Text Size:AAA

CAMKI/CAMK1  Protein, Antibody, ELISA Kit, cDNA Clone

Expression host: E. coli  
50 µg 
20 µg 
Add to Cart
  • Slide 1

CAMKI/CAMK1 Related Area

CAMKI/CAMK1 Related Pathways

CAMKI/CAMK1 Related Protein, Antibody, cDNA Gene, and ELISA Kits

CAMKI/CAMK1 Related Protein, Antibody, cDNA Gene, and ELISA Kits

Featured Reagent Products

CAMKI/CAMK1 Summary & Protein Information

CAMKI/CAMK1 Background

Catalytic activity: ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation: ENZYME REGULATION: Activated by Ca(2+)/calmodulin. Binding of calmodulin results in conformational change that relieves intrasteric autoinhibition and allows phosphorylation of Thr-177 within the activation loop by CaMKK1 or CaMKK2. Phosphorylation of Thr-177 results in several fold increase in total activity. Unlike CaMK4, is unable to exhibit autonomous activity after Ca(2+)/calmodulin activation. {ECO:0000269|PubMed:23028635, ECO:0000269|PubMed:7641687}.
Subunit structure: Monomer. Interacts with XPO1 (By similarity). Interacts with MARK2, ARHGEF7/BETAPIX and GIT1. {ECO:0000250, ECO:0000269|PubMed:17442826, ECO:0000269|PubMed:18184567}.
Domain: The autoinhibitory domain overlaps with the calmodulin binding region and interacts in the inactive folded state with the catalytic domain as a pseudosubstrate. {ECO:0000269|PubMed:23028635}.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominantly cytoplasmic. {ECO:0000250}.
Tissue specificity: Widely expressed. Expressed in cells of the zona glomerulosa of the adrenal cortex. {ECO:0000269|PubMed:12193581, ECO:0000269|PubMed:17056143}.
Post-translational: Phosphorylated by CaMKK1 and CaMKK2 on Thr-177. {ECO:0000269|PubMed:11395482, ECO:0000269|PubMed:7641687, ECO:0000269|PubMed:9662074}.; Polybiquitinated by the E3 ubiquitin-protein ligase complex SCF(FBXL12), leading to proteasomal degradation. {ECO:0000269|PubMed:23707388}.
Sequence similarity: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily. {ECO:0000305}.; Contains 1 protein kinase domain. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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.

CAMKI/CAMK1 Alternative Name

CAMKI, [homo-sapiens]
caM-KI,CAMK1,CAMKI,caMKI-alpha,MGC120317,MGC120318, [human]
AI505105,Camk1,caM-KI,CaMKIalpha,caMKI-alpha,D6Ertd263e, [mouse]
AI505105,CaMKIalpha,D6Ertd263e, [mus-musculus]

CAMKI/CAMK1 Related Studies

  • 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.