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P68400

- CSK21_HUMAN

UniProt

P68400 - CSK21_HUMAN

Protein

Casein kinase II subunit alpha

Gene

CSNK2A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (23 Nov 2004)
      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. 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.6 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.1 Publication

    Enzyme regulationi

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

    Sites

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

    Regions

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

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. Hsp90 protein binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein N-terminus binding Source: UniProtKB
    5. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. chaperone-mediated protein folding Source: UniProtKB
    3. mitotic cell cycle Source: Reactome
    4. mitotic spindle checkpoint Source: UniProtKB
    5. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    6. positive regulation of cell growth Source: UniProtKB
    7. positive regulation of cell proliferation Source: UniProtKB
    8. positive regulation of protein catabolic process Source: UniProtKB
    9. positive regulation of Wnt signaling pathway Source: UniProtKB
    10. protein phosphorylation Source: UniProtKB
    11. regulation of transcription, DNA-templated Source: UniProtKB-KW
    12. rhythmic process Source: UniProtKB-KW
    13. signal transduction Source: ProtInc
    14. transcription, DNA-templated Source: UniProtKB-KW
    15. 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

    ReactomeiREACT_150260. Condensation of Prometaphase Chromosomes.
    REACT_200668. WNT mediated activation of DVL.
    REACT_22272. Signal transduction by L1.
    SignaLinkiP68400.

    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:CK2A1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:2457. CSNK2A1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleus Source: UniProtKB
    3. NuRD complex Source: BHF-UCL
    4. plasma membrane Source: ProtInc
    5. Sin3 complex Source: BHF-UCL

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26957.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 391391Casein kinase II subunit alphaPRO_0000085883Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei344 – 3441Phosphothreonine; by CDK11 Publication
    Modified residuei360 – 3601Phosphothreonine; by CDK11 Publication
    Modified residuei362 – 3621Phosphoserine; by CDK11 Publication
    Modified residuei370 – 3701Phosphoserine; by CDK11 Publication

    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.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP68400.
    PaxDbiP68400.
    PRIDEiP68400.

    PTM databases

    PhosphoSiteiP68400.

    Miscellaneous databases

    PMAP-CutDBB4DYS6.

    Expressioni

    Gene expression databases

    ArrayExpressiP68400.
    BgeeiP68400.
    CleanExiHS_CSNK2A1.
    GenevestigatoriP68400.

    Organism-specific databases

    HPAiCAB020680.

    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 (isoform PML-12).8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CBX4O00257-32EBI-347804,EBI-4392727
    CSNK2A2P197843EBI-347804,EBI-347451
    CSNK2BP6787013EBI-347804,EBI-348169
    HDAC1Q135472EBI-347804,EBI-301834
    KIF5CO602824EBI-347804,EBI-717170
    PMLP295902EBI-347804,EBI-295890
    SIRT1Q96EB64EBI-347804,EBI-1802965
    SLC39A7Q925044EBI-347804,EBI-1051105
    TP53P046372EBI-347804,EBI-366083

    Protein-protein interaction databases

    BioGridi107841. 348 interactions.
    DIPiDIP-32682N.
    IntActiP68400. 217 interactions.
    MINTiMINT-142347.
    STRINGi9606.ENSP00000217244.

    Structurei

    Secondary structure

    1
    391
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 123
    Turni13 – 186
    Helixi21 – 244
    Helixi26 – 283
    Helixi36 – 383
    Beta strandi39 – 479
    Beta strandi49 – 5810
    Turni59 – 613
    Beta strandi64 – 707
    Helixi75 – 8814
    Beta strandi97 – 1026
    Turni104 – 1063
    Beta strandi107 – 1148
    Helixi121 – 1244
    Helixi125 – 1273
    Helixi130 – 14920
    Helixi159 – 1613
    Beta strandi162 – 1654
    Helixi166 – 1683
    Beta strandi170 – 1734
    Helixi176 – 1783
    Helixi195 – 1973
    Helixi200 – 2034
    Helixi212 – 22716
    Beta strandi230 – 2334
    Helixi238 – 24912
    Helixi251 – 26111
    Helixi267 – 2693
    Turni270 – 2723
    Helixi281 – 2844
    Turni287 – 2893
    Helixi290 – 2923
    Helixi295 – 30410
    Helixi309 – 3113
    Helixi315 – 3184
    Helixi322 – 3243
    Helixi325 – 3317
    Beta strandi333 – 3353

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP68400.
    SMRiP68400. Positions 2-359.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP68400.

    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.
    HOGENOMiHOG000233021.
    HOVERGENiHBG107282.
    KOiK03097.
    OMAiNNTDFRS.
    OrthoDBiEOG7QG446.
    PhylomeDBiP68400.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P68400-1) [UniParc]FASTAAdd to Basket

    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.

    « 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 QARMGSSSMP GGSTPVSSAN 350
    MMSGISSVPT PSPLGPLAGS PVIAAANPLG MPVPAAAGAQ Q 391
    Length:391
    Mass (Da):45,144
    Last modified:November 23, 2004 - v1
    Checksum:iD3B6F5D13FF7422D
    GO
    Isoform 2 (identifier: P68400-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:255
    Mass (Da):29,181
    Checksum:iABCEE52F34E7431B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti128 – 1281L → F in CAA49758. (PubMed:8420794)Curated
    Sequence conflicti256 – 2561D → G in CAA49758. (PubMed:8420794)Curated
    Sequence conflicti287 – 2871S → R in CAA49758. (PubMed:8420794)Curated
    Sequence conflicti351 – 3511M → V in CAA49758. (PubMed:8420794)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 136136Missing in isoform 2. 1 PublicationVSP_041925Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS13003.1. [P68400-1]
    CCDS13004.1. [P68400-2]
    PIRiA30319.
    RefSeqiNP_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]
    UniGeneiHs.644056.
    Hs.654675.
    Hs.741126.

    Genome annotation databases

    EnsembliENST00000217244; ENSP00000217244; ENSG00000101266. [P68400-1]
    ENST00000349736; ENSP00000339247; ENSG00000101266. [P68400-1]
    ENST00000400217; ENSP00000383076; ENSG00000101266. [P68400-2]
    GeneIDi1457.
    KEGGihsa:1457.
    UCSCiuc002wdw.1. human. [P68400-1]

    Polymorphism databases

    DMDMi55977123.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS13003.1. [P68400-1 ]
    CCDS13004.1. [P68400-2 ]
    PIRi A30319.
    RefSeqi NP_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 ]
    UniGenei Hs.644056.
    Hs.654675.
    Hs.741126.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    3AXW X-ray 2.50 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 [» ]
    3Q04 X-ray 1.80 A 3-330 [» ]
    3Q9W X-ray 1.70 A 1-336 [» ]
    3Q9X X-ray 2.20 A/B 1-336 [» ]
    3Q9Y X-ray 1.80 A 1-336 [» ]
    3Q9Z X-ray 2.20 A/B 1-336 [» ]
    3QA0 X-ray 2.50 A/B 1-336 [» ]
    3R0T X-ray 1.75 A 1-337 [» ]
    3RPS X-ray 2.30 A/B 1-335 [» ]
    3TAX X-ray 1.88 B/D 340-352 [» ]
    3U4U X-ray 2.20 A 1-333 [» ]
    3U87 X-ray 2.90 A/B 1-325 [» ]
    3U9C X-ray 3.20 A/B 1-335 [» ]
    3W8L X-ray 2.40 A/B 1-335 [» ]
    3WAR X-ray 1.04 A 1-335 [» ]
    4DGL X-ray 3.00 C/D 1-335 [» ]
    4FBX X-ray 2.33 A 1-335 [» ]
    4GRB X-ray 2.15 A 1-333 [» ]
    4GUB X-ray 2.20 A 1-333 [» ]
    4GYW X-ray 1.70 B/D 340-352 [» ]
    4GYY X-ray 1.85 B/D 340-352 [» ]
    4GZ3 X-ray 1.90 B/D 340-352 [» ]
    4IB5 X-ray 2.20 A/B/C 1-335 [» ]
    4KWP X-ray 1.25 A 1-336 [» ]
    4MD7 X-ray 3.10 E/F/G/H 1-391 [» ]
    4MD8 X-ray 3.30 E/F/G/H 1-391 [» ]
    4MD9 X-ray 3.50 E/F/G/H/K/L/M/P 1-336 [» ]
    4NH1 X-ray 3.30 A/B 1-335 [» ]
    ProteinModelPortali P68400.
    SMRi P68400. Positions 2-359.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107841. 348 interactions.
    DIPi DIP-32682N.
    IntActi P68400. 217 interactions.
    MINTi MINT-142347.
    STRINGi 9606.ENSP00000217244.

    Chemistry

    BindingDBi P68400.
    ChEMBLi CHEMBL3629.
    GuidetoPHARMACOLOGYi 1549.

    PTM databases

    PhosphoSitei P68400.

    Polymorphism databases

    DMDMi 55977123.

    Proteomic databases

    MaxQBi P68400.
    PaxDbi P68400.
    PRIDEi P68400.

    Protocols and materials databases

    DNASUi 1457.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000217244 ; ENSP00000217244 ; ENSG00000101266 . [P68400-1 ]
    ENST00000349736 ; ENSP00000339247 ; ENSG00000101266 . [P68400-1 ]
    ENST00000400217 ; ENSP00000383076 ; ENSG00000101266 . [P68400-2 ]
    GeneIDi 1457.
    KEGGi hsa:1457.
    UCSCi uc002wdw.1. human. [P68400-1 ]

    Organism-specific databases

    CTDi 1457.
    GeneCardsi GC20M000459.
    HGNCi HGNC:2457. CSNK2A1.
    HPAi CAB020680.
    MIMi 115440. gene.
    neXtProti NX_P68400.
    PharmGKBi PA26957.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233021.
    HOVERGENi HBG107282.
    KOi K03097.
    OMAi NNTDFRS.
    OrthoDBi EOG7QG446.
    PhylomeDBi P68400.
    TreeFami TF300483.

    Enzyme and pathway databases

    Reactomei REACT_150260. Condensation of Prometaphase Chromosomes.
    REACT_200668. WNT mediated activation of DVL.
    REACT_22272. Signal transduction by L1.
    SignaLinki P68400.

    Miscellaneous databases

    ChiTaRSi CSNK2A1. human.
    EvolutionaryTracei P68400.
    GeneWikii Casein_kinase_2,_alpha_1.
    GenomeRNAii 1457.
    NextBioi 5989.
    PMAP-CutDB B4DYS6.
    PROi P68400.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P68400.
    Bgeei P68400.
    CleanExi HS_CSNK2A1.
    Genevestigatori P68400.

    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. "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.
      , 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.
      , 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.
      , 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. 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. 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.

    Entry informationi

    Entry nameiCSK21_HUMAN
    AccessioniPrimary (citable) accession number: P68400
    Secondary accession number(s): B4DYS6
    , D3DVV8, P19138, P20426, Q14013, Q5U065
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 23, 2004
    Last sequence update: November 23, 2004
    Last modified: October 1, 2014
    This is version 123 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    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. 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.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3