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CaM Kinase 4/CaMKIV  タンパク質

All CAMK4 Reagents

発現宿主: Baculovirus-Insect Cells  
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10664-H09B-20
10664-H09B-50
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発現宿主: Baculovirus-Insect Cells  
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50838-M20B-20
50838-M20B-50
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発現宿主: Baculovirus-Insect Cells  
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50838-MNCB-20
50838-MNCB-50
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CaM Kinase 4/CaMKIV 関連経路

CaM Kinase 4/CaMKIV サマリー & タンパク質情報

CaM Kinase 4/CaMKIV 背景

遺伝子の概要: The product of this gene belongs to the serine/threonine protein kinase family, and to the Ca(2+)/calmodulin-dependent protein kinase subfamily. This enzyme is a multifunctional serine/threonine protein kinase with limited tissue distribution, that has been implicated in transcriptional regulation in lymphocytes, neurons and male germ cells.
General information above from NCBI
触媒活性: ATP + a protein = ADP + a phosphoprotein.
酵素調節: Activated by Ca(2+)/calmodulin. Binding of calmodulin results in conformational change that relieves intrasteric autoinhibition and allows phosphorylation of Thr-200 within the activation loop by CaMKK1 or CaMKK2. Phosphorylation of Thr-200 results in a 10-20-fold increase in total activity to generate Ca(2+)/calmodulin-independent activity. Autophosphorylation of the N-terminus Ser-12 and Ser-13 is required for full activation. Inactivated by protein phosphatase 2A (PPP2CA/PPP2CB) which dephosphorylates Thr-200, thereby terminating autonomous activity and helping to maintain the enzyme in its autoinhibited state.
サブユニット構造: Monomer (By similarity). Interacts with protein phosphatase 2A (PPP2CA/PPP2CB); the interaction is mutually exclusive with binding to Ca(2+)/calmodulin.
ドメイン: The autoinhibitory domain overlaps with the calmodulin binding region and interacts in the inactive folded state with the catalytic domain as a pseudosubstrate.
細胞内位置: Cytoplasm. Nucleus. Note=Localized in hippocampal neuron nuclei. In spermatids, associated with chromatin and nuclear matrix (By similarity).
組織特異性: Expressed in brain, thymus, CD4 T-cells, testis and epithelial ovarian cancer tissue.
発生段階: Expressed during differentiation of monocyte- derived dendritic cells (at protein level).
翻訳後: Phosphorylated by CaMKK1 and CaMKK2 on Thr-200. Dephosphorylated by protein phosphatase 2A. Autophosphorylated on Ser-12 and Ser-13.
Glycosylation at Ser-189 modulates the phosphorylation of CaMK4 at Thr-200 and negatively regulates its activity toward CREB1 in basal conditions and during early inomycin stimulation.
シーケンスの類似性: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily.
Contains 1 protein kinase domain.
General information above from UniProt

Ca2+/ calmodulin-dependent protein kinase 4 (CAMKⅣ) belongs to the serine/threonine protein kinase family, and to the Ca2+/calmodulin-dependent protein kinase subfamily which is widely recognized as an essential enzyme implicated in the phophoinositide amplification cascade. Ca2+/calmodulin dependent protein kinase (CAMK) can be activated by the introcellular increased Ca2+ and then apt to combine with the target protein. Ca2+/ calmodulin-dependent protein kinase 4 (CAMKⅣ) is a multifunctional CaM-dependent kinase protein with limited tissue distribution, that has been implicated in transcriptional regulation in lymphocytes, neurons and male germ cells. All of the isforms of this family, including myosin light chain kinase, phosphorylase kinase, CaMK1, CaMKⅢ and CaMKⅣ have EF-hand structure.

CaM Kinase 4/CaMKIV 代替名

CAMK,IV,CaMKIV,CaMK-GR, [homo-sapiens]
caMK,CaMK IV,CaMK-GR,CAMK4,IV,MGC36771, [human]
A430110E23Rik,Camk4,CaMKIV,CaMKIV/Gr,AI666733,caMK IV,D18Bwg0362e, [mouse]
CaMKIV,AI666733,CaMKIV/Gr,D18Bwg0362e,A430110E23Rik, [mus-musculus]

CaM Kinase 4/CaMKIV 関連研究

  • Feliciano DM, et al. (2009) Repression of Ca2+/calmodulin-dependent protein kinase IV signaling accelerates retinoic acid-induced differentiation of human neuroblastoma cells. J Biol Chem. 284 (39): 26466-81.
  • Zhao X, et al. (2001). The modular nature of histone deacetylase HDAC4 confers phosphorylation-dependent intracellular trafficking. J Biol Chem. 276 (37): 35042-8.
  • Racioppi L, et al. (2008) Calcium/calmodulin-dependent kinase IV in immune and inflammatory responses: novel routes for an ancient traveller.
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