P68400 (CSK21_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Casein kinase II subunit alpha
Short name=CK II alpha
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.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apopotosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV. Ref.11 Ref.12 Ref.14 Ref.17
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Constitutively active protein kinase whose activity is not directly affected by phosphorylation. Seems to be regulated by level of expression and localization.
Subunit structure	Heterotetramer composed of two catalytic subunits (alpha chain and/or alpha' chain) and two regulatory subunits (beta chains). The tetramer can exist as a combination of 2 alpha/2 beta, 2 alpha'/2 beta or 1 alpha/1 alpha'/2 beta subunits. Also part of a CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, which forms following UV irradiation. Interacts with RNPS1. Ref.11 Ref.13 Ref.15 Ref.27
Post-translational modification	Phosphorylated at Thr-344, Thr-360, Ser-362 and Ser-370 by CDK1 in prophase and metaphase and dephosphorylated during anaphase. Phosphorylation does not directly affect casein kinase 2 activity, but may contribute to its regulation by forming binding sites for interacting proteins and/or targeting it to different compartments. Ref.10 Ref.16 Ref.18
Miscellaneous	Can use both ATP and GTP as phosphoryl donors. Phosphorylation by casein kinase 2 has been estimated to represent up to one quarter of the eukaryotic phosphoproteome. Casein kinase 2 has been found to be inccreased at protein level and up-regulated at the level of enzyme activity in the majority of cancers. However, elevated levels of casein kinase 2 are present in certain normal organs such as brain and testes.
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CK2 subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Apoptosis Cell cycle Transcription Transcription regulation Wnt signaling pathway
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	Wnt receptor signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW axon guidance Traceable author statement. Source: Reactome cell cycle Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	NuRD complex Inferred from direct assay. Source: BHF-UCL Sin3 complex Inferred from direct assay. Source: BHF-UCL cytosol Traceable author statement. Source: Reactome plasma membrane Traceable author statement. Source: ProtInc
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein N-terminus binding Inferred from physical interaction. Source: UniProtKB protein serine/threonine kinase activity Traceable author statement Ref.2. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CBX4	O00257-3	2	EBI-347804,EBI-4392727
CSNK2A2	P19784	2	EBI-347804,EBI-347451
CSNK2B	P67870	10	EBI-347804,EBI-348169
KIF5C	O60282	4	EBI-347804,EBI-717170
PML	P29590	2	EBI-347804,EBI-295890
SIRT1	Q96EB6	2	EBI-347804,EBI-1802965

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P68400-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P68400-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-136: Missing.

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

Region

36 – 41

6

Interaction with beta subunit By similarity

Sites

Active site

156

1

Proton acceptor

Binding site

68

1

ATP By similarity

Amino acid modifications

Modified residue

2

1

Phosphoserine Ref.16 Ref.18

Modified residue

7

1

Phosphoserine Ref.18

Modified residue

50

1

Phosphotyrosine Ref.18

Modified residue

102

1

N6-acetyllysine Ref.19

Modified residue

125

1

Phosphotyrosine Ref.18

Modified residue

127

1

Phosphothreonine Ref.18

Modified residue

194

1

Phosphoserine Ref.16

Modified residue

255

1

Phosphotyrosine Ref.18

Modified residue

277

1

Phosphoserine Ref.18

Modified residue

287

1

Phosphoserine Ref.18

Modified residue

344

1

Phosphothreonine; by CDK1 Ref.10

Modified residue

360

1

Phosphothreonine; by CDK1 Ref.10

Modified residue

362

1

Phosphoserine; by CDK1 Ref.10 Ref.16

Modified residue

370

1

Phosphoserine; by CDK1 Ref.10 Ref.16

Natural variations

Alternative sequence

1 – 136

136

Missing in isoform 2.

VSP_041925

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)
	Isoform 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
	Isoform 2 [UniParc]. Checksum: ABCEE52F34E7431B	FASTA	255	29,181
	10 20 30 40 50 60 MYEILKALDY CHSMGIMHRD VKPHNVMIDH EHRKLRLIDW GLAEFYHPGQ EYNVRVASRY 70 80 90 100 110 120 FKGPELLVDY QMYDYSLDMW SLGCMLASMI FRKEPFFHGH DNYDQLVRIA KVLGTEDLYD 130 140 150 160 170 180 YIDKYNIELD PRFNDILGRH SRKRWERFVH SENQHLVSPE ALDFLDKLLR YDHQSRLTAR 190 200 210 220 230 240 EAMEHPYFYT VVKDQARMGS SSMPGGSTPV SSANMMSGIS SVPTPSPLGP LAGSPVIAAA 250 NPLGMPVPAA AGAQQ

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] (ISOFORM 1).
[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] (ISOFORM 1).
[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 / MRNA] (ISOFORM 1).
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[5]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]	"Human protein factory for converting the transcriptome into an in vitro-expressed proteome." Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N. Nat. Methods 5:1011-1017(2008) [PubMed: 19054851] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]	"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].
[8]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"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] (ISOFORM 1). Tissue: Lung, Muscle and Uterus.
[10]	"Phosphorylation of casein kinase II by p34cdc2. Identification of phosphorylation sites using phosphorylation site mutants in vitro." Bosc D.G., Slominski E., Sichler C., Litchfield D.W. J. Biol. Chem. 270:25872-25878(1995) [PubMed: 7592773] [Abstract] Cited for: PHOSPHORYLATION AT THR-344; THR-360; SER-362 AND SER-370.
[11]	"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.
[12]	"Protein kinase CK2 is involved in G2 arrest and apoptosis following spindle damage in epithelial cells." Sayed M., Pelech S., Wong C., Marotta A., Salh B. Oncogene 20:6994-7005(2001) [PubMed: 11704824] [Abstract] Cited for: FUNCTION IN CELL CYCLE.
[13]	"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.
[14]	"Caspase-2 primes cancer cells for TRAIL-mediated apoptosis by processing procaspase-8." Shin S., Lee Y., Kim W., Ko H., Choi H., Kim K. EMBO J. 24:3532-3542(2005) [PubMed: 16193064] [Abstract] Cited for: FUNCTION IN APOPTOSIS.
[15]	"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.
[16]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-194; SER-362 AND SER-370, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Evidence for regulation of mitotic progression through temporal phosphorylation and dephosphorylation of CK2alpha." St-Denis N.A., Derksen D.R., Litchfield D.W. Mol. Cell. Biol. 29:2068-2081(2009) [PubMed: 19188443] [Abstract] Cited for: FUNCTION IN CELL CYCLE.
[18]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-7; TYR-50; TYR-125; THR-127; TYR-255; SER-277 AND SER-287, MASS SPECTROMETRY.
[19]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-102, MASS SPECTROMETRY.
[20]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]	"One-thousand-and-one substrates of protein kinase CK2?" Meggio F., Pinna L.A. FASEB J. 17:349-368(2003) [PubMed: 12631575] [Abstract] Cited for: REVIEW ON FUNCTION.
[22]	"Protein kinase CK2 in health and disease: Protein kinase CK2: from structures to insights." Niefind K., Raaf J., Issinger O.G. Cell. Mol. Life Sci. 66:1800-1816(2009) [PubMed: 19387553] [Abstract] Cited for: REVIEW ON STRUCTURE.
[23]	"Protein kinase CK2 in health and disease: From birth to death: the role of protein kinase CK2 in the regulation of cell proliferation and survival." St-Denis N.A., Litchfield D.W. Cell. Mol. Life Sci. 66:1817-1829(2009) [PubMed: 19387552] [Abstract] Cited for: REVIEW ON FUNCTION.
[24]	"Protein kinase CK2 in health and disease: Cellular functions of protein kinase CK2: a dynamic affair." Filhol O., Cochet C. Cell. Mol. Life Sci. 66:1830-1839(2009) [PubMed: 19387551] [Abstract] Cited for: REVIEW ON FUNCTION.
[25]	"Protein kinase CK2 in health and disease: CK2: the kinase controlling the Hsp90 chaperone machinery." Miyata Y. Cell. Mol. Life Sci. 66:1840-1849(2009) [PubMed: 19387550] [Abstract] Cited for: REVIEW ON FUNCTION IN REGULATION OF HSP90.
[26]	"Protein kinase CK2 in health and disease: CK2 and its role in Wnt and NF-kappaB signaling: linking development and cancer." Dominguez I., Sonenshein G.E., Seldin D.C. Cell. Mol. Life Sci. 66:1850-1857(2009) [PubMed: 19387549] [Abstract] Cited for: REVIEW ON FUNCTION IN WNT SIGNALING.
[27]	"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.
[28]	"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.
[29]	"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

EMBL
GenBank
DDBJ

J02853 mRNA. Translation: AAA56821.1.
M55265 mRNA. Translation: AAA35503.1.
S53149 mRNA. Translation: ABB72474.1.
X70251 Genomic DNA. Translation: CAA49758.1.
AK302583 mRNA. Translation: BAG63838.1.
BT019792 mRNA. Translation: AAV38595.1.
AB451279 mRNA. Translation: BAG70093.1.
AL049761 Genomic DNA. Translation: CAB65624.1.
CH471133 Genomic DNA. Translation: EAX10665.1.
CH471133 Genomic DNA. Translation: EAX10666.1.
CH471133 Genomic DNA. Translation: EAX10667.1.
CH471133 Genomic DNA. Translation: EAX10668.1.
CH471133 Genomic DNA. Translation: EAX10669.1.
BC011668 mRNA. Translation: AAH11668.1.
BC053532 mRNA. Translation: AAH53532.1.
BC071167 mRNA. Translation: AAH71167.1.

IPI

IPI00744507.

PIR

A30319.

RefSeq

NP_001886.1. NM_001895.3.
NP_808227.1. NM_177559.2.
NP_808228.1. NM_177560.2.

UniGene

Hs.644056.
Hs.654675.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
2PVR	X-ray	1.60	A	2-335	[»]
2ZJW	X-ray	2.40	A	1-335	[»]
3AMY	X-ray	2.30	A	1-335	[»]
3AT2	X-ray	1.60	A	1-335	[»]
3AT3	X-ray	2.60	A	1-335	[»]
3AT4	X-ray	2.20	A	1-335	[»]
3BQC	X-ray	1.50	A	1-335	[»]
3C13	X-ray	1.95	A	1-335	[»]
3FWQ	X-ray	2.30	A/B	1-335	[»]
3H30	X-ray	1.56	A/B	1-334	[»]
3JUH	X-ray	1.66	A/B	1-335	[»]
3MB6	X-ray	1.75	A	1-331	[»]
3MB7	X-ray	1.65	A	1-331	[»]
3NGA	X-ray	2.71	A/B	1-333	[»]
3NSZ	X-ray	1.30	A	2-331	[»]
3OWJ	X-ray	1.85	A	1-331	[»]
3OWK	X-ray	1.80	A	1-331	[»]
3OWL	X-ray	2.10	A	1-331	[»]
3PE1	X-ray	1.60	A	1-337	[»]
3PE2	X-ray	1.90	A	1-337	[»]
3PE4	X-ray	1.95	B/D	340-352	[»]
3RP0	X-ray	3.00	A/B/C/D	1-329	[»]
3RPS	X-ray	2.30	A/B	1-335	[»]
3TAX	X-ray	1.88	B/D	340-352	[»]

ProteinModelPortal

P68400.

SMR

P68400. Positions 2-328.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-32682N.

IntAct

P68400. 25 interactions.

MINT

MINT-142347.

STRING

P68400.

PTM databases

PhosphoSite

P68400.

Polymorphism databases

DMDM

55977123.

Proteomic databases

PRIDE

P68400.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000217244; ENSP00000217244; ENSG00000101266.
ENST00000349736; ENSP00000339247; ENSG00000101266.

GeneID

1457.

KEGG

hsa:1457.

UCSC

uc002wdw.1. human.

Organism-specific databases

CTD

1457.

GeneCards

GC20M000414.

H-InvDB

HIX0015555.

HGNC

HGNC:2457. CSNK2A1.

HPA

CAB020680.

MIM

115440. gene.

neXtProt

NX_P68400.

PharmGKB

PA26957.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG12460.

HOVERGEN

HBG107282.

OrthoDB

EOG4J118H.

PhylomeDB

P68400.

Enzyme and pathway databases

Pathway_Interaction_DB

alphasynuclein_pathway. Alpha-synuclein signaling.
nfkappabatypicalpathway. Atypical NF-kappaB pathway.
bcr_5pathway. BCR signaling pathway.
wnt_canonical_pathway. Canonical Wnt signaling pathway.
lis1pathway. Lissencephaly gene (LIS1) in neuronal migration and development.
pdgfrapathway. PDGFR-alpha signaling pathway.
ps1pathway. Presenilin action in Notch and Wnt signaling.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.
p38alphabetadownstreampathway. Signaling mediated by p38-alpha and p38-beta.

Reactome

REACT_111045. Developmental Biology.

Gene expression databases

ArrayExpress

P68400.

Bgee

P68400.

CleanEx

HS_CSNK2A1.

Genevestigator

P68400.

GermOnline

ENSG00000101266. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_kinase-like_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR002290. Ser/Thr_kinase_dom.
[Graphical view]

KO

K03097.

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

5989.

SOURCE

Search...

Entry information

Entry name

CSK21_HUMAN

Accession

Primary (citable) accession number: P68400
Secondary accession number(s): B4DYS6 , D3DVV8, P19138, P20426, Q14013, Q5U065

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 23, 2004
Last sequence update:	November 23, 2004
Last modified:	January 25, 2012
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.