+ |
PRKD2 | up-regulates activity
phosphorylation
|
HDAC7 |
0.448 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275933 |
Ser155 |
FPLRKTVsEPNLKLR |
|
|
pmid |
sentence |
18692497 |
Histone deacetylase (HDAC) 5 and 7, two members of the class II of classical HDAC [62], are in vivo substrates of PKD3 and PKD [63]. In response to a variety of signals, including phorbol esters, T cell receptor engagement, vascular endothelial growth factor and angiotensin stimulation, the activity of HDAC5 and 7 are regulated by a mechanism that involves PKD3 and PKD-mediated phosphorylation of the highly conserved Ser259 and Ser498 residues that are located in N-terminus of class II HDACs [63–67]. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275935 |
Ser358 |
WPLSRTRsEPLPPSA |
|
|
pmid |
sentence |
18692497 |
Histone deacetylase (HDAC) 5 and 7, two members of the class II of classical HDAC [62], are in vivo substrates of PKD3 and PKD [63]. In response to a variety of signals, including phorbol esters, T cell receptor engagement, vascular endothelial growth factor and angiotensin stimulation, the activity of HDAC5 and 7 are regulated by a mechanism that involves PKD3 and PKD-mediated phosphorylation of the highly conserved Ser259 and Ser498 residues that are located in N-terminus of class II HDACs [63–67]. |
|
Publications: |
2 |
+ |
PRKD2 | up-regulates activity
phosphorylation
|
MFF |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275947 |
Ser155 |
GRLKRERsMSENAVR |
|
|
pmid |
sentence |
34010649 |
The mitochondrial fission factor (MFF), the main mitochondrial receptor for the Dynamin-related protein 1 (DRP1), is directly phosphorylated by Protein Kinase D (PKD) specifically during mitosis. PKD-dependent MFF phosphorylation is required and sufficient for mitochondrial fission in mitotic but not in interphasic cells.|PKD directly phosphorylates MFF on serines 155, 172, and 275 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275941 |
Ser172 |
GQLVRNDsLWHRSDS |
|
|
pmid |
sentence |
34010649 |
The mitochondrial fission factor (MFF), the main mitochondrial receptor for the Dynamin-related protein 1 (DRP1), is directly phosphorylated by Protein Kinase D (PKD) specifically during mitosis. PKD-dependent MFF phosphorylation is required and sufficient for mitochondrial fission in mitotic but not in interphasic cells.|PKD directly phosphorylates MFF on serines 155, 172, and 275 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275949 |
Ser275 |
DNVRYGIsNIDTTIE |
|
|
pmid |
sentence |
34010649 |
The mitochondrial fission factor (MFF), the main mitochondrial receptor for the Dynamin-related protein 1 (DRP1), is directly phosphorylated by Protein Kinase D (PKD) specifically during mitosis. PKD-dependent MFF phosphorylation is required and sufficient for mitochondrial fission in mitotic but not in interphasic cells.|PKD directly phosphorylates MFF on serines 155, 172, and 275 |
|
Publications: |
3 |
+ |
PRKD2 | up-regulates activity
phosphorylation
|
HDAC5 |
0.299 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275927 |
Ser259 |
FPLRKTAsEPNLKVR |
|
|
pmid |
sentence |
18692497 |
Histone deacetylase (HDAC) 5 and 7, two members of the class II of classical HDAC [62], are in vivo substrates of PKD3 and PKD [63]. In response to a variety of signals, including phorbol esters, T cell receptor engagement, vascular endothelial growth factor and angiotensin stimulation, the activity of HDAC5 and 7 are regulated by a mechanism that involves PKD3 and PKD-mediated phosphorylation of the highly conserved Ser259 and Ser498 residues that are located in N-terminus of class II HDACs [63–67]. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275929 |
Ser498 |
RPLSRTQsSPLPQSP |
|
|
pmid |
sentence |
18692497 |
Histone deacetylase (HDAC) 5 and 7, two members of the class II of classical HDAC [62], are in vivo substrates of PKD3 and PKD [63]. In response to a variety of signals, including phorbol esters, T cell receptor engagement, vascular endothelial growth factor and angiotensin stimulation, the activity of HDAC5 and 7 are regulated by a mechanism that involves PKD3 and PKD-mediated phosphorylation of the highly conserved Ser259 and Ser498 residues that are located in N-terminus of class II HDACs [63–67]. |
|
Publications: |
2 |
+ |
PRKD2 | up-regulates
phosphorylation
|
PI4KB |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-148880 |
Ser294 |
SNLKRTAsNPKVENE |
Homo sapiens |
|
pmid |
sentence |
16912074 |
Binding of 14-3-3 proteins to pi4kiiibeta involved the pkd phosphorylation site ser294, evident from reduced 14-3-3 binding to a s294a pi4kiiibeta mutant. Phospho-specific binding of 14-3-3 proteins to phosphatidylinositol 4-kinase iii beta protects from dephosphorylation and stabilizes lipid kinase activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKCH | up-regulates
phosphorylation
|
PRKD2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-89423 |
Ser706 |
ARIIGEKsFRRSVVG |
Homo sapiens |
|
pmid |
sentence |
12058027 |
Thus, pkd2 is likely to be a novel downstream target of specific pkcs upon the stimulation of ags-b cells with gastrin. Our data suggest a two-step mechanism of activation of pkd2 via endogenously produced diacylglycerol and the activation of pkcs. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-89427 |
Ser710 |
GEKSFRRsVVGTPAY |
Homo sapiens |
|
pmid |
sentence |
12058027 |
Thus, pkd2 is likely to be a novel downstream target of specific pkcs upon the stimulation of ags-b cells with gastrin. Our data suggest a two-step mechanism of activation of pkd2 via endogenously produced diacylglycerol and the activation of pkcs. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-89431 |
Ser876 |
QGLAERIsVL |
Homo sapiens |
|
pmid |
sentence |
12058027 |
Thus, pkd2 is likely to be a novel downstream target of specific pkcs upon the stimulation of ags-b cells with gastrin. Our data suggest a two-step mechanism of activation of pkd2 via endogenously produced diacylglycerol and the activation of pkcs. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
PRKCH | up-regulates activity
phosphorylation
|
PRKD2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275958 |
Ser706 |
ARIIGEKsFRRSVVG |
|
|
pmid |
sentence |
12058027 |
Our data demonstrate that gastrin-stimulated PKD2 activation involves a heterotrimeric G alpha(q) protein as well as the activation of phospholipase C. Furthermore, we show that PKD2 can be activated by classical and novel members of the protein kinase C (PKC) family such as PKC alpha, PKC epsilon, and PKC eta.|The position of PKD2 phosphorylated at Ser876 and Ser706/Ser710 is indicated by anarrowhead. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275957 |
Ser710 |
GEKSFRRsVVGTPAY |
|
|
pmid |
sentence |
12058027 |
Our data demonstrate that gastrin-stimulated PKD2 activation involves a heterotrimeric G alpha(q) protein as well as the activation of phospholipase C. Furthermore, we show that PKD2 can be activated by classical and novel members of the protein kinase C (PKC) family such as PKC alpha, PKC epsilon, and PKC eta.|The position of PKD2 phosphorylated at Ser876 and Ser706/Ser710 is indicated by anarrowhead. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275956 |
Ser876 |
QGLAERIsVL |
|
|
pmid |
sentence |
12058027 |
Our data demonstrate that gastrin-stimulated PKD2 activation involves a heterotrimeric G alpha(q) protein as well as the activation of phospholipase C. Furthermore, we show that PKD2 can be activated by classical and novel members of the protein kinase C (PKC) family such as PKC alpha, PKC epsilon, and PKC eta.|The position of PKD2 phosphorylated at Ser876 and Ser706/Ser710 is indicated by anarrowhead. |
|
Publications: |
3 |
+ |
PRKCA | up-regulates activity
phosphorylation
|
PRKD2 |
0.371 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275955 |
Ser706 |
ARIIGEKsFRRSVVG |
|
|
pmid |
sentence |
12058027 |
Our data demonstrate that gastrin-stimulated PKD2 activation involves a heterotrimeric G alpha(q) protein as well as the activation of phospholipase C. Furthermore, we show that PKD2 can be activated by classical and novel members of the protein kinase C (PKC) family such as PKC alpha, PKC epsilon, and PKC eta.|The position of PKD2 phosphorylated at Ser876 and Ser706/Ser710 is indicated by anarrowhead. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275954 |
Ser710 |
GEKSFRRsVVGTPAY |
|
|
pmid |
sentence |
12058027 |
Our data demonstrate that gastrin-stimulated PKD2 activation involves a heterotrimeric G alpha(q) protein as well as the activation of phospholipase C. Furthermore, we show that PKD2 can be activated by classical and novel members of the protein kinase C (PKC) family such as PKC alpha, PKC epsilon, and PKC eta.|The position of PKD2 phosphorylated at Ser876 and Ser706/Ser710 is indicated by anarrowhead. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275953 |
Ser876 |
QGLAERIsVL |
|
|
pmid |
sentence |
12058027 |
Our data demonstrate that gastrin-stimulated PKD2 activation involves a heterotrimeric G alpha(q) protein as well as the activation of phospholipase C. Furthermore, we show that PKD2 can be activated by classical and novel members of the protein kinase C (PKC) family such as PKC alpha, PKC epsilon, and PKC eta.|The position of PKD2 phosphorylated at Ser876 and Ser706/Ser710 is indicated by anarrowhead. |
|
Publications: |
3 |
+ |
PKA | up-regulates activity
phosphorylation
|
PRKD2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275952 |
Ser706 |
ARIIGEKsFRRSVVG |
|
|
pmid |
sentence |
12058027 |
Our data demonstrate that gastrin-stimulated PKD2 activation involves a heterotrimeric G alpha(q) protein as well as the activation of phospholipase C. Furthermore, we show that PKD2 can be activated by classical and novel members of the protein kinase C (PKC) family such as PKC alpha, PKC epsilon, and PKC eta.|The position of PKD2 phosphorylated at Ser876 and Ser706/Ser710 is indicated by anarrowhead. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275951 |
Ser710 |
GEKSFRRsVVGTPAY |
|
|
pmid |
sentence |
12058027 |
Our data demonstrate that gastrin-stimulated PKD2 activation involves a heterotrimeric G alpha(q) protein as well as the activation of phospholipase C. Furthermore, we show that PKD2 can be activated by classical and novel members of the protein kinase C (PKC) family such as PKC alpha, PKC epsilon, and PKC eta.|The position of PKD2 phosphorylated at Ser876 and Ser706/Ser710 is indicated by anarrowhead. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275950 |
Ser876 |
QGLAERIsVL |
|
|
pmid |
sentence |
12058027 |
Our data demonstrate that gastrin-stimulated PKD2 activation involves a heterotrimeric G alpha(q) protein as well as the activation of phospholipase C. Furthermore, we show that PKD2 can be activated by classical and novel members of the protein kinase C (PKC) family such as PKC alpha, PKC epsilon, and PKC eta.|The position of PKD2 phosphorylated at Ser876 and Ser706/Ser710 is indicated by anarrowhead. |
|
Publications: |
3 |
+ |
PRKCE | up-regulates
phosphorylation
|
PRKD2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-89411 |
Ser706 |
ARIIGEKsFRRSVVG |
Homo sapiens |
|
pmid |
sentence |
12058027 |
Furthermore, we show that pkd2 can be activated by classical and novel members of the protein kinase c (pkc) family such as pkc alpha, pkc epsilon, and pkc eta. These pkcs are activated by gastrin in ags-b cells. Thus, pkd2 is likely to be a novel downstream target of specific pkcs upon the stimulation of ags-b cells with gastrin. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-89415 |
Ser710 |
GEKSFRRsVVGTPAY |
Homo sapiens |
|
pmid |
sentence |
12058027 |
In cells transfected with pkc? Or pkc? The phosphorylation of ser876 was markedly more pronounced than the phosphorylation of ser706/ser710 / the phosphorylation of ser706/ser710 in pkd2 reflects the activation of the kinase. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-89419 |
Ser876 |
QGLAERIsVL |
Homo sapiens |
|
pmid |
sentence |
12058027 |
Furthermore, we show that pkd2 can be activated by classical and novel members of the protein kinase c (pkc) family such as pkc alpha, pkc epsilon, and pkc eta. These pkcs are activated by gastrin in ags-b cells. Thus, pkd2 is likely to be a novel downstream target of specific pkcs upon the stimulation of ags-b cells with gastrin. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
PRKCE | up-regulates activity
phosphorylation
|
PRKD2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275961 |
Ser706 |
ARIIGEKsFRRSVVG |
|
|
pmid |
sentence |
12058027 |
Our data demonstrate that gastrin-stimulated PKD2 activation involves a heterotrimeric G alpha(q) protein as well as the activation of phospholipase C. Furthermore, we show that PKD2 can be activated by classical and novel members of the protein kinase C (PKC) family such as PKC alpha, PKC epsilon, and PKC eta.|The position of PKD2 phosphorylated at Ser876 and Ser706/Ser710 is indicated by anarrowhead. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275960 |
Ser710 |
GEKSFRRsVVGTPAY |
|
|
pmid |
sentence |
12058027 |
Our data demonstrate that gastrin-stimulated PKD2 activation involves a heterotrimeric G alpha(q) protein as well as the activation of phospholipase C. Furthermore, we show that PKD2 can be activated by classical and novel members of the protein kinase C (PKC) family such as PKC alpha, PKC epsilon, and PKC eta.|The position of PKD2 phosphorylated at Ser876 and Ser706/Ser710 is indicated by anarrowhead. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275959 |
Ser876 |
QGLAERIsVL |
|
|
pmid |
sentence |
12058027 |
Our data demonstrate that gastrin-stimulated PKD2 activation involves a heterotrimeric G alpha(q) protein as well as the activation of phospholipase C. Furthermore, we show that PKD2 can be activated by classical and novel members of the protein kinase C (PKC) family such as PKC alpha, PKC epsilon, and PKC eta.|The position of PKD2 phosphorylated at Ser876 and Ser706/Ser710 is indicated by anarrowhead. |
|
Publications: |
3 |
+ |
PRKD2 | up-regulates activity
phosphorylation
|
PKD2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276284 |
Ser801 |
SSLPRPMsSRSFPRS |
Canis lupus familiaris |
MDCK Cell |
pmid |
sentence |
20881056 |
Here, we report the identification of a previously unrecognized phosphorylation site within the polycystin-2 C terminus (Ser801), and we demonstrate that it is phosphorylated by protein kinase D. These results suggest that growth factor-stimulated, protein kinase D-mediated phosphorylation of polycystin-2 is essential for its ER channel function and links extracellular stimuli to its effects on cell growth and intracellular calcium regulation. |
|
Publications: |
1 |
Organism: |
Canis Lupus Familiaris |
+ |
PRKD2 | up-regulates
phosphorylation
|
PRKD2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-83834 |
Ser876 |
QGLAERIsVL |
Homo sapiens |
|
pmid |
sentence |
11062248 |
The addition of phorbol 12,13-dibutyrate in the presence of dioleoylphosphatidylserine stimulated the autophosphorylation of pkd2 in a synergistic fashion.In addition, we could identify the c-terminal ser(876) residue as an in vivo phosphorylation site within pkd2. Phosphorylation of ser(876) of pkd2 correlated with the activation status of the kinase. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKD2 | down-regulates
phosphorylation
|
SSH1 |
0.296 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-173441 |
Ser937 |
SNLTRSSsSDSIHSV |
Homo sapiens |
|
pmid |
sentence |
21525957 |
Phosphorylation of ser 402 impedes phosphatase activity of slingshot 1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKD2 | down-regulates activity
phosphorylation
|
SSH1 |
0.296 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275937 |
Ser978 |
SPLKRSHsLAKLGSL |
|
|
pmid |
sentence |
21832093 |
Active PKD Isoforms Phosphorylate and Inactivate SSH1L|Here, we show that active PKD3 also mediates SSH1L phosphorylation at Ser-978 and binding to 14-3-3, further confirming the involvement of all three PKD isoforms in negatively regulating this phosphatase |
|
Publications: |
1 |