serine residues 405 and 418 increases its association with n-wasp. Thus, pak1, by controlling the interaction between cortactin and n-wasp, could regulate the polymerization of actin during clathrin-independent endocytosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-169694 |
Ser418 |
TEERLPSsPVYEDAA |
Homo sapiens |
|
| pmid |
sentence |
| 21079800 |
Strikingly, we find that pak1 phosphorylation of cortactin on serine residues 405 and 418 increases its association with n-wasp. Thus, pak1, by controlling the interaction between cortactin and n-wasp, could regulate the polymerization of actin during clathrin-independent endocytosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-165220 |
Ser418 |
TEERLPSsPVYEDAA |
Homo sapiens |
|
| pmid |
sentence |
| 20444238 |
Strikingly, we find that pak1 phosphorylation of cortactin on serine residues 405 and 418 increases its association with n-wasp. Thus, pak1, by controlling the interaction between cortactin and n-wasp, could regulate the polymerization of actin during clathrin-independent endocytosis. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| Pathways: | T cell activation |
| + |
PAK1 | up-regulates activity
phosphorylation
|
FXR1 |
0.274 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273713 |
Ser420 |
SERKDELsDWSLAGE |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 20417602 |
Identification of Ser420 in FXR1 as a PAK1 Kinase Target. During zebrafish muscle development, FXR1 Ser420 phosphorylation is needed for protein function. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
PAK1 | up-regulates
phosphorylation
|
PLK1 |
0.534 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178353 |
Ser49 |
EVLVDPRsRRRYVRG |
Homo sapiens |
|
| pmid |
sentence |
| 18427546 |
We show here that pak1 is required for cell proliferation, mitotic progression and plk1 activity in hela cells. phosphorylation of plk1 on ser 49 is important for metaphase-associated events. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK1 | down-regulates
phosphorylation
|
NF2 |
0.631 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-159764 |
Ser518 |
DTDMKRLsMEIEKEK |
Homo sapiens |
|
| pmid |
sentence |
| 18071304 |
Merlin contains a c-terminal serine 518, which is phosphorylated both by p21-activated kinase (pak) and protein kinase a (pka) (shaw et al., 2001;kissil et al., 2002;xiao et al., 2002;alfthan et al., 2004). Phosphorylation at this site is predicted to result in a more open conformation incapable of inhibiting cell growth, |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK1 |
phosphorylation
|
VIM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134520 |
Ser56 |
SRSLYASsPGGVYAT |
Homo sapiens |
|
| pmid |
sentence |
| 15766329 |
In the present study, pak1 was able to phosphorylate vimentin on ser-56 in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Smooth Muscle |
| + |
PPM1F | down-regulates activity
dephosphorylation
|
PAK1 |
0.399 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248530 |
Ser57 |
KKDRFYRsILPGDKT |
Rattus norvegicus |
|
| pmid |
sentence |
| 11864573 |
The p21-activated kinase PAK is negatively regulated by POPX1 and POPX2, a pair of serine/threonine phosphatases of the PP2C family|POPX Can Dephosphorylate and Downregulate PAK| To confirm that POPX2 acts on αPAK phospho-Thr422, a key regulator of activity in the kinase activation loop [9], we used phospho-specific antibodies against αPAK P-Thr422 (Figure 3B, lower panel), which proved to be an excellent substrate for POPX2. Similarly, complete loss of αPAK P-Ser57 with 0.2 μg POPX2 contrasts with the slight loss observed with 1.5 μg PP1. On the basis of these results, we suggest PAK is a substrate of POPX. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248531 |
Thr423 |
PEQSKRStMVGTPYW |
Rattus norvegicus |
|
| pmid |
sentence |
| 11864573 |
The p21-activated kinase PAK is negatively regulated by POPX1 and POPX2, a pair of serine/threonine phosphatases of the PP2C family|POPX Can Dephosphorylate and Downregulate PAK| To confirm that POPX2 acts on αPAK phospho-Thr422, a key regulator of activity in the kinase activation loop [9], we used phospho-specific antibodies against αPAK P-Thr422 (Figure 3B, lower panel), which proved to be an excellent substrate for POPX2. Similarly, complete loss of αPAK P-Ser57 with 0.2 μg POPX2 contrasts with the slight loss observed with 1.5 μg PP1. On the basis of these results, we suggest PAK is a substrate of POPX. |
|
| Publications: |
2 |
Organism: |
Rattus Norvegicus |
| + |
PPM1E | down-regulates activity
dephosphorylation
|
PAK1 |
0.307 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248760 |
Ser57 |
KKDRFYRsILPGDKT |
Rattus norvegicus |
|
| pmid |
sentence |
| 11864573 |
The p21-activated kinase PAK is negatively regulated by POPX1 and POPX2, a pair of serine/threonine phosphatases of the PP2C family|POPX Can Dephosphorylate and Downregulate PAK| To confirm that POPX2 acts on αPAK phospho-Thr422, a key regulator of activity in the kinase activation loop [9], we used phospho-specific antibodies against αPAK P-Thr422 (Figure 3B, lower panel), which proved to be an excellent substrate for POPX2. Similarly, complete loss of αPAK P-Ser57 with 0.2 μg POPX2 contrasts with the slight loss observed with 1.5 μg PP1. On the basis of these results, we suggest PAK is a substrate of POPX. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248761 |
Thr423 |
PEQSKRStMVGTPYW |
Rattus norvegicus |
|
| pmid |
sentence |
| 11864573 |
The p21-activated kinase PAK is negatively regulated by POPX1 and POPX2, a pair of serine/threonine phosphatases of the PP2C family|POPX Can Dephosphorylate and Downregulate PAK| To confirm that POPX2 acts on αPAK phospho-Thr422, a key regulator of activity in the kinase activation loop [9], we used phospho-specific antibodies against αPAK P-Thr422 (Figure 3B, lower panel), which proved to be an excellent substrate for POPX2. Similarly, complete loss of αPAK P-Ser57 with 0.2 μg POPX2 contrasts with the slight loss observed with 1.5 μg PP1. On the basis of these results, we suggest PAK is a substrate of POPX. |
|
| Publications: |
2 |
Organism: |
Rattus Norvegicus |
| + |
PAK1 | up-regulates activity
phosphorylation
|
SYN1 |
0.356 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250235 |
Ser605 |
AGPTRQAsQAGPVPR |
Rattus norvegicus |
PC-12 Cell |
| pmid |
sentence |
| 12237306 |
Synapsin I is phosphorylated at Ser603 by p21-activated kinases. the Ser603 residue must be one of the pivotal sites for the release |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PAK1 | up-regulates activity
phosphorylation
|
MAP3K1 |
0.519 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236006 |
Ser67 |
RQLRKVRsVELDQLP |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12228228 |
We found that pak1 phosphorylated mekk1 on serine 67 of its amino-terminal regulatory domain. mekk1 activity was increased modestly following pak phosphorylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EGFR Signaling, Toll like receptors |
| + |
PAK1 | up-regulates
phosphorylation
|
CTNNB1 |
0.539 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-175944 |
Ser675 |
QDYKKRLsVELTSSL |
Homo sapiens |
|
| pmid |
sentence |
| 21822311 |
Pak1 directly phosphorylates _-catenin proteins at ser675 site and this leads to more stable and transcriptional active _-catenin |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK1 | up-regulates activity
phosphorylation
|
MORC2 |
0.373 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273714 |
Ser739 |
ATPSRKRsVAVSDEE |
Homo sapiens |
BGC-823 Cell |
| pmid |
sentence |
| 25888627 |
We demonstrate that PAK1-mediated MORC2 phosphorylation promotes cell cycle progression, defective phosphorylation of MORC2-S677A results in attenuated cell proliferation and tumorigenicity of gastric cancer cells, which is significantly enhanced in overexpression of phospho-mimic MORC2-S677E form, suggesting the importance of MORC2 phosphorylation in tumorigenesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK1 | down-regulates
phosphorylation
|
BAD |
0.341 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-177271 |
Ser74 |
VEIRSRHsSYPAGTE |
Homo sapiens |
|
| pmid |
sentence |
| 22096607 |
Bad is a pro-apoptotic member of the bcl-2 family of proteins, which can be phosphorylated on numerous sites to modulate binding to bcl-2 and 14-3-3 proteins and inhibit its pro-apoptotic activities. Together, these findings demonstrate that pak1 phosphorylates bad directly at s111, but phosphorylated s112 through raf-1. These two sites of bad serve as redundant regulatory sites for bcl-2 binding |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-73529 |
Ser75 |
EIRSRHSsYPAGTED |
Homo sapiens |
|
| pmid |
sentence |
| 10611223 |
Pak phosphorylates bad in vitro and in vivo on ser112 and ser136, resulting in a markedly reduced interaction between bad and bcl-2 or bcl-x(l) and the increased association of bad with 14-3-3tau. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-73533 |
Ser99 |
PFRGRSRsAPPNLWA |
Homo sapiens |
|
| pmid |
sentence |
| 10611223 |
Pak phosphorylates bad in vitro and in vivo on ser112 and ser136, resulting in a markedly reduced interaction between bad and bcl-2 or bcl-x(l) and the increased association of bad with 14-3-3tau. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PAK1 | down-regulates activity
phosphorylation
|
SORT1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273718 |
Ser793 |
RFLVHRYsVLQQHAE |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 31767632 |
PAKs specifically phosphorylate Ser15 of the sortilin-cd and alter its trafficking. It can be concluded that PAK1-3 may indeed instigate the phosphorylation of sortilin and that they target a single serine residue (Ser15) located in the kinase domain-binding site of the sortilin-cd. Full-length sortilins with the serine at position 793 (residue 15 in the cytoplasmic domain) (for the sequence, see Fig. 2). Phosphorylation (Ser15) downregulates the sortilin–AP-1 interaction. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK1 | down-regulates
phosphorylation
|
DYNLL1 |
0.386 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-159995 |
Ser88 |
VAILLFKsG |
Homo sapiens |
|
| pmid |
sentence |
| 18084006 |
Dlc1 phosphorylation on ser(88) by p21-activated kinase 1 (pak1), a signaling nodule, promotes mammalian cell survival by regulating its interaction with bim and the stability of bim. Here we discovered that phosphorylation of ser(88), which juxtapose each other at the interface of the dlc dimer, disrupts dlc1 dimer formation and consequently impairs its interaction with bim |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Breast |
| + |
PAK1 | down-regulates
phosphorylation
|
ARHGEF2 |
0.36 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187573 |
Ser886 |
PVDPRRRsLPAGDAL |
Homo sapiens |
|
| pmid |
sentence |
| 19667072 |
We identify gef-h1 as a binding target and substrate for p21-activated kinase 1 (pak1), we show that phosphorylation of gef-h1 at ser(885) by pak1 induces 14-3-3 binding to the exchange factor and relocation of 14-3-3 to microtubules. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK1 | up-regulates quantity by stabilization
phosphorylation
|
ATG5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275835 |
Thr101 |
SALPWNItVHFKSFP |
|
|
| pmid |
sentence |
| 36528756 |
Here, we identified USP13 as an essential deubiquitinase that stabilizes ATG5 in a process that depends on the PAK1 serine/threonine-protein kinase and which enhances autophagy and promotes IM resistance in GIST cells. |As PAK1-mediated phosphorylation at residue T101 protects ATG5 from ubiquitination-dependent degradation |
|
| Publications: |
1 |
| + |
STK11 | down-regulates
phosphorylation
|
PAK1 |
0.249 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164814 |
Thr109 |
QWARLLQtSNITKSE |
Homo sapiens |
|
| pmid |
sentence |
| 20400510 |
Lkb1 suppresses p21-activated kinase-1 (pak1) by phosphorylation of thr109 in the p21-binding domain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK1 | up-regulates
phosphorylation
|
ARPC1B |
0.545 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121642 |
Thr21 |
HAWNKDRtQIAICPN |
Homo sapiens |
|
| pmid |
sentence |
| 14749719 |
The formation of new branched actin filament networks at the cell cortex of migrating cells is choreographed by the actin-related protein (arp) 2/3 complex. Despite the fundamental role of the arp2/3 complex in actin nucleation and branching, upstream signals that control the functions of p41-arc, a putative regulatory component of the mammalian arp2/3 complex. Pak1 phosphorylation of p41-arc regulates its localization with the arp2/3 complex in the cortical nucleation regions of cells. Pak1 phosphorylates p41-arc on threonine 21 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK1 | down-regulates activity
phosphorylation
|
PAK1 |
0.412 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249432 |
Thr212 |
VIEPLPVtPTRDVAT |
Rattus norvegicus |
Smooth Muscle |
| pmid |
sentence |
| 15542607 |
We also show that ERK2 phosphorylates PAK1 on Thr(212) in vitro and that Thr(212) is phosphorylated in smooth muscle cells following PDGF-BB treatment in an adhesion- and MEK/ERK-dependent fashion. Expression of a phosphomimic variant, PAK-T212E, does not alter ERK association, but markedly attenuates downstream ERK signaling. Taken together, these data suggest that PAK1 may facilitate ERK signaling by serving as a scaffold to recruit Raf, MEK, and ERK to adhesion complexes, and that subsequent growth factor-stimulated phosphorylation of PAK-Thr(212) by ERK may serve to provide a negative feedback signal |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
CDK5 | down-regulates activity
phosphorylation
|
PAK1 |
0.521 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249328 |
Thr212 |
VIEPLPVtPTRDVAT |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 11604394 |
Our previous work revealed that the neuronal p35/Cdk5 kinase associates with Pak1 in a RacGTP-dependent manner, causing hyperphosphorylation and down-regulation of Pak1 kinase activity. We have now demonstrated direct phosphorylation of Pak1 on threonine 212 by the p35/Cdk5 kinase. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
PAK1 | up-regulates
phosphorylation
|
PA2G4 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160963 |
Thr261 |
QYGLKMKtSRAFFSE |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 18283314 |
We found that pak1 phosphorylated ebp1 in vitro and mapped the phosphorylation site to threonine 261. these studies demonstrate for the first time that ebp1 is a substrate of pak1 and the importance of the pak1 phosphorylation site for the functional activity of ebp1 in breast cancer cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK1 | up-regulates
phosphorylation
|
AURKA |
0.393 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-205110 |
Thr288 |
APSSRRTtLCGTLDY |
Homo sapiens |
|
| pmid |
sentence |
| 24867643 |
The upstream pak1 kinase can phosphorylate aurora a at t288, autophosphorylation appears to be the essential mode of activation. Our experiments suggest that phosphorylation of t288 is important for regulation of the aurora2 kinase both for its activity and its stability |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK3 | down-regulates
phosphorylation
|
PAK1 |
0.343 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-123074 |
Thr292 |
YTAMDVAtGQEVAIK |
Homo sapiens |
|
| pmid |
sentence |
| 14993270 |
Activated erk can phosphorylate t292 in the prs, and this blocks the ability of pak to phosphorylate s298 and of rac-pak signaling to enhance mek1-erk complex formation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PDPK1 | up-regulates activity
phosphorylation
|
PAK1 |
0.364 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250267 |
Thr423 |
PEQSKRStMVGTPYW |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 10995762 |
P21-activated kinase (PAK1) is phosphorylated and activated by 3-phosphoinositide-dependent kinase-1 (PDK1). We identify threonine 423, a conserved threonine in the activation loop of kinase subdomain VIII, as the PDK1 phosphorylation site on PAK1. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| Pathways: | EGFR Signaling, T cell activation |
| + |
PAK1 | up-regulates
phosphorylation
|
PGM1 |
0.35 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-127135 |
Thr467 |
SANDKVYtVEKADNF |
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 15378030 |
The signaling kinase p21-activated kinase 1 (pak1) binds to, phosphorylates and enhances the enzymatic activity of phosphoglucomutase 1 (pgm), |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK1 | up-regulates activity
phosphorylation
|
LIMK1 |
0.598 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-72142 |
Thr508 |
PDRKKRYtVVGNPYW |
Homo sapiens |
|
| pmid |
sentence |
| 10559936 |
Activation of lim-kinase by pak1 couplesp21-activated kinase (pak1) phosphorylates lim-kinase at threonine residue 508 within lim-kinase's activation loop |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK1 | up-regulates activity
phosphorylation
|
NLRP3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277547 |
Thr659 |
KIEINLStRMDHMVS |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 33432150 |
Pak1 phosphorylates NLRP3 to promote inflammasome activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
OXSR1 | down-regulates activity
phosphorylation
|
PAK1 |
0.39 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250210 |
Thr84 |
LPSDFEHtIHVGFDA |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 14707132 |
OSR1 phosphorylated threonine 84 in the N-terminal regulatory domain of PAK1. phosphorylation of PAK1 by OSR1 desensitizes PAK1 to activation by small G proteins, providing a modulatory input to PAK1 activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERK1/2 | down-regulates
phosphorylation
|
PAK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270186 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14993270 |
Activated erk can phosphorylate t292 in the prs, and this blocks the ability of pak to phosphorylate s298 and of rac-pak signaling to enhance mek1-erk complex formation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EGFR Signaling, T cell activation, Toll like receptors |
| + |
NCK1 | up-regulates
binding
|
PAK1 |
0.697 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235947 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11157752 |
Both nck and grb4 proteins could associate with receptor tyrosine kinases and the sh3-binding proteins pak, sos1, and prk2, and they synergized with v-abl and sos to induce gene expression via the transcription factor elk-1. Association of nck with pak1 may serve to link this important regulatory kinase to cell activation by growth factor receptors. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236324 |
|
|
Chlorocebus aethiops |
|
| pmid |
sentence |
| 8824201 |
We describe here a specific interaction of the Nck adapter molecule with PAK1 both in vitro and in vivo. Association of Nck with PAK1 may serve to link this important regulatory kinase to cell activation by growth factor receptors. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, Chlorocebus Aethiops |
| Pathways: | EGFR Signaling, T cell activation |
| + |
PAK1 | down-regulates
phosphorylation
|
WEE1 |
0.304 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-123528 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15037762 |
Kinases targeted sequentially to the neck, cla4/pak and cdc5/polo, are responsible for stepwise phosphorylation and down-regulation of swe1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPM1F | down-regulates
dephosphorylation
|
PAK1 |
0.399 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-162146 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20016286 |
Pop x2, a pp 2c serine/threonine phosphatase, is known to dephosphorylate pak and downregulate its activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDC42 | up-regulates activity
binding
|
PAK1 |
0.941 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248243 |
|
|
Mus musculus |
Brain |
| pmid |
sentence |
| 8107774 |
A new brain serine/threonine protein kinase may be a target for the p21ras-related proteins Cdc42 and Rac1. The kinase sequence is related to that of the yeast protein STE20, implicated in pheromone-response pathways. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
Gbeta | down-regulates
phosphorylation
|
PAK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270086 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14993270 |
Activated erk can phosphorylate t292 in the prs, and this blocks the ability of pak to phosphorylate s298 and of rac-pak signaling to enhance mek1-erk complex formation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RAC2 | up-regulates
binding
|
PAK1 |
0.774 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-59546 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9705280 |
This report shows that rac1 binds to and stimulates the kinase activity of pak1 approximately 2- and 4-5-fold, respectively, better than rac2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NCK1 | up-regulates activity
binding
|
PAK1 |
0.697 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236512 |
|
|
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 10026169 |
Both nck and grb4 proteins could associate with receptor tyrosine kinases and the sh3-binding proteins pak, sos1, and prk2, and they synergized with v-abl and sos to induce gene expression via the transcription factor elk-1. Association of nck with pak1 may serve to link this important regulatory kinase to cell activation by growth factor receptors. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | EGFR Signaling, T cell activation |
| + |
PAK1 | up-regulates 
|
F-actin_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277768 |
|
|
Homo sapiens |
Prostate Cancer Cell Line |
| pmid |
sentence |
| 29572236 |
RAC1 activation induces the actin remodeling and membrane ruffling necessary to form macropinosomes by activating PAK kinases |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | T cell activation |
| + |
CRIPAK | up-regulates
binding
|
PAK1 |
0.425 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141467 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 16278681 |
We further found that cripak interacted with pak1 through the n-terminal regulatory domain and inhibited pak1 kinase in both in vitro and in vivo assays. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Breast |
| + |
PAK1 |
phosphorylation
|
Histone H3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265363 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12151336 |
Histone h3 is a substrate of pak1 both in vitro and in vivo, and it specifically interacted with pak1 but not pak2 or pak3. Site-directed mutagenesis indicated that pak1 phosphorylates histone h3 on ser10. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK1 | down-regulates activity
phosphorylation
|
MYLK |
0.538 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250317 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 10092231 |
P21-activated kinase 1 (PAK1) phosphorylates MLCK, resulting in decreased MLCK activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK1 | down-regulates
phosphorylation
|
PGAM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270283 |
|
|
Homo sapiens |
Neutrophil |
| pmid |
sentence |
| 12189148 |
Activated pak1 inhibits glycolysis by association of its catalytic domain with pgam-b and subsequent phosphorylation of the enzyme on serine residues 23 and 118, thereby abolishing pgam activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK1 | up-regulates activity
phosphorylation
|
MEK1/2 |
0.564 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244924 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12876277 |
We find that adhesion to fibronectin induces pak1-dependent phosphorylation of mek1 on s298 and that this phosphorylation is necessary for efficient activation of mek1 and subsequent mapk activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EGFR Signaling, T cell activation, Toll like receptors |
| + |
PAK1 | down-regulates activity
phosphorylation
|
BCL6 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253930 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22723377 |
The transcriptional repressor B-cell lymphoma (BCL)-6 downregulates genes involved in cell-cycle progression and becomes inactivated following phosphorylation by the Rac1 GTPase-activated protein kinase PAK1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RAC1 | up-regulates activity
binding
|
PAK1 |
0.782 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248236 |
|
|
Mus musculus |
Brain |
| pmid |
sentence |
| 8107774 |
A new brain serine/threonine protein kinase may be a target for the p21ras-related proteins Cdc42 and Rac1. The kinase sequence is related to that of the yeast protein STE20, implicated in pheromone-response pathways. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PAK1 | down-regulates activity
binding
|
PAK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236338 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11804587 |
We show that pak1 forms homodimers in vivo and that its dimerization is regulated by the intracellular level of gtp-cdc42 or gtp-rac1. The dimerized pak1 adopts a trans-inhibited conformation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EGFR Signaling, T cell activation, Toll like receptors |
3.0
PAK1
- 
- 