DB code: M00197

RLCP classification 3.103.126600.1165 : Transfer
CATH domain 3.30.200.20 : Phosphorylase Kinase; domain 1 Catalytic domain
1.10.510.10 : Transferase(Phosphotransferase); domain 1 Catalytic domain
1.10.1820.10 : protein kinase ck2 holoenzyme, chain C, domain 1
2.20.25.20 : N-terminal domain of TfIIb
E.C. 2.7.11.1
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
1.10.510.10 : Transferase(Phosphotransferase); domain 1 M00125 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 1 M00125 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

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam RefSeq
P28020 Casein kinase II subunit alpha
CK II
EC 2.7.11.1
PF00069 (Pkinase)
[Graphical View]
P68400 Casein kinase II subunit alpha
CK II alpha
EC 2.7.11.1
PF00069 (Pkinase)
[Graphical View]
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)
Q6INV5
Ck2a1 protein
PF00069 (Pkinase)
[Graphical View]
NP_001084124.1 (Protein)
NM_001090655.1 (DNA/RNA sequence)
P19784 Casein kinase II subunit alpha''
CK II alpha''
EC 2.7.11.1
PF00069 (Pkinase)
[Graphical View]
NP_001887.1 (Protein)
NM_001896.2 (DNA/RNA sequence)
P28021 Casein kinase II subunit beta
CK II beta
Phosvitin
PF01214 (CK_II_beta)
[Graphical View]
NP_001084126.1 (Protein)
NM_001090657.1 (DNA/RNA sequence)
P67870 Casein kinase II subunit beta
CK II beta
Phosvitin
Protein G5a
PF01214 (CK_II_beta)
[Graphical View]
NP_001311.3 (Protein)
NM_001320.5 (DNA/RNA sequence)

KEGG enzyme name
Non-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

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P28020 CSK21_XENLA ATP + a protein = ADP + a phosphoprotein. Tetramer composed of an alpha chain, an alpha' and two beta chains.
P68400 CSK21_HUMAN ATP + a protein = ADP + a phosphoprotein. 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.
Q6INV5 Q6INV5_XENLA
P19784 CSK22_HUMAN ATP + a protein = ADP + a phosphoprotein. 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.
P28021 CSK2B_XENLA Tetramer composed of an alpha subunit, an alpha' subunit and two beta subunits (By similarity).
P67870 CSK2B_HUMAN 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.

KEGG Pathways
Map code Pathways E.C.

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00305 C00038 C00002 C00017 C00008 C00562
E.C.
Compound Magnesium Zinc ATP Protein ADP Phosphoprotein
Type divalent metal (Ca2+, Mg2+) heavy metal amine group,nucleotide peptide/protein amine group,nucleotide peptide/protein,phosphate group/phosphate ion
ChEBI 18420
18420
29105
29105
15422
15422
16761
16761
PubChem 888
888
32051
32051
5957
5957
6022
6022
1jwhA01 Unbound Unbound Analogue:ANP Unbound Unbound Unbound
1jwhB01 Unbound Unbound Unbound Unbound Unbound Unbound
1na7A01 Unbound Unbound Unbound Unbound Unbound Unbound
1pjkA01 Unbound Unbound Analogue:ANP Unbound Unbound Unbound
1ymiA02 Unbound Unbound Analogue:ANP Unbound Unbound Unbound
2pvrA02 Unbound Unbound Analogue:ANP Unbound Unbound Unbound
2zjwA02 Unbound Unbound Unbound Unbound Unbound Unbound
3bqcA02 Unbound Unbound Unbound Unbound Unbound Unbound
3c13A02 Unbound Unbound Unbound Unbound Unbound Unbound
3fwqA02 Unbound Unbound Unbound Unbound Unbound Unbound
3fwqB02 Unbound Unbound Unbound Unbound Unbound Unbound
3h30A02 Unbound Unbound Unbound Unbound Unbound Unbound
3h30B02 Unbound Unbound Unbound Unbound Unbound Unbound
3juhA02 Unbound Unbound Analogue:ANP Unbound Unbound Unbound
3juhB02 Unbound Unbound Analogue:ANP Unbound Unbound Unbound
3mb6A02 Unbound Unbound Unbound Unbound Unbound Unbound
3mb7A02 Unbound Unbound Unbound Unbound Unbound Unbound
3ngaA02 Unbound Unbound Unbound Unbound Unbound Unbound
3ngaB02 Unbound Unbound Unbound Unbound Unbound Unbound
3nszA02 Unbound Unbound Unbound Unbound Analogue:ANP Unbound
3e3bX02 Unbound Unbound Unbound Unbound Unbound Unbound
3ofmA02 Unbound Unbound Unbound Unbound Unbound Unbound
1jwhA02 Unbound Unbound Unbound Unbound Unbound Unbound
1jwhB02 Unbound Unbound Unbound Unbound Unbound Unbound
1na7A02 Unbound Unbound Unbound Unbound Unbound Unbound
1pjkA02 Unbound Unbound Unbound Unbound Unbound Unbound
1ymiA01 Unbound Unbound Unbound Unbound Unbound Unbound
2pvrA01 Unbound Unbound Unbound Unbound Unbound Unbound
2zjwA01 Unbound Unbound Unbound Unbound Unbound Unbound
3bqcA01 Unbound Unbound Unbound Unbound Unbound Unbound
3c13A01 Unbound Unbound Unbound Unbound Unbound Unbound
3fwqA01 Unbound Unbound Unbound Unbound Unbound Unbound
3fwqB01 Unbound Unbound Unbound Unbound Unbound Unbound
3h30A01 Unbound Unbound Unbound Unbound Unbound Unbound
3h30B01 Unbound Unbound Unbound Unbound Unbound Unbound
3juhA01 Unbound Unbound Unbound Unbound Unbound Unbound
3juhB01 Unbound Unbound Unbound Unbound Unbound Unbound
3mb6A01 Unbound Unbound Unbound Unbound Unbound Unbound
3mb7A01 Unbound Unbound Unbound Unbound Unbound Unbound
3ngaA01 Unbound Unbound Unbound Unbound Unbound Unbound
3ngaB01 Unbound Unbound Unbound Unbound Unbound Unbound
3nszA01 Bound:2x_MG Unbound Unbound Unbound Unbound Unbound
3e3bX01 Unbound Unbound Unbound Unbound Unbound Unbound
3ofmA01 Unbound Unbound Unbound Unbound Unbound Unbound
1rqfA01 Unbound Unbound Unbound Unbound Unbound Unbound
1rqfB01 Unbound Unbound Unbound Unbound Unbound Unbound
1rqfD01 Unbound Unbound Unbound Unbound Unbound Unbound
1rqfE01 Unbound Unbound Unbound Unbound Unbound Unbound
1rqfG01 Unbound Unbound Unbound Unbound Unbound Unbound
1rqfH01 Unbound Unbound Unbound Unbound Unbound Unbound
1rqfJ01 Unbound Unbound Unbound Unbound Unbound Unbound
1rqfK01 Unbound Unbound Unbound Unbound Unbound Unbound
1jwhC01 Unbound Unbound Unbound Unbound Unbound Unbound
1jwhD01 Unbound Unbound Unbound Unbound Unbound Unbound
1qf8A01 Unbound Unbound Unbound Unbound Unbound Unbound
1qf8B01 Unbound Unbound Unbound Unbound Unbound Unbound
3eedA01 Unbound Unbound Unbound Unbound Unbound Unbound
3eedB01 Unbound Unbound Unbound Unbound Unbound Unbound
1rqfA02 Unbound Bound:_ZN Unbound Unbound Unbound Unbound
1rqfB02 Unbound Bound:_ZN Unbound Unbound Unbound Unbound
1rqfD02 Unbound Bound:_ZN Unbound Unbound Unbound Unbound
1rqfE02 Unbound Bound:_ZN Unbound Unbound Unbound Unbound
1rqfG02 Unbound Bound:_ZN Unbound Unbound Unbound Unbound
1rqfH02 Unbound Bound:_ZN Unbound Unbound Unbound Unbound
1rqfJ02 Unbound Bound:_ZN Unbound Unbound Unbound Unbound
1rqfK02 Unbound Bound:_ZN Unbound Unbound Unbound Unbound
1jwhC02 Unbound Bound:_ZN Unbound Unbound Unbound Unbound
1jwhD02 Unbound Bound:_ZN Unbound Unbound Unbound Unbound
1qf8A02 Unbound Bound:_ZN Unbound Unbound Unbound Unbound
1qf8B02 Unbound Bound:_ZN Unbound Unbound Unbound Unbound
3eedA02 Unbound Bound:_ZN Unbound Unbound Unbound Unbound
3eedB02 Unbound Bound:_ZN Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [2], [8]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1jwhA01 LYS 68 LYS 49;TYR 50;SER 51
1jwhB01 LYS 68 LYS 49;TYR 50;SER 51
1na7A01 LYS 68 LYS 49;TYR 50;SER 51 mutant E27A, K76N
1pjkA01 LYS 68 LYS 49;TYR 50;SER 51
1ymiA02 LYS 68 LYS 49;TYR 50;SER 51 mutant V66A
2pvrA02 LYS 68 LYS 49;TYR 50;SER 51
2zjwA02 LYS 68 LYS 49;TYR 50;SER 51
3bqcA02 LYS 68 LYS 49;TYR 50;SER 51
3c13A02 LYS 68 LYS 49;TYR 50;SER 51
3fwqA02 LYS 68 LYS 49;TYR 50;SER 51
3fwqB02 LYS 68 LYS 49;TYR 50;SER 51
3h30A02 LYS 68 LYS 49;TYR 50;SER 51
3h30B02 LYS 68 LYS 49;TYR 50;SER 51
3juhA02 LYS 68 LYS 49;TYR 50;SER 51
3juhB02 LYS 68 LYS 49;TYR 50;SER 51
3mb6A02 LYS 68 LYS 49;TYR 50;SER 51
3mb7A02 LYS 68 LYS 49;TYR 50;SER 51
3ngaA02 LYS 68 LYS 49;TYR 50;SER 51
3ngaB02 LYS 68 LYS 49;TYR 50;SER 51
3nszA02 LYS 68 LYS 49;TYR 50;SER 51
3e3bX02 LYS 69 LYS 50;TYR 51;SER 52
3ofmA02 LYS 69 LYS 50;TYR 51;SER 52
1jwhA02 ASP 156;LYS 158 ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
1jwhB02 ASP 156;LYS 158 ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
1na7A02 ASP 156;LYS 158 ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
1pjkA02 ASP 156;LYS 158 ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
1ymiA01 ASP 156;LYS 158 ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding) mutant M163L
2pvrA01 ASP 156;LYS 158 ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
2zjwA01 ASP 156;LYS 158 ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
3bqcA01 ASP 156;LYS 158 ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
3c13A01 ASP 156;LYS 158 ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
3fwqA01 ASP 156;LYS 158 ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
3fwqB01 ASP 156;LYS 158 ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
3h30A01 ASP 156;LYS 158 ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
3h30B01 ASP 156;LYS 158 ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
3juhA01 ASP 156;LYS 158 ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
3juhB01 ASP 156;LYS 158 ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
3mb6A01 ASP 156;LYS 158 ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
3mb7A01 ASP 156;LYS 158 ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
3ngaA01 ASP 156;LYS 158 ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
3ngaB01 ASP 156;LYS 158 ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
3nszA01 ASP 156;LYS 158 ASN 161(Magnesium-2 binding);ASP 175(Magnesium-1 binding)
3e3bX01 ASP 157;LYS 159 ASN 162(Magnesium-2 binding);ASP 176(Magnesium-1 binding)
3ofmA01 ASP 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 for Catalytic Mechanism
References Sections No. of steps in catalysis

References
[1]
Resource
Comments
Medline ID
PubMed ID 7735313
Journal Cell Mol Biol Res
Year 1994
Volume 40
Pages 391-9
Authors Boldyreff B, Meggio F, Pinna LA, Issinger OG
Title Protein kinase CK2 structure-function relationship: effects of the beta subunit on reconstitution and activity.
Related PDB
Related UniProtKB
[2]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS)
Medline ID 98232491
PubMed ID 9564028
Journal EMBO J
Year 1998
Volume 17
Pages 2451-62
Authors Niefind K, Guerra B, Pinna LA, Issinger OG, Schomburg D
Title Crystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at 2.1 A resolution.
Related PDB 1a6o
Related UniProtKB P28523
[3]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10357806
Journal EMBO J
Year 1999
Volume 18
Pages 2930-40
Authors Chantalat L, Leroy D, Filhol O, Nueda A, Benitez MJ, Chambaz EM, Cochet C, Dideberg O
Title Crystal structure of the human protein kinase CK2 regulatory subunit reveals its zinc finger-mediated dimerization.
Related PDB 1qf8
Related UniProtKB
[4]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10581548
Journal Nat Struct Biol
Year 1999
Volume 6
Pages 1100-3
Authors Niefind K, Putter M, Guerra B, Issinger OG, Schomburg D
Title GTP plus water mimic ATP in the active site of protein kinase CK2.
Related PDB 1daw 1day
Related UniProtKB
[5]
Resource
Comments X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-337, AND SUBUNIT.
Medline ID
PubMed ID 11092945
Journal Acta Crystallogr D Biol Crystallogr
Year 2000
Volume 56
Pages 1680-4
Authors Niefind K, Guerra B, Ermakowa I, Issinger OG
Title Crystallization and preliminary characterization of crystals of human protein kinase CK2.
Related PDB
Related UniProtKB P68400 P67870
[6]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10931203
Journal Eur J Biochem
Year 2000
Volume 267
Pages 5184-90
Authors Battistutta R, Sarno S, De Moliner E, Marin O, Issinger OG, Zanotti G, Pinna LA
Title The 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 PDB 1ds5
Related UniProtKB
[7]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10882732
Journal J Biol Chem
Year 2000
Volume 275
Pages 29618-22
Authors Battistutta R, Sarno S, De Moliner E, Papinutto E, Zanotti G, Pinna LA
Title The replacement of ATP by the competitive inhibitor emodin induces conformational modifications in the catalytic site of protein kinase CK2.
Related PDB 1f0q
Related UniProtKB
[8]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11574463
Journal EMBO J
Year 2001
Volume 20
Pages 5320-31
Authors Niefind K, Guerra B, Ermakowa I, Issinger OG
Title Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme.
Related PDB 1jwh
Related UniProtKB
[9]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11604527
Journal Protein Sci
Year 2001
Volume 10
Pages 2200-6
Authors Battistutta R, De Moliner E, Sarno S, Zanotti G, Pinna LA
Title Structural features underlying selective inhibition of protein kinase CK2 by ATP site-directed tetrabromo-2-benzotriazole.
Related PDB 1j91 1jam
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 12417343
Journal FEBS Lett
Year 2002
Volume 531
Pages 363-8
Authors Tapia J, Jacob G, Allende CC, Allende JE
Title Role of the carboxyl terminus on the catalytic activity of protein kinase CK2alpha subunit.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 11956194
Journal J Biol Chem
Year 2002
Volume 277
Pages 22509-14
Authors Sarno S, Ghisellini P, Pinna LA
Title 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.
Related PDB
Related UniProtKB
[12]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-329.
Medline ID
PubMed ID 14646071
Journal Acta Crystallogr D Biol Crystallogr
Year 2003
Volume 59
Pages 2133-9
Authors Pechkova E, Zanotti G, Nicolini C
Title Three-dimensional atomic structure of a catalytic subunit mutant of human protein kinase CK2.
Related PDB 1na7
Related UniProtKB P68400
[13]
Resource
Comments
Medline ID
PubMed ID 12396231
Journal Biochem J
Year 2003
Volume 369
Pages 1-15
Authors Litchfield DW
Title Protein kinase CK2: structure, regulation and role in cellular decisions of life and death.
Related PDB
Related UniProtKB
[14]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 12816539
Journal Biochem J
Year 2003
Volume 374
Pages 639-46
Authors Sarno 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
Title Biochemical 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 PDB 1om1
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 12740046
Journal BMC Struct Biol
Year 2003
Volume 3
Pages 4
Authors Rekha N, Srinivasan N
Title Structural basis of regulation and substrate specificity of protein kinase CK2 deduced from the modeling of protein-protein interactions.
Related PDB
Related UniProtKB
[16]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 12419810
Journal J Biol Chem
Year 2003
Volume 278
Pages 1831-6
Authors De Moliner E, Moro S, Sarno S, Zagotto G, Zanotti G, Pinna LA, Battistutta R
Title Inhibition of protein kinase CK2 by anthraquinone-related compounds. A structural insight.
Related PDB 1m2p 1m2q 1m2r
Related UniProtKB
[17]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-335.
Medline ID
PubMed ID 12860116
Journal J Mol Biol
Year 2003
Volume 330
Pages 925-34
Authors Ermakova I, Boldyreff B, Issinger OG, Niefind K
Title Crystal structure of a C-terminal deletion mutant of human protein kinase CK2 catalytic subunit.
Related PDB 1pjk
Related UniProtKB P68400
[18]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 15388915
Journal Acta Crystallogr D Biol Crystallogr
Year 2004
Volume 60
Pages 1698-704
Authors Bertrand L, Sayed MF, Pei XY, Parisini E, Dhanaraj V, Bolanos-Garcia VM, Allende JE, Blundell TL
Title Structure of the regulatory subunit of CK2 in the presence of a p21WAF1 peptide demonstrates flexibility of the acidic loop.
Related PDB 1rqf
Related UniProtKB
[19]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 16298300
Journal Chem Biol
Year 2005
Volume 12
Pages 1211-9
Authors Battistutta R, Mazzorana M, Sarno S, Kazimierczuk Z, Zanotti G, Pinna LA
Title Inspecting the structure-activity relationship of protein kinase CK2 inhibitors derived from tetrabromo-benzimidazole.
Related PDB 1zoe 1zog 1zoh
Related UniProtKB
[20]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 15740749
Journal J Mol Biol
Year 2005
Volume 347
Pages 399-414
Authors Yde CW, Ermakova I, Issinger OG, Niefind K
Title Inclining the purine base binding plane in protein kinase CK2 by exchanging the flanking side-chains generates a preference for ATP as a cosubstrate.
Related PDB 1lp4 1lpu 1lr4 1ymi
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 16335523
Journal Mol Cell Biochem
Year 2005
Volume 274
Pages 3-14
Authors Niefind K, Issinger OG
Title Primary and secondary interactions between CK2alpha and CK2beta lead to ring-like structures in the crystals of the CK2 holoenzyme.
Related PDB
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 16342414
Journal Mol Cell Biochem
Year 2005
Volume 274
Pages 163-70
Authors Poole A, Poore T, Bandhakavi S, McCann RO, Hanna DE, Glover CV
Title A global view of CK2 function and regulation.
Related PDB
Related UniProtKB
[23]
Resource
Comments
Medline ID
PubMed ID 16806200
Journal FEBS Lett
Year 2006
Volume 580
Pages 3948-52
Authors Salvi M, Sarno S, Marin O, Meggio F, Itarte E, Pinna LA
Title Discrimination between the activity of protein kinase CK2 holoenzyme and its catalytic subunits.
Related PDB
Related UniProtKB
[24]
Resource
Comments
Medline ID
PubMed ID 17524418
Journal J Mol Biol
Year 2007
Volume 370
Pages 427-38
Authors Niefind K, Yde CW, Ermakova I, Issinger OG
Title Evolved 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 PDB 2pvr
Related UniProtKB
[25]
Resource
Comments
Medline ID
PubMed ID 18291315
Journal Chem Biol
Year 2008
Volume 15
Pages 111-7
Authors Raaf J, Brunstein E, Issinger OG, Niefind K
Title The CK2 alpha/CK2 beta interface of human protein kinase CK2 harbors a binding pocket for small molecules.
Related PDB 3h30 3juh
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 18242640
Journal J Mol Biol
Year 2008
Volume 377
Pages 1-8
Authors Raaf J, Klopffleisch K, Issinger OG, Niefind K
Title The catalytic subunit of human protein kinase CK2 structurally deviates from its maize homologue in complex with the nucleotide competitive inhibitor emodin.
Related PDB 3bqc 3c13
Related UniProtKB
[27]
Resource
Comments
Medline ID
PubMed ID 18824508
Journal Protein Sci
Year 2008
Volume 17
Pages 2180-6
Authors Raaf J, Brunstein E, Issinger OG, Niefind K
Title The interaction of CK2alpha and CK2beta, the subunits of protein kinase CK2, requires CK2beta in a preformed conformation and is enthalpically driven.
Related PDB 3eed
Related UniProtKB
[28]
Resource
Comments
Medline ID
PubMed ID 19193990
Journal Acta Crystallogr Sect F Struct Biol Cryst Commun
Year 2009
Volume 65
Pages 75-9
Authors Nakaniwa T, Kinoshita T, Sekiguchi Y, Tada T, Nakanishi I, Kitaura K, Suzuki Y, Ohno H, Hirasawa A, Tsujimoto G
Title Structure of human protein kinase CK2 alpha 2 with a potent indazole-derivative inhibitor.
Related PDB 3e3b
Related UniProtKB
[29]
Resource
Comments
Medline ID
PubMed ID 19361447
Journal J Mol Biol
Year 2009
Volume 386
Pages 1212-21
Authors Raaf J, Issinger OG, Niefind K
Title First inactive conformation of CK2 alpha, the catalytic subunit of protein kinase CK2.
Related PDB 3fwq
Related UniProtKB
[30]
Resource
Comments
Medline ID
PubMed ID 19414254
Journal Bioorg Med Chem Lett
Year 2009
Volume 19
Pages 2920-3
Authors Sekiguchi Y, Nakaniwa T, Kinoshita T, Nakanishi I, Kitaura K, Hirasawa A, Tsujimoto G, Tada T
Title Structural insight into human CK2alpha in complex with the potent inhibitor ellagic acid.
Related PDB 2zjw
Related UniProtKB
[31]
Resource
Comments
Medline ID
PubMed ID 20400536
Journal FASEB J
Year 2010
Volume 24
Pages 3171-85
Authors Lopez-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
Title New potent dual inhibitors of CK2 and Pim kinases: discovery and structural insights.
Related PDB 3mb6 3mb7
Related UniProtKB
[32]
Resource
Comments
Medline ID
PubMed ID 21093442
Journal FEBS Lett
Year 2011
Volume 585
Pages 104-10
Authors Ferguson AD, Sheth PR, Basso AD, Paliwal S, Gray K, Fischmann TO, Le HV
Title Structural basis of CX-4945 binding to human protein kinase CK2.
Related PDB 3nga 3nsz
Related UniProtKB
[33]
Resource
Comments
Medline ID
PubMed ID 21241709
Journal J Mol Biol
Year 2011
Volume 407
Pages 1-12
Authors Bischoff N, Olsen B, Raaf J, Bretner M, Issinger OG, Niefind K
Title Structure of the human protein kinase CK2 catalytic subunit CK2alpha' and interaction thermodynamics with the regulatory subunit CK2beta.
Related PDB 3ofm
Related UniProtKB

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.

Created Updated
2004-03-25 2011-05-02