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Q16566 (KCC4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calcium/calmodulin-dependent protein kinase type IV

Short name=CaMK IV
EC=2.7.11.17
Alternative name(s):
CaM kinase-GR
Gene names
Name:CAMK4
Synonyms:CAMK, CAMK-GR, CAMKIV
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.17 Ref.18

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

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. Ref.10 Ref.15 Ref.16

Subunit structure

Monomer By similarity. Interacts with protein phosphatase 2A (PPP2CA/PPP2CB); the interaction is mutually exclusive with binding to Ca2+/calmodulin. Ref.15

Subcellular location

Cytoplasm. Nucleus. Note: Localized in hippocampal neuron nuclei. In spermatids, associated with chromatin and nuclear matrix By similarity. Ref.8 Ref.9

Tissue specificity

Expressed in brain, thymus, CD4 T-cells, testis and epithelial ovarian cancer tissue. Ref.6 Ref.7 Ref.14

Developmental stage

Expressed during differentiation of monocyte-derived dendritic cells (at protein level). Ref.17

Domain

The autoinhibitory domain overlaps with the calmodulin binding region and interacts in the inactive folded state with the catalytic domain as a pseudosubstrate. Ref.7 Ref.16

Post-translational modification

Phosphorylated by CaMKK1 and CaMKK2 on Thr-200. Dephosphorylated by protein phosphatase 2A. Autophosphorylated on Ser-12 and Ser-13. Ref.10 Ref.15 Ref.20

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.

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily.

Contains 1 protein kinase domain.

Sequence caution

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

Ontologies

Keywords
   Biological processAdaptive immunity
Immunity
Inflammatory response
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   LigandATP-binding
Calcium
Calmodulin-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of phospholipase C activity

Traceable author statement. Source: Reactome

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Traceable author statement. Source: Reactome

long-term memory

Inferred from genetic interaction Ref.18. Source: UniProtKB

myeloid dendritic cell differentiation

Inferred from mutant phenotype Ref.17. Source: UniProtKB

neuron-neuron synaptic transmission

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

nucleocytoplasmic transport

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein export from nucleus

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.11. Source: UniProtKB

protein phosphorylation

Traceable author statement Ref.1. Source: ProtInc

regulation of T cell differentiation in thymus

Traceable author statement Ref.23. Source: UniProtKB

regulation of osteoclast differentiation

Traceable author statement Ref.23. Source: UniProtKB

signal transduction

Traceable author statement. Source: Reactome

synaptic transmission

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

nucleolus

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

calmodulin-dependent protein kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 473473Calcium/calmodulin-dependent protein kinase type IV
PRO_0000086106

Regions

Domain46 – 300255Protein kinase
Nucleotide binding52 – 609ATP By similarity
Region305 – 32117Autoinhibitory domain
Region306 – 32318PP2A-binding
Region322 – 34120Calmodulin-binding Potential

Sites

Active site1641Proton acceptor By similarity
Binding site751ATP By similarity

Amino acid modifications

Modified residue121Phosphoserine; by autocatalysis Ref.10
Modified residue131Phosphoserine; by autocatalysis Ref.10
Modified residue2001Phosphothreonine; by CaMKK1 and CaMKK2 Ref.10 Ref.15 Ref.20
Modified residue3361Phosphoserine; by autocatalysis
Modified residue3601Phosphoserine Ref.24
Glycosylation571O-linked (GlcNAc) Ref.20
Glycosylation581O-linked (GlcNAc) Ref.20
Glycosylation1371O-linked (GlcNAc) Ref.20
Glycosylation1891O-linked (GlcNAc) Ref.20
Glycosylation3441O-linked (GlcNAc) Ref.20
Glycosylation3451O-linked (GlcNAc) Ref.20
Glycosylation3561O-linked (GlcNAc) Ref.20

Natural variations

Natural variant1501E → G in a lung adenocarcinoma sample; somatic mutation. Ref.27
VAR_040604
Natural variant1781D → N. Ref.27
Corresponds to variant rs35548075 [ dbSNP | Ensembl ].
VAR_040605
Natural variant4651Q → R. Ref.27
Corresponds to variant rs56360861 [ dbSNP | Ensembl ].
VAR_040606
Natural variant4691I → M in a lung large cell carcinoma sample; somatic mutation. Ref.27
VAR_040607

Experimental info

Mutagenesis121S → A: Loss of activity. Ref.10 Ref.15
Mutagenesis131S → A: Loss of activity. Ref.10 Ref.15
Mutagenesis57 – 582TS → AA: Loss of phosphorylation of CREB1. Ref.15
Mutagenesis751K → E: Loss of activity; dominant negative form. Ref.13 Ref.15
Mutagenesis1891S → A: Increases phosphorylation of CREB1 2-fold. Decreases total O-linked glycosylation 2-fold. Increases ATP-binding affinity. Ref.15 Ref.20
Mutagenesis2001T → A: Loss of activation by CaMKK1 or CaMKK2. Ref.11 Ref.15
Mutagenesis309 – 3124HMDT → DEDD: Fully active Ca2+/CaM-independent kinase; when associated with 320-A-A-321. Ref.7 Ref.15
Mutagenesis320 – 3212FN → DD: Fully active Ca2+/CaM-independent kinase; when associated with 309-A--A-312. Loss of interaction with PPP2CA/PPP2CB. Ref.15

Secondary structure

............................................... 473
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q16566 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: EFEE51E5612326DC

FASTA47351,926
        10         20         30         40         50         60 
MLKVTVPSCS ASSCSSVTAS AAPGTASLVP DYWIDGSNRD ALSDFFEVES ELGRGATSIV 

        70         80         90        100        110        120 
YRCKQKGTQK PYALKVLKKT VDKKIVRTEI GVLLRLSHPN IIKLKEIFET PTEISLVLEL 

       130        140        150        160        170        180 
VTGGELFDRI VEKGYYSERD AADAVKQILE AVAYLHENGI VHRDLKPENL LYATPAPDAP 

       190        200        210        220        230        240 
LKIADFGLSK IVEHQVLMKT VCGTPGYCAP EILRGCAYGP EVDMWSVGII TYILLCGFEP 

       250        260        270        280        290        300 
FYDERGDQFM FRRILNCEYY FISPWWDEVS LNAKDLVRKL IVLDPKKRLT TFQALQHPWV 

       310        320        330        340        350        360 
TGKAANFVHM DTAQKKLQEF NARRKLKAAV KAVVASSRLG SASSSHGSIQ ESHKASRDPS 

       370        380        390        400        410        420 
PIQDGNEDMK AIPEGEKIQG DGAQAAVKGA QAELMKVQAL EKVKGADINA EEAPKMVPKA 

       430        440        450        460        470 
VEDGIKVADL ELEEGLAEEK LKTVEEAAAP REGQGSSAVG FEVPQQDVIL PEY 

« Hide

References

« Hide 'large scale' references
[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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA53036.
RefSeqNP_001735.1. NM_001744.4.
UniGeneHs.591269.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2W4OX-ray2.17A15-340[»]
ProteinModelPortalQ16566.
SMRQ16566. Positions 34-444.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107264. 7 interactions.
DIPDIP-41997N.
IntActQ16566. 1 interaction.
MINTMINT-192934.
STRING9606.ENSP00000282356.

Chemistry

BindingDBQ16566.
ChEMBLCHEMBL2494.
GuidetoPHARMACOLOGY1955.

PTM databases

PhosphoSiteQ16566.

Polymorphism databases

DMDM2499586.

Proteomic databases

PaxDbQ16566.
PeptideAtlasQ16566.
PRIDEQ16566.

Protocols and materials databases

DNASU814.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000282356; ENSP00000282356; ENSG00000152495.
ENST00000512453; ENSP00000422634; ENSG00000152495.
GeneID814.
KEGGhsa:814.
UCSCuc003kpf.3. human.

Organism-specific databases

CTD814.
GeneCardsGC05P110587.
HGNCHGNC:1464. CAMK4.
HPACAB004347.
HPA011753.
HPA017206.
MIM114080. gene.
neXtProtNX_Q16566.
PharmGKBPA26050.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233016.
HOVERGENHBG108055.
InParanoidQ16566.
KOK05869.
OMACEQFGLS.
PhylomeDBQ16566.
TreeFamTF351230.

Enzyme and pathway databases

BRENDA2.7.11.17. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_13685. Neuronal System.
REACT_6900. Immune System.
SignaLinkQ16566.

Gene expression databases

ArrayExpressQ16566.
BgeeQ16566.
CleanExHS_CAMK4.
GenevestigatorQ16566.

Family and domain databases

InterProIPR011009. 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]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCAMK4. human.
EvolutionaryTraceQ16566.
GeneWikiCAMK4.
GenomeRNAi814.
NextBio3300.
PMAP-CutDBQ16566.
PROQ16566.
SOURCESearch...

Entry information

Entry nameKCC4_HUMAN
AccessionPrimary (citable) accession number: Q16566
Secondary accession number(s): D3DSZ7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

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SIMILARITY comments

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Human and mouse protein kinases

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PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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