| + | 
              
              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
               | 
              HDAC7 | 
              
              0.438 | 
                    
						
							
								
									| 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 | down-regulates activity   
              phosphorylation
               | 
              SET | 
              
              0.2 | 
                    
						
							
								
									| Identifier | 
									Residue | 
									Sequence | 
									Organism | 
									Cell Line | 
								 
							
								
								
									| SIGNOR-279560 | 
									Ser171 | 
									S-->I | 
									Homo sapiens | 
									 | 
								
								 
									| pmid | 
									sentence | 
								 
								 
									| 23251465 | 
								
									In conclusion, the roles of protein kinase D2 and its substrate SET in T cell activation were investigated and we found that protein kinase D2 phosphorylates Ser171 of SET, which resulted in the reduction of its inhibitory effect on PP2A phosphatase activity. | 
								 
						 
                     | 
              
               
			   
					| Publications: | 
					
				
					1 | 
					Organism: | 
							Homo Sapiens | 
				
              | + | 
              
              PRKD2 | up-regulates activity   
              phosphorylation
               | 
              HDAC5 | 
              
              0.295 | 
                    
						
							
								
									| 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 | 
				
              | + | 
              
              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 | 
				
              | + | 
              
              PRKCA | up-regulates activity   
              phosphorylation
               | 
              PRKD2 | 
              
              0.392 | 
                    
						
							
								
									| 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 | 
				
              | + | 
              
              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 | 
				
              | + | 
              
              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 | 
				
              | + | 
              
              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 | 
              
              0.293 | 
                    
						
							
								
									| 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 | 
              
              0.293 | 
                    
						
							
								
									| 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 | 
				
              | + | 
              
              PRKD2 | down-regulates activity   
              phosphorylation
               | 
              BCL6 | 
              
              0.2 | 
                    
						
							
								
									| Identifier | 
									Residue | 
									Sequence | 
									Organism | 
									Cell Line | 
								 
							
								
								
									| SIGNOR-279651 | 
									 | 
									 | 
									Homo sapiens | 
									 | 
								
								 
									| pmid | 
									sentence | 
								 
								 
									| 31980486 | 
								
									Prkd2 directly binds to Bcl6 and Prkd2-dependent phosphorylation of Bcl6 is necessary to constrain Bcl6 to the cytoplasm, thereby limiting TFH development. | 
								 
						 
                     | 
              
               
			   
					| Publications: | 
					
				
					1 | 
					Organism: | 
							Homo Sapiens |