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Validated All-in-One™ qPCR Primer for CSNK2A1(NM_001895.3) Search again
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
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].
Gene References into function
- uPA-dependent VSMC adhesion is a function of selective Vn phosphorylation by the ectoprotein kinase CK2
- Generation of mutants of CK2alpha which are dependent on the beta-subunit for catalytic activity
- HIV-1 Rev transactivator: a beta-subunit directed substrate and effector of protein kinase CK2
- Protein kinase CK2: signaling and tumorigenesis in the mammary gland.
- Response of cancer cells to molecular interruption of the CK2 signal.
- Functional specialization of CK2 isoforms and characterization of isoform-specific binding partners
- Characterization of CK2 holoenzyme variants with regard to crystallization
- Transcriptional coordination of the genes encoding catalytic (CK2alpha) and regulatory (CK2beta) subunits of human protein kinase CK2.
- Consequences of CK2 signaling to the nuclear matrix.
- Localization of individual subunits of protein kinase CK2 to the endoplasmic reticulum and to the Golgi apparatus
- Interactions between protein kinase CK2 and Pin1. Evidence for phosphorylation-dependent interactions.
- Unique activation mechanism of protein kinase CK2. The N-terminal segment is essential for constitutive activity of the catalytic subunit but not of the holoenzyme
- Protein kinase CK2 dependent phosphorylation of the E2 ubiquitin conjugating enzyme UBC3B induces its interaction with beta-TRCp and enhances beta-catenin degradation [UBC3B]
- FGF-1 binds to both the catalytic alpha-subunit and to the regulatory beta-subunit of CK2. FGF-1 & CK2 alpha are shown to interact in vivo. A correlation between the mitogenic potential of FGF-1 mutants & their ability to bind to CK2 alpha was observed.
- Data point to a particular role of the catalytic alpha and alpha' subunits of protein kinase CK2, which may be different from their roles in the holoenzyme.
- This protein is associated with the COP9 signalosome.
- HSF1 activation by heat is correlated with the thermal activation of nuclear CK2 and overexpression of CK2 activates HSF1
- results indicate that protein kinase CKII may control IkappaBalpha and p27Kip1 degradation and thereby G1/S phase transition through the phosphorylation of threonine 10 within CKBBP1 protein
- Crystal structure of a C-terminal deletion mutant of human protein kinase CK2 catalytic subunit
- Evaluation of different pathways involved in death signaling suggest that the regulation of a critical proapoptotic step in HuH-7 cells by CK2alpha" is mediated by a JNK signaling cascade.
- structure activity relationship: the PA 382-384 mutant exhibits an increased thermal and proteolytic stability
- might play an important role in vivo in regulating the function and transport activity of ABCA1 and possibly of other members of the ABCA subfamily
- Utilizing a kinase-driven assay biochemical purification, the authors identified casein kinase II (CKII) from HeLa cell nuclear extract as a cellular phosphoprotein pp32 kinase.
- CK2 acts as an inhibitor of Cdk5 in the brain
- Involvement of ubiquitous protein kinase CK2 in angiogenesis. Naturally derived CK2 inhibitors may be useful for treatment of proliferative retinopathies.
- CK2 regulates the DNA-binding ability of SSRP1 and that this regulation may be responsive to specific cell stresses.
- Data demonstrate that CK2alpha possesses sophisticated structural adaptations in favour of dual-cosubstrate specificity.
- constitutive phosphorylation by CK2 may be required for maximal activation of Akt/PKB
- CK2 may have the capacity to differentially regulate U1 and U6 transcription even though SNAP(C) is universally utilized for human snRNA gene transcription
- multiple kinases, including CK2 and GSK3beta, participate in PTEN phosphorylation and GSK3beta may provide feedback regulation of PTEN
- Protein kinase CK2 is characterized by an extremely high stability that might be due to its association with other intracellular proteins, enhanced half-life or lower vulnerability towards proteolytic degradation.
- protein kinase CK2 is inactive in CCVs because of the fact that it is bound to the clathrin-coated vesicle (CCV) membrane via an interaction between phosphatidylinositol 4,5-bisphosphate in the CCV membrane and the active site in CK2
- In vitro phosphorylation of eIF2beta also pointed to Ser2 as a preferred site for CK2 phosphorylation
- CK2 may be involved in the regulation of cell cycle progression by associating with and phosphorylating a key molecule for translation initiation.
- casein kinase 2 induces PACS-1 binding of nephrocystin and targeting to cilia
- CK2 is potentially a highly plausible target for cancer therapy.
- phosphorylation of the (T300) residue is dependent on CK2 and is a necessary and functional prerequisite for TSPY's transport into the nucleus
- Dynamics of nucleolar reformation is ATP/GTP-dependent, sensitive to temperature, and creatin kinase-2 driven.
- CK2 regulates NKX3-1 in prostate cells.
- Based on its retinal localization, CK2 may be considered a new immunohistochemical astrocytic marker, and combination of CK2 inhibitors and octreotide may be a promising future treatment for proliferative retinopathies.
- role of CK2beta for cell survival and might allow the design of novel proapoptotic agents targeting this protein
- CK2 activity in Chinese Hamster Ovary (CHO) cells is entirely accounted for by the holoenzyme.
- v-Src-dependent down-regulation of the Ste20-like kinase SLK through casein kinase II.
- These studies suggested that CK2 might regulate SAG-SCF E3 ligase activity through modulating SAG's stability, rather than its enzymatic activity directly.
- CK2 has the potential to regulate Pol I transcription at multiple levels, in preinitiation complex (PIC) formation, activation, and reinitiation of transcription.
- CK2 plays an active role in NF-kappaB signaling in intestinal epithelial cell lines and may represent a possible target for intervention.
- CK2-site phosphorylation of p53 is induced in DeltaNp63 expressing basal stem cells in UVB irradiated human skin
- CK2 is required for the assembly and cycling of Wnt-enhancer complexes in vivo.
- findings demonstrate that the pleiotropic protein kinase CK2 binds wild-type CFTR near F508 and phosphorylates nucleotide-binding domain 1 at Ser-511 in vivo and that mutation of Ser-511 disrupts CFTR channel gating
- Results describe the 1.6 A resolution crystal structure of a fully active C-terminal deletion mutant of human CK2alpha liganded by two sulfate ions, and compare this structure systematically with representative structures of related CMGC kinases.
- extracellular phosphorylation of collagen XVII by ecto-CK2 inhibits its shedding by TACE and represents novel mechanism to regulate adhesion and motility of epithelial cells
- Suggest a novel role of CK2 in breast cancer resistance to antiestrogens.
- cytotoxic adaptor function of NS1 was confirmed with fusion peptides, where the tropomyosin-binding domain of NS1 and CKIIalpha are physically linked
- CK2 phosphorylation triggers an allosteric inhibition of the SNAP190 Myb DNA binding domain
- EB2-mediated production of infectious EBV virions is regulated by CK2 phosphorylation at one or more of the serine residues Ser-55, -56, and -57
- ABC50 N-terminal region interacts with eukaryotic initiation factor eIF2 and is a target for regulatory phosphorylation by CK2
- The number of predicted CK2 sites correlated with the degree of in vitro and in vivo phosphorylation of NS5A by CK2. CK2-dependent phosphorylation of NS5A is heterogeneous among different HCV genotypes and clinical isolates.
- CK2 may be a key mediator for HDAC1 and HDAC2 activation under hypoxia in tumor cells
- splicing activity is significantly influenced by the CK2-hPrp3p interaction
- Human herpesvirus 6Binduces p53 Ser392 phosphorylation by an atypical pathway independent of CK2 protein and p38 kinases.
- The complex structure between a C-terminal deletion mutant of human CK2alpha and the ATP-competitive inhibitor emodin is studies in comparison with with a previously published complex structure of emodin and maize CK2alpha.
- CK2-mediated phosphorylation of TRF1 plays an important role in modulating telomere length homeostasis by determining the levels of TRF1 at telomeres
- Protease activated receptor 1 activation of platelet is associated with an increase in protein kinase CK2 activity
- CK2 is tightly associated with TAFII250 and is the principal activity responsible for TAFII250-mediated phosphorylation of Mdm2.
- Studies in yeast and in human cells demonstrate that the different forms of CK2 interact with a large number of cellular proteins.
- Transcript amounts of the subunits CK2alpha and CK2beta and holoenzyme CK2 activity in 34 muscle biopsies of human patients with different muscle pathologies, were determined.
- CK2 involvement in the phenomenon of the drug resistance was investigated.
- Casein kinase II activity is increased by the binding of haptoglobin 1-1-hemoglobin to CD163.
- CK2 activity was investigated both in vitro and in cultured cells by using anti-[pSer13]-Cdc37 antibody.
- These data identify a key post-translational mechanism that controls PML protein levels in cancer cells and suggest that CK2 inhibitors may be beneficial anti-cancer drugs.
- These results suggest that one of the modes of CK2-mediated modulation of apoptotic activity is via its impact on cellular inhibitors of apoptosis proteins.
- A crystal of a C-terminally truncated variant of human CK2alpha to which two molecules of the inhibitor 5,6-dichloro-1-beta-D-ribo-furanosyl-benzimidazole (DRB) are bound, is analyzsed.
- CK2 binds to the NHE3 C terminus and stimulates basal NHE3 activity by phosphorylating a separate single site on the NHE3 C terminus
- CK2 may be involved in the regulation of cell cycle progression through the phosphorylation of a key molecule for translation initiation and of nuclear substrates upon activation of CK2 by itself.
- CK2 catalyzes the phosphorylation of tyrosine residues in mammalian cells.
- KIF5C, a member of the kinesin 1 heavy chain family, is a substrate for protein kinase CK2.
- InsP(6) specifically binds to CK2alpha and disrupts the interaction between CK2alpha and Nopp140 with an IC(50) value of 25 microM, thereby attenuating the Nopp140-mediated repression of CK2 activity.
- study presents unbound three-dimensional structure of a CK2beta construct that is fully capable of CK2alpha recruitment and quantify its affinity to CK2alpha thermodynamically
- DNA methylation-dependent down-regulation of transcription factors Sp1, Ets1 and NF-kappaB might be involved in silencing of the CKII alpha and CKII alpha' genes during cellular senescence.
- PrP protein can bind to protein kinase CK2 both in native and recombinant forms in vitro.
- Using shotgun mass spectrometry, we found this protein differentially expressed in the dorsolateral prefrontal cortex from patients with schizophrenia.
