Protein Domain : IPR000756

Type:  Domain Name:  Diacylglycerol kinase, accessory domain
Description:  Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity []:Serine/threonine-protein kinasesTyrosine-protein kinasesDual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)Protein kinase function is evolutionarily conserved from Escherichia coli to human []. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation []. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [].Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. The DAG kinase domain is assumed to be an accessory domain. Upon cell stimulation, DAG kinase converts DAG into phosphatidate, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity. It catalyses the reaction: ATP + 1,2-diacylglycerol = ADP +1,2-diacylglycerol 3-phosphate. The enzyme is stimulated by calcium and phosphatidylserine and phosphorylated by protein kinase C. This domain is always associated with . Short Name:  Diacylglycerol_kin_accessory

0 Child Features

0 Contains

2 Cross Referencess


1 Found In

DB identifier Type Name
IPR016961 Family Diacylglycerol kinase, plant

2 GO Annotations

GO Term Gene Name Organism
GO:0004143 IPR000756
GO:0007205 IPR000756

0 Parent Features

1185 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
439175 D8R0Y4 PAC:15421748 Selaginella moellendorffii 446  
90522 D8RD89 PAC:15413342 Selaginella moellendorffii 719  
110542 D8S7I3 PAC:15408151 Selaginella moellendorffii 455  
115839 D8SFW2 PAC:15402741 Selaginella moellendorffii 496  
evm.model.supercontig_12.23 PAC:16406781 Carica papaya 159  
evm.model.supercontig_34.77 PAC:16418025 Carica papaya 249  
evm.model.supercontig_34.78 PAC:16418026 Carica papaya 490  
evm.model.supercontig_3663.1 PAC:16418527 Carica papaya 93  
evm.model.supercontig_37.51 PAC:16418724 Carica papaya 299  
evm.model.supercontig_450.4 PAC:16420345 Carica papaya 487  
evm.model.supercontig_94.22 PAC:16428758 Carica papaya 585  
29749.m000143 B9T0H8 PAC:16807791 Ricinus communis 484  
29983.m003279 B9RW81 PAC:16815044 Ricinus communis 490  
30027.m000834 B9SIF7 PAC:16815927 Ricinus communis 526  
30138.m004002 B9RLR5 PAC:16819368 Ricinus communis 724  
Cucsa.063780.1 PAC:16955011 Cucumis sativus 485  
Cucsa.074390.1 PAC:16955635 Cucumis sativus 478  
Cucsa.074390.2 PAC:16955636 Cucumis sativus 478  
Cucsa.089460.1 A0A0A0LK87 PAC:16957147 Cucumis sativus 493  
Cucsa.113110.1 A0A0A0LSU0 PAC:16960277 Cucumis sativus 731  
Cucsa.119630.1 A0A0A0KG08 PAC:16961008 Cucumis sativus 486  
Cucsa.119630.2 PAC:16961009 Cucumis sativus 389  
Cucsa.119630.3 PAC:16961010 Cucumis sativus 384  
GSVIVT01011328001 PAC:17823211 Vitis vinifera 215  
GSVIVT01007909001 D7SI39 PAC:17820611 Vitis vinifera 731  
GSVIVT01013349001 D7UD84 PAC:17824627 Vitis vinifera 125  
GSVIVT01029102001 PAC:17836031 Vitis vinifera 477  
GSVIVT01003084001 D7TG44 PAC:17818265 Vitis vinifera 91  
GSVIVT01003089001 D7TG48 PAC:17818269 Vitis vinifera 226  
GSVIVT01003096001 PAC:17818272 Vitis vinifera 225  

5 Publications

First Author Title Year Journal Volume Pages PubMed ID