Relation Results

Identifier	Residue	Sequence	Organism
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
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

Identifier	Residue	Sequence	Organism
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

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

Identifier	Residue	Sequence	Organism
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
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

Identifier	Residue	Sequence	Organism
SIGNOR-280237	Ser118	QVKIWRRsFDIPPPP	Homo sapiens
pmid	sentence
24567357	The ability of Pak1 to phosphorylate wild-type PGAM2 was increased after exposure of the cells to etoposide (XREF_FIG).\|Bar, 20 \u00b5m. (E) Primary mouse embryonic fibroblasts at early passages were treated with 20 \u00b5M etoposide in the presence of 20 \u00b5M MG132, and cell lysates were immunoblotted with antibodies against Pak1 and phospho-Ser118 in phosphoglycerate mutase as indicated. (F) Pak1 kinase phosphorylates PGAM2 at Ser118 in vitro.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-91602	Ser118	QVKIWRRsYDVPPPP	Homo sapiens
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-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
SIGNOR-91606	Ser23	WNLENRFsGWYDADL	Homo sapiens
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:

4

Organism:

Homo Sapiens

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

Identifier	Residue	Sequence	Organism
SIGNOR-279418	Ser133	DVLEFYNsKKTSNSQ	Homo sapiens
pmid	sentence
30664689	Although, MLK3 can phosphorylate PAK1 on Ser133 and Ser204 sites, PAK1S133A mutant is constitutively active, whereas, PAK1S204A is not activated by MLK3.\|MLK3 was able to directly phosphorylate PAK1 on two Serine residues of which Ser204 is critical for MLK3-induced PAK1 activation and downstream functions.

Identifier	Residue	Sequence	Organism
SIGNOR-279417	Ser204	TKSVYTRsVIEPLPV	Homo sapiens
pmid	sentence
30664689	Although, MLK3 can phosphorylate PAK1 on Ser133 and Ser204 sites, PAK1S133A mutant is constitutively active, whereas, PAK1S204A is not activated by MLK3.\|MLK3 was able to directly phosphorylate PAK1 on two Serine residues of which Ser204 is critical for MLK3-induced PAK1 activation and downstream functions.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-279378	Ser135	APPAPAAsPAASSRP	Homo sapiens
pmid	sentence
33704464	In this article, we found that Ser-135 and Thr-180 of RPA1 are directly phosphorylated by PAK1 in a DOCK7-Rac1/Cdc42-dependent manner.\|We further explored the biological role of PAK1 in replication stress and found that depletion of PAK1 resulted in decreased RPA1 and RPA2 chromatin loading and RPA2 foci formation ( Figure 4I-K ) .

Identifier	Residue	Sequence	Organism
SIGNOR-279379	Thr180	LSHTSGGtQSKVVPI	Homo sapiens
pmid	sentence
33704464	In this article, we found that Ser-135 and Thr-180 of RPA1 are directly phosphorylated by PAK1 in a DOCK7-Rac1/Cdc42-dependent manner.\|We further explored the biological role of PAK1 in replication stress and found that depletion of PAK1 resulted in decreased RPA1 and RPA2 chromatin loading and RPA2 foci formation ( Figure 4I-K ) .

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
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
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
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

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence	Organism
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
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

Identifier	Residue	Sequence	Organism
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.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence
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

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence
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

Identifier	Residue	Sequence
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

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence	Organism
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
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
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

Identifier	Residue	Sequence	Organism
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
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
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

Identifier	Residue	Sequence	Organism
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
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
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

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

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence	Organism
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
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

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

Identifier	Residue	Sequence	Organism
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

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

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

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

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence	Organism
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
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

Identifier	Residue	Sequence	Organism
SIGNOR-278968	Ser3486	QPAPKQDsSPHLTSQ	Homo sapiens
pmid	sentence
15824732	Pak1 phosphorylation sites in SHARP were mapped to Ser3486 and Thr3568 within the SHARP repression domain.

Publications:

1

Organism:

Homo Sapiens

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

Identifier	Residue	Sequence	Organism
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
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
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.

Identifier	Residue	Sequence	Organism
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.

Publications:

4

Organism:

Homo Sapiens

Pathways:

T cell activation

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

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence	Organism
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
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

Identifier	Residue	Sequence	Organism
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
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

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

Identifier	Residue	Sequence	Organism
SIGNOR-279377	Ser62	FGPARNDsVIVADQT	Homo sapiens
pmid	sentence
28918037	Overall, our results unequivocally confirmed that Pak1 physically interacts with ATF2 and phosphorylates ATF2 on the Ser62 residue, and this process secludes ATF2 in the cytoplasm.

Publications:

1

Organism:

Homo Sapiens

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

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence	Organism
SIGNOR-278414	Ser739	ATPSRKRsVAVSDEE	Homo sapiens
pmid	sentence
23260667	In support of this notion, selective knockdown of endogenous PAK1 significantly reduced the association of MORC2 with chromatin (XREF_FIG, compare lane 4 with 3).\|PAK1 phosphorylation of MORC2 on serine 739 regulates an ATPase-dependent chromatin remodeling following DSB damage and facilitates efficient DSB repair.

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:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
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
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
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

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

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence
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

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence	Organism
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

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

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

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

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence	Organism
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

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

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

Identifier	Residue	Sequence	Organism
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

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.

Identifier	Residue	Organism
SIGNOR-278967		Homo sapiens
pmid	sentence
33432150	Pak1 phosphorylates NLRP3 and triggers inflammasome activation.

Publications:

2

Organism:

Homo Sapiens

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

Identifier	Residue	Sequence	Organism
SIGNOR-278398	Tyr153	TDKSAEDyNSSNALN	Homo sapiens
pmid	sentence
26944939	Etk kinase directly phosphorylates and activates PAK1 in response to estrogen.\|We demonstrated that estrogen-activated Etk directly phosphorylated PAK1 on Tyr153.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
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

Identifier	Residue	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

Identifier	Residue	Organism
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

Identifier	Residue	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

Identifier	Residue	Organism
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

Identifier	Residue	Organism
SIGNOR-279307		Homo sapiens
pmid	sentence
32421151	Pak1 phosphorylates the N-terminus of Mid1 to promote its association with cortical nodes.\|Pak1 promotes Mid1 localization to cortical nodes.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	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

Identifier	Residue	Organism
SIGNOR-279244		Homo sapiens
pmid	sentence
29780159	Taken together, our data demonstrate that PAK1 interacts with STIM1 and phosphorylates specific STIM1 cytosolic domains.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
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	Organism
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

Identifier	Residue	Organism
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

Identifier	Residue	Organism
SIGNOR-280054		Homo sapiens
pmid	sentence
15684429	PAK1 negatively regulates the activity of the Rho exchange factor NET1.\|Specifically, PAK1 phosphorylates NET1 on three sites in vitro : serines 152, 153, and 538.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	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.

Identifier	Residue	Organism
SIGNOR-270282		Homo sapiens
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

Identifier	Residue	Organism
SIGNOR-279243		Homo sapiens
pmid	sentence
25766321	(a) PAK1 phosphorylates RUFY3 in vitro.\|Taken together, these results indicate that PAK1 can upregulate RUFY3 protein expression.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
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

Identifier	Residue	Organism
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

Identifier	Residue	Organism
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

Identifier	Residue	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

Identifier	Residue	Organism
SIGNOR-279242		Homo sapiens
pmid	sentence
12560069	Pak1 efficiently phosphorylated GST-FKHR.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-278449		Homo sapiens
pmid	sentence
22105346	The Rac effector PAK1 was also transiently activated upon cell-cell adhesion and directly phosphorylated Ajuba (Thr172).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	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

Identifier	Residue	Organism
SIGNOR-280053		Homo sapiens
pmid	sentence
25860930	It has been shown that PAK1 phosphorylates and activates MLC2, leading to cell motility [ xref ].

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
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

Identifier	Residue	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

Identifier	Residue	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

Name	PAK1 View Modifications
Full Name	Serine/threonine-protein kinase PAK 1
Synonyms	Alpha-PAK, p21-activated kinase 1, PAK-1, p65-PAK
Primary ID	Q13153
Links	- -
Type	protein
Relations	119
Pathways	EGFR Signaling, Macropinocytosis , T cell activation
Function	Protein kinase involved in intracellular signaling pathways downstream of integrins and receptor-type kinases that plays an important role in cytoskeleton dynamics, in cell adhesion, migration, proliferation, apoptosis, mitosis, and in vesicle-mediated transport processes (PubMed:30290153). Can directly phosphorylate BAD and protects cells against apoptosis. Activated by interaction with CDC42 and RAC1. Functions as GTPase effector that links the Rho-related GTPases CDC42 and RAC1 to the JNK MAP kinase pathway. Phosphorylates and activates MAP2K1, and thereby mediates activation of downstream MAP kinases. Involved in the reorganization of the actin cytoskeleton, actin stress fibers and of focal adhesion complexes. Phosphorylates the tubulin chaperone TBCB and thereby plays a role in the regulation of microtubule biogenesis and organization of the tubulin cytoskeleton. Plays a role in the regulation of insulin secretion in response to elevated glucose levels. Part of a ternary complex that contains PAK1, DVL1 and MUSK that is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ). Activity is inhibited in cells undergoing apoptosis, potentially due to binding of CDC2L1 and CDC2L2. Phosphorylates MYL9/MLC2. Phosphorylates RAF1 at 'Ser-338' and 'Ser-339' resulting in

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