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Protein

Casein kinase II subunit alpha

Gene

Csnk2a1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Phosphorylates CCAR2 at 'Thr-454' (By similarity).By similarity2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Constitutively active protein kinase whose activity is not directly affected by phosphorylation. Seems to be regulated by level of expression and localization (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei68 – 681ATPPROSITE-ProRule annotation
Active sitei156 – 1561Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi45 – 539ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Biological rhythms, Cell cycle, Transcription, Transcription regulation, Wnt signaling pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 3474.
ReactomeiREACT_283383. Condensation of Prometaphase Chromosomes.
REACT_337993. WNT mediated activation of DVL.
REACT_353319. Signal transduction by L1.

Names & Taxonomyi

Protein namesi
Recommended name:
Casein kinase II subunit alpha (EC:2.7.11.1)
Short name:
CK II alpha
Gene namesi
Name:Csnk2a1
Synonyms:Ckiia
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componentsi: Chromosome 1, Chromosome 2

Organism-specific databases

MGIiMGI:88543. Csnk2a1.

Subcellular locationi

  • Nucleus By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Embryonic lethality at 10.5 dpc.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 391391Casein kinase II subunit alphaPRO_0000085884Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei344 – 3441Phosphothreonine; by CDK1By similarity
Modified residuei360 – 3601Phosphothreonine; by CDK1By similarity
Modified residuei362 – 3621Phosphoserine; by CDK1By similarity
Modified residuei370 – 3701Phosphoserine; by CDK1By similarity

Post-translational modificationi

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).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ60737.
PaxDbiQ60737.
PRIDEiQ60737.

PTM databases

PhosphoSiteiQ60737.

Expressioni

Gene expression databases

BgeeiQ60737.
CleanExiMM_CSNK2A1.
ExpressionAtlasiQ60737. baseline and differential.
GenevisibleiQ60737. MM.

Interactioni

Subunit structurei

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 (By similarity). Interacts with RNPS1 (By similarity). Interacts with SNAI1 (PubMed:19923321). Interacts with PML and CCAR2 (By similarity).By similarity1 Publication

Protein-protein interaction databases

BioGridi198942. 6 interactions.
DIPiDIP-32409N.
IntActiQ60737. 11 interactions.
MINTiMINT-121842.
STRINGi10090.ENSMUSP00000096829.

Structurei

3D structure databases

ProteinModelPortaliQ60737.
SMRiQ60737. Positions 2-359.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 324286Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni36 – 416Interaction with beta subunitBy similarity

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CK2 subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00390000004215.
HOGENOMiHOG000233021.
HOVERGENiHBG107282.
InParanoidiQ60737.
KOiK03097.
OMAiNMPRSYW.
OrthoDBiEOG7QG446.
TreeFamiTF300483.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q60737-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGPVPSRAR VYTDVNTHRP REYWDYESHV VEWGNQDDYQ LVRKLGRGKY
60 70 80 90 100
SEVFEAINIT NNEKVVVKIL KPVKKKKIKR EIKILENLRG GPNIITLADI
110 120 130 140 150
VKDPVSRTPA LVFEHVNNTD FKQLYQTLTD YDIRFYMYEI LKALDYCHSM
160 170 180 190 200
GIMHRDVKPH NVMIDHEHRK LRLIDWGLAE FYHPGQEYNV RVASRYFKGP
210 220 230 240 250
ELLVDYQMYD YSLDMWSLGC MLASMIFRKE PFFHGHDNYD QLVRIAKVLG
260 270 280 290 300
TEDLYDYIDK YNIELDPRFN DILGRHSRKR WERFVHSENQ HLVSPEALDF
310 320 330 340 350
LDKLLRYDHQ SRLTAREAME HPYFYTVVKD QARMSSTSMA GGSTPVSSAN
360 370 380 390
MMSGISSVPT PSPLGPLAGS PVIAAANSLG IPVPAAAGAQ Q
Length:391
Mass (Da):45,134
Last modified:July 27, 2011 - v2
Checksum:iC7A5F7CC8099230D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti315 – 3151A → V in AAA64563 (PubMed:7846532).Curated
Sequence conflicti323 – 3231Y → F in AAA64563 (PubMed:7846532).Curated
Sequence conflicti330 – 3301D → N in AAA64563 (PubMed:7846532).Curated
Sequence conflicti360 – 3601T → S in AAA64563 (PubMed:7846532).Curated
Sequence conflicti384 – 3841P → Q in AAA64563 (PubMed:7846532).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS16879.1.
PIRiI49141.
RefSeqiNP_031814.2. NM_007788.3.
XP_006498720.1. XM_006498657.2.
XP_011237574.1. XM_011239272.1.
UniGeneiMm.23692.

Genome annotation databases

EnsembliENSMUST00000099224; ENSMUSP00000096829; ENSMUSG00000074698.
ENSMUST00000190422; ENSMUSP00000140515; ENSMUSG00000101523.
GeneIDi12995.
KEGGimmu:12995.
UCSCiuc008nfa.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS16879.1.
PIRiI49141.
RefSeqiNP_031814.2. NM_007788.3.
XP_006498720.1. XM_006498657.2.
XP_011237574.1. XM_011239272.1.
UniGeneiMm.23692.

3D structure databases

ProteinModelPortaliQ60737.
SMRiQ60737. Positions 2-359.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198942. 6 interactions.
DIPiDIP-32409N.
IntActiQ60737. 11 interactions.
MINTiMINT-121842.
STRINGi10090.ENSMUSP00000096829.

Chemistry

ChEMBLiCHEMBL3537.

PTM databases

PhosphoSiteiQ60737.

Proteomic databases

MaxQBiQ60737.
PaxDbiQ60737.
PRIDEiQ60737.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000099224; ENSMUSP00000096829; ENSMUSG00000074698.
ENSMUST00000190422; ENSMUSP00000140515; ENSMUSG00000101523.
GeneIDi12995.
KEGGimmu:12995.
UCSCiuc008nfa.2. mouse.

Organism-specific databases

CTDi1457.
MGIiMGI:88543. Csnk2a1.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00390000004215.
HOGENOMiHOG000233021.
HOVERGENiHBG107282.
InParanoidiQ60737.
KOiK03097.
OMAiNMPRSYW.
OrthoDBiEOG7QG446.
TreeFamiTF300483.

Enzyme and pathway databases

BRENDAi2.7.11.1. 3474.
ReactomeiREACT_283383. Condensation of Prometaphase Chromosomes.
REACT_337993. WNT mediated activation of DVL.
REACT_353319. Signal transduction by L1.

Miscellaneous databases

ChiTaRSiCsnk2a1. mouse.
NextBioi282804.
PROiQ60737.
SOURCEiSearch...

Gene expression databases

BgeeiQ60737.
CleanExiMM_CSNK2A1.
ExpressionAtlasiQ60737. baseline and differential.
GenevisibleiQ60737. MM.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiCSK21_MOUSE
AccessioniPrimary (citable) accession number: Q60737
Secondary accession number(s): Q8R0X4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 27, 2011
Last modified: July 22, 2015
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.