EzCatDB: M00197
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DB codeM00197
RLCP classification3.103.126600.1165 : Transfer
CATH domainDomain 13.30.200.20 : Phosphorylase Kinase; domain 1Catalytic domain
Domain 21.10.510.10 : Transferase(Phosphotransferase); domain 1Catalytic domain
Domain 31.10.1820.10 : protein kinase ck2 holoenzyme, chain C, domain 1
Domain 42.20.25.20 : N-terminal domain of TfIIb
E.C.2.7.11.1

CATH domainRelated DB codes (homologues)
1.10.510.10 : Transferase(Phosphotransferase); domain 1M00125,M00124,M00131,T00224,M00127,M00129,M00130,M00132,M00136,M00196,M00198,M00304,M00323,M00325,M00326,M00327,M00328,M00329,M00330,M00331,M00332,M00333,M00335,M00339,M00344
3.30.200.20 : Phosphorylase Kinase; domain 1M00125,M00124,M00131,T00224,M00127,M00129,M00130,M00132,M00136,M00196,M00198,M00304,M00323,M00325,M00326,M00327,M00328,M00329,M00330,M00331,M00332,M00333,M00335,M00339,M00344,D00298

Enzyme Name
UniProtKBKEGG

P28020P68400Q6INV5P19784P28021P67870
Protein nameCasein kinase II subunit alphaCasein kinase II subunit alpha
Casein kinase II subunit alpha''Casein kinase II subunit betaCasein kinase II subunit betaNon-specific serine/threonine protein kinase
A-kinase
AP50 kinase
ATP-protein transphosphorylase
Calcium-dependent protein kinase C
Calcium/phospholipid-dependent protein kinase
cAMP-dependent protein kinase
cAMP-dependent protein kinase A
Casein kinase
Casein kinase (phosphorylating)
Casein kinase 2
Casein kinase I
Casein kinase II
cGMP-dependent protein kinase
CK-2
CKI
CKII
Cyclic AMP-dependent protein kinase
Cyclic AMP-dependent protein kinase A
Cyclic monophosphate-dependent protein kinase
Cyclic nucleotide-dependent protein kinase
Cyclin-dependent kinase
Cytidine 3',5'-cyclic monophosphate-responsive protein kinase
dsk1
Glycogen synthase a kinase
Glycogen synthase kinase
HIPK2
Hpr kinase
Hydroxyalkyl-protein kinase
Hydroxyalkyl-protein kinase
M phase-specific cdc2 kinase
Mitogen-activated S6 kinase
p82 kinase
Phosphorylase b kinase kinase
PKA
Protein glutamyl kinase
Protein kinase (phosphorylating)
Protein kinase A
Protein kinase CK2
Protein kinase p58
Protein phosphokinase
Protein serine kinase
Protein serine-threonine kinase
Protein-aspartyl kinase
Protein-cysteine kinase
Protein-serine kinase
Prp4 protein kinase
Raf kinase
Raf-1
Ribosomal protein S6 kinase II
Ribosomal S6 protein kinase
Serine kinase
Serine protein kinase
Serine-specific protein kinase
Serine(threonine) protein kinase
Serine/threonine protein kinase
STK32
T-antigen kinase
Threonine-specific protein kinase
Twitchin kinase
Type-2 casein kinase
betaIIPKC
epsilon PKC
Wee 1-like kinase
Wee-kinase
WEE1Hu
SynonymsCK II
EC 2.7.11.1
CK II alpha
EC 2.7.11.1
Ck2a1 protein
CK II alpha''
EC 2.7.11.1
CK II beta
Phosvitin
CK II beta
Phosvitin
Protein G5a
RefSeq
NP_001886.1 (Protein)
NM_001895.3 (DNA/RNA sequence)
NP_808227.1 (Protein)
NM_177559.2 (DNA/RNA sequence)
NP_808228.1 (Protein)
NM_177560.2 (DNA/RNA sequence)
NP_001084124.1 (Protein)
NM_001090655.1 (DNA/RNA sequence)
NP_001887.1 (Protein)
NM_001896.2 (DNA/RNA sequence)
NP_001084126.1 (Protein)
NM_001090657.1 (DNA/RNA sequence)
NP_001311.3 (Protein)
NM_001320.5 (DNA/RNA sequence)
PfamPF00069 (Pkinase)
[Graphical view]
PF00069 (Pkinase)
[Graphical view]
PF00069 (Pkinase)
[Graphical view]
PF00069 (Pkinase)
[Graphical view]
PF01214 (CK_II_beta)
[Graphical view]
PF01214 (CK_II_beta)
[Graphical view]


UniProtKB:Accession NumberP28020P68400Q6INV5P19784P28021P67870
Entry nameCSK21_XENLACSK21_HUMANQ6INV5_XENLACSK22_HUMANCSK2B_XENLACSK2B_HUMAN
ActivityATP + a protein = ADP + a phosphoprotein.ATP + a protein = ADP + a phosphoprotein.
ATP + a protein = ADP + a phosphoprotein.

SubunitTetramer composed of an alpha chain, an alpha' and two beta chains.Tetramer composed of an alpha chain, an alpha' and two beta chains. Also component of a CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, the complex associating following UV irradiation. Interacts with RNPS1.
Tetramer composed of an alpha chain, an alpha' and two beta chains. Also component of a CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, the complex associating following UV irradiation.Tetramer composed of an alpha subunit, an alpha' subunit and two beta subunits (By similarity).Tetramer composed of an alpha subunit, an alpha' subunit and two beta subunits. Interacts with CD163. Also component of a CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, the complex associating following UV irradiation.
Subcellular location





Cofactor






Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00305C00038C00002C00017C00008C00562
CompoundMagnesiumZincATPProteinADPPhosphoprotein
Typedivalent metal (Ca2+, Mg2+)heavy metalamine group,nucleotidepeptide/proteinamine group,nucleotidepeptide/protein,phosphate group/phosphate ion
ChEBI18420
29105
15422

16761

PubChem888
32051
5957

6022

              
1jwhA01UnboundUnboundAnalogue:ANPUnboundUnboundUnbound
1jwhB01UnboundUnboundUnboundUnboundUnboundUnbound
1na7A01UnboundUnboundUnboundUnboundUnboundUnbound
1pjkA01UnboundUnboundAnalogue:ANPUnboundUnboundUnbound
1ymiA02UnboundUnboundAnalogue:ANPUnboundUnboundUnbound
2pvrA02UnboundUnboundAnalogue:ANPUnboundUnboundUnbound
2zjwA02UnboundUnboundUnboundUnboundUnboundUnbound
3bqcA02UnboundUnboundUnboundUnboundUnboundUnbound
3c13A02UnboundUnboundUnboundUnboundUnboundUnbound
3fwqA02UnboundUnboundUnboundUnboundUnboundUnbound
3fwqB02UnboundUnboundUnboundUnboundUnboundUnbound
3h30A02UnboundUnboundUnboundUnboundUnboundUnbound
3h30B02UnboundUnboundUnboundUnboundUnboundUnbound
3juhA02UnboundUnboundAnalogue:ANPUnboundUnboundUnbound
3juhB02UnboundUnboundAnalogue:ANPUnboundUnboundUnbound
3mb6A02UnboundUnboundUnboundUnboundUnboundUnbound
3mb7A02UnboundUnboundUnboundUnboundUnboundUnbound
3ngaA02UnboundUnboundUnboundUnboundUnboundUnbound
3ngaB02UnboundUnboundUnboundUnboundUnboundUnbound
3nszA02UnboundUnboundUnboundUnboundAnalogue:ANPUnbound
3e3bX02UnboundUnboundUnboundUnboundUnboundUnbound
3ofmA02UnboundUnboundUnboundUnboundUnboundUnbound
1jwhA02UnboundUnboundUnboundUnboundUnboundUnbound
1jwhB02UnboundUnboundUnboundUnboundUnboundUnbound
1na7A02UnboundUnboundUnboundUnboundUnboundUnbound
1pjkA02UnboundUnboundUnboundUnboundUnboundUnbound
1ymiA01UnboundUnboundUnboundUnboundUnboundUnbound
2pvrA01UnboundUnboundUnboundUnboundUnboundUnbound
2zjwA01UnboundUnboundUnboundUnboundUnboundUnbound
3bqcA01UnboundUnboundUnboundUnboundUnboundUnbound
3c13A01UnboundUnboundUnboundUnboundUnboundUnbound
3fwqA01UnboundUnboundUnboundUnboundUnboundUnbound
3fwqB01UnboundUnboundUnboundUnboundUnboundUnbound
3h30A01UnboundUnboundUnboundUnboundUnboundUnbound
3h30B01UnboundUnboundUnboundUnboundUnboundUnbound
3juhA01UnboundUnboundUnboundUnboundUnboundUnbound
3juhB01UnboundUnboundUnboundUnboundUnboundUnbound
3mb6A01UnboundUnboundUnboundUnboundUnboundUnbound
3mb7A01UnboundUnboundUnboundUnboundUnboundUnbound
3ngaA01UnboundUnboundUnboundUnboundUnboundUnbound
3ngaB01UnboundUnboundUnboundUnboundUnboundUnbound
3nszA01Bound:2x_MGUnboundUnboundUnboundUnboundUnbound
3e3bX01UnboundUnboundUnboundUnboundUnboundUnbound
3ofmA01UnboundUnboundUnboundUnboundUnboundUnbound
1rqfA01UnboundUnboundUnboundUnboundUnboundUnbound
1rqfB01UnboundUnboundUnboundUnboundUnboundUnbound
1rqfD01UnboundUnboundUnboundUnboundUnboundUnbound
1rqfE01UnboundUnboundUnboundUnboundUnboundUnbound
1rqfG01UnboundUnboundUnboundUnboundUnboundUnbound
1rqfH01UnboundUnboundUnboundUnboundUnboundUnbound
1rqfJ01UnboundUnboundUnboundUnboundUnboundUnbound
1rqfK01UnboundUnboundUnboundUnboundUnboundUnbound
1jwhC01UnboundUnboundUnboundUnboundUnboundUnbound
1jwhD01UnboundUnboundUnboundUnboundUnboundUnbound
1qf8A01UnboundUnboundUnboundUnboundUnboundUnbound
1qf8B01UnboundUnboundUnboundUnboundUnboundUnbound
3eedA01UnboundUnboundUnboundUnboundUnboundUnbound
3eedB01UnboundUnboundUnboundUnboundUnboundUnbound
1rqfA02UnboundBound:_ZNUnboundUnboundUnboundUnbound
1rqfB02UnboundBound:_ZNUnboundUnboundUnboundUnbound
1rqfD02UnboundBound:_ZNUnboundUnboundUnboundUnbound
1rqfE02UnboundBound:_ZNUnboundUnboundUnboundUnbound
1rqfG02UnboundBound:_ZNUnboundUnboundUnboundUnbound
1rqfH02UnboundBound:_ZNUnboundUnboundUnboundUnbound
1rqfJ02UnboundBound:_ZNUnboundUnboundUnboundUnbound
1rqfK02UnboundBound:_ZNUnboundUnboundUnboundUnbound
1jwhC02UnboundBound:_ZNUnboundUnboundUnboundUnbound
1jwhD02UnboundBound:_ZNUnboundUnboundUnboundUnbound
1qf8A02UnboundBound:_ZNUnboundUnboundUnboundUnbound
1qf8B02UnboundBound:_ZNUnboundUnboundUnboundUnbound
3eedA02UnboundBound:_ZNUnboundUnboundUnboundUnbound
3eedB02UnboundBound:_ZNUnboundUnboundUnboundUnbound

Active-site residues
resource
literature [2], [8]
pdbCatalytic residuesCofactor-binding residuesMain-chain involved in catalysiscomment
            
1jwhA01LYS 68
 
LYS 49;TYR 50;SER 51
 
1jwhB01LYS 68
 
LYS 49;TYR 50;SER 51
 
1na7A01LYS 68
 
LYS 49;TYR 50;SER 51
mutant E27A, K76N
1pjkA01LYS 68
 
LYS 49;TYR 50;SER 51
 
1ymiA02LYS 68
 
LYS 49;TYR 50;SER 51
mutant V66A
2pvrA02LYS 68
 
LYS 49;TYR 50;SER 51
 
2zjwA02LYS 68
 
LYS 49;TYR 50;SER 51
 
3bqcA02LYS 68
 
LYS 49;TYR 50;SER 51
 
3c13A02LYS 68
 
LYS 49;TYR 50;SER 51
 
3fwqA02LYS 68
 
LYS 49;TYR 50;SER 51
 
3fwqB02LYS 68
 
LYS 49;TYR 50;SER 51
 
3h30A02LYS 68
 
LYS 49;TYR 50;SER 51
 
3h30B02LYS 68
 
LYS 49;TYR 50;SER 51
 
3juhA02LYS 68
 
LYS 49;TYR 50;SER 51
 
3juhB02LYS 68
 
LYS 49;TYR 50;SER 51
 
3mb6A02LYS 68
 
LYS 49;TYR 50;SER 51
 
3mb7A02LYS 68
 
LYS 49;TYR 50;SER 51
 
3ngaA02LYS 68
 
LYS 49;TYR 50;SER 51
 
3ngaB02LYS 68
 
LYS 49;TYR 50;SER 51
 
3nszA02LYS 68
 
LYS 49;TYR 50;SER 51
 
3e3bX02LYS 69
 
LYS 50;TYR 51;SER 52
 
3ofmA02LYS 69
 
LYS 50;TYR 51;SER 52
 
1jwhA02ASP 156;LYS 158
ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
 
 
1jwhB02ASP 156;LYS 158
ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
 
 
1na7A02ASP 156;LYS 158
ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
 
 
1pjkA02ASP 156;LYS 158
ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
 
 
1ymiA01ASP 156;LYS 158
ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
 
mutant M163L
2pvrA01ASP 156;LYS 158
ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
 
 
2zjwA01ASP 156;LYS 158
ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
 
 
3bqcA01ASP 156;LYS 158
ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
 
 
3c13A01ASP 156;LYS 158
ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
 
 
3fwqA01ASP 156;LYS 158
ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
 
 
3fwqB01ASP 156;LYS 158
ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
 
 
3h30A01ASP 156;LYS 158
ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
 
 
3h30B01ASP 156;LYS 158
ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
 
 
3juhA01ASP 156;LYS 158
ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
 
 
3juhB01ASP 156;LYS 158
ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
 
 
3mb6A01ASP 156;LYS 158
ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
 
 
3mb7A01ASP 156;LYS 158
ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
 
 
3ngaA01ASP 156;LYS 158
ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
 
 
3ngaB01ASP 156;LYS 158
ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
 
 
3nszA01ASP 156;LYS 158
ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
 
 
3e3bX01ASP 157;LYS 159
ASN 162(Magnesium-2 binding);ASP 176(Magnesium-1 binding)
 
 
3ofmA01ASP 157;LYS 159
ASN 162(Magnesium-2 binding);ASP 176(Magnesium-1 binding)
 
 
1rqfA01 
 
 
 
1rqfB01 
 
 
invisible 59-66
1rqfD01 
 
 
invisible 59-65
1rqfE01 
 
 
 
1rqfG01 
 
 
invisible 59-67
1rqfH01 
 
 
invisible 59-67
1rqfJ01 
 
 
 
1rqfK01 
 
 
invisible 59-66
1jwhC01 
 
 
 
1jwhD01 
 
 
 
1qf8A01 
 
 
invisible 60-65
1qf8B01 
 
 
invisible 59-66
3eedA01 
 
 
invisible 60-64
3eedB01 
 
 
invisible 60-64
1rqfA02 
CYS 109;CYS 114;CYS 137;CYS 140(Zinc binding)
 
 
1rqfB02 
CYS 109;CYS 114;CYS 137;CYS 140(Zinc binding)
 
 
1rqfD02 
CYS 109;CYS 114;CYS 137;CYS 140(Zinc binding)
 
 
1rqfE02 
CYS 109;CYS 114;CYS 137;CYS 140(Zinc binding)
 
 
1rqfG02 
CYS 109;CYS 114;CYS 137;CYS 140(Zinc binding)
 
 
1rqfH02 
CYS 109;CYS 114;CYS 137;CYS 140(Zinc binding)
 
 
1rqfJ02 
CYS 109;CYS 114;CYS 137;CYS 140(Zinc binding)
 
 
1rqfK02 
CYS 109;CYS 114;CYS 137;CYS 140(Zinc binding)
 
 
1jwhC02 
CYS 109;CYS 114;CYS 137;CYS 140(Zinc binding)
 
 
1jwhD02 
CYS 109;CYS 114;CYS 137;CYS 140(Zinc binding)
 
 
1qf8A02 
CYS 109;CYS 114;CYS 137;CYS 140(Zinc binding)
 
 
1qf8B02 
CYS 109;CYS 114;CYS 137;CYS 140(Zinc binding)
 
 
3eedA02 
CYS 109;CYS 114;CYS 137;CYS 140(Zinc binding)
 
 
3eedB02 
CYS 109;CYS 114;CYS 137;CYS 140(Zinc binding)
 
 


references
[1]
PubMed ID7735313
JournalCell Mol Biol Res
Year1994
Volume40
Pages391-9
AuthorsBoldyreff B, Meggio F, Pinna LA, Issinger OG
TitleProtein kinase CK2 structure-function relationship: effects of the beta subunit on reconstitution and activity.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS)
Medline ID98232491
PubMed ID9564028
JournalEMBO J
Year1998
Volume17
Pages2451-62
AuthorsNiefind K, Guerra B, Pinna LA, Issinger OG, Schomburg D
TitleCrystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at 2.1 A resolution.
Related PDB1a6o
Related UniProtKBP28523
[3]
CommentsX-ray crystallography
PubMed ID10357806
JournalEMBO J
Year1999
Volume18
Pages2930-40
AuthorsChantalat L, Leroy D, Filhol O, Nueda A, Benitez MJ, Chambaz EM, Cochet C, Dideberg O
TitleCrystal structure of the human protein kinase CK2 regulatory subunit reveals its zinc finger-mediated dimerization.
Related PDB1qf8
[4]
CommentsX-ray crystallography
PubMed ID10581548
JournalNat Struct Biol
Year1999
Volume6
Pages1100-3
AuthorsNiefind K, Putter M, Guerra B, Issinger OG, Schomburg D
TitleGTP plus water mimic ATP in the active site of protein kinase CK2.
Related PDB1daw,1day
[5]
CommentsX-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-337, AND SUBUNIT.
PubMed ID11092945
JournalActa Crystallogr D Biol Crystallogr
Year2000
Volume56
Pages1680-4
AuthorsNiefind K, Guerra B, Ermakowa I, Issinger OG
TitleCrystallization and preliminary characterization of crystals of human protein kinase CK2.
Related UniProtKBP68400,P67870
[6]
CommentsX-ray crystallography
PubMed ID10931203
JournalEur J Biochem
Year2000
Volume267
Pages5184-90
AuthorsBattistutta R, Sarno S, De Moliner E, Marin O, Issinger OG, Zanotti G, Pinna LA
TitleThe crystal structure of the complex of Zea mays alpha subunit with a fragment of human beta subunit provides the clue to the architecture of protein kinase CK2 holoenzyme.
Related PDB1ds5
[7]
CommentsX-ray crystallography
PubMed ID10882732
JournalJ Biol Chem
Year2000
Volume275
Pages29618-22
AuthorsBattistutta R, Sarno S, De Moliner E, Papinutto E, Zanotti G, Pinna LA
TitleThe replacement of ATP by the competitive inhibitor emodin induces conformational modifications in the catalytic site of protein kinase CK2.
Related PDB1f0q
[8]
CommentsX-ray crystallography
PubMed ID11574463
JournalEMBO J
Year2001
Volume20
Pages5320-31
AuthorsNiefind K, Guerra B, Ermakowa I, Issinger OG
TitleCrystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme.
Related PDB1jwh
[9]
CommentsX-ray crystallography
PubMed ID11604527
JournalProtein Sci
Year2001
Volume10
Pages2200-6
AuthorsBattistutta R, De Moliner E, Sarno S, Zanotti G, Pinna LA
TitleStructural features underlying selective inhibition of protein kinase CK2 by ATP site-directed tetrabromo-2-benzotriazole.
Related PDB1j91,1jam
[10]
PubMed ID12417343
JournalFEBS Lett
Year2002
Volume531
Pages363-8
AuthorsTapia J, Jacob G, Allende CC, Allende JE
TitleRole of the carboxyl terminus on the catalytic activity of protein kinase CK2alpha subunit.
[11]
PubMed ID11956194
JournalJ Biol Chem
Year2002
Volume277
Pages22509-14
AuthorsSarno S, Ghisellini P, Pinna LA
TitleUnique activation mechanism of protein kinase CK2. The N-terminal segment is essential for constitutive activity of the catalytic subunit but not of the holoenzyme.
[12]
CommentsX-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-329.
PubMed ID14646071
JournalActa Crystallogr D Biol Crystallogr
Year2003
Volume59
Pages2133-9
AuthorsPechkova E, Zanotti G, Nicolini C
TitleThree-dimensional atomic structure of a catalytic subunit mutant of human protein kinase CK2.
Related PDB1na7
Related UniProtKBP68400
[13]
PubMed ID12396231
JournalBiochem J
Year2003
Volume369
Pages1-15
AuthorsLitchfield DW
TitleProtein kinase CK2: structure, regulation and role in cellular decisions of life and death.
[14]
CommentsX-ray crystallography
PubMed ID12816539
JournalBiochem J
Year2003
Volume374
Pages639-46
AuthorsSarno S, de Moliner E, Ruzzene M, Pagano MA, Battistutta R, Bain J, Fabbro D, Schoepfer J, Elliott M, Furet P, Meggio F, Zanotti G, Pinna LA
TitleBiochemical and three-dimensional-structural study of the specific inhibition of protein kinase CK2 by [5-oxo-5,6-dihydroindolo-(1,2-a)quinazolin-7-yl]acetic acid (IQA).
Related PDB1om1
[15]
PubMed ID12740046
JournalBMC Struct Biol
Year2003
Volume3
Pages4
AuthorsRekha N, Srinivasan N
TitleStructural basis of regulation and substrate specificity of protein kinase CK2 deduced from the modeling of protein-protein interactions.
[16]
CommentsX-ray crystallography
PubMed ID12419810
JournalJ Biol Chem
Year2003
Volume278
Pages1831-6
AuthorsDe Moliner E, Moro S, Sarno S, Zagotto G, Zanotti G, Pinna LA, Battistutta R
TitleInhibition of protein kinase CK2 by anthraquinone-related compounds. A structural insight.
Related PDB1m2p,1m2q,1m2r
[17]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-335.
PubMed ID12860116
JournalJ Mol Biol
Year2003
Volume330
Pages925-34
AuthorsErmakova I, Boldyreff B, Issinger OG, Niefind K
TitleCrystal structure of a C-terminal deletion mutant of human protein kinase CK2 catalytic subunit.
Related PDB1pjk
Related UniProtKBP68400
[18]
CommentsX-ray crystallography
PubMed ID15388915
JournalActa Crystallogr D Biol Crystallogr
Year2004
Volume60
Pages1698-704
AuthorsBertrand L, Sayed MF, Pei XY, Parisini E, Dhanaraj V, Bolanos-Garcia VM, Allende JE, Blundell TL
TitleStructure of the regulatory subunit of CK2 in the presence of a p21WAF1 peptide demonstrates flexibility of the acidic loop.
Related PDB1rqf
[19]
CommentsX-ray crystallography
PubMed ID16298300
JournalChem Biol
Year2005
Volume12
Pages1211-9
AuthorsBattistutta R, Mazzorana M, Sarno S, Kazimierczuk Z, Zanotti G, Pinna LA
TitleInspecting the structure-activity relationship of protein kinase CK2 inhibitors derived from tetrabromo-benzimidazole.
Related PDB1zoe,1zog,1zoh
[20]
CommentsX-ray crystallography
PubMed ID15740749
JournalJ Mol Biol
Year2005
Volume347
Pages399-414
AuthorsYde CW, Ermakova I, Issinger OG, Niefind K
TitleInclining the purine base binding plane in protein kinase CK2 by exchanging the flanking side-chains generates a preference for ATP as a cosubstrate.
Related PDB1lp4,1lpu,1lr4,1ymi
[21]
PubMed ID16335523
JournalMol Cell Biochem
Year2005
Volume274
Pages3-14
AuthorsNiefind K, Issinger OG
TitlePrimary and secondary interactions between CK2alpha and CK2beta lead to ring-like structures in the crystals of the CK2 holoenzyme.
[22]
PubMed ID16342414
JournalMol Cell Biochem
Year2005
Volume274
Pages163-70
AuthorsPoole A, Poore T, Bandhakavi S, McCann RO, Hanna DE, Glover CV
TitleA global view of CK2 function and regulation.
[23]
PubMed ID16806200
JournalFEBS Lett
Year2006
Volume580
Pages3948-52
AuthorsSalvi M, Sarno S, Marin O, Meggio F, Itarte E, Pinna LA
TitleDiscrimination between the activity of protein kinase CK2 holoenzyme and its catalytic subunits.
[24]
PubMed ID17524418
JournalJ Mol Biol
Year2007
Volume370
Pages427-38
AuthorsNiefind K, Yde CW, Ermakova I, Issinger OG
TitleEvolved to be active: sulfate ions define substrate recognition sites of CK2alpha and emphasise its exceptional role within the CMGC family of eukaryotic protein kinases.
Related PDB2pvr
[25]
PubMed ID18291315
JournalChem Biol
Year2008
Volume15
Pages111-7
AuthorsRaaf J, Brunstein E, Issinger OG, Niefind K
TitleThe CK2 alpha/CK2 beta interface of human protein kinase CK2 harbors a binding pocket for small molecules.
Related PDB3h30,3juh
[26]
PubMed ID18242640
JournalJ Mol Biol
Year2008
Volume377
Pages1-8
AuthorsRaaf J, Klopffleisch K, Issinger OG, Niefind K
TitleThe catalytic subunit of human protein kinase CK2 structurally deviates from its maize homologue in complex with the nucleotide competitive inhibitor emodin.
Related PDB3bqc,3c13
[27]
PubMed ID18824508
JournalProtein Sci
Year2008
Volume17
Pages2180-6
AuthorsRaaf J, Brunstein E, Issinger OG, Niefind K
TitleThe interaction of CK2alpha and CK2beta, the subunits of protein kinase CK2, requires CK2beta in a preformed conformation and is enthalpically driven.
Related PDB3eed
[28]
PubMed ID19193990
JournalActa Crystallogr Sect F Struct Biol Cryst Commun
Year2009
Volume65
Pages75-9
AuthorsNakaniwa T, Kinoshita T, Sekiguchi Y, Tada T, Nakanishi I, Kitaura K, Suzuki Y, Ohno H, Hirasawa A, Tsujimoto G
TitleStructure of human protein kinase CK2 alpha 2 with a potent indazole-derivative inhibitor.
Related PDB3e3b
[29]
PubMed ID19361447
JournalJ Mol Biol
Year2009
Volume386
Pages1212-21
AuthorsRaaf J, Issinger OG, Niefind K
TitleFirst inactive conformation of CK2 alpha, the catalytic subunit of protein kinase CK2.
Related PDB3fwq
[30]
PubMed ID19414254
JournalBioorg Med Chem Lett
Year2009
Volume19
Pages2920-3
AuthorsSekiguchi Y, Nakaniwa T, Kinoshita T, Nakanishi I, Kitaura K, Hirasawa A, Tsujimoto G, Tada T
TitleStructural insight into human CK2alpha in complex with the potent inhibitor ellagic acid.
Related PDB2zjw
[31]
PubMed ID20400536
JournalFASEB J
Year2010
Volume24
Pages3171-85
AuthorsLopez-Ramos M, Prudent R, Moucadel V, Sautel CF, Barette C, Lafanechere L, Mouawad L, Grierson D, Schmidt F, Florent JC, Filippakopoulos P, Bullock AN, Knapp S, Reiser JB, Cochet C
TitleNew potent dual inhibitors of CK2 and Pim kinases: discovery and structural insights.
Related PDB3mb6,3mb7
[32]
PubMed ID21093442
JournalFEBS Lett
Year2011
Volume585
Pages104-10
AuthorsFerguson AD, Sheth PR, Basso AD, Paliwal S, Gray K, Fischmann TO, Le HV
TitleStructural basis of CX-4945 binding to human protein kinase CK2.
Related PDB3nga,3nsz
[33]
PubMed ID21241709
JournalJ Mol Biol
Year2011
Volume407
Pages1-12
AuthorsBischoff N, Olsen B, Raaf J, Bretner M, Issinger OG, Niefind K
TitleStructure of the human protein kinase CK2 catalytic subunit CK2alpha' and interaction thermodynamics with the regulatory subunit CK2beta.
Related PDB3ofm

comments
This enzyme forms tetramer composed of two alpha and two beta subunits. Alpha subunit may alternate with isomer alpha' sununit.
This enzyme seems to be homologous to cell division kinase 5 (M00196) and phosphorylase linase (M00198 in EzCatDB), and share the active site. Thus, its catalytic mechanism must be the same as those enzymes.

createdupdated
2004-03-252011-05-02


Copyright: Nozomi Nagano, JST & CBRC-AIST
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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
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Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
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