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Q60737

- CSK21_MOUSE

UniProt

Q60737 - CSK21_MOUSE

Protein

Casein kinase II subunit alpha

Gene

Csnk2a1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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 By similarity.By similarity

    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

    1. ATP binding Source: UniProtKB-KW
    2. beta-catenin binding Source: MGI
    3. kinase activity Source: MGI
    4. protein binding Source: MGI
    5. protein phosphatase regulator activity Source: MGI
    6. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. mitotic spindle checkpoint Source: UniProtKB
    2. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    3. positive regulation of cell growth Source: UniProtKB
    4. positive regulation of cell proliferation Source: UniProtKB
    5. positive regulation of protein catabolic process Source: UniProtKB
    6. positive regulation of Wnt signaling pathway Source: UniProtKB
    7. protein autophosphorylation Source: MGI
    8. protein phosphorylation Source: MGI
    9. regulation of transcription, DNA-templated Source: UniProtKB-KW
    10. rhythmic process Source: UniProtKB-KW
    11. transcription, DNA-templated Source: UniProtKB-KW
    12. Wnt signaling pathway Source: UniProtKB-KW

    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_196632. Condensation of Prometaphase Chromosomes.
    REACT_215461. Signal transduction by L1.
    REACT_225118. WNT mediated activation of DVL.

    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: Chromosome 2

    Organism-specific databases

    MGIiMGI:88543. Csnk2a1.

    Subcellular locationi

    GO - Cellular componenti

    1. protein kinase CK2 complex Source: MGI

    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

    ArrayExpressiQ60737.
    BgeeiQ60737.
    CleanExiMM_CSNK2A1.
    GenevestigatoriQ60737.

    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. Interacts with RNPS1. Interacts with SNAI1. Interacts with PML By similarity.By similarity

    Protein-protein interaction databases

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

    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.
    InParanoidiQ8R0X4.
    KOiK03097.
    OMAiNNTDFRS.
    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_dom.
    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

    MSGPVPSRAR VYTDVNTHRP REYWDYESHV VEWGNQDDYQ LVRKLGRGKY    50
    SEVFEAINIT NNEKVVVKIL KPVKKKKIKR EIKILENLRG GPNIITLADI 100
    VKDPVSRTPA LVFEHVNNTD FKQLYQTLTD YDIRFYMYEI LKALDYCHSM 150
    GIMHRDVKPH NVMIDHEHRK LRLIDWGLAE FYHPGQEYNV RVASRYFKGP 200
    ELLVDYQMYD YSLDMWSLGC MLASMIFRKE PFFHGHDNYD QLVRIAKVLG 250
    TEDLYDYIDK YNIELDPRFN DILGRHSRKR WERFVHSENQ HLVSPEALDF 300
    LDKLLRYDHQ SRLTAREAME HPYFYTVVKD QARMSSTSMA GGSTPVSSAN 350
    MMSGISSVPT PSPLGPLAGS PVIAAANSLG IPVPAAAGAQ Q 391
    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:
    EMBL
    GenBank
    DDBJ
    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_006498657.1.
    UniGeneiMm.23692.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS16879.1.
    PIRi I49141.
    RefSeqi NP_031814.2. NM_007788.3.
    XP_006498720.1. XM_006498657.1.
    UniGenei Mm.23692.

    3D structure databases

    ProteinModelPortali Q60737.
    SMRi Q60737. Positions 2-359.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198942. 6 interactions.
    DIPi DIP-32409N.
    IntActi Q60737. 11 interactions.
    MINTi MINT-121842.

    Chemistry

    BindingDBi Q60737.
    ChEMBLi CHEMBL3537.

    PTM databases

    PhosphoSitei Q60737.

    Proteomic databases

    MaxQBi Q60737.
    PaxDbi Q60737.
    PRIDEi Q60737.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000099224 ; ENSMUSP00000096829 ; ENSMUSG00000074698 .
    GeneIDi 12995.
    KEGGi mmu:12995.
    UCSCi uc008nfa.2. mouse.

    Organism-specific databases

    CTDi 1457.
    MGIi MGI:88543. Csnk2a1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00390000004215.
    HOGENOMi HOG000233021.
    HOVERGENi HBG107282.
    InParanoidi Q8R0X4.
    KOi K03097.
    OMAi NNTDFRS.
    OrthoDBi EOG7QG446.
    TreeFami TF300483.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 3474.
    Reactomei REACT_196632. Condensation of Prometaphase Chromosomes.
    REACT_215461. Signal transduction by L1.
    REACT_225118. WNT mediated activation of DVL.

    Miscellaneous databases

    ChiTaRSi CSNK2A1. mouse.
    NextBioi 282804.
    PROi Q60737.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q60737.
    Bgeei Q60737.
    CleanExi MM_CSNK2A1.
    Genevestigatori Q60737.

    Family and domain databases

    InterProi IPR011009. 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 ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 137 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