CK2, CKII, CK2β, And, Andante
0.946 (longest cDNA)
Tetramer of two alpha and two beta subunits.
Phosphorylated by alpha subunit.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\CkIIβ using the Feature Mapper tool.
GBrowse - Visual display of RNA-Seq signalsView Dmel\CkIIβ in GBrowse 2
Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see GBrowse for alignment of the cDNAs and ESTs to the gene model.
For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.
Source for merge of: CkIIβ mbu
The 'Andante' mutant chromosome carries two independent EMS-induced mutations, one in dy (dyQ189stop) and one in CkIIβ (CkIIβAnd). The dyQ189stop mutation has no effect on rhythmicity, rather the CkIIβAnd allele is responsible for the circadian long-period phenotype of the mutant chromosome.
Splice isoforms CkIIβ-VIIc and -VIId are dispensable for viability and for formation of normal mushroom bodies.
dsRNA made from templates generated with primers directed against this gene tested in RNAi screen for effects on Kc167 and S2R+ cell morphology.
The number of neurons forming the adult mushroom body is greatly reduced in CkIIβ hypomorphs.
Casein kinase II specifically phosphorylates a set of serine residues within the cact PEST domain.
Casein kinase II phosphorylates Ser468 (a residue in the PEST domain) of cact in vitro.
Genetic mosaic analysis identifies the tissues that require the CkIIβ product.
Serine 2 and Serine 4 residues are major sites of autophosphorylation of the β subunit of casein kinase (as shown by the construction of A2 and A4 mutants in vitro). Autophosphorylation of this subunit reduces the phosphorylation of some substrate proteins in vitro (calmodulin, elongation factor 1, glycogen synthase) but not of others (casein).
Recombinant CkII in vitro binds to spermine and this interaction is concomitant with a striking effect on the structural polymeric organisation on the kinase which in the presence of the polyamine exhibits a ring-like structure.
Chimeric β subunits of human and Drosophila cDNA reveal that the N terminal region of the CkIIβ subunit is responsible for the requirement for the redox state during renaturation, and is also responsible for solubility and electrophoretic mobility. of S.cerevisiae deleted for both genes.
Recombinant Casein kinase reconstituted from human and Drosophila, α and β subunits demonstrate that CkIIβ is responsible for renaturation and reconstitution of Casein kinase II dependent on the redox conditions.