Reviewed, UniProtKB/Swiss-Prot P68400 (CSK21_HUMAN)

Names and origin

Protein names

Recommended name:
    Casein kinase II subunit alpha
      Short name=CK II
    EC=2.7.11.1

Gene names

Name:	CSNK2A1
Synonyms:	CK2A1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	391 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. The alpha and alpha' chains contain the catalytic site. Participates in Wnt signaling. CK2 phosphorylates 'Ser-392' of p53/TP53 following UV irradiation.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	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.
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CK2 subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Wnt signaling pathway
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	Wnt receptor signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW protein amino acid phosphorylation Ref.2 Traceable author statement. Source: ProtInc
Cellular component	nucleus Traceable author statement. Source: ProtInc plasma membrane Traceable author statement. Source: ProtInc
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro protein N-terminus binding Inferred from physical interaction. Source: UniProtKB protein serine/threonine kinase activity Ref.2 Traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARRB1	P49407	1	EBI-347804,EBI-743313
CSNK2B	P67870	2	EBI-347804,EBI-348169
PML	P29590	2	EBI-347804,EBI-295890
RNPS1	Q15287	1	EBI-347804,EBI-395959
SET	Q01105	1	EBI-347804,EBI-1053182
SPTBN1	Q01082-2	1	EBI-347804,EBI-351584
YWHAB	P31946	1	EBI-347804,EBI-359815

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 391

391

Casein kinase II subunit alpha

PRO_0000085883

Regions

Domain

39 – 324

286

Protein kinase

Nucleotide binding

45 – 53

9

ATP By similarity

Sites

Active site

156

1

Proton acceptor

Binding site

68

1

ATP By similarity

Experimental info

Sequence conflict

128

1

L → F in CAA49758. Ref.3

Sequence conflict

256

1

D → G in CAA49758. Ref.3

Sequence conflict

287

1

S → R in CAA49758. Ref.3

Sequence conflict

351

1

M → V in CAA49758. Ref.3

Secondary structure

1

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391

Helix Strand Turn

Details...

Beta strand

10 – 12

3

Helix

15 – 18

4

Helix

21 – 24

4

Helix

26 – 28

3

Helix

36 – 38

3

Beta strand

39 – 47

9

Beta strand

49 – 58

10

Turn

59 – 61

3

Beta strand

64 – 70

7

Helix

75 – 87

13

Beta strand

97 – 102

6

Turn

104 – 106

3

Beta strand

108 – 113

6

Helix

121 – 124

4

Helix

130 – 149

20

Helix

159 – 161

3

Beta strand

162 – 165

4

Turn

166 – 169

4

Beta strand

170 – 173

4

Helix

195 – 197

3

Helix

200 – 203

4

Helix

212 – 227

16

Beta strand

230 – 233

4

Helix

238 – 249

12

Helix

252 – 260

9

Helix

267 – 270

4

Turn

281 – 284

4

Turn

287 – 289

3

Helix

290 – 292

3

Helix

295 – 304

10

Helix

315 – 319

5

Helix

322 – 324

3

Sequences

	Sequence		Length	Mass (Da)
	P68400-1 [UniParc]. Last modified November 23, 2004. Version 1. Checksum: D3B6F5D13FF7422D	FASTA	391	45,144
	10 20 30 40 50 60 MSGPVPSRAR VYTDVNTHRP REYWDYESHV VEWGNQDDYQ LVRKLGRGKY SEVFEAINIT 70 80 90 100 110 120 NNEKVVVKIL KPVKKKKIKR EIKILENLRG GPNIITLADI VKDPVSRTPA LVFEHVNNTD 130 140 150 160 170 180 FKQLYQTLTD YDIRFYMYEI LKALDYCHSM GIMHRDVKPH NVMIDHEHRK LRLIDWGLAE 190 200 210 220 230 240 FYHPGQEYNV RVASRYFKGP ELLVDYQMYD YSLDMWSLGC MLASMIFRKE PFFHGHDNYD 250 260 270 280 290 300 QLVRIAKVLG TEDLYDYIDK YNIELDPRFN DILGRHSRKR WERFVHSENQ HLVSPEALDF 310 320 330 340 350 360 LDKLLRYDHQ SRLTAREAME HPYFYTVVKD QARMGSSSMP GGSTPVSSAN MMSGISSVPT 370 380 390 PSPLGPLAGS PVIAAANPLG MPVPAAAGAQ Q

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of the human casein kinase II alpha subunit." Meisner H., Heller-Harrison R., Buxton J., Czech M.P. Biochemistry 28:4072-4076(1989) [PubMed: 2752008] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Isolation and characterization of human cDNA clones encoding the alpha and the alpha' subunits of casein kinase II." Lozeman F.J., Litchfield D.W., Piening C., Takio K., Walsh K.A., Krebs E.G. Biochemistry 29:8436-8447(1990) [PubMed: 2174700] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Structure and sequence of an intronless gene for human casein kinase II-alpha subunit." Devilat I., Carvallo P. FEBS Lett. 316:114-118(1993) [PubMed: 8420794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung, Muscle and Uterus.
[6]	"A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1." Keller D.M., Zeng X., Wang Y., Zhang Q.H., Kapoor M., Shu H., Goodman R., Lozano G., Zhao Y., Lu H. Mol. Cell 7:283-292(2001) [PubMed: 11239457] [Abstract] Cited for: FUNCTION, INTERACTION WITH SSRP1 AND SUPT16H.
[7]	"p53 serine 392 phosphorylation increases after UV through induction of the assembly of the CK2.hSPT16.SSRP1 complex." Keller D.M., Lu H. J. Biol. Chem. 277:50206-50213(2002) [PubMed: 12393879] [Abstract] Cited for: INTERACTION WITH SSRP1 AND SUPT16H.
[8]	"Activation of pre-mRNA splicing by human RNPS1 is regulated by CK2 phosphorylation." Trembley J.H., Tatsumi S., Sakashita E., Loyer P., Slaughter C.A., Suzuki H., Endo H., Kidd V.J., Mayeda A. Mol. Cell. Biol. 25:1446-1457(2005) [PubMed: 15684395] [Abstract] Cited for: INTERACTION WITH RNPS1.
[9]	"Crystallization and preliminary characterization of crystals of human protein kinase CK2." Niefind K., Guerra B., Ermakowa I., Issinger O.G. Acta Crystallogr. D 56:1680-1684(2000) [PubMed: 11092945] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-337, SUBUNIT.
[10]	"Three-dimensional atomic structure of a catalytic subunit mutant of human protein kinase CK2." Pechkova E., Zanotti G., Nicolini C. Acta Crystallogr. D 59:2133-2139(2003) [PubMed: 14646071] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-329.
[11]	"Crystal structure of a C-terminal deletion mutant of human protein kinase CK2 catalytic subunit." Ermakova I., Boldyreff B., Issinger O.G., Niefind K. J. Mol. Biol. 330:925-934(2003) [PubMed: 12860116] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-335.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

J02853 mRNA. Translation: AAA56821.1.
M55265 mRNA. Translation: AAA35503.1.
X70251 Genomic DNA. Translation: CAA49758.1.
AL049761 Genomic DNA. Translation: CAB65624.1.
BC011668 mRNA. Translation: AAH11668.1.
BC053532 mRNA. Translation: AAH53532.1.
BC071167 mRNA. Translation: AAH71167.1.

PIR

A30319.

RefSeq

NP_001886.1.
NP_808227.1.
NP_808228.1.

UniGene

Hs.654675
Hs.701971

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JWH	X-ray	3.10	A/B	1-337	[»]
1NA7	X-ray	2.40	A	1-329	[»]
1PJK	X-ray	2.50	A	2-335	[»]
1YMI	X-ray	1.66	A	2-335	[»]
2PVR	X-ray	1.60	A	2-335	[»]
2RKP	X-ray	1.56	A	1-335	[»]
3BQC	X-ray	1.50	A	1-335	[»]
3BW5	X-ray	1.66	A	1-335	[»]
3C13	X-ray	1.95	A	1-335	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P68400.

PTM databases

PhosphoSite

P68400.

Genome annotation databases

Ensembl

ENSG00000101266. Homo sapiens. [Contig view]

GeneID

1457.

KEGG

hsa:1457.

Organism-specific databases

H-InvDB

HIX0015555.

HGNC

HGNC:2457. CSNK2A1.

MIM

115440. gene.

PharmGKB

PA26957.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOVERGEN

P68400.

Gene expression databases

ArrayExpress

P68400.

CleanEx

HS_CSNK2A1.

GermOnline

ENSG00000101266. Homo sapiens.

Family and domain databases

InterPro

IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_bd_CS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

ProDom

PD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

PROSITE