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P67870

- CSK2B_HUMAN

UniProt

P67870 - CSK2B_HUMAN

Protein

Casein kinase II subunit beta

Gene

CSNK2B

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 (11 Oct 2004)
      Previous versions | rss
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    Functioni

    Participates in Wnt signaling By similarity. Plays a complex role in regulating the basal catalytic activity of the alpha subunit.By similarity2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi109 – 1091Zinc
    Metal bindingi114 – 1141Zinc
    Metal bindingi137 – 1371Zinc
    Metal bindingi140 – 1401Zinc

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. protein domain specific binding Source: UniProtKB
    5. protein kinase regulator activity Source: UniProtKB
    6. receptor binding Source: BHF-UCL
    7. transcription factor binding Source: BHF-UCL

    GO - Biological processi

    1. adiponectin-activated signaling pathway Source: BHF-UCL
    2. axon guidance Source: Reactome
    3. cellular protein complex assembly Source: BHF-UCL
    4. endothelial tube morphogenesis Source: BHF-UCL
    5. mitotic cell cycle Source: Reactome
    6. negative regulation of blood vessel endothelial cell migration Source: BHF-UCL
    7. negative regulation of cell proliferation Source: BHF-UCL
    8. positive regulation of activin receptor signaling pathway Source: BHF-UCL
    9. positive regulation of pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
    10. protein phosphorylation Source: GOC
    11. regulation of DNA binding Source: BHF-UCL
    12. regulation of protein kinase activity Source: GOC
    13. signal transduction Source: UniProtKB
    14. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Biological processi

    Wnt signaling pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_150260. Condensation of Prometaphase Chromosomes.
    REACT_200668. WNT mediated activation of DVL.
    REACT_22272. Signal transduction by L1.
    SignaLinkiP67870.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Casein kinase II subunit beta
    Short name:
    CK II beta
    Alternative name(s):
    Phosvitin
    Protein G5a
    Gene namesi
    Name:CSNK2B
    Synonyms:CK2N, G5A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:2460. CSNK2B.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. nucleus Source: UniProtKB
    5. protein kinase CK2 complex Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26960.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 215214Casein kinase II subunit betaPRO_0000068236Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine
    Modified residuei2 – 21Phosphoserine; by autocatalysis2 Publications
    Modified residuei3 – 31Phosphoserine; by autocatalysis2 Publications
    Modified residuei209 – 2091Phosphoserine5 Publications
    Modified residuei212 – 2121N6-acetyllysine1 Publication

    Post-translational modificationi

    Phosphorylated by alpha subunit.6 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP67870.
    PaxDbiP67870.
    PRIDEiP67870.

    Expressioni

    Gene expression databases

    BgeeiP67870.
    CleanExiHS_CSNK2B.
    GenevestigatoriP67870.

    Organism-specific databases

    HPAiCAB004349.
    CAB013087.
    CAB016059.
    HPA005944.

    Interactioni

    Subunit structurei

    Tetramer composed of an alpha subunit, an alpha' subunit and two beta subunits. The beta subunit dimerization is mediated by zinc ions. Interacts with TCTEX1D3 By similarity. Interacts with CD163. Also component of a CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, the complex associating following UV irradiation. Interacts with MUSK; mediates phosphorylation of MUSK by CK2. Interacts with FGF1; this interaction is increased in the presence of FIBP, suggesting a possible cooperative interaction between CSNKB and FIBP in binding to FGF1.By similarity7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself7EBI-348169,EBI-348169
    CACNA1AO005552EBI-348169,EBI-766279
    CBX4O00257-32EBI-348169,EBI-4392727
    Clip1Q9JK252EBI-348169,EBI-908338From a different organism.
    ClockO087852EBI-348169,EBI-79859From a different organism.
    CSNK2A1P6840013EBI-348169,EBI-347804
    CSNK2A2P197846EBI-348169,EBI-347451
    PACS1Q6VY073EBI-348169,EBI-2555014
    SIRT1Q96EB65EBI-348169,EBI-1802965

    Protein-protein interaction databases

    BioGridi107843. 210 interactions.
    DIPiDIP-131N.
    IntActiP67870. 178 interactions.
    MINTiMINT-88683.
    STRINGi9606.ENSP00000415615.

    Structurei

    Secondary structure

    1
    215
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 157
    Turni17 – 204
    Helixi27 – 315
    Helixi33 – 364
    Helixi39 – 413
    Beta strandi43 – 453
    Helixi46 – 538
    Beta strandi59 – 613
    Helixi67 – 8721
    Helixi91 – 10212
    Turni103 – 1064
    Helixi112 – 1143
    Beta strandi120 – 1223
    Beta strandi134 – 1363
    Turni138 – 1403
    Beta strandi142 – 1443
    Helixi149 – 1513
    Beta strandi152 – 1554
    Helixi156 – 1583
    Turni159 – 1624
    Helixi163 – 1708
    Helixi172 – 1743
    Beta strandi187 – 1893
    Beta strandi190 – 1923
    Helixi195 – 1984
    Turni199 – 2013
    Helixi202 – 2054

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DS5X-ray3.16E/F/G/H181-203[»]
    1JWHX-ray3.10C/D1-215[»]
    1QF8X-ray1.74A/B1-182[»]
    3EEDX-ray2.80A/B1-193[»]
    4DGLX-ray3.00A/B1-215[»]
    4MD7X-ray3.10A/B/C/D1-215[»]
    4MD8X-ray3.30A/B/C/D1-215[»]
    4MD9X-ray3.50A/B/C/D/I/J/N/O1-215[»]
    4NH1X-ray3.30C/D1-215[»]
    ProteinModelPortaliP67870.
    SMRiP67870. Positions 7-207.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP67870.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni188 – 1936Interaction with alpha subunitBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi55 – 6410Asp/Glu-rich (acidic)

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG5041.
    HOGENOMiHOG000039270.
    HOVERGENiHBG051131.
    InParanoidiP67870.
    KOiK03115.
    PhylomeDBiP67870.
    TreeFamiTF314462.

    Family and domain databases

    Gene3Di1.10.1820.10. 1 hit.
    2.20.25.20. 1 hit.
    InterProiIPR016149. Casein_kin_II_reg-sub_a-hlx.
    IPR016150. Casein_kin_II_reg-sub_b-sht.
    IPR000704. Casein_kinase_II_reg-sub.
    [Graphical view]
    PANTHERiPTHR11740. PTHR11740. 1 hit.
    PfamiPF01214. CK_II_beta. 1 hit.
    [Graphical view]
    PRINTSiPR00472. CASNKINASEII.
    SMARTiSM01085. CK_II_beta. 1 hit.
    [Graphical view]
    SUPFAMiSSF57798. SSF57798. 1 hit.
    PROSITEiPS01101. CK2_BETA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P67870-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSSEEVSWI SWFCGLRGNE FFCEVDEDYI QDKFNLTGLN EQVPHYRQAL    50
    DMILDLEPDE ELEDNPNQSD LIEQAAEMLY GLIHARYILT NRGIAQMLEK 100
    YQQGDFGYCP RVYCENQPML PIGLSDIPGE AMVKLYCPKC MDVYTPKSSR 150
    HHHTDGAYFG TGFPHMLFMV HPEYRPKRPA NQFVPRLYGF KIHPMAYQLQ 200
    LQAASNFKSP VKTIR 215
    Length:215
    Mass (Da):24,942
    Last modified:October 11, 2004 - v1
    Checksum:iE465B1E699B0E0EC
    GO

    Sequence cautioni

    The sequence CAI18393.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti194 – 1941P → A in AAA52123. (PubMed:2513884)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16937 mRNA. Translation: CAA34811.1.
    X16312 mRNA. Translation: CAA34379.1.
    M30448 mRNA. Translation: AAA52123.1.
    X57152 Genomic DNA. Translation: CAA40442.1.
    AY113186 mRNA. Translation: AAM50092.1.
    CR541699 mRNA. Translation: CAG46500.1.
    AF129756 Genomic DNA. Translation: AAD18081.1.
    BA000025 Genomic DNA. Translation: BAB63386.1.
    DQ314868 Genomic DNA. Translation: ABC40727.1.
    AK311860 mRNA. Translation: BAG34801.1.
    AL662899 Genomic DNA. Translation: CAI96141.1.
    AL662899 Genomic DNA. Translation: CAI18393.2. Different initiation.
    AL670886 Genomic DNA. Translation: CAI17800.1.
    AL805934 Genomic DNA. Translation: CAI18523.1.
    BX511262 Genomic DNA. Translation: CAM45825.1.
    CR753842 Genomic DNA. Translation: CAQ06572.1.
    CR354443 Genomic DNA. Translation: CAQ07002.1.
    CR759761 Genomic DNA. Translation: CAQ10879.1.
    CH471081 Genomic DNA. Translation: EAX03473.1.
    BC112017 mRNA. Translation: AAI12018.1.
    BC112019 mRNA. Translation: AAI12020.1.
    CCDSiCCDS4712.1.
    PIRiA39459.
    RefSeqiNP_001269314.1. NM_001282385.1.
    NP_001311.3. NM_001320.6.
    UniGeneiHs.73527.

    Genome annotation databases

    EnsembliENST00000375865; ENSP00000365025; ENSG00000204435.
    ENST00000375866; ENSP00000365026; ENSG00000204435.
    ENST00000375882; ENSP00000365042; ENSG00000204435.
    ENST00000383427; ENSP00000372919; ENSG00000206406.
    ENST00000383433; ENSP00000372925; ENSG00000206406.
    ENST00000400110; ENSP00000382980; ENSG00000206406.
    ENST00000412802; ENSP00000413469; ENSG00000224774.
    ENST00000418230; ENSP00000411322; ENSG00000228875.
    ENST00000422567; ENSP00000407018; ENSG00000224398.
    ENST00000429633; ENSP00000409510; ENSG00000230700.
    ENST00000431476; ENSP00000394855; ENSG00000224398.
    ENST00000436169; ENSP00000412520; ENSG00000224398.
    ENST00000443673; ENSP00000400188; ENSG00000230700.
    ENST00000448596; ENSP00000391038; ENSG00000232960.
    ENST00000451917; ENSP00000415303; ENSG00000224774.
    ENST00000452985; ENSP00000415237; ENSG00000228875.
    ENST00000453234; ENSP00000395275; ENSG00000224774.
    ENST00000454382; ENSP00000390900; ENSG00000232960.
    ENST00000454511; ENSP00000393756; ENSG00000232960.
    ENST00000455161; ENSP00000407379; ENSG00000230700.
    ENST00000458330; ENSP00000410802; ENSG00000228875.
    GeneIDi1460.
    KEGGihsa:1460.
    UCSCiuc003nvr.1. human.

    Polymorphism databases

    DMDMi54037520.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16937 mRNA. Translation: CAA34811.1 .
    X16312 mRNA. Translation: CAA34379.1 .
    M30448 mRNA. Translation: AAA52123.1 .
    X57152 Genomic DNA. Translation: CAA40442.1 .
    AY113186 mRNA. Translation: AAM50092.1 .
    CR541699 mRNA. Translation: CAG46500.1 .
    AF129756 Genomic DNA. Translation: AAD18081.1 .
    BA000025 Genomic DNA. Translation: BAB63386.1 .
    DQ314868 Genomic DNA. Translation: ABC40727.1 .
    AK311860 mRNA. Translation: BAG34801.1 .
    AL662899 Genomic DNA. Translation: CAI96141.1 .
    AL662899 Genomic DNA. Translation: CAI18393.2 . Different initiation.
    AL670886 Genomic DNA. Translation: CAI17800.1 .
    AL805934 Genomic DNA. Translation: CAI18523.1 .
    BX511262 Genomic DNA. Translation: CAM45825.1 .
    CR753842 Genomic DNA. Translation: CAQ06572.1 .
    CR354443 Genomic DNA. Translation: CAQ07002.1 .
    CR759761 Genomic DNA. Translation: CAQ10879.1 .
    CH471081 Genomic DNA. Translation: EAX03473.1 .
    BC112017 mRNA. Translation: AAI12018.1 .
    BC112019 mRNA. Translation: AAI12020.1 .
    CCDSi CCDS4712.1.
    PIRi A39459.
    RefSeqi NP_001269314.1. NM_001282385.1.
    NP_001311.3. NM_001320.6.
    UniGenei Hs.73527.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DS5 X-ray 3.16 E/F/G/H 181-203 [» ]
    1JWH X-ray 3.10 C/D 1-215 [» ]
    1QF8 X-ray 1.74 A/B 1-182 [» ]
    3EED X-ray 2.80 A/B 1-193 [» ]
    4DGL X-ray 3.00 A/B 1-215 [» ]
    4MD7 X-ray 3.10 A/B/C/D 1-215 [» ]
    4MD8 X-ray 3.30 A/B/C/D 1-215 [» ]
    4MD9 X-ray 3.50 A/B/C/D/I/J/N/O 1-215 [» ]
    4NH1 X-ray 3.30 C/D 1-215 [» ]
    ProteinModelPortali P67870.
    SMRi P67870. Positions 7-207.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107843. 210 interactions.
    DIPi DIP-131N.
    IntActi P67870. 178 interactions.
    MINTi MINT-88683.
    STRINGi 9606.ENSP00000415615.

    Chemistry

    BindingDBi P67870.
    ChEMBLi CHEMBL2358.

    Polymorphism databases

    DMDMi 54037520.

    Proteomic databases

    MaxQBi P67870.
    PaxDbi P67870.
    PRIDEi P67870.

    Protocols and materials databases

    DNASUi 1460.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375865 ; ENSP00000365025 ; ENSG00000204435 .
    ENST00000375866 ; ENSP00000365026 ; ENSG00000204435 .
    ENST00000375882 ; ENSP00000365042 ; ENSG00000204435 .
    ENST00000383427 ; ENSP00000372919 ; ENSG00000206406 .
    ENST00000383433 ; ENSP00000372925 ; ENSG00000206406 .
    ENST00000400110 ; ENSP00000382980 ; ENSG00000206406 .
    ENST00000412802 ; ENSP00000413469 ; ENSG00000224774 .
    ENST00000418230 ; ENSP00000411322 ; ENSG00000228875 .
    ENST00000422567 ; ENSP00000407018 ; ENSG00000224398 .
    ENST00000429633 ; ENSP00000409510 ; ENSG00000230700 .
    ENST00000431476 ; ENSP00000394855 ; ENSG00000224398 .
    ENST00000436169 ; ENSP00000412520 ; ENSG00000224398 .
    ENST00000443673 ; ENSP00000400188 ; ENSG00000230700 .
    ENST00000448596 ; ENSP00000391038 ; ENSG00000232960 .
    ENST00000451917 ; ENSP00000415303 ; ENSG00000224774 .
    ENST00000452985 ; ENSP00000415237 ; ENSG00000228875 .
    ENST00000453234 ; ENSP00000395275 ; ENSG00000224774 .
    ENST00000454382 ; ENSP00000390900 ; ENSG00000232960 .
    ENST00000454511 ; ENSP00000393756 ; ENSG00000232960 .
    ENST00000455161 ; ENSP00000407379 ; ENSG00000230700 .
    ENST00000458330 ; ENSP00000410802 ; ENSG00000228875 .
    GeneIDi 1460.
    KEGGi hsa:1460.
    UCSCi uc003nvr.1. human.

    Organism-specific databases

    CTDi 1460.
    GeneCardsi GC06P031633.
    GC06Pj31620.
    GC06Pk31615.
    GC06Pl31672.
    GC06Pm31709.
    GC06Pn31623.
    GC06Po31622.
    HGNCi HGNC:2460. CSNK2B.
    HPAi CAB004349.
    CAB013087.
    CAB016059.
    HPA005944.
    MIMi 115441. gene.
    neXtProti NX_P67870.
    PharmGKBi PA26960.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5041.
    HOGENOMi HOG000039270.
    HOVERGENi HBG051131.
    InParanoidi P67870.
    KOi K03115.
    PhylomeDBi P67870.
    TreeFami TF314462.

    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 P67870.

    Miscellaneous databases

    EvolutionaryTracei P67870.
    GeneWikii CSNK2B.
    GenomeRNAii 1460.
    NextBioi 6001.
    PROi P67870.
    SOURCEi Search...

    Gene expression databases

    Bgeei P67870.
    CleanExi HS_CSNK2B.
    Genevestigatori P67870.

    Family and domain databases

    Gene3Di 1.10.1820.10. 1 hit.
    2.20.25.20. 1 hit.
    InterProi IPR016149. Casein_kin_II_reg-sub_a-hlx.
    IPR016150. Casein_kin_II_reg-sub_b-sht.
    IPR000704. Casein_kinase_II_reg-sub.
    [Graphical view ]
    PANTHERi PTHR11740. PTHR11740. 1 hit.
    Pfami PF01214. CK_II_beta. 1 hit.
    [Graphical view ]
    PRINTSi PR00472. CASNKINASEII.
    SMARTi SM01085. CK_II_beta. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57798. SSF57798. 1 hit.
    PROSITEi PS01101. CK2_BETA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human phosvitin/casein kinase type II. Molecular cloning and sequencing of full-length cDNA encoding subunit beta."
      Jakobi R., Voss H., Pyerin W.
      Eur. J. Biochem. 183:227-233(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Expression of the cDNA for the beta subunit of human casein kinase II confers partial UV resistance on xeroderma pigmentosum cells."
      Teitz T., Eli D., Penner M., Bakhanashvili M., Naiman T., Timme T.L., Wood C.M., Moses R.E., Canaani D.
      Mutat. Res. 236:85-97(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Cloning and characterization of a cDNA encoding the beta subunit of human casein kinase II."
      Heller-Harrison R.A., Meisner H., Czech M.P.
      Biochemistry 28:9053-9058(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Structure of the gene encoding human casein kinase II subunit beta."
      Voss A., Wirkner U., Jacobi R., Hewitt N., Schwager C., Zimmermann J., Ansorge W., Pyerin W.
      J. Biol. Chem. 266:13706-13711(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Sequencing of full-length cDNA encoding the alpha and beta subunits of human casein kinase II from human platelets and megakaryocytic cells. Expression of the casein kinase IIalpha intronless gene in a megakaryocytic cell line."
      Singh L.S., Kalafatis M.
      Biochemistry 41:8935-8940(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
      Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
      Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."
      Shiina S., Tamiya G., Oka A., Inoko H.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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].
      Tissue: Brain.
    10. NHLBI resequencing and genotyping service (RS&G)
      Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    11. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    12. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    13. "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: Brain.
    14. "Stimulation of casein kinase II by epidermal growth factor: relationship between the physiological activity of the kinase and the phosphorylation state of its beta subunit."
      Ackerman P., Glover C.V., Osheroff N.
      Proc. Natl. Acad. Sci. U.S.A. 87:821-825(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    15. "Interaction of CD163 with the regulatory subunit of casein kinase II (CKII) and dependence of CD163 signaling on CKII and protein kinase C."
      Ritter M., Buechler C., Kapinsky M., Schmitz G.
      Eur. J. Immunol. 31:999-1009(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CD163.
    16. "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.
    17. "Identification of ribosome-binding protein p34 as an intracellular protein that binds acidic fibroblast growth factor."
      Skjerpen C.S., Wesche J., Olsnes S.
      J. Biol. Chem. 277:23864-23871(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FGF1.
    18. "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.
    19. "Casein kinase 2-dependent serine phosphorylation of MuSK regulates acetylcholine receptor aggregation at the neuromuscular junction."
      Cheusova T., Khan M.A., Schubert S.W., Gavin A.C., Buchou T., Jacob G., Sticht H., Allende J., Boldyreff B., Brenner H.R., Hashemolhosseini S.
      Genes Dev. 20:1800-1816(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF MUSK, INTERACTION WITH MUSK.
    20. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "Crystal structure of the human protein kinase CK2 regulatory subunit reveals its zinc finger-mediated dimerization."
      Chantalat L., Leroy D., Filhol O., Nueda A., Benitez M.J., Chambaz E.M., Cochet C., Dideberg O.
      EMBO J. 18:2930-2940(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 1-182, SUBUNIT, ZINC-BINDING SITES.
    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) IN COMPLEX WITH CSNK2A1, ZINC-BINDING SITES, SUBUNIT, PHOSPHORYLATION AT SER-2 AND SER-3.

    Entry informationi

    Entry nameiCSK2B_HUMAN
    AccessioniPrimary (citable) accession number: P67870
    Secondary accession number(s): B0UXA9
    , P07312, P13862, Q4VX47
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: October 11, 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3