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Q60737 (CSK21_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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:Ckiia
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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. 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 By similarity. Ref.6 Ref.7

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 By similarity.

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 By similarity. Ref.9

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 By similarity.

Disruption phenotype

Embryonic lethality at 10.5 dpc. Ref.8

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.

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
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic spindle checkpoint

Inferred from sequence or structural similarity. Source: UniProtKB

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

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of Wnt signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell growth

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay PubMed 18191828. Source: MGI

protein phosphorylation

Inferred from direct assay PubMed 12432063PubMed 15284227PubMed 18191828. Source: MGI

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

rhythmic process

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentprotein kinase CK2 complex

Traceable author statement PubMed 12432063. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

beta-catenin binding

Inferred from direct assay PubMed 12432063. Source: MGI

kinase activity

Inferred from direct assay PubMed 15284227. Source: MGI

protein binding

Inferred from physical interaction PubMed 12432063PubMed 15284227. Source: MGI

protein phosphatase regulator activity

Inferred from direct assay PubMed 15284227. Source: MGI

protein serine/threonine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 391391Casein kinase II subunit alpha
PRO_0000085884

Regions

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

Sites

Active site1561Proton acceptor By similarity
Binding site681ATP By similarity

Amino acid modifications

Modified residue3441Phosphothreonine; by CDK1 By similarity
Modified residue3601Phosphothreonine; by CDK1 By similarity
Modified residue3621Phosphoserine; by CDK1 By similarity
Modified residue3701Phosphoserine; by CDK1 By similarity

Experimental info

Sequence conflict3151A → V in AAA64563. Ref.1
Sequence conflict3231Y → F in AAA64563. Ref.1
Sequence conflict3301D → N in AAA64563. Ref.1
Sequence conflict3601T → S in AAA64563. Ref.1
Sequence conflict3841P → Q in AAA64563. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q60737 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: C7A5F7CC8099230D

FASTA39145,134
        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 QARMSSTSMA GGSTPVSSAN MMSGISSVPT 

       370        380        390 
PSPLGPLAGS PVIAAANSLG IPVPAAAGAQ Q 

« Hide

References

« Hide 'large scale' references
[1]"Casein kinase II alpha transgene-induced murine lymphoma: relation to theileriosis in cattle."
Seldin D.C., Leder P.
Science 267:894-897(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: FVB/N.
Tissue: Spleen.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Inner ear and Liver.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6 and FVB/N.
Tissue: Mammary tumor.
[6]"Endogenous protein kinase CK2 participates in Wnt signaling in mammary epithelial cells."
Song D.H., Sussman D.J., Seldin D.C.
J. Biol. Chem. 275:23790-23797(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Phosphorylation of murine caspase-9 by the protein kinase casein kinase 2 regulates its cleavage by caspase-8."
McDonnell M.A., Abedin M.J., Melendez M., Platikanova T.N., Ecklund J.R., Ahmed K., Kelekar A.
J. Biol. Chem. 283:20149-20158(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN APOPTOSIS.
[8]"The alpha catalytic subunit of protein kinase CK2 is required for mouse embryonic development."
Lou D.Y., Dominguez I., Toselli P., Landesman-Bollag E., O'Brien C., Seldin D.C.
Mol. Cell. Biol. 28:131-139(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[9]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U17112 mRNA. Translation: AAA64563.1.
AK146032 mRNA. Translation: BAE26845.1.
AK158077 mRNA. Translation: BAE34350.1.
AL831735 Genomic DNA. Translation: CAM24731.1.
CH466551 Genomic DNA. Translation: EDL05953.1.
BC026149 mRNA. Translation: AAH26149.1.
BC060742 mRNA. Translation: AAH60742.1.
BC089343 mRNA. Translation: AAH89343.1.
CCDSCCDS16879.1.
PIRI49141.
RefSeqNP_031814.2. NM_007788.3.
XP_006498720.1. XM_006498657.1.
UniGeneMm.23692.

3D structure databases

ProteinModelPortalQ60737.
SMRQ60737. Positions 2-359.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198942. 6 interactions.
DIPDIP-32409N.
IntActQ60737. 11 interactions.
MINTMINT-121842.

Chemistry

BindingDBQ60737.
ChEMBLCHEMBL3537.

PTM databases

PhosphoSiteQ60737.

Proteomic databases

MaxQBQ60737.
PaxDbQ60737.
PRIDEQ60737.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000099224; ENSMUSP00000096829; ENSMUSG00000074698.
GeneID12995.
KEGGmmu:12995.
UCSCuc008nfa.2. mouse.

Organism-specific databases

CTD1457.
MGIMGI:88543. Csnk2a1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00390000004215.
HOGENOMHOG000233021.
HOVERGENHBG107282.
InParanoidQ8R0X4.
KOK03097.
OMANNTDFRS.
OrthoDBEOG7QG446.
TreeFamTF300483.

Enzyme and pathway databases

BRENDA2.7.11.1. 3474.

Gene expression databases

ArrayExpressQ60737.
BgeeQ60737.
CleanExMM_CSNK2A1.
GenevestigatorQ60737.

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. mouse.
NextBio282804.
PROQ60737.
SOURCESearch...

Entry information

Entry nameCSK21_MOUSE
AccessionPrimary (citable) accession number: Q60737
Secondary accession number(s): Q8R0X4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot