| + |
PAK2 | down-regulates activity 
phosphorylation
|
PREX2 |
0.365 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277182 |
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 |
| + |
PAK2 | down-regulates activity
phosphorylation
|
MYLK |
0.516 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250222 |
Ser1208 |
MKSRRPKsSLPPVLG |
in vitro |
|
| pmid |
sentence |
| 10748018 |
PAK2 can directly phosphorylate MLCK, inhibiting its activity and limiting the development of isometric tension. PAK2 catalyzes MLCK phosphorylation on serine residues 439 and 991. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250223 |
Ser1760 |
RAIGRLSsMAMISGL |
in vitro |
|
| pmid |
sentence |
| 10748018 |
PAK2 can directly phosphorylate MLCK, inhibiting its activity and limiting the development of isometric tension. PAK2 catalyzes MLCK phosphorylation on serine residues 439 and 991. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PAK2 | up-regulates activity 
phosphorylation
|
PAK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250228 |
Ser141 |
TVKQKYLsFTPPEKD |
in vitro |
|
| pmid |
sentence |
| 10075701 |
Eight autophosphorylation sites were identified in Cdc42-activated gamma-PAK, six of which are in common with those previously reported in alpha-PAK, while Ser-19 and Ser-165 appear to be uniquely phosphorylated in the gamma-form. Further, the phosphorylation of Ser-141, Ser-165, and Thr-402 was found to correlate with gamma-PAK activation. Autophosphorylation of γ-PAK with MgATP alone takes place at Ser-19, Ser-20, Ser-55, Ser-192, and Ser-197. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250224 |
Ser19 |
PAPPVRMsSTIFSTG |
in vitro |
|
| pmid |
sentence |
| 10075701 |
Eight autophosphorylation sites were identified in Cdc42-activated gamma-PAK, six of which are in common with those previously reported in alpha-PAK, while Ser-19 and Ser-165 appear to be uniquely phosphorylated in the gamma-form. Further, the phosphorylation of Ser-141, Ser-165, and Thr-402 was found to correlate with gamma-PAK activation. The information resulting from manual Edman degradation and from automated sequencing clearly identified Ser-192, Ser-197, and Thr-402 as the phosphorylation sites |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250225 |
Ser192 |
PRPDHTKsIYTRSVI |
in vitro |
|
| pmid |
sentence |
| 10075701 |
Eight autophosphorylation sites were identified in Cdc42-activated gamma-PAK, six of which are in common with those previously reported in alpha-PAK, while Ser-19 and Ser-165 appear to be uniquely phosphorylated in the gamma-form. Further, the phosphorylation of Ser-141, Ser-165, and Thr-402 was found to correlate with gamma-PAK activation. The information resulting from manual Edman degradation and from automated sequencing clearly identified Ser-192, Ser-197, and Thr-402 as the phosphorylation sites |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250226 |
Ser197 |
TKSIYTRsVIDPVPA |
in vitro |
|
| pmid |
sentence |
| 10075701 |
Eight autophosphorylation sites were identified in Cdc42-activated gamma-PAK, six of which are in common with those previously reported in alpha-PAK, while Ser-19 and Ser-165 appear to be uniquely phosphorylated in the gamma-form. Further, the phosphorylation of Ser-141, Ser-165, and Thr-402 was found to correlate with gamma-PAK activation. The information resulting from manual Edman degradation and from automated sequencing clearly identified Ser-192, Ser-197, and Thr-402 as the phosphorylation sites |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250227 |
Ser20 |
APPVRMSsTIFSTGG |
in vitro |
|
| pmid |
sentence |
| 10075701 |
Eight autophosphorylation sites were identified in Cdc42-activated gamma-PAK, six of which are in common with those previously reported in alpha-PAK, while Ser-19 and Ser-165 appear to be uniquely phosphorylated in the gamma-form. Further, the phosphorylation of Ser-141, Ser-165, and Thr-402 was found to correlate with gamma-PAK activation. Autophosphorylation of γ-PAK with MgATP alone takes place at Ser-19, Ser-20, Ser-55, Ser-192, and Ser-197. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250229 |
Ser55 |
KPRHKIIsIFSGTEK |
in vitro |
|
| pmid |
sentence |
| 10075701 |
Eight autophosphorylation sites were identified in Cdc42-activated gamma-PAK, six of which are in common with those previously reported in alpha-PAK, while Ser-19 and Ser-165 appear to be uniquely phosphorylated in the gamma-form. Further, the phosphorylation of Ser-141, Ser-165, and Thr-402 was found to correlate with gamma-PAK activation. Autophosphorylation of γ-PAK with MgATP alone takes place at Ser-19, Ser-20, Ser-55, Ser-192, and Ser-197. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250230 |
Thr402 |
PEQSKRStMVGTPYW |
in vitro |
|
| pmid |
sentence |
| 10075701 |
Eight autophosphorylation sites were identified in Cdc42-activated gamma-PAK, six of which are in common with those previously reported in alpha-PAK, while Ser-19 and Ser-165 appear to be uniquely phosphorylated in the gamma-form. Further, the phosphorylation of Ser-141, Ser-165, and Thr-402 was found to correlate with gamma-PAK activation. The information resulting from manual Edman degradation and from automated sequencing clearly identified Ser-192, Ser-197, and Thr-402 as the phosphorylation sites |
|
| Publications: |
7 |
Organism: |
In Vitro |
| + |
PAK2 | up-regulates
phosphorylation
|
PAK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-140907 |
Ser141 |
TVKQKYLsFTPPEKD |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16204230 |
Pak2 is autophosphorylated at eight sites;ser-141 and ser-165 in the regulatory domain and thr-402 in the activation loop are identified as key sites in activation of the protein kinase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-147874 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16837009 |
A dimeric kinase assembly underlying autophosphorylation in the p21 activated kinasesa key step in the activation process is the phosphorylation of the activation loop of one pak kinase domain by another, but little is known about the underlying recognition events that make this phosphorylation specific. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PAK2 | up-regulates activity
phosphorylation
|
MYL12A |
0.477 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263020 |
Ser19 |
KRPQRATsNVFAMFD |
in vitro |
|
| pmid |
sentence |
| 10047984 |
In this study we report that gamma-PAK, which is activated by the GTP-binding proteins Cdc42 and Rac, catalyses phosphorylation of intact non-muscle myosin II and isolated recombinant RLC. Phosphopeptide maps and phosphoamino acid analysis revealed that gamma-PAK phosphorylates Ser-19 but does not phosphorylate Thr-18.Taken together, these data suggest that myosin II activation by the p21-activated family of kinases may be physiologically important in regulating cytoskeletal organization. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKAA2 |
phosphorylation
|
PAK2 |
0.244 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-195110 |
Ser20 |
APPVRMSsTIFSTGG |
Homo sapiens |
|
| pmid |
sentence |
| 22137581 |
Together, these results indicate that ampk phosphorylates endogenous ppp1r12c at s452 and pak2 at s20 in human cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AMPK |
phosphorylation
|
PAK2 |
0.244 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216612 |
Ser20 |
APPVRMSsTIFSTGG |
Homo sapiens |
|
| pmid |
sentence |
| 22137581 |
Together, these results indicate that ampk phosphorylates endogenous ppp1r12c at s452 and pak2 at s20 in human cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK2 | up-regulates
phosphorylation
|
PRL |
0.344 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186211 |
Ser207 |
LHCLRRDsHKIDNYL |
Homo sapiens |
|
| pmid |
sentence |
| 19555049 |
Phosphorylated form of prolactin has a higher affinity for heparin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK2 |
phosphorylation
|
RPS6 |
0.312 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250231 |
Ser235 |
IAKRRRLsSLRASTS |
in vitro |
|
| pmid |
sentence |
| 1985906 |
The synthetic peptide AKRRRLSSLRASTSKSESSQK (S6-21) which corresponds to the carboxyl-terminal 21 amino acids of human ribosomal protein S6 was synthesized and tested as a substrate for S6/H4 kinase purified from human placenta. The principal phosphorylation sites were serines in the acidic carboxyl-terminal domain of the peptide. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250232 |
Ser236 |
AKRRRLSsLRASTSK |
in vitro |
|
| pmid |
sentence |
| 1985906 |
The synthetic peptide AKRRRLSSLRASTSKSESSQK (S6-21) which corresponds to the carboxyl-terminal 21 amino acids of human ribosomal protein S6 was synthesized and tested as a substrate for S6/H4 kinase purified from human placenta. The principal phosphorylation sites were serines in the acidic carboxyl-terminal domain of the peptide. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250233 |
Ser240 |
RLSSLRAsTSKSESS |
in vitro |
|
| pmid |
sentence |
| 1985906 |
The synthetic peptide AKRRRLSSLRASTSKSESSQK (S6-21) which corresponds to the carboxyl-terminal 21 amino acids of human ribosomal protein S6 was synthesized and tested as a substrate for S6/H4 kinase purified from human placenta. The principal phosphorylation sites were serines in the acidic carboxyl-terminal domain of the peptide. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250234 |
Ser242 |
SSLRASTsKSESSQK |
in vitro |
|
| pmid |
sentence |
| 1985906 |
The synthetic peptide AKRRRLSSLRASTSKSESSQK (S6-21) which corresponds to the carboxyl-terminal 21 amino acids of human ribosomal protein S6 was synthesized and tested as a substrate for S6/H4 kinase purified from human placenta. The principal phosphorylation sites were serines in the acidic carboxyl-terminal domain of the peptide. |
|
| Publications: |
4 |
Organism: |
In Vitro |
| + |
PAK2 | down-regulates
phosphorylation
|
CASP7 |
0.356 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173655 |
Ser239 |
WRSPGRGsWFVQALC |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 21555521 |
Pak2 can bind with caspase-7 and phosphorylate caspase-7 at the ser-30, thr-173, and ser-239 sites. Functionally, the phosphorylation of caspase-7 decreases its activity, thereby inhibiting cellular apoptosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173659 |
Ser30 |
DAKPDRSsFVPSLFS |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 21555521 |
Pak2 can bind with caspase-7 and phosphorylate caspase-7 at the ser-30, thr-173, and ser-239 sites. Functionally, the phosphorylation of caspase-7 decreases its activity, thereby inhibiting cellular apoptosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173663 |
Thr173 |
FRGDRCKtLLEKPKL |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 21555521 |
Pak2 can bind with caspase-7 and phosphorylate caspase-7 at the ser-30, thr-173, and ser-239 sites. Functionally, the phosphorylation of caspase-7 decreases its activity, thereby inhibiting cellular apoptosis. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PAK2 | down-regulates activity
phosphorylation
|
VIM |
0.31 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250237 |
Ser26 |
GTASRPSsSRSYVTT |
in vitro |
|
| pmid |
sentence |
| 11895474 |
In vitro analyses revealed that vimentin served as an excellent substrate for PAK. This phosphorylated vimentin lost the potential to form 10 nm filaments. We identified Ser25, Ser38, Ser50, Ser65 and Ser72 in the amino-terminal head domain as the major phosphorylation sites on vimentin for PAK. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250239 |
Ser39 |
TTSTRTYsLGSALRP |
in vitro |
|
| pmid |
sentence |
| 11895474 |
In vitro analyses revealed that vimentin served as an excellent substrate for PAK. This phosphorylated vimentin lost the potential to form 10 nm filaments. We identified Ser25, Ser38, Ser50, Ser65 and Ser72 in the amino-terminal head domain as the major phosphorylation sites on vimentin for PAK.  |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250241 |
Ser66 |
GVYATRSsAVRLRSS |
in vitro |
|
| pmid |
sentence |
| 11895474 |
In vitro analyses revealed that vimentin served as an excellent substrate for PAK. This phosphorylated vimentin lost the potential to form 10 nm filaments. We identified Ser25, Ser38, Ser50, Ser65 and Ser72 in the amino-terminal head domain as the major phosphorylation sites on vimentin for PAK. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250243 |
Ser73 |
SAVRLRSsVPGVRLL |
in vitro |
|
| pmid |
sentence |
| 11895474 |
In vitro analyses revealed that vimentin served as an excellent substrate for PAK. This phosphorylated vimentin lost the potential to form 10 nm filaments. We identified Ser25, Ser38, Ser50, Ser65 and Ser72 in the amino-terminal head domain as the major phosphorylation sites on vimentin for PAK. |
|
| Publications: |
4 |
Organism: |
In Vitro |
| + |
PAK2 | down-regulates activity
phosphorylation
|
MKNK1 |
0.428 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250221 |
Ser39 |
RRGRATDsLPGKFED |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15234964 |
Phosphorylation of Mnk1 by caspase-activated Pak2/gamma-PAK inhibits phosphorylation and interaction of eIF4G with Mnk. When 293T cells are subjected to apoptotic induction by hydrogen peroxide, Mnk1 is phosphorylated at both Thr(22) and Ser(27). These results indicate a role for Pak2 in the down-regulation of translation initiation in apoptosis by phosphorylation of Mnk1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK2 | down-regulates
phosphorylation
|
NF2 |
0.495 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-159768 |
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 |
| + |
PAK2 | down-regulates
phosphorylation
|
ABL1 |
0.422 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160215 |
Ser618 |
APTPPKRsSSFREMD |
Homo sapiens |
|
| pmid |
sentence |
| 18161990 |
The interaction of c-abl with the abl interactor protein abi2 is shown to be negatively regulated by phosphorylation of serines 637 and 638. These serines are adjacent to the pxxp motif (ptppkrs637s638sfr) that binds the sh3 domain of abi. phosphorylation of c-abl by pak2 inhibits the interaction between the sh3 domain of abi2 and the pxxp motif of c-abl. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160219 |
Ser619 |
PTPPKRSsSFREMDG |
Homo sapiens |
|
| pmid |
sentence |
| 18161990 |
The interaction of c-abl with the abl interactor protein abi2 is shown to be negatively regulated by phosphorylation of serines 637 and 638. These serines are adjacent to the pxxp motif (ptppkrs637s638sfr) that binds the sh3 domain of abi. phosphorylation of c-abl by pak2 inhibits the interaction between the sh3 domain of abi2 and the pxxp motif of c-abl. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PAK2 | down-regulates activity
phosphorylation
|
SORT1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273717 |
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 |
| + |
PAK2 |
phosphorylation
|
SYN1 |
0.33 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250236 |
Ser9 |
NYLRRRLsDSNFMAN |
Rattus norvegicus |
|
| pmid |
sentence |
| 12237306 |
Recombinant PAK2 could also phosphorylate the Ser9 and Ser551 residues. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
CDK12 | up-regulates activity
phosphorylation
|
PAK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273109 |
Thr134 |
LKFYDSNtVKQKYLS |
Homo sapiens |
HGC-27 Cell |
| pmid |
sentence |
| 32483448 |
Mechanistically, CDK12 directly binds to and phosphorylates PAK2 at T134/T169 to activate MAPK signaling pathway |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273110 |
Thr169 |
TEAPAVVtEEEDDDE |
Homo sapiens |
HGC-27 Cell |
| pmid |
sentence |
| 32483448 |
Mechanistically, CDK12 directly binds to and phosphorylates PAK2 at T134/T169 to activate MAPK signaling pathway |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CyclinK/CDK12 | up-regulates activity
phosphorylation
|
PAK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273111 |
Thr134 |
LKFYDSNtVKQKYLS |
Homo sapiens |
HGC-27 Cell |
| pmid |
sentence |
| 32483448 |
Mechanistically, CDK12 directly binds to and phosphorylates PAK2 at T134/T169 to activate MAPK signaling pathway |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273112 |
Thr169 |
TEAPAVVtEEEDDDE |
Homo sapiens |
HGC-27 Cell |
| pmid |
sentence |
| 32483448 |
Mechanistically, CDK12 directly binds to and phosphorylates PAK2 at T134/T169 to activate MAPK signaling pathway |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PAK2 | up-regulates
phosphorylation
|
JUN |
0.272 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-170760 |
Thr2 |
tAKMETTF |
Homo sapiens |
Melanoma Cell |
| pmid |
sentence |
| 21177766 |
P21-activated protein kinase (pak2)-mediated c-jun phosphorylation at 5 threonine sites promotes cell transformationour data showed that pak2 binds and phosphorylates c-jun at five threonine sites (thr2, thr8, thr89, thr93 and thr286) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-170764 |
Thr286 |
RLEEKVKtLKAQNSE |
Homo sapiens |
Melanoma Cell |
| pmid |
sentence |
| 21177766 |
P21-activated protein kinase (pak2)-mediated c-jun phosphorylation at 5 threonine sites promotes cell transformationour data showed that pak2 binds and phosphorylates c-jun at five threonine sites (thr2, thr8, thr89, thr93 and thr286) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-170768 |
Thr8 |
MTAKMETtFYDDALN |
Homo sapiens |
Melanoma Cell |
| pmid |
sentence |
| 21177766 |
P21-activated protein kinase (pak2)-mediated c-jun phosphorylation at 5 threonine sites promotes cell transformationour data showed that pak2 binds and phosphorylates c-jun at five threonine sites (thr2, thr8, thr89, thr93 and thr286) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-170772 |
Thr89 |
QSSNGHItTTPTPTQ |
Homo sapiens |
Melanoma Cell |
| pmid |
sentence |
| 21177766 |
P21-activated protein kinase (pak2)-mediated c-jun phosphorylation at 5 threonine sites promotes cell transformationour data showed that pak2 binds and phosphorylates c-jun at five threonine sites (thr2, thr8, thr89, thr93 and thr286) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-170776 |
Thr93 |
GHITTTPtPTQFLCP |
Homo sapiens |
Melanoma Cell |
| pmid |
sentence |
| 21177766 |
P21-activated protein kinase (pak2)-mediated c-jun phosphorylation at 5 threonine sites promotes cell transformationour data showed that pak2 binds and phosphorylates c-jun at five threonine sites (thr2, thr8, thr89, thr93 and thr286) |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| + |
PAK2 | down-regulates activity
phosphorylation
|
MYC |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278489 |
Thr358 |
ISNNRKCtSPRSSDT |
Homo sapiens |
|
| pmid |
sentence |
| 14749374 |
Here we demonstrate that Pak2 phosphorylates Myc at three sites (T358, S373, and T400) and affects Myc functions both in vitro and in vivo. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278490 |
Thr400 |
T-->E |
Homo sapiens |
|
| pmid |
sentence |
| 14749374 |
Here we demonstrate that Pak2 phosphorylates Myc at three sites (T358, S373, and T400) and affects Myc functions both in vitro and in vivo. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
SRC | up-regulates
phosphorylation
|
PAK2 |
0.546 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-92460 |
Tyr130 |
VLDVLKFyDSNTVKQ |
Homo sapiens |
|
| pmid |
sentence |
| 12215529 |
Pak2 became tyrosine phosphorylated in its n-terminal regulatory domain, where y130 was identified as the major phosphoacceptor site. Tyrosine phosphorylation-mediated superactivation of pak2 could be induced by overexpression of different src kinases or by inhibiting cellular tyrosine phosphatases with pervanadate and could be blocked by the src kinase inhibitor pp1 or by mutating the y130 residue. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPM1F | down-regulates
dephosphorylation
|
PAK2 |
0.263 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-162149 |
|
|
Homo sapiens |
Breast Cancer Cell, MCF-7 Cell |
| 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
|
PAK2 |
0.882 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248253 |
|
|
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 |
| + |
hsa-miR-23b-3p | down-regulates quantity by repression
post transcriptional regulation
|
PAK2 |
0.4 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277961 |
|
|
Homo sapiens |
HCT-116 Cell |
| pmid |
sentence |
| 22109528 |
MiR-23b, which is downregulated in human colon cancer samples, potently mediates the multiple steps of metastasis, including tumour growth, invasion and angiogenesis in vivo . | Mutation of the putative miR-23b site(s) in the 3′-UTR of FZD7, MAP3K1 (MEKK1), PAK2, TGFβR2, RRAS2 or uPA resulted in an abrogated responsiveness to miR-23b. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RAC1 | up-regulates activity
binding
|
PAK2 |
0.741 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248250 |
|
|
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 |
3.0
PAK2
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