+ |
PRKCQ | up-regulates activity
phosphorylation
|
ARHGEF6 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272169 |
Ser225 |
KSSERPLsPKAVKGF |
|
|
pmid |
sentence |
25694429 |
Recently, we have reported that the active form of Rac 1 GTPase binds to the glycogen phosphorylase muscle isoform (PYGM) and modulates its enzymatic activity leading to T cell proliferation.|More specifically, αPIX, a known guanine nucleotide exchange factor for the small GTPases of the Rho family, preferentially Rac 1, mediates PYGM activation in Kit 225 T cells stimulated with IL-2. Using directed mutagenesis, phosphorylation of αPIX Rho-GEF serines 225 and 488 is required for activation of the Rac 1/PYGM pathway. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272168 |
Ser488 |
LSASPRMsGFIYQGK |
|
|
pmid |
sentence |
25694429 |
Recently, we have reported that the active form of Rac 1 GTPase binds to the glycogen phosphorylase muscle isoform (PYGM) and modulates its enzymatic activity leading to T cell proliferation.|More specifically, αPIX, a known guanine nucleotide exchange factor for the small GTPases of the Rho family, preferentially Rac 1, mediates PYGM activation in Kit 225 T cells stimulated with IL-2. Using directed mutagenesis, phosphorylation of αPIX Rho-GEF serines 225 and 488 is required for activation of the Rac 1/PYGM pathway. |
|
Publications: |
2 |
+ |
PRKACA | down-regulates activity
phosphorylation
|
ARHGEF6 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272162 |
Ser640 |
RKTERKPsEEEYVIR |
Homo sapiens |
Blood Platelet |
pmid |
sentence |
26507661 |
ARHGEF6 is a Rho guanine nucleotide exchange factor for Rac1 and constitutively bound to GIT1. NO and PGI2 activate PKG and PKA, respectively and both kinases phosphorylate ARHGEF6 on Ser-684 and possibly on Ser-640. Phosphorylation of ARHGEF6 results in the assembly of a GIT1-ARHGEF6–14-3-3 complex. These changes might contribute to PGI2- and NO-mediated Rac1 inhibition. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272159 |
Ser684 |
GSSTRKDsIPQVLLP |
Homo sapiens |
Blood Platelet |
pmid |
sentence |
26507661 |
Screening for potential mediators of this effect resulted in the identification of the Rac1-specific GTPase-activating protein ARHGAP17 and the guanine nucleotide exchange factor ARHGEF6 as new PKA and PKG substrates in platelets. We mapped the PKA/PKG phosphorylation sites to serine 702 on ARHGAP17 using Phos-tag gels and to serine 684 on ARHGEF6. |we show that ARHGEF6 is constitutively linked to GIT1, a GAP of Arf family small G proteins, and that ARHGEF6 phosphorylation enables binding of the 14-3-3 adaptor protein to the ARHGEF6/GIT1 complex. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
PKC | down-regulates activity
phosphorylation
|
ARHGEF6 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272164 |
Ser640 |
RKTERKPsEEEYVIR |
Homo sapiens |
Blood Platelet |
pmid |
sentence |
26507661 |
ARHGEF6 is a Rho guanine nucleotide exchange factor for Rac1 and constitutively bound to GIT1. NO and PGI2 activate PKG and PKA, respectively and both kinases phosphorylate ARHGEF6 on Ser-684 and possibly on Ser-640. Phosphorylation of ARHGEF6 results in the assembly of a GIT1-ARHGEF6–14-3-3 complex. These changes might contribute to PGI2- and NO-mediated Rac1 inhibition. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272161 |
Ser684 |
GSSTRKDsIPQVLLP |
Homo sapiens |
Blood Platelet |
pmid |
sentence |
26507661 |
Screening for potential mediators of this effect resulted in the identification of the Rac1-specific GTPase-activating protein ARHGAP17 and the guanine nucleotide exchange factor ARHGEF6 as new PKA and PKG substrates in platelets. We mapped the PKA/PKG phosphorylation sites to serine 702 on ARHGAP17 using Phos-tag gels and to serine 684 on ARHGEF6. |we show that ARHGEF6 is constitutively linked to GIT1, a GAP of Arf family small G proteins, and that ARHGEF6 phosphorylation enables binding of the 14-3-3 adaptor protein to the ARHGEF6/GIT1 complex. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
PKA | down-regulates activity
phosphorylation
|
ARHGEF6 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272163 |
Ser640 |
RKTERKPsEEEYVIR |
Homo sapiens |
Blood Platelet |
pmid |
sentence |
26507661 |
ARHGEF6 is a Rho guanine nucleotide exchange factor for Rac1 and constitutively bound to GIT1. NO and PGI2 activate PKG and PKA, respectively and both kinases phosphorylate ARHGEF6 on Ser-684 and possibly on Ser-640. Phosphorylation of ARHGEF6 results in the assembly of a GIT1-ARHGEF6–14-3-3 complex. These changes might contribute to PGI2- and NO-mediated Rac1 inhibition. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272160 |
Ser684 |
GSSTRKDsIPQVLLP |
Homo sapiens |
Blood Platelet |
pmid |
sentence |
26507661 |
Screening for potential mediators of this effect resulted in the identification of the Rac1-specific GTPase-activating protein ARHGAP17 and the guanine nucleotide exchange factor ARHGEF6 as new PKA and PKG substrates in platelets. We mapped the PKA/PKG phosphorylation sites to serine 702 on ARHGAP17 using Phos-tag gels and to serine 684 on ARHGEF6. |we show that ARHGEF6 is constitutively linked to GIT1, a GAP of Arf family small G proteins, and that ARHGEF6 phosphorylation enables binding of the 14-3-3 adaptor protein to the ARHGEF6/GIT1 complex. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
ARHGEF6 | up-regulates activity
guanine nucleotide exchange factor
|
RAC1 |
0.607 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272167 |
|
|
Homo sapiens |
Blood Platelet |
pmid |
sentence |
26507661 |
ARHGEF6 is a Rho guanine nucleotide exchange factor for Rac1 and constitutively bound to GIT1. NO and PGI2 activate PKG and PKA, respectively and both kinases phosphorylate ARHGEF6 on Ser-684 and possibly on Ser-640. Phosphorylation of ARHGEF6 results in the assembly of a GIT1-ARHGEF6–14-3-3 complex. These changes might contribute to PGI2- and NO-mediated Rac1 inhibition. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ARHGEF6 | up-regulates
|
Cell_migration |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272237 |
|
|
Homo sapiens |
Hep-G2 Cell |
pmid |
sentence |
23776207 |
Expression of the phospho-mimicking ACAP4 mutant promotes ARF6-dependent cell migration. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ASAP3 | up-regulates activity
binding
|
ARHGEF6 |
0.298 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272235 |
|
|
Homo sapiens |
Hep-G2 Cell |
pmid |
sentence |
23776207 |
ArfGAP With Coiled-Coil, Ankyrin Repeat And PH Domains 4 (ACAP4) is an ADP-ribosylation factor 6 (ARF6) GTPase-activating protein essential for EGF-elicited cell migration. |The crystal structure of the catalytic core of ACAP4 in a complex with ARF6 reveals the structural determinants underlying ACAP4 selectivity and specificity as an ARF6 GTPase-activating protein |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GIT1 | up-regulates activity
binding
|
ARHGEF6 |
0.846 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272165 |
|
|
Homo sapiens |
Blood Platelet |
pmid |
sentence |
26507661 |
Screening for potential mediators of this effect resulted in the identification of the Rac1-specific GTPase-activating protein ARHGAP17 and the guanine nucleotide exchange factor ARHGEF6 as new PKA and PKG substrates in platelets. We mapped the PKA/PKG phosphorylation sites to serine 702 on ARHGAP17 using Phos-tag gels and to serine 684 on ARHGEF6. |we show that ARHGEF6 is constitutively linked to GIT1, a GAP of Arf family small G proteins, and that ARHGEF6 phosphorylation enables binding of the 14-3-3 adaptor protein to the ARHGEF6/GIT1 complex. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ARHGEF6 | up-regulates
|
Actin_cytoskeleton_reorganization |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272236 |
|
|
Homo sapiens |
Hep-G2 Cell |
pmid |
sentence |
23776207 |
Activation of ARF6 promotes cortical actin assembly (9) and plasma membrane remodeling |
|
Publications: |
1 |
Organism: |
Homo Sapiens |