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Casein kinase 2, alpha 1 polypeptide

protein kinase CK2, CKII
Casein kinase II is a serine/threonine protein kinase that phosphorylates acidic proteins such as casein. The kinase exists as a tetramer and is composed of an alpha, an alpha-prime, and two beta subunits. The alpha subunits contain the catalytic activity while the beta subunits undergo autophosphorylation. The protein encoded by this gene represents the alpha subunit. While this gene is found on chromosome 20, a related transcribed pseudogene is found on chromosome 11. Three transcript variants encoding two different proteins have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, ACID, V1a, fibrillin-1, HAD
Papers using protein kinase CK2 antibodies
Cellular cofactors affecting hepatitis C virus infection and replication.
Garcia-Sastre Adolfo, In PLoS Pathogens, 2006
... The anti-human CKII α (A300-197A) and CKII α′ (A300-199A) purified rabbit polyclonal antibodies were obtained Bethyl Labs ...
Papers on protein kinase CK2
Surfactant Protein A Enhances Constitutive Immune Functions of Clathrin Heavy Chain and Clathrin Adaptor Protein AP2.
Stamme et al., Germany. In Am J Respir Cell Mol Biol, Feb 2016
Kinetic studies employing confocal microscopy, Western analysis, and immunomagnetic sorting revealed that SP-A transiently enhances the basal protein expression of CHC and α-adaptin depending on early activation of protein kinase CK2 and Akt1 in primary AMs from rats, SP-A+/+, and SP-A-/- mice as well as in vivo when intratracheally administered to SP-A+/+ mice.
Toward selective CK2alpha and CK2alpha' inhibitors: Development of a novel whole-cell kinase assay by Autodisplay of catalytic CK2alpha'.
Jose et al., Münster, Germany. In J Pharm Biomed Anal, Feb 2016
UNASSIGNED: Human protein kinase CK2 is an emerging target for the development of novel anti-cancer therapeutics.
Synthesis of novel polybrominated benzimidazole derivatives-potential CK2 inhibitors with anticancer and proapoptotic activity.
Bretner et al., Warsaw, Poland. In Bioorg Med Chem, Jan 2016
UNASSIGNED: The efficient method for the synthesis of novel cell permeable inhibitors of protein kinase CK2 with anticancer and proapoptotic activity has been developed.
Increased occurrence of protein kinase CK2 in astrocytes in Alzheimer's disease pathology.
Hoozemans et al., Amsterdam, Netherlands. In J Neuroinflammation, Dec 2015
BACKGROUND: Alzheimer's disease (AD) is the most common neurodegenerative disease.
Protein kinase CK2 in breast cancer: the CK2β regulatory subunit takes center stage in epithelial plasticity.
Cochet et al., Grenoble, France. In Cell Mol Life Sci, Sep 2015
Structurally, protein kinase CK2 consists of two catalytic subunits (α and α') and two regulatory subunits (β), which play a critical role in targeting specific CK2 substrates.
Protein kinase CK2 enables regulatory T cells to suppress excessive TH2 responses in vivo.
Bopp et al., Mainz, Germany. In Nat Immunol, Mar 2015
Through the use of Treg cell-specific gene targeting, we found that the suppression of allergic immune responses in the lungs mediated by T helper type 2 (TH2) cells was dependent on the activity of the protein kinase CK2.
Protein Kinase CK2 Expression Predicts Relapse Survival in ERα Dependent Breast Cancer, and Modulates ERα Expression in Vitro.
Williams et al., New Orleans, United States. In Int J Environ Res Public Health, 2014
The heterotetrameric protein kinase CK2 has been associated with oncogenic transformation, and our previous studies have shown that it may affect estrogenic signaling.
Emerging roles of protein kinase CK2 in abscisic acid signaling.
Riera et al., Barcelona, Spain. In Front Plant Sci, 2014
This review summarizes recent advances that taken together suggest a prominent role of protein kinase CK2 in ABA signaling and related processes.
Casein kinase: the triple meaning of a misnomer.
Pinna et al., In Biochem J, 2014
These fall into three main classes: two of them, later renamed as protein kinases CK1 (casein kinase 1, also known as CKI) and CK2 (also known as CKII), are pleiotropic members of the kinome functionally unrelated to casein, whereas G-CK, or genuine casein kinase, responsible for the phosphorylation of casein in the Golgi apparatus of the lactating mammary gland, has only been identified recently with Fam20C [family with sequence similarity 20C; also known as DMP-4 (dentin matrix protein-4)], a member of the four-jointed family of atypical protein kinases, being responsible for the phosphorylation of many secreted proteins.
Expanding roles of protein kinase CK2 in regulating plant growth and development.
Huq et al., Austin, United States. In J Exp Bot, 2014
Protein kinase CK2 (formerly known as casein kinase II) is a ubiquitious Ser/Thr kinase present in all eukaryotes.
Chemical proteomics and functional proteomics strategies for protein kinase inhibitor validation and protein kinase substrate identification: applications to protein kinase CK2.
Litchfield et al., London, Canada. In Biochim Biophys Acta, 2013
We utilized these strategies to evaluate small molecule inhibitors of protein kinase CK2, a constitutively active kinase that has recently emerged as target for anti-cancer therapy in clinical trials.
Recovery of RNA polymerase III transcription from the glycerol-repressed state: revisiting the role of protein kinase CK2 in Maf1 phosphoregulation.
Willis et al., United States. In J Biol Chem, 2012
Recovery of RNA polymerase III transcription from the glycerol-repressed state: revisiting the role of protein kinase CK2 in Maf1 phosphoregulation.
Low-density crystal packing of human protein kinase CK2 catalytic subunit in complex with resorufin or other ligands: a tool to study the unique hinge-region plasticity of the enzyme without packing bias.
Niefind et al., Köln, Germany. In Acta Crystallogr D Biol Crystallogr, 2012
analysis of crystal packing of human protein kinase CK2 catalytic subunit in complex with resorufin or other ligands
Protein kinase CK2 protects multiple myeloma cells from ER stress-induced apoptosis and from the cytotoxic effect of HSP90 inhibition through regulation of the unfolded protein response.
Piazza et al., Padova, Italy. In Clin Cancer Res, 2012
Results suggest CK2 as a novel regulator of the endoplasmic reticulum (ER) stress/unfolded protein response (UPR) cascades and HSP90 function in myeloma cells and offer the groundwork to design novel combination treatments for this disease.
Nucleocytoplasmic shuttling of human inositol phosphate multikinase is influenced by CK2 phosphorylation.
Mayr et al., Hamburg, Germany. In Biol Chem, 2012
Phosphorylation of S284 by protein kinase CK2 significantly decreases nuclear targeting of IPMK in HEK-293 cells.
Protein kinase CK2 localizes to sites of DNA double-strand break regulating the cellular response to DNA damage.
Guerra et al., Odense, Denmark. In Bmc Mol Biol, 2011
Protein kinase CK2 co-localizes with gamma-H2AX to sites of genetic lesions and modulation of its expression levels affects the cellular DNA damage response.
Protein kinase CK2 links extracellular growth factor signaling with the control of p27(Kip1) stability in the heart.
von Harsdorf et al., Toronto, Canada. In Nat Med, 2008
Here we show that angiotensin II, a major cardiac growth factor, induces the proteasomal degradation of p27 through protein kinase CK2-alpha'-dependent phosphorylation.
The reverse in-gel kinase assay to profile physiological kinase substrates.
Bieberich et al., Baltimore, United States. In Nat Methods, 2007
Using the alpha catalytic subunit of protein kinase CK2 (CK2alpha) as a paradigm, we developed an in-gel method to facilitate identification of physiologic kinase substrates.
The protein kinase CK2 facilitates repair of chromosomal DNA single-strand breaks.
Caldecott et al., Brighton, United Kingdom. In Cell, 2004
CK2 was the first protein kinase identified and is required for the proliferation and survival of mammalian cells.
CDC5 and CKII control adaptation to the yeast DNA damage checkpoint.
Hartwell et al., Seattle, United States. In Cell, 1997
A single double-stranded DNA (dsDNA) break will cause yeast cells to arrest in G2/M at the DNA damage checkpoint.
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