| + |
PRKD1 | down-regulates activity 
phosphorylation
|
SNAI1 |
0.479 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-168537 |
Ser11 |
SFLVRKPsDPNRKPN |
Homo sapiens |
|
| pmid |
sentence |
| 20940406 |
Pkd1 phosphorylates ser(11) (s11) on transcription factor snail, a master emt regulator and repressor of e-cadherin expression, triggering nuclear export of snail via 14-3-3_ binding. Pkd1 regulates the expression of e-cadherin at the promoter level through direct phosphorylation of the transcriptional repressor snai1. Pkd1-mediated phosphorylation of snai1 occurs in the nucleus and generates a nuclear, inactive dna/snai1 complex that shows decreased interaction with its co-repressor ajuba. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKD1 | up-regulates activity 
phosphorylation
|
ATP7B |
0.302 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272295 |
Ser1121 |
AHSERPLsAPASHLN |
Homo sapiens |
Hep-G2 Cell |
| pmid |
sentence |
| 21189263 |
ATP7B trafficking was markedly reduced by the Ser-478/481/1121/1453 to Ala mutation. We conclude that PKD plays a key role in copper-dependent serine phosphorylation, permitting high levels of ATP7B protein expression and trafficking. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272294 |
Ser1453 |
DDDGDKWsLLLNGRD |
Homo sapiens |
Hep-G2 Cell |
| pmid |
sentence |
| 21189263 |
ATP7B trafficking was markedly reduced by the Ser-478/481/1121/1453 to Ala mutation. We conclude that PKD plays a key role in copper-dependent serine phosphorylation, permitting high levels of ATP7B protein expression and trafficking. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272296 |
Ser478 |
APDILAKsPQSTRAV |
Homo sapiens |
Hep-G2 Cell |
| pmid |
sentence |
| 21189263 |
ATP7B trafficking was markedly reduced by the Ser-478/481/1121/1453 to Ala mutation. We conclude that PKD plays a key role in copper-dependent serine phosphorylation, permitting high levels of ATP7B protein expression and trafficking. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272293 |
Ser481 |
ILAKSPQsTRAVAPQ |
Homo sapiens |
Hep-G2 Cell |
| pmid |
sentence |
| 21189263 |
ATP7B trafficking was markedly reduced by the Ser-478/481/1121/1453 to Ala mutation. We conclude that PKD plays a key role in copper-dependent serine phosphorylation, permitting high levels of ATP7B protein expression and trafficking. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
PRKD1 | down-regulates
phosphorylation
|
BAD |
0.311 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163920 |
Ser118 |
GRELRRMsDEFVDSF |
Homo sapiens |
|
| pmid |
sentence |
| 20179209 |
Pkcs phosphorylate bad under in vitro conditions, and the association of phosphorylated bad with pkc-mu or pkc-epsilon, as shown by immunoprecipitation, indicated direct involvement of pkcs in bad phosphorylation. To confirm these results, cells overexpressing pegfp-n1, wt-bad, or bad with a single site mutated (ser112ala;ser136ala;ser155ala), two sites mutated (ser(112/136)ala;ser(112/155)ala;ser(136/155)ala), or the triple mutant were tested. Igf-i protected completely against rapamycin-induced apoptosis in cells overexpressing wt-bad and mutants having either one or two sites of phosphorylation mutated |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163924 |
Ser75 |
EIRSRHSsYPAGTED |
Homo sapiens |
|
| pmid |
sentence |
| 20179209 |
Pkcs phosphorylate bad under in vitro conditions, and the association of phosphorylated bad with pkc-mu or pkc-epsilon, as shown by immunoprecipitation, indicated direct involvement of pkcs in bad phosphorylation. To confirm these results, cells overexpressing pegfp-n1, wt-bad, or bad with a single site mutated (ser112ala;ser136ala;ser155ala), two sites mutated (ser(112/136)ala;ser(112/155)ala;ser(136/155)ala), or the triple mutant were tested. Igf-i protected completely against rapamycin-induced apoptosis in cells overexpressing wt-bad and mutants having either one or two sites of phosphorylation mutated |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163928 |
Ser99 |
PFRGRSRsAPPNLWA |
Homo sapiens |
|
| pmid |
sentence |
| 20179209 |
Pkcs phosphorylate bad under in vitro conditions, and the association of phosphorylated bad with pkc-mu or pkc-epsilon, as shown by immunoprecipitation, indicated direct involvement of pkcs in bad phosphorylation. To confirm these results, cells overexpressing pegfp-n1, wt-bad, or bad with a single site mutated (ser112ala;ser136ala;ser155ala), two sites mutated (ser(112/136)ala;ser(112/155)ala;ser(136/155)ala), or the triple mutant were tested. Igf-i protected completely against rapamycin-induced apoptosis in cells overexpressing wt-bad and mutants having either one or two sites of phosphorylation mutated |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PRKD1 | down-regulates
phosphorylation
|
DLC1 |
0.381 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-169994 |
Ser1244 |
NTLKRENsSPRVMQR |
Homo sapiens |
|
| pmid |
sentence |
| 21087603 |
The tumor suppressor protein dlc1 is regulated by pkd-mediated gap domain phosphorylation.Our results thus show that pkd-mediated phosphorylation of dlc1 on serine 807 negatively regulates dlc1 cellular function. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKD1 | down-regulates activity
phosphorylation
|
PLCG1 |
0.413 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248846 |
Ser1248 |
HGRAREGsFESRYQQ |
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 1370476 |
Thus, phosphorylation of PLC-gamma 1 by PKC or PKA at serine 1248 may modulate the interaction of PLC-gamma 1 with the protein tyrosine kinase or the protein tyrosine phosphatase; this altered interaction may, at least in part, be responsible for the decreased tyrosine phosphorylation of PLC-gamma 1 seen in PMA- and forskolin-treated Jurkat cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKD1 | up-regulates
phosphorylation
|
ARFIP1 |
0.396 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-202101 |
Ser132 |
LELVRKWsLNTYKCT |
Homo sapiens |
|
| pmid |
sentence |
| 23695357 |
We report that arfaptins contain an amphipathic helix (ah) preceding the bar domain, which is essential for their binding to phosphatidylinositol 4-phosphate (pi(4)p)-containing liposomes and the tgn of mammalian cells. The binding of arfaptin1, but not arfaptin2, to pi(4)p is regulated by protein kinase d (pkd) mediated phosphorylation at ser100 within the ah. We also found that only arfaptin1 is required for the pkd-dependent trafficking of chromogranin a by the regulated secretory pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKD1 | down-regulates
phosphorylation
|
CERT1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-156500 |
Ser132 |
SSLRRHGsMVSLVSG |
Homo sapiens |
|
| pmid |
sentence |
| 17591919 |
In this study, we identify cert as a novel in vivo pkd substrate. Phosphorylation on serine 132 by pkd decreases the affinity of cert toward its lipid target phosphatidylinositol 4-phosphate at golgi membranes and reduces ceramide transfer activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKD1 | up-regulates activity
phosphorylation
|
PIK3R1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276426 |
Ser154 |
STLYRTQsSSNLAEL |
Homo sapiens |
HL-60 Cell |
| pmid |
sentence |
| 23129748 |
PKD1 phosphorylates p85α to enhance its interaction with PTEN, leading to polarized PTEN activity, thereby regulating neutrophil migration. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKD1 | down-regulates
phosphorylation
|
HDAC7 |
0.492 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-132894 |
Ser155 |
FPLRKTVsEPNLKLR |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 15623513 |
Protein kinase d1 (pkd1) was activated after tcr engagement, interacted with hdac7, and phosphorylated three serines (ser155, ser318, and ser448) at its n terminus, leading to its export from the nucleus. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-132898 |
Ser358 |
WPLSRTRsEPLPPSA |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 15623513 |
Protein kinase d1 (pkd1) was activated after tcr engagement, interacted with hdac7, and phosphorylated three serines (ser155, ser318, and ser448) at its n terminus, leading to its export from the nucleus. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-132902 |
Ser486 |
RPLSRAQsSPAAPAS |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 15623513 |
Protein kinase d1 (pkd1) was activated after tcr engagement, interacted with hdac7, and phosphorylated three serines (ser155, ser318, and ser448) at its n terminus, leading to its export from the nucleus. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179430 |
Ser486 |
RPLSRAQsSPAAPAS |
Homo sapiens |
|
| pmid |
sentence |
| 18617643 |
We show for the first time that vegf stimulated phosphorylation of hdac7 at the sites of ser178, ser344, and ser479we found that phospholipase cgamma/protein kinase c/protein kinase d1 (pkd1)-dependent signal pathway mediated hdac7 phosphorylation and cytoplasmic accumulation by vegf. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178713 |
Ser486 |
RPLSRAQsSPAAPAS |
Homo sapiens |
|
| pmid |
sentence |
| 18509061 |
We show for the first time that vegf stimulated phosphorylation of hdac7 at the sites of ser178, ser344, and ser479we found that phospholipase cgamma/protein kinase c/protein kinase d1 (pkd1)-dependent signal pathway mediated hdac7 phosphorylation and cytoplasmic accumulation by vegf. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| + |
PRKD1 |
phosphorylation
|
HDAC7 |
0.492 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249275 |
Ser155 |
FPLRKTVsEPNLKLR |
in vitro |
|
| pmid |
sentence |
| 15738054 |
We demonstrate that protein kinase D (PKD; also known as PKCmi), which is activated upon engagement of the TCR, stimulates HDAC7 nuclear export by direct phosphorylation on four serine residues. Conversely, selective PKD inhibition blocks TCR-induced HDAC7 nuclear export and Nur77 expression. In addition, an HDAC7 mutant specifically deficient in phosphorylation by PKD blocks TCR-mediated apoptosis. | PKD1 phosphorylates S155, S181, S321, and S449 of HDAC7 in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249273 |
Ser181 |
NPLLRKEsAPPSLRR |
in vitro |
|
| pmid |
sentence |
| 15738054 |
We demonstrate that protein kinase D (PKD; also known as PKCmi), which is activated upon engagement of the TCR, stimulates HDAC7 nuclear export by direct phosphorylation on four serine residues. Conversely, selective PKD inhibition blocks TCR-induced HDAC7 nuclear export and Nur77 expression. In addition, an HDAC7 mutant specifically deficient in phosphorylation by PKD blocks TCR-mediated apoptosis. | PKD1 phosphorylates S155, S181, S321, and S449 of HDAC7 in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249274 |
Ser358 |
WPLSRTRsEPLPPSA |
in vitro |
|
| pmid |
sentence |
| 15738054 |
We demonstrate that protein kinase D (PKD; also known as PKCmi), which is activated upon engagement of the TCR, stimulates HDAC7 nuclear export by direct phosphorylation on four serine residues. Conversely, selective PKD inhibition blocks TCR-induced HDAC7 nuclear export and Nur77 expression. In addition, an HDAC7 mutant specifically deficient in phosphorylation by PKD blocks TCR-mediated apoptosis. | PKD1 phosphorylates S155, S181, S321, and S449 of HDAC7 in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249276 |
Ser486 |
RPLSRAQsSPAAPAS |
in vitro |
|
| pmid |
sentence |
| 15738054 |
We demonstrate that protein kinase D (PKD; also known as PKCmi), which is activated upon engagement of the TCR, stimulates HDAC7 nuclear export by direct phosphorylation on four serine residues. Conversely, selective PKD inhibition blocks TCR-induced HDAC7 nuclear export and Nur77 expression. In addition, an HDAC7 mutant specifically deficient in phosphorylation by PKD blocks TCR-mediated apoptosis. | PKD1 phosphorylates S155, S181, S321, and S449 of HDAC7 in vitro. |
|
| Publications: |
4 |
Organism: |
In Vitro |
| + |
PRKD1 | up-regulates activity
phosphorylation
|
MFF |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275943 |
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-277558 |
Ser155 |
GRLKRERsMSENAVR |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 34010649 |
PKD directly phosphorylates MFF on serines 155, 172, and 275 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277559 |
Ser172 |
GQLVRNDsLWHRSDS |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 34010649 |
PKD directly phosphorylates MFF on serines 155, 172, and 275 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275942 |
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-275948 |
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 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277557 |
Ser275 |
DNVRYGIsNIDTTIE |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 34010649 |
PKD directly phosphorylates MFF on serines 155, 172, and 275 |
|
| Publications: |
6 |
Organism: |
, Homo Sapiens |
| + |
PRKD1 | up-regulates activity
phosphorylation
|
REM1 |
0.365 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273832 |
Ser18 |
TPLHRRAsTPLPLSP |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 22076634 |
We found that activation of protein kinase D1, a protein kinase downstream of α(1)-adrenergic signaling, leads to direct phosphorylation of Rem1 at Ser18. This results in an increase of the channel activity and plasma membrane expression observed by using a combination of electrophysiology, live cell confocal microscopy, and immunohistochemistry in heterologous expression system and neonatal cardiomyocytes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKD1 | up-regulates
phosphorylation
|
CACNA1C |
0.258 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-177481 |
Ser1981 |
ASLGRRAsFHLECLK |
Homo sapiens |
|
| pmid |
sentence |
| 22100296 |
Both the expression of a dominant-negative mutant of pkd and the mutation of serine 1884 but not serine 1930, putative targets of pkd, strongly reduced l-type calcium currents and single channel activity without affecting the channel's expression at the plasma membrane. Our results suggest that serine 1884 is essential for the regulation of hcav1.2 by pkd. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKD1 | up-regulates
phosphorylation
|
PRKD1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-78676 |
Ser205 |
GVRRRRLsNVSLTGV |
Homo sapiens |
|
| pmid |
sentence |
| 10867018 |
Activation of the serine/threonine kinase, protein kinase d (pkd/pkc mu) via a phorbol ester/pkc-dependent pathway involves phosphorylation events. the second autophosphorylation site (ser(203)) lies in that region of the regulatory domain |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182480 |
Ser910 |
KALGERVsIL |
Homo sapiens |
|
| pmid |
sentence |
| 19029298 |
We show that pkd1-ser916 autophosphorylation does not necessarily correlate with pkd1 activity. Rather, autophosphorylation at ser916 is required for subsequent autophosphorylation at ser748. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-70525 |
Ser910 |
KALGERVsIL |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 10473617 |
Activation of the serine kinase protein kinase d (pkd)/pkcmicro is controlled by the phosphorylation of two serine residues within its activation loop via a pkc-dependent signaling cascade. In this study we have identified the c-terminal serine 916 residue as an in vivo phosphorylation site within active pkd/pkcmu. moreover, using different mutants of pkd/pkcmu, we show that serine 916 is not trans-phosphorylated by an upstream kinase but is rather an autophosphorylation event that occurs following activation of pkd/pkcmu. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PRKD1 | down-regulates
phosphorylation
|
OSBP |
0.457 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-171756 |
Ser240 |
TALQRSLsELESLKL |
Homo sapiens |
|
| pmid |
sentence |
| 21285358 |
Pkd attenuates the function of both cert and osbp by phosphorylation at their respective ser(132) and ser(240) residues (phosphorylation inhibition) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKD1 | up-regulates activity
phosphorylation
|
PTPN7 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276046 |
Ser246 |
QYQEERRsVKHILFS |
in vitro |
|
| pmid |
sentence |
| 16479000 |
HePTP is phosphorylated by PKC isozymes at Ser-225 in vitro. While all isozymes phosphorylated Ser-225 predominantly and Ser-113 to a lesser extent (Fig. (Fig.5),5), they differed strikingly in how much 32P they incorporated into HePTP during the 30-min assay. PKC θ was the most efficient, while PKC ζ and PKC μ were clearly less potent; PKC δ, ɛ, and η were quite inefficient. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKD1 | down-regulates activity
phosphorylation
|
HDAC5 |
0.532 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249270 |
Ser259 |
FPLRKTAsEPNLKVR |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 15367659 |
Here, we demonstrate that signaling by protein kinase C (PKC) is sufficient and, in some cases, necessary to drive nuclear export of class II HDAC5 in cardiomyocytes. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
PRKD1 | down-regulates activity
phosphorylation
|
KCNH2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277612 |
Ser284 |
ASVRRASsADDIEAM |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29949809 |
Based on LC-MS results from in vivo and HEK293 cell experiments we chose four KV11.1 mutant candidates for further functional analysis. Ablation of the putative PKD phosphorylation site in the mutant S284A increased the maximal current indicating S284 as a main PKD target in KV11.1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKD1 |
phosphorylation
|
RIN1 |
0.413 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-170877 |
Ser292 |
QLLRRESsVGYRVPA |
Homo sapiens |
|
| pmid |
sentence |
| 21209314 |
Here, we report the identification of serine 292 in rin1 as an in vivo pkd phosphorylation site. we demonstrate that phosphorylation at serine 292 controls rin1-mediated inhibition of cell migration by modulating the activation of abl kinases. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-113964 |
Ser351 |
RPLLRSMsAAFCSLL |
Homo sapiens |
|
| pmid |
sentence |
| 11784866 |
Serine 351 is a substrate for protein kinase d (pkd [also known as pkcmu]) in vitro and in vivo. These data suggest that the normal localization and function of rin1, as well as its ability to compete with raf, are regulated in part by 14-3-3 binding, which in turn is controlled by pkd phosphorylation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKD1 | up-regulates
phosphorylation
|
PI4KB |
0.416 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-148876 |
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 |
| + |
PRKD1 | down-regulates
phosphorylation
|
CTTN |
0.433 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164756 |
Ser298 |
EKLAKHEsQQDYSKG |
Homo sapiens |
|
| pmid |
sentence |
| 20363754 |
Pkd phosphorylates cortactin in vitro and in vivo at serine 298 thereby generating a 14-3-3 binding motif. In vitro, a phosphorylation-deficient cortactin-s298a protein accelerated vca-arp-cortactin-mediated synergistic actin polymerization and showed reduced f-actin binding |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182502 |
Ser348 |
EAVTSKTsNIRANFE |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 19038333 |
Here we have investigated the possible role of pkd as a cortactin kinase. Using a mass spectrometric approach, we found that pkd phosphorylates cortactin on ser 298 examination of cortactin phosphorylation kinetics revealed that ser 298 serves as a priming site for subsequent phosphorylation of ser 348 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKD1 | down-regulates activity
phosphorylation
|
CFL1 |
0.341 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275944 |
Ser3 |
sGVAVSDG |
|
|
| pmid |
sentence |
| 19329994 |
PKD1 regulates cofilin S3-phosphorylation|Both, oxidative stress as well as RhoA activation enhanced cofilin phosphorylation at S3, implicating an increased inhibition due to PKD1-mediated signalling events |
|
| Publications: |
1 |
| + |
PRKD1 | down-regulates
phosphorylation
|
RIN1 |
0.413 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-113960 |
Ser351 |
RPLLRSMsAAFCSLL |
Homo sapiens |
|
| pmid |
sentence |
| 11784866 |
Rin1 also binds to 14-3-3 proteins through a sequence including serine 351. Mutation of this residue abolished the 14-3-3 binding capacity of rin1 and led to more efficient blockade of ras-mediated transformation. The mutant protein, rin1(s351a), showed a shift in localization to the plasma membrane. Serine 351 is a substrate for protein kinase d (pkd [also known as pkcmu]) in vitro and in vivo. These data suggest that the normal localization and function of rin1, as well as its ability to compete with raf, are regulated in part by 14-3-3 binding, which in turn is controlled by pkd phosphorylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKD1 | up-regulates activity
phosphorylation
|
FAM83G |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264764 |
Ser356 |
YALVKAKsVDEIAKI |
Cricetulus griseus |
|
| pmid |
sentence |
| 32570757 |
Taken together, these data demonstrate that FAM83G S356 phosphorylation modulates HSP27 phosphorylation and apoptosis regulation and that HSP27 is a counterpart of FAM83G.|an active form of PKD1/PKCm could phosphorylate the FAM83G peptide, including the S356 portion.|We also demonstrated that the phosphorylation of the FAM83G S356 residue was required for the reduction of the live cell number, as the CHO cells were unaffected upon the overexpression of a FAM83G S356A mutant resistant to S356 phosphorylation. |
|
| Publications: |
1 |
Organism: |
Cricetulus Griseus |
| + |
PRKD1 | up-regulates activity
phosphorylation
|
RTKN |
0.364 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275511 |
Ser448 |
QALAKQGsLYHEMAI |
|
|
| pmid |
sentence |
| 22228765 |
Here, we show that rhotekin, an effector of RhoA GTPase, is a novel substrate of PKD. We identified Ser-435 in rhotekin as the potential site targeted by PKD in vivo. Expression of a phosphomimetic S435E rhotekin mutant resulted in an increase of endogenous active RhoA GTPase levels. Phosphorylation of rhotekin by PKD2 modulates the anchoring of the RhoA in the plasma membrane. |
|
| Publications: |
1 |
| + |
PRKD1 | up-regulates activity
phosphorylation
|
PAK4 |
0.255 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275930 |
Ser474 |
KEVPRRKsLVGTPYW |
|
|
| pmid |
sentence |
| 24840177 |
When PKD3 was knocked-down using isoform-specific shRNA (PKD3-shRNA), PAK4 activity (judged by its phosphorylation status at the activation loop using the pS474-PAK4 antibody) was decreased |
|
| Publications: |
1 |
| + |
PRKD1 | down-regulates
phosphorylation
|
HDAC5 |
0.532 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-198662 |
Ser498 |
RPLSRTQsSPLPQSP |
Homo sapiens |
|
| pmid |
sentence |
| 22865920 |
When phosphorylated by camk/pkd, class iia hdacs bind 14-3-3 chaperone proteins, which facilitates their nuclear export, thereby relieving hdac-mediated transcriptional repression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKD1 | up-regulates
phosphorylation
|
PTRH2 |
0.305 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-180085 |
Ser5 |
sLVMEYLA |
Homo sapiens |
|
| pmid |
sentence |
| 18703509 |
Overexpression of constitutively active pkd or pkd activation by treatment with phorbol 12-myristate 13-acetate results in phosphorylation of two serine residues (ser5 and ser87) in a form of bit1 that is confined to the cytoplasm and concomitantly increases the apoptotic activity of cytoplasmic bit1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-180089 |
Ser87 |
GKVAAQCsHAAVSAY |
Homo sapiens |
|
| pmid |
sentence |
| 18703509 |
Overexpression of constitutively active pkd or pkd activation by treatment with phorbol 12-myristate 13-acetate results in phosphorylation of two serine residues (ser5 and ser87) in a form of bit1 that is confined to the cytoplasm and concomitantly increases the apoptotic activity of cytoplasmic bit1 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKD1 |
phosphorylation
|
PRKD1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249046 |
Ser738 |
ARIIGEKsFRRSVVG |
in vitro |
|
| pmid |
sentence |
| 10867018 |
The last two autophosphorylation sites (Ser(744) and Ser(748)) are located in the activation loop but are only phosphorylated in the isolated PKD-catalytic domain and not in the full-length PKD; they may affect enzyme catalysis but are not involved in the activation of wild-type PKD by phorbol ester. | These results indicate that neither of the activation loop serines is involved in PDBu-induced activation but that they may be involved in catalysis or in maintaining the conformation of the enzyme prot |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249047 |
Ser742 |
GEKSFRRsVVGTPAY |
in vitro |
|
| pmid |
sentence |
| 10867018 |
The last two autophosphorylation sites (Ser(744) and Ser(748)) are located in the activation loop but are only phosphorylated in the isolated PKD-catalytic domain and not in the full-length PKD; they may affect enzyme catalysis but are not involved in the activation of wild-type PKD by phorbol ester. | These results indicate that neither of the activation loop serines is involved in PDBu-induced activation but that they may be involved in catalysis or in maintaining the conformation of the enzyme prot |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PRKCA | up-regulates
phosphorylation
|
PRKD1 |
0.421 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-66666 |
Ser738 |
ARIIGEKsFRRSVVG |
Homo sapiens |
|
| pmid |
sentence |
| 10197446 |
These results provide direct evidence that pkd becomes activated in vivo as a consequence of pkc-mediated phosphorylation of serines 744 and 748. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-66670 |
Ser742 |
GEKSFRRsVVGTPAY |
Homo sapiens |
|
| pmid |
sentence |
| 10197446 |
These results provide direct evidence that pkd becomes activated in vivo as a consequence of pkc-mediated phosphorylation of serines 744 and 748. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCH | up-regulates
phosphorylation
|
PRKD1 |
0.362 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-66730 |
Ser738 |
ARIIGEKsFRRSVVG |
Homo sapiens |
|
| pmid |
sentence |
| 10197446 |
These results provide direct evidence that pkd becomes activated in vivo as a consequence of pkc-mediated phosphorylation of serines 744 and 748. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-66734 |
Ser742 |
GEKSFRRsVVGTPAY |
Homo sapiens |
|
| pmid |
sentence |
| 10197446 |
These results provide direct evidence that pkd becomes activated in vivo as a consequence of pkc-mediated phosphorylation of serines 744 and 748. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCD | up-regulates
phosphorylation
|
PRKD1 |
0.273 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-123449 |
Ser738 |
ARIIGEKsFRRSVVG |
Homo sapiens |
|
| pmid |
sentence |
| 15024053 |
Here we show that activation of pkd in response to oxidative stress requires two sequential signaling events, i.e., phosphorylation of tyr463 by abl, which in turn promotes a second step, phosphorylation of the pkd activation loop (ser738/ser742). We show that this is mediated by pkcdelta (protein kinase cdelta) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-123453 |
Ser742 |
GEKSFRRsVVGTPAY |
Homo sapiens |
|
| pmid |
sentence |
| 15024053 |
Here we show that activation of pkd in response to oxidative stress requires two sequential signaling events, i.e., phosphorylation of tyr463 by abl, which in turn promotes a second step, phosphorylation of the pkd activation loop (ser738/ser742). We show that this is mediated by pkcdelta (protein kinase cdelta) |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PKA | up-regulates activity
phosphorylation
|
PRKD1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275925 |
Ser742 |
GEKSFRRsVVGTPAY |
|
|
| 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 |
| + |
PRKD1 | up-regulates activity
phosphorylation
|
PKD2 |
0.472 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259829 |
Ser801 |
SSLPRPMsSRSFPRS |
Homo sapiens |
HEK-293 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. Phosphorylation at this site was significantly increased in response to serum and epidermal growth factor stimulation.We confirmed previous studies showing that PC2 mediated Ca2+ release from the ER can be stimulated by ATP.Phosphorylation at Ser801 seems to be permissive for this activity without altering the subcellular localization nor homophilic and heterophilic (with PC1) interactions of wild-type PC2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKD1 | up-regulates
phosphorylation
|
TLR5 |
0.361 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-154473 |
Ser805 |
YQLMKHQsIRGFVQK |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 17442957 |
Pkd phosphorylated the tlr5-derived target peptide in vitro, and phosphorylation of the putative target serine 805 in hek 293t cell-derived tlr5 was identified by mass spectrometry. These results demonstrate that both pkd1 and pkd2 are required for inflammatory responses following tlr2, tlr4, or tlr5 activation, although pkd1 is more strongly involved |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKD1 |
phosphorylation
|
KIDINS220 |
0.534 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249052 |
Ser918 |
RTITRQMsFDLTKLL |
Rattus norvegicus |
|
| pmid |
sentence |
| 10998417 |
Our results provide the first physiological substrate for PKD and indicate that Kidins220 is phosphorylated by PKD at serine 919 in vivo. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PRKD1 | down-regulates
phosphorylation
|
SSH1 |
0.494 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173437 |
Ser937 |
SNLTRSSsSDSIHSV |
Homo sapiens |
|
| pmid |
sentence |
| 21525957 |
Phosphorylation of ser 402 impedes phosphatase activity of slingshot 1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186467 |
Ser937 |
SNLTRSSsSDSIHSV |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 19567672 |
Pkd-mediated phosphorylation of serines 937 and 978 regulates ssh1l subcellular localization by binding of 14-3-3 proteins 14-3-3 proteins associate with ssh1l when phosphorylated at serines 937 and 978, thereby sequestering ssh1l in the cytoplasm and preventing translocation of the phosphatase to f-actin_rich membrane protrusions |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186471 |
Ser978 |
SPLKRSHsLAKLGSL |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 19567672 |
Pkd-mediated phosphorylation of serines 937 and 978 regulates ssh1l subcellular localization by binding of 14-3-3 proteins 14-3-3 proteins associate with ssh1l when phosphorylated at serines 937 and 978, thereby sequestering ssh1l in the cytoplasm and preventing translocation of the phosphatase to f-actin_rich membrane protrusions |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PRKD1 | down-regulates activity
phosphorylation
|
SSH1 |
0.494 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275936 |
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 |
| + |
PRKD1 | up-regulates activity
phosphorylation
|
SSH1 |
0.494 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275939 |
Ser99 |
KLAVRLEsAWADRVR |
|
|
| pmid |
sentence |
| 23841590 |
Protein kinase D-mediated phosphorylation at Ser99 regulates localization of p21-activated kinase n 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). Phosphorylation of PAK4 at Ser99 also mediates binding to 14-3-3 protein, and is required for the formation of a PAK4-LIMK-PKD1 complex that regulates cofilin activity and directed cell migration| |
|
| Publications: |
1 |
| + |
PRKD1 | up-regulates
phosphorylation
|
CTNNB1 |
0.398 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183384 |
Thr112 |
EGMQIPStQFDAAHP |
Homo sapiens |
Prostate Gland Cancer Cell |
| pmid |
sentence |
| 19141652 |
This study provides evidence that pkd1 interacts with and phosphorylates beta-catenin at thr(112) and thr(120) we postulate that pkd1 phosphorylation is required to maintain _-catenin transcription activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183388 |
Thr120 |
QFDAAHPtNVQRLAE |
Homo sapiens |
Prostate Gland Cancer Cell |
| pmid |
sentence |
| 19141652 |
This study provides evidence that pkd1 interacts with and phosphorylates beta-catenin at thr(112) and thr(120) we postulate that pkd1 phosphorylation is required to maintain _-catenin transcription activity. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKD1 | down-regulates
phosphorylation
|
PIP4K2A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-145370 |
Thr376 |
KAAHAAKtVKHGAGA |
Homo sapiens |
|
| pmid |
sentence |
| 16563698 |
We conclude that the type ii pip kinases are physiological targets for pkd phosphorylation, and that this modification is likely to regulate inositol lipid turnover by inhibition of these lipid kinases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKD1 | up-regulates activity
phosphorylation
|
PPP1R14A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-123226 |
Thr38 |
QKRHARVtVKYDRRE |
Homo sapiens |
|
| pmid |
sentence |
| 32471307 |
A major kinase for GPCR‐induced CPI‐17 phosphorylation is PKC which is activated by the PLCbeta‐produced signaling messenger diacylglycerol (DAG). It phosphorylates CPI‐17 at Thr38 residue that directly docks at the active site of MLCP, thereby inhibiting its activity and promoting an increase of phosphorylation of myosin and of other MLCP.| CPI-17 can be also directly phosphorylated at Thr38 residue by MYPT1-associated kinase [222], by PAK, which is downstream of Rac and/or Cdc42 cascade [223], by Rho-associated coiled-coil kinase (ROCK) [224] and by PKN [225]. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249260 |
Thr38 |
QKRHARVtVKYDRRE |
Homo sapiens |
|
| pmid |
sentence |
| 32471307 |
A major kinase for GPCR‐induced CPI‐17 phosphorylation is PKC which is activated by the PLCbeta‐produced signaling messenger diacylglycerol (DAG). It phosphorylates CPI‐17 at Thr38 residue that directly docks at the active site of MLCP, thereby inhibiting its activity and promoting an increase of phosphorylation of myosin and of other MLCP. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
SRC | up-regulates activity
phosphorylation
|
PRKD1 |
0.421 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247320 |
Tyr432 |
KEGWMVHyTSKDTLR |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 12637538 |
Here we report that PKD is tyrosine-phosphorylated within the PH domain, leading to activation. This phosphorylation is mediated by a pathway that consists of the Src and Abl tyrosine kinases and occurs in response to stimulation with pervanadate and oxidative stress. Mutational analysis revealed three tyrosine phosphorylation sites (Tyr(432), Tyr(463), and Tyr(502)), which are regulated by the Src-Abl pathway, and phosphorylation of only one of these (Tyr(463)) leads to PKD activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247324 |
Tyr463 |
NDTGSRYyKEIPLSE |
Homo sapiens |
|
| pmid |
sentence |
| 12637538 |
Here we report that PKD is tyrosine-phosphorylated within the PH domain, leading to activation. This phosphorylation is mediated by a pathway that consists of the Src and Abl tyrosine kinases and occurs in response to stimulation with pervanadate and oxidative stress. Mutational analysis revealed three tyrosine phosphorylation sites (Tyr(432), Tyr(463), and Tyr(502)), which are regulated by the Src-Abl pathway, and phosphorylation of only one of these (Tyr(463)) leads to PKD activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247328 |
Tyr502 |
TTANVVYyVGENVVN |
Homo sapiens |
|
| pmid |
sentence |
| 12637538 |
Here we report that PKD is tyrosine-phosphorylated within the PH domain, leading to activation. This phosphorylation is mediated by a pathway that consists of the Src and Abl tyrosine kinases and occurs in response to stimulation with pervanadate and oxidative stress. Mutational analysis revealed three tyrosine phosphorylation sites (Tyr(432), Tyr(463), and Tyr(502)), which are regulated by the Src-Abl pathway, and phosphorylation of only one of these (Tyr(463)) leads to PKD activation. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
ABL1 |
phosphorylation
|
PRKD1 |
0.345 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246211 |
Tyr432 |
KEGWMVHyTSKDTLR |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 12637538 |
Here we report that PKD is tyrosine-phosphorylated within the PH domain, leading to activation. [..] Mutation of the other two sites, Tyr432 and Tyr502, had no significant influence on PKD activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246215 |
Tyr502 |
TTANVVYyVGENVVN |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 12637538 |
Here we report that PKD is tyrosine-phosphorylated within the PH domain, leading to activation. [..] Mutation of the other two sites, Tyr432 and Tyr502, had no significant influence on PKD activity. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ABL1 | up-regulates activity
phosphorylation
|
PRKD1 |
0.345 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251430 |
Tyr463 |
NDTGSRYyKEIPLSE |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 12637538 |
Abl Phosphorylates and Activates PKD through Tyr463 Phosphorylation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260791 |
Tyr463 |
NDTGSRYyKEIPLSE |
Homo sapiens |
|
| pmid |
sentence |
| 12637538 |
We show that Abl directly phosphorylates PKD at Tyr(463) in vitro, and in cells phosphorylation of this site is sufficient to mediate full activation of PKD |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ABL1 | up-regulates
phosphorylation
|
PRKD1 |
0.345 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-99255 |
Tyr463 |
NDTGSRYyKEIPLSE |
Homo sapiens |
|
| pmid |
sentence |
| 12637538 |
By using a phospho-specific antibody, we show that abl directly phosphorylates pkd at tyr(463) in vitro, and in cells phosphorylation of this site is sufficient to mediate full activation of pkd |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SRC | up-regulates
phosphorylation
|
PRKD1 |
0.421 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157716 |
Tyr95 |
KFPECGFyGMYDKIL |
Homo sapiens |
|
| pmid |
sentence |
| 17804414 |
Critical for the regulation of pkd1 activity in response to oxidative stress are src- and abl-mediated tyrosine phosphorylations that eventually lead to protein kinase cdelta (pkcdelta)-mediated activation of pkd1. our data suggest that pkd1 phosphorylation at tyr95 generates a binding motif for pkcdelta, and that oxidative stress-mediated pkcdelta/pkd interaction results in pkd1 activation loop phosphorylation and activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKD1 | up-regulates
phosphorylation
|
CDH1 |
0.463 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-133856 |
|
|
Homo sapiens |
Prostate Gland Cancer Cell |
| pmid |
sentence |
| 15695390 |
Our study has identified e-cadherin as a novel substrate of pkd1, and phosphorylation of e-cadherin by pkd1 is associated with increased cellular aggregation and decreased cellular motility in prostate cancer. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
YWHAQ | down-regulates 
|
PRKD1 |
0.332 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-65951 |
|
|
in vitro |
|
| pmid |
sentence |
| 10092600 |
14-3-3tau strongly down-regulates pkcmu kinase activity in vitro |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MAPK13 | down-regulates
phosphorylation
|
PRKD1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183280 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19135240 |
P38delta catalyzes an inhibitory phosphorylation of pkd1, thereby attenuating stimulated insulin secretion. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PRKD1
- 
- 