| + |
PRKD3 | up-regulates activity 
phosphorylation
|
MFF |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275945 |
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-275940 |
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-275946 |
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 |
| + |
PRKD3 | up-regulates activity
phosphorylation
|
HDAC7 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275932 |
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-275934 |
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 |
| + |
PRKD3 | up-regulates activity
phosphorylation
|
HDAC5 |
0.268 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275926 |
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-275928 |
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 |
| + |
PRKD3 |
phosphorylation
|
GIT1 |
0.374 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-191839 |
Ser46 |
RSLGRHIsIVKHLRH |
Homo sapiens |
|
| pmid |
sentence |
| 22893698 |
We propose that phosphorylation of git1 on serine 46 by pkd3 represents a molecular switch by which git1 localization, paxillin trafficking, and cellular protrusive activity are regulated. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKD3 | up-regulates activity
phosphorylation
|
PAK4 |
0.256 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275931 |
Ser474 |
KEVPRRKsLVGTPYW |
|
|
| pmid |
sentence |
| 23841590 |
PAK4 activity is regulated by an autoinhibitory domain that is released upon RhoGTPase binding as well as phosphorylation at Ser474 in the activation loop of the kinase domain. In the present study, we add another level of complexity to PAK4 regulation by showing that phosphorylation at Ser99 is required for its targeting to the leading edge. This phosphorylation is mediated by PKD1 (protein kinase D1) |
|
| Publications: |
1 |
| + |
PKA | up-regulates activity
phosphorylation
|
PRKD3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275924 |
Ser731 |
ARIIGEKsFRRSVVG |
|
|
| pmid |
sentence |
| 18692497 |
The results presented in this study indicate that during mitosis, PKD3 and PKD are phosphorylated at Ser(731) and Ser(744) within their activation loop by a mechanism that requires protein kinase C. Mitosis-associated PKD3 Ser(731) and PKD Ser(744) phosphorylation is related to the catalytic activation of these kinases as evidenced by in vivo phosphorylation of histone deacetylase 5, a substrate of PKD and PKD3. |
|
| Publications: |
1 |
| + |
PRKD3 | down-regulates activity 
phosphorylation
|
SSH1 |
0.293 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275938 |
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 |
3.0
PRKD3
- 
- 