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P19139

- CSK21_RAT

UniProt

P19139 - CSK21_RAT

Protein

Casein kinase II subunit alpha

Gene

Csnk2a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (01 Feb 1995)
      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 By similarity. 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 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

    1. ATP binding Source: UniProtKB-KW
    2. protein phosphatase regulator activity Source: Ensembl
    3. 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: Ensembl
    8. protein phosphorylation Source: UniProtKB
    9. regulation of cell growth Source: RGD
    10. regulation of cell proliferation Source: RGD
    11. regulation of transcription, DNA-templated Source: UniProtKB-KW
    12. rhythmic process Source: UniProtKB-KW
    13. transcription, DNA-templated Source: UniProtKB-KW
    14. 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. 5301.
    ReactomeiREACT_198291. Condensation of Prometaphase Chromosomes.
    REACT_205007. 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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 3

    Organism-specific databases

    RGDi621663. Csnk2a1.

    Subcellular locationi

    GO - Cellular componenti

    1. protein kinase CK2 complex Source: RGD

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 391391Casein kinase II subunit alphaPRO_0000085886Add
    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

    PaxDbiP19139.
    PRIDEiP19139.

    PTM databases

    PhosphoSiteiP19139.

    Expressioni

    Gene expression databases

    GenevestigatoriP19139.

    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 By similarity. Interacts with PML By similarity.By similarity

    Protein-protein interaction databases

    BioGridi250484. 4 interactions.
    IntActiP19139. 4 interactions.
    MINTiMINT-3372564.
    STRINGi10116.ENSRNOP00000007558.

    Structurei

    Secondary structure

    1
    391
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 123
    Turni15 – 184
    Helixi21 – 244
    Helixi26 – 283
    Helixi36 – 383
    Beta strandi39 – 435
    Beta strandi52 – 587
    Turni59 – 613
    Beta strandi64 – 696
    Helixi75 – 8814
    Beta strandi97 – 1026
    Beta strandi109 – 1146
    Helixi122 – 1254
    Helixi130 – 14920
    Helixi159 – 1613
    Beta strandi162 – 1654
    Turni166 – 1694
    Beta strandi170 – 1734
    Helixi195 – 1973
    Helixi200 – 2034
    Helixi212 – 22615
    Beta strandi230 – 2334
    Helixi240 – 24910
    Helixi251 – 26010
    Helixi267 – 2715
    Helixi281 – 2844
    Turni287 – 2926
    Helixi295 – 30410
    Helixi309 – 3113
    Helixi315 – 3195
    Helixi322 – 3243
    Helixi325 – 3284

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2R7IX-ray3.00A/B/C/D1-335[»]
    ProteinModelPortaliP19139.
    SMRiP19139. Positions 2-334.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19139.

    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 subunit

    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.
    InParanoidiP19139.
    KOiK03097.
    OMAiNNTDFRS.
    OrthoDBiEOG7QG446.
    PhylomeDBiP19139.
    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.

    P19139-1 [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 QARMSSAGMA GGSTPVSSAN 350
    MMSGISSVPT PSPLGPLAGS PVIAAANSLG IPVPAAAGAQ Q 391
    Length:391
    Mass (Da):45,073
    Last modified:February 1, 1995 - v2
    Checksum:i83A4E2CC80824F66
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L15618 mRNA. Translation: AAA74462.1.
    BC091130 mRNA. Translation: AAH91130.1.
    J02853 mRNA. No translation available.
    PIRiB30319.
    RefSeqiNP_446276.1. NM_053824.2.
    XP_006235282.1. XM_006235220.1.
    XP_006235283.1. XM_006235221.1.
    XP_006235284.1. XM_006235222.1.
    UniGeneiRn.203090.
    Rn.4231.

    Genome annotation databases

    EnsembliENSRNOT00000007558; ENSRNOP00000007558; ENSRNOG00000005276.
    GeneIDi116549.
    KEGGirno:116549.
    UCSCiRGD:621663. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L15618 mRNA. Translation: AAA74462.1 .
    BC091130 mRNA. Translation: AAH91130.1 .
    J02853 mRNA. No translation available.
    PIRi B30319.
    RefSeqi NP_446276.1. NM_053824.2.
    XP_006235282.1. XM_006235220.1.
    XP_006235283.1. XM_006235221.1.
    XP_006235284.1. XM_006235222.1.
    UniGenei Rn.203090.
    Rn.4231.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2R7I X-ray 3.00 A/B/C/D 1-335 [» ]
    ProteinModelPortali P19139.
    SMRi P19139. Positions 2-334.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 250484. 4 interactions.
    IntActi P19139. 4 interactions.
    MINTi MINT-3372564.
    STRINGi 10116.ENSRNOP00000007558.

    Chemistry

    BindingDBi P19139.

    PTM databases

    PhosphoSitei P19139.

    Proteomic databases

    PaxDbi P19139.
    PRIDEi P19139.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000007558 ; ENSRNOP00000007558 ; ENSRNOG00000005276 .
    GeneIDi 116549.
    KEGGi rno:116549.
    UCSCi RGD:621663. rat.

    Organism-specific databases

    CTDi 1457.
    RGDi 621663. Csnk2a1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00390000004215.
    HOGENOMi HOG000233021.
    HOVERGENi HBG107282.
    InParanoidi P19139.
    KOi K03097.
    OMAi NNTDFRS.
    OrthoDBi EOG7QG446.
    PhylomeDBi P19139.
    TreeFami TF300483.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 5301.
    Reactomei REACT_198291. Condensation of Prometaphase Chromosomes.
    REACT_205007. WNT mediated activation of DVL.

    Miscellaneous databases

    EvolutionaryTracei P19139.
    NextBioi 619175.
    PROi P19139.

    Gene expression databases

    Genevestigatori P19139.

    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. "Cloning of cDNAs encoding the alpha and beta subunits of rat casein kinase 2 (CK-2): investigation of molecular regulation of CK-2 by androgens in rat ventral prostate."
      Ahmed K., Davis A., Hanten J., Lambert D., McIvor R.S., Goueli S.A.
      Cell. Mol. Biol. Res. 39:451-462(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "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].
      Tissue: Spleen.
    3. "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] OF 8-391.
    4. Cited for: PROTEIN SEQUENCE OF 22-68; 90-107; 173-191; 229-244; 248-268 AND 284-306, FUNCTION.
    5. "Phosphorylation by protein kinase CK2: a signaling switch for the caspase-inhibiting protein ARC."
      Li P.F., Li J., Mueller E.C., Otto A., Dietz R., von Harsdorf R.
      Mol. Cell 10:247-258(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN APOPTOSIS.
    6. "Crystal structures of catalytic and regulatory subunits of rat protein kinase CK2."
      Zhou W., Qin X., Yan X., Xie X., Li L., Fang S., Long J., Adelman J., Tang W.-J., Shen Y.
      Chin. Sci. Bull. 54:220-226(2009)
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-335.

    Entry informationi

    Entry nameiCSK21_RAT
    AccessioniPrimary (citable) accession number: P19139
    Secondary accession number(s): Q5BKC1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 130 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3