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Q16566

- KCC4_HUMAN

UniProt

Q16566 - KCC4_HUMAN

Protein

Calcium/calmodulin-dependent protein kinase type IV

Gene

CAMK4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK4 signaling cascade and regulates, mainly by phosphorylation, the activity of several transcription activators, such as CREB1, MEF2D, JUN and RORA, which play pivotal roles in immune response, inflammation, and memory consolidation. In the thymus, regulates the CD4+/CD8+ double positive thymocytes selection threshold during T-cell ontogeny. In CD4 memory T-cells, is required to link T-cell antigen receptor (TCR) signaling to the production of IL2, IFNG and IL4 (through the regulation of CREB and MEF2). Regulates the differentiation and survival phases of osteoclasts and dendritic cells (DCs). Mediates DCs survival by linking TLR4 and the regulation of temporal expression of BCL2. Phosphorylates the transcription activator CREB1 on 'Ser-133' in hippocampal neuron nuclei and contribute to memory consolidation and long term potentiation (LTP) in the hippocampus. Can activate the MAP kinases MAPK1/ERK2, MAPK8/JNK1 and MAPK14/p38 and stimulate transcription through the phosphorylation of ELK1 and ATF2. Can also phosphorylate in vitro CREBBP, PRM2, MEF2A and STMN1/OP18.8 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Activated by Ca2+/calmodulin. Binding of calmodulin results in conformational change that relieves intrasteric autoinhibition and allows phosphorylation of Thr-200 within the activation loop by CaMKK1 or CaMKK2. Phosphorylation of Thr-200 results in a 10-20-fold increase in total activity to generate Ca2+/calmodulin-independent activity. Autophosphorylation of the N-terminus Ser-12 and Ser-13 is required for full activation. Inactivated by protein phosphatase 2A (PPP2CA/PPP2CB) which dephosphorylates Thr-200, thereby terminating autonomous activity and helping to maintain the enzyme in its autoinhibited state.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei75 – 751ATPPROSITE-ProRule annotation
    Active sitei164 – 1641Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi52 – 609ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. calmodulin-dependent protein kinase activity Source: UniProtKB-EC

    GO - Biological processi

    1. activation of phospholipase C activity Source: Reactome
    2. epidermal growth factor receptor signaling pathway Source: Reactome
    3. fibroblast growth factor receptor signaling pathway Source: Reactome
    4. inflammatory response Source: UniProtKB-KW
    5. innate immune response Source: Reactome
    6. long-term memory Source: UniProtKB
    7. myeloid dendritic cell differentiation Source: UniProtKB
    8. neuron-neuron synaptic transmission Source: Ensembl
    9. neurotrophin TRK receptor signaling pathway Source: Reactome
    10. nucleocytoplasmic transport Source: Ensembl
    11. positive regulation of protein export from nucleus Source: Ensembl
    12. positive regulation of transcription, DNA-templated Source: UniProtKB
    13. protein phosphorylation Source: ProtInc
    14. regulation of osteoclast differentiation Source: UniProtKB
    15. regulation of T cell differentiation in thymus Source: UniProtKB
    16. signal transduction Source: Reactome
    17. synaptic transmission Source: Reactome

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Adaptive immunity, Immunity, Inflammatory response

    Keywords - Ligandi

    ATP-binding, Calcium, Calmodulin-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.17. 2681.
    ReactomeiREACT_15502. CaMK IV-mediated phosphorylation of CREB.
    REACT_200608. Transcriptional activation of mitochondrial biogenesis.
    REACT_20652. Activation of CaMK IV.
    REACT_20661. CREB phosphorylation through the activation of CaMKK.
    SignaLinkiQ16566.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calcium/calmodulin-dependent protein kinase type IV (EC:2.7.11.17)
    Short name:
    CaMK IV
    Alternative name(s):
    CaM kinase-GR
    Gene namesi
    Name:CAMK4
    Synonyms:CAMK, CAMK-GR, CAMKIV
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:1464. CAMK4.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Localized in hippocampal neuron nuclei. In spermatids, associated with chromatin and nuclear matrix By similarity.By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. nucleolus Source: HPA
    4. nucleoplasm Source: Reactome
    5. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi12 – 121S → A: Loss of activity. 1 Publication
    Mutagenesisi13 – 131S → A: Loss of activity. 1 Publication
    Mutagenesisi57 – 582TS → AA: Loss of phosphorylation of CREB1.
    Mutagenesisi75 – 751K → E: Loss of activity; dominant negative form. 1 Publication
    Mutagenesisi189 – 1891S → A: Increases phosphorylation of CREB1 2-fold. Decreases total O-linked glycosylation 2-fold. Increases ATP-binding affinity. 1 Publication
    Mutagenesisi200 – 2001T → A: Loss of activation by CaMKK1 or CaMKK2. 1 Publication
    Mutagenesisi309 – 3124HMDT → DEDD: Fully active Ca2+/CaM-independent kinase; when associated with 320-A-A-321.
    Mutagenesisi320 – 3212FN → DD: Fully active Ca2+/CaM-independent kinase; when associated with 309-A--A-312. Loss of interaction with PPP2CA/PPP2CB.

    Organism-specific databases

    PharmGKBiPA26050.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 473473Calcium/calmodulin-dependent protein kinase type IVPRO_0000086106Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei12 – 121Phosphoserine; by autocatalysis1 Publication
    Modified residuei13 – 131Phosphoserine; by autocatalysis1 Publication
    Glycosylationi57 – 571O-linked (GlcNAc)1 Publication
    Glycosylationi58 – 581O-linked (GlcNAc)1 Publication
    Glycosylationi137 – 1371O-linked (GlcNAc)1 Publication
    Glycosylationi189 – 1891O-linked (GlcNAc)1 Publication
    Modified residuei200 – 2001Phosphothreonine; by CaMKK1 and CaMKK23 Publications
    Modified residuei336 – 3361Phosphoserine; by autocatalysisBy similarity
    Glycosylationi344 – 3441O-linked (GlcNAc)1 Publication
    Glycosylationi345 – 3451O-linked (GlcNAc)1 Publication
    Glycosylationi356 – 3561O-linked (GlcNAc)1 Publication
    Modified residuei360 – 3601Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated by CaMKK1 and CaMKK2 on Thr-200. Dephosphorylated by protein phosphatase 2A. Autophosphorylated on Ser-12 and Ser-13.4 Publications
    Glycosylation at Ser-189 modulates the phosphorylation of CaMK4 at Thr-200 and negatively regulates its activity toward CREB1 in basal conditions and during early inomycin stimulation.3 Publications

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ16566.
    PaxDbiQ16566.
    PeptideAtlasiQ16566.
    PRIDEiQ16566.

    PTM databases

    PhosphoSiteiQ16566.

    Miscellaneous databases

    PMAP-CutDBQ16566.

    Expressioni

    Tissue specificityi

    Expressed in brain, thymus, CD4 T-cells, testis and epithelial ovarian cancer tissue.3 Publications

    Developmental stagei

    Expressed during differentiation of monocyte-derived dendritic cells (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ16566.
    BgeeiQ16566.
    CleanExiHS_CAMK4.
    GenevestigatoriQ16566.

    Organism-specific databases

    HPAiCAB004347.
    HPA011753.
    HPA017206.

    Interactioni

    Subunit structurei

    Monomer By similarity. Interacts with protein phosphatase 2A (PPP2CA/PPP2CB); the interaction is mutually exclusive with binding to Ca2+/calmodulin.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi107264. 7 interactions.
    DIPiDIP-41997N.
    IntActiQ16566. 1 interaction.
    MINTiMINT-192934.
    STRINGi9606.ENSP00000282356.

    Structurei

    Secondary structure

    1
    473
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi36 – 383
    Helixi42 – 443
    Beta strandi46 – 549
    Beta strandi56 – 6510
    Turni66 – 683
    Beta strandi71 – 788
    Helixi91 – 955
    Beta strandi104 – 1096
    Beta strandi111 – 1188
    Helixi126 – 1305
    Helixi138 – 15720
    Helixi167 – 1693
    Beta strandi170 – 1767
    Beta strandi181 – 1833
    Helixi205 – 2073
    Helixi210 – 2134
    Helixi221 – 23616
    Helixi247 – 2559
    Turni263 – 2686
    Helixi271 – 2788
    Helixi285 – 2873
    Helixi291 – 2966
    Turni298 – 3014
    Helixi311 – 33525

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2W4OX-ray2.17A15-340[»]
    ProteinModelPortaliQ16566.
    SMRiQ16566. Positions 34-444.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16566.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini46 – 300255Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni305 – 32117Autoinhibitory domainAdd
    BLAST
    Regioni306 – 32318PP2A-bindingAdd
    BLAST
    Regioni322 – 34120Calmodulin-bindingSequence AnalysisAdd
    BLAST

    Domaini

    The autoinhibitory domain overlaps with the calmodulin binding region and interacts in the inactive folded state with the catalytic domain as a pseudosubstrate.1 Publication

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233016.
    HOVERGENiHBG108055.
    InParanoidiQ16566.
    KOiK05869.
    OMAiPIQDGNE.
    PhylomeDBiQ16566.
    TreeFamiTF351230.

    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.

    Q16566-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLKVTVPSCS ASSCSSVTAS AAPGTASLVP DYWIDGSNRD ALSDFFEVES    50
    ELGRGATSIV YRCKQKGTQK PYALKVLKKT VDKKIVRTEI GVLLRLSHPN 100
    IIKLKEIFET PTEISLVLEL VTGGELFDRI VEKGYYSERD AADAVKQILE 150
    AVAYLHENGI VHRDLKPENL LYATPAPDAP LKIADFGLSK IVEHQVLMKT 200
    VCGTPGYCAP EILRGCAYGP EVDMWSVGII TYILLCGFEP FYDERGDQFM 250
    FRRILNCEYY FISPWWDEVS LNAKDLVRKL IVLDPKKRLT TFQALQHPWV 300
    TGKAANFVHM DTAQKKLQEF NARRKLKAAV KAVVASSRLG SASSSHGSIQ 350
    ESHKASRDPS PIQDGNEDMK AIPEGEKIQG DGAQAAVKGA QAELMKVQAL 400
    EKVKGADINA EEAPKMVPKA VEDGIKVADL ELEEGLAEEK LKTVEEAAAP 450
    REGQGSSAVG FEVPQQDVIL PEY 473
    Length:473
    Mass (Da):51,926
    Last modified:November 1, 1996 - v1
    Checksum:iEFEE51E5612326DC
    GO

    Sequence cautioni

    The sequence AAH16695.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti150 – 1501E → G in a lung adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_040604
    Natural varianti178 – 1781D → N.1 Publication
    Corresponds to variant rs35548075 [ dbSNP | Ensembl ].
    VAR_040605
    Natural varianti465 – 4651Q → R.1 Publication
    Corresponds to variant rs56360861 [ dbSNP | Ensembl ].
    VAR_040606
    Natural varianti469 – 4691I → M in a lung large cell carcinoma sample; somatic mutation. 1 Publication
    VAR_040607

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D30742 mRNA. Translation: BAA06403.1.
    L17000 mRNA. Translation: AAA35639.1.
    L24959 mRNA. Translation: AAA18251.1.
    CH471086 Genomic DNA. Translation: EAW49033.1.
    CH471086 Genomic DNA. Translation: EAW49034.1.
    BC016695 mRNA. Translation: AAH16695.2. Different initiation.
    BC025687 mRNA. Translation: AAH25687.1.
    CCDSiCCDS4103.1.
    PIRiA53036.
    RefSeqiNP_001735.1. NM_001744.4.
    UniGeneiHs.591269.

    Genome annotation databases

    EnsembliENST00000282356; ENSP00000282356; ENSG00000152495.
    ENST00000512453; ENSP00000422634; ENSG00000152495.
    GeneIDi814.
    KEGGihsa:814.
    UCSCiuc003kpf.3. human.

    Polymorphism databases

    DMDMi2499586.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D30742 mRNA. Translation: BAA06403.1 .
    L17000 mRNA. Translation: AAA35639.1 .
    L24959 mRNA. Translation: AAA18251.1 .
    CH471086 Genomic DNA. Translation: EAW49033.1 .
    CH471086 Genomic DNA. Translation: EAW49034.1 .
    BC016695 mRNA. Translation: AAH16695.2 . Different initiation.
    BC025687 mRNA. Translation: AAH25687.1 .
    CCDSi CCDS4103.1.
    PIRi A53036.
    RefSeqi NP_001735.1. NM_001744.4.
    UniGenei Hs.591269.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2W4O X-ray 2.17 A 15-340 [» ]
    ProteinModelPortali Q16566.
    SMRi Q16566. Positions 34-444.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107264. 7 interactions.
    DIPi DIP-41997N.
    IntActi Q16566. 1 interaction.
    MINTi MINT-192934.
    STRINGi 9606.ENSP00000282356.

    Chemistry

    BindingDBi Q16566.
    ChEMBLi CHEMBL2494.
    GuidetoPHARMACOLOGYi 1955.

    PTM databases

    PhosphoSitei Q16566.

    Polymorphism databases

    DMDMi 2499586.

    Proteomic databases

    MaxQBi Q16566.
    PaxDbi Q16566.
    PeptideAtlasi Q16566.
    PRIDEi Q16566.

    Protocols and materials databases

    DNASUi 814.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000282356 ; ENSP00000282356 ; ENSG00000152495 .
    ENST00000512453 ; ENSP00000422634 ; ENSG00000152495 .
    GeneIDi 814.
    KEGGi hsa:814.
    UCSCi uc003kpf.3. human.

    Organism-specific databases

    CTDi 814.
    GeneCardsi GC05P110587.
    HGNCi HGNC:1464. CAMK4.
    HPAi CAB004347.
    HPA011753.
    HPA017206.
    MIMi 114080. gene.
    neXtProti NX_Q16566.
    PharmGKBi PA26050.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233016.
    HOVERGENi HBG108055.
    InParanoidi Q16566.
    KOi K05869.
    OMAi PIQDGNE.
    PhylomeDBi Q16566.
    TreeFami TF351230.

    Enzyme and pathway databases

    BRENDAi 2.7.11.17. 2681.
    Reactomei REACT_15502. CaMK IV-mediated phosphorylation of CREB.
    REACT_200608. Transcriptional activation of mitochondrial biogenesis.
    REACT_20652. Activation of CaMK IV.
    REACT_20661. CREB phosphorylation through the activation of CaMKK.
    SignaLinki Q16566.

    Miscellaneous databases

    ChiTaRSi CAMK4. human.
    EvolutionaryTracei Q16566.
    GeneWikii CAMK4.
    GenomeRNAii 814.
    NextBioi 3300.
    PMAP-CutDB Q16566.
    PROi Q16566.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16566.
    Bgeei Q16566.
    CleanExi HS_CAMK4.
    Genevestigatori Q16566.

    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. "cDNA cloning and expression of human calmodulin-dependent protein kinase IV."
      Kitani T., Okuno S., Fujisawa H.
      J. Biochem. 115:637-640(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The cDNA sequence and characterization of the Ca2+/calmodulin-dependent protein kinase-Gr from human brain and thymus."
      Bland M.M., Monroe R.S., Ohmstede C.A.
      Gene 142:191-197(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Cerebellum and Thymus.
    3. "A Ca2+/calmodulin-dependent protein kinase, CaM kinase-Gr, expressed after transformation of primary human B lymphocytes by Epstein-Barr virus (EBV) is induced by the EBV oncogene LMP1."
      Mosialos G., Hanissian S.H., Jawahar S., Vara L., Kieff E., Chatila T.A.
      J. Virol. 68:1697-1705(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Blood.
    4. 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].
      Tissue: Brain and Lung.
    6. "Expression of a Ca2+/calmodulin-dependent protein kinase, CaM kinase-Gr, in human T lymphocytes. Regulation of kinase activity by T cell receptor signaling."
      Hanissian S.H., Frangakis M., Bland M.M., Jawahar S., Chatila T.A.
      J. Biol. Chem. 268:20055-20063(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    7. "Activation mechanisms for Ca2+/calmodulin-dependent protein kinase IV. Identification of a brain CaM-kinase IV kinase."
      Tokumitsu H., Brickey D.A., Glod J., Hidaka H., Sikela J., Soderling T.R.
      J. Biol. Chem. 269:28640-28647(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, DOMAIN AUTOINHIBITORY, MUTAGENESIS OF 309-HIS--THR-312 AND 320-PHE-ASN-321.
    8. "Calcium/calmodulin-dependent protein kinase types II and IV differentially regulate CREB-dependent gene expression."
      Matthews R.P., Guthrie C.R., Wailes L.M., Zhao X., Means A.R., McKnight G.S.
      Mol. Cell. Biol. 14:6107-6116(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CREB1, SUBCELLULAR LOCATION.
    9. "CREB phosphorylation and dephosphorylation: a Ca(2+)- and stimulus duration-dependent switch for hippocampal gene expression."
      Bito H., Deisseroth K., Tsien R.W.
      Cell 87:1203-1214(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    10. "A unique phosphorylation-dependent mechanism for the activation of Ca2+/calmodulin-dependent protein kinase type IV/GR."
      Chatila T., Anderson K.A., Ho N., Means A.R.
      J. Biol. Chem. 271:21542-21548(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, PHOSPHORYLATION AT SER-12; SER-13 AND THR-200, MUTAGENESIS OF SER-12 AND SER-13.
    11. "Regulation of mitogen-activated protein kinases by a calcium/calmodulin-dependent protein kinase cascade."
      Enslen H., Tokumitsu H., Stork P.J., Davis R.J., Soderling T.R.
      Proc. Natl. Acad. Sci. U.S.A. 93:10803-10808(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF ELK1; JUN AND ATF2, MUTAGENESIS OF THR-200.
    12. "Regulation of microtubule dynamics by Ca2+/calmodulin-dependent kinase IV/Gr-dependent phosphorylation of oncoprotein 18."
      Melander Gradin H., Marklund U., Larsson N., Chatila T.A., Gullberg M.
      Mol. Cell. Biol. 17:3459-3467(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF STMN1.
    13. "Ca(2+)-dependent gene expression mediated by MEF2 transcription factors."
      Blaeser F., Ho N., Prywes R., Chatila T.A.
      J. Biol. Chem. 275:197-209(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF MEF2D, MUTAGENESIS OF LYS-75.
    14. "Ca(2+)/calmodulin-dependent protein kinase IV expression in epithelial ovarian cancer."
      Takai N., Miyazaki T., Nishida M., Nasu K., Miyakawa I.
      Cancer Lett. 183:185-193(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    15. "Regulation and function of the calcium/calmodulin-dependent protein kinase IV/protein serine/threonine phosphatase 2A signaling complex."
      Anderson K.A., Noeldner P.K., Reece K., Wadzinski B.E., Means A.R.
      J. Biol. Chem. 279:31708-31716(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, INTERACTION WITH PROTEIN PHOSPHATASE 2A, PHOSPHORYLATION AT THR-200, MUTAGENESIS OF 320-PHE-ASN-321.
    16. "The autonomous activity of calcium/calmodulin-dependent protein kinase IV is required for its role in transcription."
      Chow F.A., Anderson K.A., Noeldner P.K., Means A.R.
      J. Biol. Chem. 280:20530-20538(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, PROTEIN PHOSPHATASE 2A BINDING DOMAIN.
    17. "Calmodulin-dependent kinase IV links Toll-like receptor 4 signaling with survival pathway of activated dendritic cells."
      Illario M., Giardino-Torchia M.L., Sankar U., Ribar T.J., Galgani M., Vitiello L., Masci A.M., Bertani F.R., Ciaglia E., Astone D., Maulucci G., Cavallo A., Vitale M., Cimini V., Pastore L., Means A.R., Rossi G., Racioppi L.
      Blood 111:723-731(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DENDRITIC CELLS LIFESPAN REGULATION, DEVELOPMENTAL STAGE.
    18. "Upregulation of calcium/calmodulin-dependent protein kinase IV improves memory formation and rescues memory loss with aging."
      Fukushima H., Maeda R., Suzuki R., Suzuki A., Nomoto M., Toyoda H., Wu L.J., Xu H., Zhao M.G., Ueda K., Kitamoto A., Mamiya N., Yoshida T., Homma S., Masushige S., Zhuo M., Kida S.
      J. Neurosci. 28:9910-9919(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Regulation of calcium/calmodulin-dependent kinase IV by O-GlcNAc modification."
      Dias W.B., Cheung W.D., Wang Z., Hart G.W.
      J. Biol. Chem. 284:21327-21337(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT THR-57 SER-58; SER-137; SER-189; SER-344; SER-345 AND SER-356, PHOSPHORYLATION AT THR-200, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF 57-THR-SER-58 AND SER-189.
    21. "Calmodulin-dependent protein kinase IV: regulation of function and expression."
      Krebs J.
      Biochim. Biophys. Acta 1448:183-189(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION, REVIEW ON ENZYME REGULATION.
    22. "Calmodulin-kinases: modulators of neuronal development and plasticity."
      Wayman G.A., Lee Y.S., Tokumitsu H., Silva A.J., Silva A., Soderling T.R.
      Neuron 59:914-931(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION IN NEURONAL PLASTICITY.
    23. "Calcium/calmodulin-dependent kinase IV in immune and inflammatory responses: novel routes for an ancient traveller."
      Racioppi L., Means A.R.
      Trends Immunol. 29:600-607(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON INVOLVEMENT IN IMMUNE AND INFLAMMATORY RESPONSE.
    24. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "Crystal structure of human CAMK4 in complex with 4-amino(sulfamoyl-phenylamino)-triazole-carbothioic acid (2,6-difluoro-phenyl)-amide)."
      Muniz J.R.C., Rellos P., Gileadi O., Fedorov O., Filippakopoulos P., Salah E., Pike A., Phillips C., Niesen F., Shrestha L., Burgess-Brown N., Bullock A., Berridge G., Vondelft F., Edwards A.M., Bountra C., Arrowsmith C.H., Weigelt J., Knapp S.
      Submitted (NOV-2008) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS) OF 15-340 IN COMPLEX WITH INHIBITOR.
    27. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLY-150; ASN-178; ARG-465 AND MET-469.

    Entry informationi

    Entry nameiKCC4_HUMAN
    AccessioniPrimary (citable) accession number: Q16566
    Secondary accession number(s): D3DSZ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 144 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 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3