CKA2/YOR061W Literature Guide Help

Other names published for CKA2: YOR29-12, CK2 subunit, YOR061W

CKA2 - Protein Physical Properties (18)

ReferenceOther Genes Addressed
Farley AR, et al.  (2011) Assessing the Components of the eIF3 Complex and their Phosphorylation Status. J Proteome Res 10(4):1481-94
Janeczko M, et al.  (2011) Interactions between subunits of protein kinase CK2 and their protein substrates influences its sensitivity to specific inhibitors. Mol Cell Biochem 356(1-2):121-6
Sajnaga E, et al.  (2008) Catalytic activity of mutants of yeast protein kinase CK2alpha. Acta Biochim Pol 55(4):767-76
Kubinski K, et al.  (2007) Yeast holoenzyme of protein kinase CK2 requires both beta and beta' regulatory subunits for its activity. Mol Cell Biochem 295(1-2):229-36
Kubinski K, et al.  (2006) Yeast elf1 factor is phosphorylated and interacts with protein kinase CK2. J Biochem Mol Biol 39(3):311-8
Domanska K, et al.  (2005) Different properties of four molecular forms of protein kinase CK2 from Saccharomyces cerevisiae. Acta Biochim Pol 52(4):947-51
Zien P, et al.  (2003) TBBz but not TBBt discriminates between two molecular forms of CK2 in vivo and its implications. Biochem Biophys Res Commun 312(3):623-8
Bidwai AP, et al.  (1994) Casein kinase II of Saccharomyces cerevisiae contains two distinct regulatory subunits, beta and beta'. Arch Biochem Biophys 309(2):348-55
Bojanowski K, et al.  (1993) DNA topoisomerase II and casein kinase II associate in a molecular complex that is catalytically active. J Biol Chem 268(30):22920-6
Cardenas ME, et al.  (1993) Casein kinase II copurifies with yeast DNA topoisomerase II and re-activates the dephosphorylated enzyme. J Cell Sci 104 ( Pt 2)():533-43
Grankowski N, et al.  (1993) Synthetic peptides and ribosomal proteins as substrate for 60S ribosomal protein kinase from yeast cells. Biochim Biophys Acta 1158(2):194-6
Bidwai AP, et al.  (1992) Purification and characterization of casein kinase II (CKII) from delta cka1 delta cka2 Saccharomyces cerevisiae rescued by Drosophila CKII subunits. The free catalytic subunit of casein kinase II is not toxic in vivo. J Biol Chem 267(26):18790-6
Birnbaum MJ and Glover VC  (1991) The phosphotransferase activity of casein kinase II is required for its physiological function in vivo. Biochem Biophys Res Commun 181(2):524-8
Padmanabha R and Glover CV  (1987) Casein kinase II of yeast contains two distinct alpha polypeptides and an unusually large beta subunit. J Biol Chem 262(4):1829-35
Meggio F, et al.  (1986) Structure and properties of casein kinase-2 from Saccharomyces cerevisiae. A comparison with the liver enzyme. Eur J Biochem 159(1):31-8
Szyszka R, et al.  (1986) Further studies on the quaternary structure of yeast casein kinase II. Acta Biochim Pol 33(1):39-46
Kudlicki W, et al.  (1984) A cytoplasmic, cyclic nucleotide-independent casein kinase II from Saccharomyces cerevisiae. Biochim Biophys Acta 784(2-3):102-7
Rigobello MP, et al.  (1982) Isolation and characterization of a type II casein kinase ('casein kinase-TS') from Saccharomyces cerevisiae. FEBS Lett 144(2):354-8