ID:KCC1D_HUMAN DESCRIPTION: RecName: Full=Calcium/calmodulin-dependent protein kinase type 1D; EC=2.7.11.17; AltName: Full=CaM kinase I delta; Short=CaM kinase ID; Short=CaM-KI delta; Short=CaMKI delta; Short=CaMKID; AltName: Full=CaMKI-like protein kinase; Short=CKLiK; FUNCTION: Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK1 signaling cascade and, upon calcium influx, activates CREB-dependent gene transcription, regulates calcium-mediated granulocyte function and respiratory burst and basal dendritic growth of hippocampal neurons. In neutrophil cells, required for cytokine-induced proliferative responses and activation of the respiratory burst. Phosphorylates the transcription activator CREB1 on 'Ser-133' in hippocampal neuron nuclei. May play a role in apoptosis of erythroleukemia cells. In vitro, phosphorylates transcription factor CREM isoform Beta. CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. ENZYME REGULATION: Activated by Ca(2+)/calmodulin. Binding of calmodulin results in conformational change that relieves intrasteric autoinhibition and allows phosphorylation of Thr-180 within the activation loop by CaMKK1 or CaMKK2. Phosphorylation of Thr-180 results in several fold increase in total activity. Unlike CaMK4, may be unable to exhibit autonomous activity after Ca(2+)/calmodulin activation. SUBCELLULAR LOCATION: Cytoplasm (Probable). Nucleus (Probable). Note=Predominantly cytoplasmic. Nuclear localization increases upon activation by KCl treatment in hippocampal neurons. TISSUE SPECIFICITY: Widely expressed. Highly and mostly expressed in polymorphonuclear leukocytes (neutrophilic and eosinophilic granulocytes) while little or no expression is observed in monocytes and lymphocytes. DEVELOPMENTAL STAGE: Expressed during hippocampal formation with high expression in the pyramidal cell layers. INDUCTION: Expression increases upon treatment of EC cells with DMSO and retinoic acid. Induced by KCL in PC12 cells. DOMAIN: The autoinhibitory domain overlaps with the calmodulin binding region and interacts in the inactive folded state with the catalytic domain as a pseudosubstrate (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily. SIMILARITY: Contains 1 protein kinase domain.
ModBase Predicted Comparative 3D Structure on Q8IU85
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