| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.63263808 |
| The interaction of CK 2 alpha with DNA can also be assayed by the nitrocellulose filter binding assay . 0.63263808^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.61398325 |
| Regulation of the DNA binding of p 53 by its interaction with protein kinase CK 2 . 0.61398325^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.79296051 |
| We demonstrate that CKII binds through its catalytic alpha and alpha ' subunits to the basic leucine zipper ( bZIP ) DNA binding domains of many transcription factors , including ATF 1 . 0.79296051^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| However , the CK 2 alpha cDNA hybridizes to several additional fragments in total human DNA . . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| A human 4 . 3 kb genomic DNA fragment , containing the information of a processed ( pseudo ) gene of casein kinase 2 subunit alpha ( CKII alpha ) was isolated and sequenced . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Incubation of the full length preparation from E . coli with purified casein kinase 2 ( CKII ) resulted in phosphorylation of the N terminal region and was accompanied by activation of the DNA ligase . ^^^ Of a variety of purified protein kinases tested , only CKII stimulated the activity of calf thymus DNA ligase 1 . ^^^ Tryptic phosphopeptide analysis of DNA ligase 1 revealed that CKII specifically phosphorylated a major peptide also apparently phosphorylated in cells , implying that CKII is a protein kinase acting on DNA ligase 1 in the cell nucleus . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| CKII phosphorylation thus acts to potentiate SRF DNA exchange rates rather than alter equilibrium binding affinity . . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| A combination of segregation analysis of rodent human hybrid cells and chromosomal in situ hybridization have localized the human CK 2 alpha DNA sequence to two loci : 11p15 . 5 p15 . 4 and 20p13 . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| The gene encoding CKII subunit beta was isolated from human genomic DNA and analyzed for its primary structure using exclusively nonradioactive procedures . ^^^ The upstream promoter region of the CKII beta gene contains multiple potential gene regulatory sequence elements , noticeable DNA structures , and the characteristics of a housekeeping gene ( more than one transcription initiation site , lack of a TATA box , presence of a CpG island , occurrence of multiple GC boxes and of nonstandard positioned CCAAT boxes ) . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| A 3 . 8 kilobase pair segment of C . elegans DNA that contains the CKII beta gene and an extensive 5 ' flanking region was cloned and sequenced . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| The c Myb nuclear oncoprotein is phosphorylated in vitro and in vivo at an N terminal site near its DNA binding domain by casein kinase 2 ( CK 2 ) or a CK 2 like activity . ^^^ The site of this phosphorylation is deleted in nearly all oncogenically activated Myb proteins , resulting in DNA binding that is independent of CK 2 . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| The present communication reports that purified mammalian CKII interacts with genomic DNA preparations in vitro . ^^^ Binding of CKII was optimum with double stranded DNA preparations ; duplex lambda phage DNA exhibited at least two types of binding sites and the high affinity system ( Kd approximately equal to 6 10 10 ( 13 ) M ) represented a binding capacity of about 1 mol CKII per mol DNA . ^^^ CKII DNA interaction was stimulated in the presence of a polyamine and inhibited by heparin . ^^^ Blotting experiments disclosed that DNA binds CKII through its alpha subunit . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Phosphorylation of transcription factor GBF 1 with the reconstituted CKA 1 ( 2 ) CKB 1 ( 2 ) enzyme resulted in stimulation of its DNA binding activity and retardation of the protein DNA complex ; these results are identical to those obtained previously with isolated nuclear CKII from broccoli . . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Whereas little evidence to any functional significance of the CKII sites in c Myc has been obtained , phosphorylation of its heterodimeric partner Max alters DNA binding properties . ^^^ CKII phosphorylation of Ser 2 and 11 in Max resulted in enhanced DNA binding kinetics of both Max / Max homo and Myc / Max heterodimers without altering steady state binding . ^^^ For c Myb mutational analysis of the CKII phosphorylation sites showed altered steady state DNA binding . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Phosphorylation by CK 2 activates the specific DNA binding function of p 53 and stimulates its ability to suppress cellular growth . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| CK 2 dependent phosphorylation of an N truncated derivative of engrailed protein purified from bacteria increased its DNA binding 2 4 fold . . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| For these studies , each subunit of human CKII was expressed in yeast as a fusion with the DNA binding domain or with the transcriptional activation domain of the yeast GAL 4 transcriptional activator . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| In addition , HSP 90 competed with DNA for binding to CKII . ^^^ Finally , SPR experiments showed that a peptide corresponding to the heparin and DNA binding site of CKII alpha binds to immobilized HSP 90 . ^^^ These results indicate that HSP 90 , DNA , and heparin compete with each other for binding to a common site of CKII alpha . ^^^ If the binding of CKII to DNA is biologically significant , it could be possibly regulated also by HSP90 . . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Seven protein kinase CK 2 alpha clones were isolated from a murine genomic DNA library . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| PstI identifies biallelic DNA polymorphism of the human casein kinase 2 alpha gene ( CSNK2A1 ) . cDNA probe of the casein kinase 2 alpha subunit gene detects a biallelic PstI polymorphism . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| The phosphorylation of the C terminus of topoisomerase 2 by CKII appears to increase the stability of the complex formed with linear DNA fragments , while dephosphorylation has the opposite effect . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Surprisingly , NF GMb was found to bind solely to single strand DNA , namely the non coding strand of the GM CSF CK 1 / CK 2 region . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| The effect of the synthetic octapeptide pyroGLU ASP ASP SER ASP GLU GLU ASN ( phosphorylated by casein kinase 2 , CKII ) on DNA transcription by RNA polymerase 2 has been studied . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| CKII phosphorylation abrogated ZEBRA ' s capacity to bind its target DNA sequences . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Moreover , the findings that DNAs as well as RNAs significantly stimulate the CK 2 catalyzed phosphorylation of p 34 in vitro and induce its conformational change , suggest that the physiological activity of p 34 bound RNA or DNA in chloroplast post transcriptional regulation is controlled by specific p 34 phosphorylation by CK II . . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Both Myc Max and Mad Max heterocomplexes are favored over Max homodimers , and , unlike Max homodimers , the DNA binding activity of the heterodimers is unaffected by CKII phosphorylation . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| SRF is phosphorylated by casein kinase 2 ( CKII ) , which causes a large increase in its DNA binding activity . ^^^ Third , we tested the activity of an SRF mutant that binds DNA at constitutively high levels irrespective of CKII phosphorylation . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| The complex of CKII beta DNA / CKII alpha protein is shown to occur within the 170 239 base pair ( bp ) segment upstream of the first transcription start site of the gene . ^^^ The DNA motif contains , in a distance of 44 bp , two GC rich boxes , 5 ' GGGGCCC and 5 ' CCCCTGGGC , and represents a novel cis acting element ; the binding of the CKII alpha protein activates the CKII beta gene promoter . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| CK 2 has been found to phosphorylate a wide variety of cytosolic and nuclear substrates which are intimately involved in regulation of DNA , RNA , and protein synthesis , and differentiation . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| In addition , after phosphorylation by CK 2 , phosphorylated p 53 lost its DNA annealing activity . ^^^ Because the C terminal domain of p 53 is both involved in the association with CK 2 and phosphorylated by it , our results suggest that either protein protein interaction or phosphorylation of this domain might control the base pairing of complementary sequences promoted by p 53 in processes related to DNA replication and repair . . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Our studies show that E 47 serves as an in vitro substrate for CKII and that CKII phosphorylated E 47 proteins no longer bind to DNA . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| CKII strongly phosphorylates fragments 7 and 10 which cover part of the activation / nuclear localization and DNA binding domains of Egr 1 . ^^^ CKII phosphorylation of Egr 1 resulted in a decrease of its DNA binding as well as its transcriptional activities . . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| CK 2 activity correlated well with DNA synthesis ( i . e . , cell proliferation ) rates from days 10 to 11 , but not from days 11 to 12 of gestation . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Phosphorylation of recombinant 1 ( kappa ) B ( beta ) by either BAK or CKII restored the capacity of this inhibitor to antagonize the DNA binding activity of c Rel . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| A high positive correlation was found between the CK 2 phosphotransferase activity and both the proliferation index and DNA synthesis during palate development . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| In this study , we demonstrate that casein kinase 2 ( CKII ) is able to phosphorylate the C terminus of Sp 1 and results in a decrease in DNA binding activity . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Cells treated with 5 , 6 dichloro 1 beta D ribofuranosylbenzimidazole ( DRB ) are inhibited in a dose dependent manner from under going DNA synthesis as measured by [ 3H ] thymidine incorporation and from expressing CK 2 . ^^^ Furthermore , a host cell specific CK 2 alpha antisense inhibits DNA synthesis in a dose dependent manner . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| The highly basic ribosomal protein L 41 interacts with the beta subunit of protein kinase CKII and stimulates phosphorylation of DNA topoisomerase IIalpha by CKII . ^^^ However , L 41 protein stimulates the phosphorylation of DNA topoisomerase IIalpha by CKII by 2 . 5 times . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| CDC 5 and CKII control adaptation to the yeast DNA damage checkpoint . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| The association of CKII with NF kappaB occurred in the cytoplasm , suggesting that this phosphorylation might be involved either in control of translocation of the activated complex or in modulation of its DNA binding properties . . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Notably , although phosphorylation by CKI and protein kinase C had no effect whatsoever on the ability of APE / Ref 1 to act at abasic sites in DNA , phosphorylation by CKII completely abolished DNA repair activity . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| In vitro , a purified preparation of CKII efficiently phosphorylated Cut repeats causing an inhibition of DNA binding . ^^^ In vivo , overexpression of the CKII alpha and beta caused a decrease in DNA binding by Cut . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| These results indicate that phosphorylation at the CK 2 site is one of the post translational mechanisms through which p 53 is activated in response to UV radiation and that different mechanisms activate p 53 after DNA damage by gamma radiation . . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Phosphorylation of PU . 1 by protein kinase CK 2 was found to up regulate its trans activation function , but not its DNA binding activity . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| DNA damage triggers DRB resistant phosphorylation of human p 53 at the CK 2 site . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Phosphorylation of the peptide at the PKC or the CKII sites clearly decreased DNA binding , and addition of a second phosphate group almost completely abolished binding . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| CKII dependent phosphorylation of the homeodomain increased Csx / Nkx2 . 5 DNA binding . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Phosphorylation of the DNA repair protein APE / REF 1 by CKII affects redox regulation of AP 1 . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Phosphorylation of yeast TBP by protein kinase CK 2 reduces its specific binding to DNA . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| The results suggest that both the CK2alpha and RAP 74 subunits travel with the elongating pol 2 molecules along the DNA template during the entire transcription cycle . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Similarly , activation of p 53 by UV irradiation or DNA damage inducing drugs had no effect on either the localisation or levels of CK2alpha , even although significant nuclear p 53 accumulation was observed . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Based on this finding , we asked if a coexpression of the beta subunit of CK 2 with p 53 in mammalian cells could inhibit the DNA binding activity of p 53 in a physiological context . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Phosphorylation of MAZ by CKII at this serine residue was required for maximum binding of MAZ to the pyrimidine rich DNA of the nuclease hypersensitive element ( NHE ) in the 5 ' end promoter region of the c myc gene . ^^^ These results suggest that phosphorylation of the serine residue at position 480 of MAZ by CKII can control the function of MAZ by altering its DNA binding activity . . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Ck 2 has been implicated in DNA replication , regulation of basal and inducible transcription , translation and control of metabolism . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| By exploiting a monoclonal antibody directed at a phospho epitope , we demonstrate that Ser 66 of DNA ligase 1 , which is part of a strong CKII consensus site , is phosphorylated in a cell cycle dependent manner . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| The physiological significance of the casein kinase 2 ( CK 2 ) mediated phosphorylation of human immunodeficiency virus type 1 ( HIV 1 ) reverse transcriptase ( RT ) on its three enzymatic activities [ RNA dependent DNA polymerase ( RDDP ) , DNA dependent DNA polymerase ( DDDP ) and ribonuclease H ( RNase H ) ] was investigated in vitro . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| After phosphorylation with protein kinase CKII ( pCKII ) these peptides are able to bind to DNA in presence of divalent cations and salt / ethanol . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| The DNA binding activity is cryptic but can be modulated through the C terminal region of the p 53 protein by several different stimuli , including phosphorylation by casein kinase 2 ( CKII ) , protein kinase C ( PKC ) or binding of the C terminal monoclonal antibody PAb 421 . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| The upstream sequence of the gene coding for human CK2alpha ( CSNK1A1 , chromosomal location 20p13 ) has been examined for promoter location and transcription factor interactions using reporter gene assays ( luciferase ; HeLa cells ) , site directed mutagenesis , electrophoretic mobility shift assays , super shifts , UV cross linking , Western blotting , and DNA affinity chromatography . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Mitotic phosphorylation of DNA topoisomerase 2 alpha by protein kinase CK 2 creates the MPM 2 phosphoepitope on Ser 1469 . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Based on the genomic DNA sequence , RNA transcripts encoding CK2alpha ' ' apparently originate from alternative splicing of a primary transcript . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| In vitro kinase assays revealed that CKII catalyzed phosphorylation increased the affinity of Jun for the DNA . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| A pea homologue of human DNA helicase 1 is localized within the dense fibrillar component of the nucleolus and stimulated by phosphorylation with CK 2 and cdc 2 protein kinases . ^^^ The DNA and RNA unwinding activities were upregulated after phosphorylation of PDH 65 with CK 2 and cdc 2 protein kinases . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| A DNA damage induced p 53 serine 392 kinase complex contains CK 2 , hSpt 16 , and SSRP 1 . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Abundant evidence relates CK 2 to the regulation of cell division . p 21 ( WAF1 / CIP1 ) is a potent inhibitor of cyclin dependent kinases and of DNA replication and acts as a key inhibitor of cell cycle progression . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Stimulation of human DNA topoisomerase 2 activity by its direct association with the beta subunit of protein kinase CKII . ^^^ DNA topoisomerase 2 copurifies with and is phosphorylated by protein kinase CKII . ^^^ Furthermore , a DNA relaxation assay demonstrated that the CKII subunit enhances topoisomerase 2 activity by physical interaction with topoisomerase II . . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Phosphorylation of c Myb by casein kinase 2 ( CK 2 ) at serines 11 and 12 has been variously implicated in the regulation of DNA binding . ^^^ C Myb protein levels , extent of CK 2 phosphorylation and DNA binding were then monitored following mitogenic stimulus and passage through the cell cycle in normal peripheral T cells and the T leukemia cell line CCRF CEM . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| TATA binding protein associated CK 2 transduces DNA damage signals to the RNA polymerase 3 transcriptional machinery . ^^^ Transcriptional repression induced by DNA damage requires CK 2 and coincides with downregulation of TBP associated CK 2 and dissociation of catalytic subunits from TBP CK 2 complexes . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Protein kinase CK 2 differentially phosphorylates maize chromosomal high mobility group B ( HMGB ) proteins modulating their stability and DNA interactions . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Also in common are Sp 1 response elements that cooperate with Ets 1 , and Sp 1 is phosphorylatable by CK 2 holoenzyme but not by individual CK2alpha , the phosphorylation negatively affecting DNA binding . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Phosphorylation of HMGB 1 by protein kinase CK 2 abolishes the interaction with Dof 2 and the stimulation of Dof 2 DNA binding . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| The possible involvement of CK 2 in the FGF induced stimulation of DNA synthesis is discussed . . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| These results , therefore , indicate that the purified kinase is a CK 2 protein kinase and may be involved in the regulation of DNA topoisomerase 1 activity . . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Protein kinase CK 2 phosphorylates the high mobility group domain protein SSRP 1 , inducing the recognition of UV damaged DNA . ^^^ The affinity of CK 2 alpha phosphorylated SSRP 1 for the DNA correlates with the degree of UV induced DNA damage . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| The inhibitors of CKII , daidzein and 5 , 6 dichlorobenzimidazole riboside , diminished the LPA induced increase in CKII activity and DNA synthesis . ^^^ These data suggest that the LPA induced DNA synthesis in VSM cells may be mediated by a signal transduction mechanism involving CKII , ERK , and p 38 K . . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Transcriptional activity and DNA binding of heat shock factor 1 involve phosphorylation on threonine 142 by CK 2 . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| The reading frame encodes a polypeptide consisting of 526 amino acid residues , containing a number of DNA binding motifs and phosphorylation sites for PKC , CK 2 , and p34cdc2 . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| In vitro , CarD ( Sa ) exhibits the specific minor groove binding to appropriately spaced AT rich DNA that is characteristic of CarD or HMGA proteins , and it is also phosphorylated by CKII . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| In the absence of ATP CK 2 kinase activated DNA relaxation about twofold . ^^^ There was also no effect of CK 2 on camptothecin induced cleavage of DNA by htopo 1 . ^^^ These results identify an accelerated movement of topoisomerase 1 between substrate molecules as a cause of the activation of DNA relaxation by CK 2 kinase . . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Cilostazol ( 10 microM ) fully restored cell proliferation with suppression of DNA fragmentation induced by TNF alpha and emodin , a CK 2 inhibitor , which were antagonized by iberiotoxin , a maxi K channel blocker . ^^^ SK N SH cells treated with antisense CK 2 oligodeoxynucleotide showed a prominent DNA fragmentation with little responsiveness to TNF alpha in the phosphorylation of PTEN , indicative of the essential role of p CK2 / CK2 in cell proliferation , and the decreased cell viability of these cells was not restored by cilostazol . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| The differentially expressed genes primarily participate in three major areas : ( 1 ) signal transduction or in the regulation of signal transduction ( extracellular signal regulated kinase 2 ( ERK 2 ) ; protein kinase CK 2 ; protein kinase B ; c jun ; NF kappaB ; ras related GTPases ; annexins ) , ( 2 ) stress response , tissue remodeling , and DNA repair ( glutathione S transferases ; procollagen c proteinase enhancer ; plasminogen activator ; tissue inhibitor of metalloprotease 3 ; apurinic / apyrimidic endonuclease ) , and ( 3 ) electron transport and energy homeostasis ( cytochrome c oxidase subunits ) . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Activation of the DNA binding ability of latent p 53 protein by protein kinase C is abolished by protein kinase CK 2 . p 53 is one of the most important regulators of cell proliferation and differentiation and of programmed cell death , triggering growth arrest and / or apoptosis in response to different cellular stress signals . ^^^ In contrast , phosphorylation by cdk 2 ( cyclin dependent kinase 2 ) / cyclin A and by the protein kinase CK 2 are both enhanced in DNA damaged cells . ^^^ Phosphorylation of p 53 by CK 2 on Ser 392 induces its DNA binding activity to a much lower extent than phosphorylation by cdk2 / cyclin A or PKC . ^^^ In addition , phosphorylation by CK 2 strongly inhibits PKC induced activation of p 53 DNA binding , while the activation of p 53 by cdk2 / cyclin A is not affected by CK 2 . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| HMGB 6 can bind DNA structure specifically , and it is a substrate for the protein kinase CK2alpha . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Phosphorylation by protein kinase CKII modulates the DNA binding activity of a chloroplast nucleoid associated protein . ^^^ We demonstrate that the DNA binding domain of MFP 1 is a substrate for CKII and that phosphorylation by CKII inhibits DNA binding . ^^^ Using site directed mutagenesis , we identify a conserved twin CKII site in the DNA binding domain that is required for the inhibition of DNA binding . ^^^ Phosphorylation of MFP 1 by chloroplast CKII as a possible means to modulate its DNA binding activity is discussed . . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| The protein kinase CK 2 facilitates repair of chromosomal DNA single strand breaks . ^^^ Moreover , we show that inhibiting XRCC 1 phosphorylation by mutation of the CK 2 phosphorylation sites or preventing CK 2 activity using a highly specific inhibitor ablates the rapid repair of cellular DNA single strand breaks by XRCC 1 . ^^^ These data identify a direct role for CK 2 in the repair of chromosomal DNA strand breaks and in maintaining genetic integrity . . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| A new report has established that casein kinase 2 ( CK 2 ) , a protein that functions in diverse cellular processes , controls the activity of the DNA repair protein XRCC 1 . ^^^ These results indicate that CK 2 is a key participant in the cellular response to DNA damage . . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| We show that the two DNA interacting domains differ in their binding properties and in their abilities to respond to CK 2 phosphorylation . . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Phosphorylation by protein kinase CK 2 changes the DNA binding properties of the human chromatin protein DEK . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| The intramolecular interaction between the two oppositely charged termini of the protein is enhanced when serine residues in the acidic tail of HMGB 1 are phosphorylated by protein kinase CK 2 , which can explain the negative effect of the phosphorylation on certain DNA interactions . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Neither the conserved extreme N terminal region , a polyglutamic acid region at the protein C terminus , nor the Ser ( 214 ) CKII phosphorylation site was required for DNA binding or activity in this model . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Here , we identify CK 1 and CK 2 as major kinases that directly bind to and phosphorylate LEF 1 inducing distinct , kinase specific changes in the LEF 1 / DNA complex . ^^^ Moreover , CK 1 dependent phosphorylation in contrast to CK 2 disrupts the association of beta catenin and LEF 1 but does not impair DNA binding of LEF 1 . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Concomitant treatment with a pan caspase inhibitor or transfection of apoptosis repressor with caspase recruitment domain markedly suppresses the apoptotic response to DNA damage by 6 TG in the CK 2 reduced cells , indicating caspase regulation by CK 2 . ^^^ CONCLUSION : CK 2 is essential for apoptosis inhibition following DNA damage induced by 6 TG , controlling caspase activity . . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| However , the DNA binding activity of TGA 2 was reduced by CK 2 treatment , whereas that of TGA 2 A was unaffected ; TGA 2 ' s DNA binding activity after incubation in a rabbit reticulocyte lysate also was substantially lower than that of comparably treated TGA 2 A . ^^^ Taken together , these results suggest that phosphorylation at the putative CK 2 phosphorylation site negatively regulates the DNA binding activity of TGA 2 . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| In addition , we show that casein kinase 2 ( CK 2 ) can phosphorylate H 4 S1 in vitro and that null or temperature sensitive CK 2 yeast mutants are defective for induction of H 4 S1 phosphorylation upon DNA damage in vivo . ^^^ CK 2 has been implicated in regulating a DNA damage response ; our data suggest that histone H 4 S1 is one of its physiological substrates . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Cooperation between small nuclear RNA activating protein complex ( SNAPC ) and TATA box binding protein antagonizes protein kinase CK 2 inhibition of DNA binding by SNAPC . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Here , we report that GAGA 519 isoform is a phosphoprotein that is phosphorylated by CK 2 at the region of the DNA binding domain . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| In contrast , DNA binding by an Alt ARNT / dioxin receptor heterodimer to the xenobiotic response element is not inhibited by phosphorylation with CKII , nor does Alt ARNT S77A behave differently from wild type Alt ARNT in the context of a dioxin receptor heterodimer . . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| CK 2 phosphorylation does not affect ATP hydrolysis by DmORC but modulates the ATP dependent DNA binding activity of DmORC . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| EmBP 2 and ZmBZ 1 are phosphorylated by protein kinase CK 2 and phosphorylation alters their DNA binding properties . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Transfection of the wildtype CK2alpha DNA increased , whereas transfection of the catalytically inactive CK2alphaA156 mutant DNA decreased CK 2 activity in the SN . ^^^ CK2alphaA156 mutant DNA also antagonized the enhancing effect of GDNF on CK 2 activity . ^^^ Further , CK2alpha wildtype DNA increased , whereas CK2alphaA156 mutant DNA decreased TH activity in the SN without altering the TH protein level . ^^^ Over expression of the CK2alpha wildtype DNA partially , but significantly , prevented the deteriorating effect of MPP+ on these measures . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| CK 2 and other clock genes have been implicated in cellular responses to DNA damage , particularly those induced by ultraviolet ( UV ) light . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Thus , overexpression of CK 2 resulted in the suppression of TRAIL induced apoptosis via its effects on the activation of caspases , DNA fragmentation , and downstream cleavage of lamin A . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| AP 1 DNA binding was also induced by TGF beta , and the action of p 38 kinase , JNK , and CK 2 converged on the activation of c Jun / AP 1 . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| The H2O2 production induced by antisense CK2alpha was associated with robust caspase 3 activity , nuclear factor kappaB nuclear translocation , cytochrome c release , and subsequent DNA fragmentation in prostate cancer cells ( ALVA 41 and PC 3 ) . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| Chromatin immunoprecipitation analysis places CK 2 at the ribosomal DNA ( rDNA ) promoter in vivo . ^^^ |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P27695 and P68400 |
Pubmed |
SVM Score :0.0 |
| NA |
|