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Q16566

- KCC4_HUMAN

UniProt

Q16566 - KCC4_HUMAN

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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

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
Complete GO annotation...

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
Complete GO annotation...

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. 1 Publication
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. 1 Publication
Mutagenesisi320 – 3212FN → DD: Fully active Ca2+/CaM-independent kinase; when associated with 309-A--A-312. Loss of interaction with PPP2CA/PPP2CB. 2 Publications

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

BgeeiQ16566.
CleanExiHS_CAMK4.
ExpressionAtlasiQ16566. baseline and differential.
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.
GeneTreeiENSGT00760000118944.
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.
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

        10         20         30         40         50
MLKVTVPSCS ASSCSSVTAS AAPGTASLVP DYWIDGSNRD ALSDFFEVES
60 70 80 90 100
ELGRGATSIV YRCKQKGTQK PYALKVLKKT VDKKIVRTEI GVLLRLSHPN
110 120 130 140 150
IIKLKEIFET PTEISLVLEL VTGGELFDRI VEKGYYSERD AADAVKQILE
160 170 180 190 200
AVAYLHENGI VHRDLKPENL LYATPAPDAP LKIADFGLSK IVEHQVLMKT
210 220 230 240 250
VCGTPGYCAP EILRGCAYGP EVDMWSVGII TYILLCGFEP FYDERGDQFM
260 270 280 290 300
FRRILNCEYY FISPWWDEVS LNAKDLVRKL IVLDPKKRLT TFQALQHPWV
310 320 330 340 350
TGKAANFVHM DTAQKKLQEF NARRKLKAAV KAVVASSRLG SASSSHGSIQ
360 370 380 390 400
ESHKASRDPS PIQDGNEDMK AIPEGEKIQG DGAQAAVKGA QAELMKVQAL
410 420 430 440 450
EKVKGADINA EEAPKMVPKA VEDGIKVADL ELEEGLAEEK LKTVEEAAAP
460 470
REGQGSSAVG FEVPQQDVIL PEY
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.
GeneTreei ENSGT00760000118944.
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

Bgeei Q16566.
CleanExi HS_CAMK4.
ExpressionAtlasi Q16566. baseline and differential.
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.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 145 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