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P68400 (CSK21_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Casein kinase II subunit alpha

Short name=CK II alpha
EC=2.7.11.1
Gene names
Name:CSNK2A1
Synonyms:CK2A1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length391 AA.
Sequence statusComplete.
Protein existenceEvidence 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 apoptosis. 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. Phosphorylates PML at 'Ser-565' and primes it for ubiquitin-mediated degradation. Plays an important role in the circadian clock function by phosphorylating ARNTL/BMAL1 at 'Ser-90' which is pivotal for its interaction with CLOCK and which controls CLOCK nuclear entry. Ref.11 Ref.12 Ref.14 Ref.16 Ref.24 Ref.26

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.24

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. Interacts with SNAI1. Interacts with PML (isoform PML-12) Ref.11 Ref.13 Ref.15 Ref.23 Ref.24 Ref.26 Ref.27 Ref.28

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

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 increased 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 processApoptosis
Biological rhythms
Cell cycle
Transcription
Transcription regulation
Wnt signaling pathway
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

axon guidance

Traceable author statement. Source: Reactome

chaperone-mediated protein folding

Traceable author statement Ref.21. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic spindle checkpoint

Inferred from mutant phenotype Ref.12. Source: UniProtKB

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from mutant phenotype Ref.14. Source: UniProtKB

positive regulation of Wnt signaling pathway

Inferred from mutant phenotype PubMed 12700239. Source: UniProtKB

positive regulation of cell growth

Inferred from direct assay Ref.24. Source: UniProtKB

positive regulation of cell proliferation

Inferred from direct assay Ref.24. Source: UniProtKB

positive regulation of protein catabolic process

Inferred from direct assay Ref.24. Source: UniProtKB

protein phosphorylation

Inferred from direct assay Ref.24Ref.26. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

rhythmic process

Inferred from electronic annotation. Source: UniProtKB-KW

signal transduction

Traceable author statement Ref.2. Source: ProtInc

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentNuRD complex

Inferred from direct assay PubMed 17827154. Source: BHF-UCL

Sin3 complex

Inferred from direct assay PubMed 17827154. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 21282530. Source: UniProtKB

plasma membrane

Traceable author statement PubMed 10799509. Source: ProtInc

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Hsp90 protein binding

Traceable author statement Ref.21. Source: UniProtKB

protein N-terminus binding

Inferred from physical interaction PubMed 11972058. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.24Ref.26. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay PubMed 12700239Ref.14Ref.24. Source: UniProtKB

Complete GO annotation...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 391391Casein kinase II subunit alpha
PRO_0000085883

Regions

Domain39 – 324286Protein kinase
Nucleotide binding45 – 539ATP By similarity
Region36 – 416Interaction with beta subunit By similarity

Sites

Active site1561Proton acceptor
Binding site681ATP By similarity

Amino acid modifications

Modified residue3441Phosphothreonine; by CDK1 Ref.10
Modified residue3601Phosphothreonine; by CDK1 Ref.10
Modified residue3621Phosphoserine; by CDK1 Ref.10
Modified residue3701Phosphoserine; by CDK1 Ref.10

Natural variations

Alternative sequence1 – 136136Missing in isoform 2.
VSP_041925

Experimental info

Sequence conflict1281L → F in CAA49758. Ref.3
Sequence conflict2561D → G in CAA49758. Ref.3
Sequence conflict2871S → R in CAA49758. Ref.3
Sequence conflict3511M → V in CAA49758. Ref.3

Secondary structure

................................................................... 391
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: D3B6F5D13FF7422D

FASTA39145,144
        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 

« Hide

Isoform 2 [UniParc].

Checksum: ABCEE52F34E7431B
Show »

FASTA25529,181

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNPS1.
[16]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL CYCLE.
[17]"One-thousand-and-one substrates of protein kinase CK2?"
Meggio F., Pinna L.A.
FASEB J. 17:349-368(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[18]"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] [Europe PMC] [Abstract]
Cited for: REVIEW ON STRUCTURE.
[19]"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] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[20]"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] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[21]"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] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION IN REGULATION OF HSP90.
[22]"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] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION IN WNT SIGNALING.
[23]"Phosphorylation of serine 11 and serine 92 as new positive regulators of human Snail1 function: potential involvement of casein kinase-2 and the cAMP-activated kinase protein kinase A."
MacPherson M.R., Molina P., Souchelnytskyi S., Wernstedt C., Martin-Perez J., Portillo F., Cano A.
Mol. Biol. Cell 21:244-253(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNAI1.
[24]"Functional polymorphism of the CK2alpha intronless gene plays oncogenic roles in lung cancer."
Hung M.S., Lin Y.C., Mao J.H., Kim I.J., Xu Z., Yang C.T., Jablons D.M., You L.
PLoS ONE 5:E11418-E11418(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH PML.
[25]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its oncogenic counterpart PML-RARA."
Rabellino A., Carter B., Konstantinidou G., Wu S.Y., Rimessi A., Byers L.A., Heymach J.V., Girard L., Chiang C.M., Teruya-Feldstein J., Scaglioni P.P.
Cancer Res. 72:2275-2284(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PML.
[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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-337, SUBUNIT.
[28]"Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme."
Niefind K., Guerra B., Ermakowa I., Issinger O.G.
EMBO J. 20:5320-5331(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-337 IN COMPLEX WITH CSNK2B, SUBUNIT.
[29]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-329.
[30]"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] [Europe PMC] [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.
CCDSCCDS13003.1. [P68400-1]
CCDS13004.1. [P68400-2]
PIRA30319.
RefSeqNP_001886.1. NM_001895.3. [P68400-1]
NP_808227.1. NM_177559.2. [P68400-1]
NP_808228.1. NM_177560.2. [P68400-2]
XP_006723611.1. XM_006723548.1. [P68400-1]
UniGeneHs.644056.
Hs.654675.
Hs.741126.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JWHX-ray3.10A/B1-337[»]
1NA7X-ray2.40A1-329[»]
1PJKX-ray2.50A2-335[»]
2PVRX-ray1.60A2-335[»]
2ZJWX-ray2.40A1-335[»]
3AMYX-ray2.30A1-335[»]
3AT2X-ray1.60A1-335[»]
3AT3X-ray2.60A1-335[»]
3AT4X-ray2.20A1-335[»]
3AXWX-ray2.50A1-335[»]
3BQCX-ray1.50A1-335[»]
3C13X-ray1.95A1-335[»]
3FWQX-ray2.30A/B1-335[»]
3H30X-ray1.56A/B1-334[»]
3JUHX-ray1.66A/B1-335[»]
3MB6X-ray1.75A1-331[»]
3MB7X-ray1.65A1-331[»]
3NGAX-ray2.71A/B1-333[»]
3NSZX-ray1.30A2-331[»]
3OWJX-ray1.85A1-331[»]
3OWKX-ray1.80A1-331[»]
3OWLX-ray2.10A1-331[»]
3PE1X-ray1.60A1-337[»]
3PE2X-ray1.90A1-337[»]
3PE4X-ray1.95B/D340-352[»]
3Q04X-ray1.80A3-330[»]
3Q9WX-ray1.70A1-336[»]
3Q9XX-ray2.20A/B1-336[»]
3Q9YX-ray1.80A1-336[»]
3Q9ZX-ray2.20A/B1-336[»]
3QA0X-ray2.50A/B1-336[»]
3R0TX-ray1.75A1-337[»]
3RPSX-ray2.30A/B1-335[»]
3TAXX-ray1.88B/D340-352[»]
3U4UX-ray2.20A1-333[»]
3U87X-ray2.90A/B1-325[»]
3U9CX-ray3.20A/B1-335[»]
3W8LX-ray2.40A/B1-335[»]
3WARX-ray1.04A1-335[»]
4DGLX-ray3.00C/D1-335[»]
4FBXX-ray2.33A1-335[»]
4GRBX-ray2.15A1-333[»]
4GUBX-ray2.20A1-333[»]
4GYWX-ray1.70B/D340-352[»]
4GYYX-ray1.85B/D340-352[»]
4GZ3X-ray1.90B/D340-352[»]
4IB5X-ray2.20A/B/C1-335[»]
4KWPX-ray1.25A1-336[»]
4MD7X-ray3.10E/F/G/H1-391[»]
4MD8X-ray3.30E/F/G/H1-391[»]
4MD9X-ray3.50E/F/G/H/K/L/M/P1-336[»]
4NH1X-ray3.30A/B1-335[»]
ProteinModelPortalP68400.
SMRP68400. Positions 2-359.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107841. 350 interactions.
DIPDIP-32682N.
IntActP68400. 215 interactions.
MINTMINT-142347.
STRING9606.ENSP00000217244.

Chemistry

BindingDBP68400.
ChEMBLCHEMBL3629.
GuidetoPHARMACOLOGY1549.

PTM databases

PhosphoSiteP68400.

Polymorphism databases

DMDM55977123.

Proteomic databases

MaxQBP68400.
PaxDbP68400.
PRIDEP68400.

Protocols and materials databases

DNASU1457.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000217244; ENSP00000217244; ENSG00000101266. [P68400-1]
ENST00000349736; ENSP00000339247; ENSG00000101266. [P68400-1]
ENST00000400217; ENSP00000383076; ENSG00000101266. [P68400-2]
GeneID1457.
KEGGhsa:1457.
UCSCuc002wdw.1. human. [P68400-1]

Organism-specific databases

CTD1457.
GeneCardsGC20M000459.
HGNCHGNC:2457. CSNK2A1.
HPACAB020680.
MIM115440. gene.
neXtProtNX_P68400.
PharmGKBPA26957.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233021.
HOVERGENHBG107282.
KOK03097.
OMANNTDFRS.
OrthoDBEOG7QG446.
PhylomeDBP68400.
TreeFamTF300483.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
SignaLinkP68400.

Gene expression databases

ArrayExpressP68400.
BgeeP68400.
CleanExHS_CSNK2A1.
GenevestigatorP68400.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCSNK2A1. human.
EvolutionaryTraceP68400.
GeneWikiCasein_kinase_2,_alpha_1.
GenomeRNAi1457.
NextBio5989.
PMAP-CutDBB4DYS6.
PROP68400.
SOURCESearch...

Entry information

Entry nameCSK21_HUMAN
AccessionPrimary (citable) accession number: P68400
Secondary accession number(s): B4DYS6 expand/collapse secondary AC list , D3DVV8, P19138, P20426, Q14013, Q5U065
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: November 23, 2004
Last modified: July 9, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM