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CAMK1D/CKLiK  Protéine

All CAMK1D Reagents

Hôte d’expression: Baculovirus-Insect Cells  
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10728-H09B-50
10728-H09B-20
50 µg 
20 µg 
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CAMK1D/CKLiK Voies apparentées

CAMK1D/CKLiK Récapitulatif et informations sur les protéines

CAMK1D/CKLiK Fond

Résumé du gène: This gene encodes a member of the Ca2+/calmodulin-dependent protein kinase 1 subfamily of serine/threonine kinases. The encoded protein may be involved in the regulation of granulocyte function through the chemokine signal transduction pathway. Alternatively spliced transcript variants encoding different isoforms of this gene have been described
General information above from NCBI
Activité catalytique: ATP + a protein = ADP + a phosphoprotein.
Régulation enzymatique: 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.
Domaine: 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).
Localisation subcellulaire: Cytoplasm (Probable). Nucleus (Probable). Note=Predominantly cytoplasmic. Nuclear localization increases upon activation by KCl treatment in hippocampal neurons.
Spécificité tissulaire: Widely expressed. Highly and mostly expressed in polymorphonuclear leukocytes (neutrophilic and eosinophilic granulocytes) while little or no expression is observed in monocytes and lymphocytes.
Stade de développement: 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.
Similarité de séquence: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily.
Contains 1 protein kinase domain.C
General information above from UniProt

Calcium/calmodulin-dependent protein kinase or CaM kinases are serine/threonine-specific protein kinases that are primarily regulated by the Calcium/calmodulin complex. These kinases show a memory effect on activation. CaM kinases activity can outlast the intracellular calcium transient that is needed to activate it. In neurons, this property is important for the induction of synaptic plasticity. Pharmacological inhibition of CaM kinases II blocks the induction of long-term potentiation. Upon activation, CaM kinases II phosphorylates postsynaptic glutamate receptors and changes the electrical properties of the synapse.

Calcium/calmodulin-dependent protein kinase type 1D, also known as CaM kinase I delta, CaM kinase ID, CaMKI-like protein kinase, CKLiK and CAMK1D, is a member of the protein kinase superfamily and CaMK subfamily. It contains one protein kinase domain. CAMK1D is broadly expressed. It is highly and mostly expressed in polymorphonuclear leukocytes (neutrophilic and eosinophilic granulocytes) while little or no expression is observed in monocytes and lymphocytes. Engineered overexpression of CAMK1D in non-tumorigenic breast epithelial cells led to increased cell proliferation, and molecular and phenotypic alterations indicative of epithelial-mesenchymal transition (EMT), including loss of cell-cell adhesions and increased cell migration and invasion. CAMK1D is a potential therapeutic target with particular relevance to clinically unfavorable basal-like tumors.

CAMK1D/CKLiK Autre dénomination

CKLiK,CaM-K1,CaMKID, [homo-sapiens]
RP11-462F15.1,CaM-K1,CAMK1D,CaMKID,CKLiK, [human]
E030025C11Rik,A630059D12Rik,Camk1d,CaMKIdelta,CKLiK,RP23-340A13.1, [mouse]
CKLiK,mCKLiK,CaMKIdelta,A630059D12Rik,E030025C11Rik, [mus-musculus]

CAMK1D/CKLiK Études apparentées

  • Lisman, JE. et al., 1985, Proc Natl Acad Sci USA. 82 (9): 3055-7.
  • Bergamaschi, A. et al., 2008, Mol Oncol. 2 (4): 327-39.
  • White RB. et al., 2008, Physiological genomics, 33 (1): 41-9.
  • Schleinitz, D. et al., 2010, Horm Metab Res. 42 (1): 14-22.
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