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

발현 숙주: E. coli  
50 µg 
20 µg 
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CAMKI/CAMK1 Related Area


CAMKI/CAMK1 요약 및 단백질 정보


유전자 요약: Calcium/calmodulin-dependent protein kinase I is expressed in many tissues and is a component of a calmodulin-dependent protein kinase cascade. Calcium/calmodulin directly activates calcium/calmodulin-dependent protein kinase I by binding to the enzyme and indirectly promotes the phosphorylation and synergistic activation of the enzyme by calcium/calmodulin-dependent protein kinase I kinase.
General information above from NCBI
촉매 활성: ATP + a protein = ADP + a phosphoprotein.
효소 조절: 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}.
하부단위 구조: Monomer. Interacts with XPO1 (By similarity). Interacts with MARK2, ARHGEF7/BETAPIX and GIT1. {ECO:0000250, ECO:0000269|PubMed:17442826, ECO:0000269|PubMed:18184567}.
도메인: 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}.
세포하 위치: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominantly cytoplasmic. {ECO:0000250}.
조직 특이성: Widely expressed. Expressed in cells of the zona glomerulosa of the adrenal cortex. {ECO:0000269|PubMed:12193581, ECO:0000269|PubMed:17056143}.
번역 후: 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}.
염기서열 유사성: 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, [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]


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  • 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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