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Information on EC 2.7.11.17 - Ca2+/calmodulin-dependent protein kinase

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EC Tree
IUBMB Comments
Requires calmodulin and Ca2+ for activity. A wide range of proteins can act as acceptor, including vimentin, synapsin, glycogen synthase, myosin light chains and the microtubule-associated tau protein. Not identical with EC 2.7.11.18 (myosin-light-chain kinase) or EC 2.7.11.26 (tau-protein kinase).
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This record set is specific for:
UNIPROT: Q84ZT8
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Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
+
a [protein]-(L-serine/L-threonine)
=
+
a [protein]-(L-serine/L-threonine) phosphate
Synonyms
caldesmon, cam kinase ii, camkiv, cam kinase, calcium/calmodulin-dependent protein kinase ii, calmodulin-dependent protein kinase, camkk2, calcium/calmodulin-dependent protein kinase, ca2+/calmodulin-dependent protein kinase, camk ii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
calcium/calmodulin-dependent protein kinase
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CaM-dependent kinase
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CAKI
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-
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caldesmon
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-
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Calspermin
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-
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CAM kinase-GR
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-
-
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CMPK
-
-
-
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kinase, caldesmon (phosphorylating)
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-
-
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kinase, microtubule-associated protein 2 (phosphorylating)
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-
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MAP kinase
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-
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MAP-2 kinase
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-
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MAP-2 protein serine kinase
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-
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microtubule associated protein kinase
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-
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microtubule-associated protein 2 kinase
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-
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peripheral plasma membrane protein CaMGUK
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-
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:protein phosphotransferase (Ca2+/calmodulin-dependent)
Requires calmodulin and Ca2+ for activity. A wide range of proteins can act as acceptor, including vimentin, synapsin, glycogen synthase, myosin light chains and the microtubule-associated tau protein. Not identical with EC 2.7.11.18 (myosin-light-chain kinase) or EC 2.7.11.26 (tau-protein kinase).
CAS REGISTRY NUMBER
COMMENTARY hide
141467-21-2
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93229-57-3
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97350-82-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + histone IIIS
ADP + phosphorylated histone IIIS
show the reaction diagram
-
-
-
?
ATP + syntide-2
ADP + phosphorylated syntide-2
show the reaction diagram
i.e. PLARTLSVAGLPGKK, synthetic peptide substrate
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-
?
ATP + syntide-2 peptide
phosphorlyated syntide-2 peptide
show the reaction diagram
syntide-2 peptide is L-prolyl-L-leucyl-L-alanyl-L-arginyl-L-threonyl-L-leucyl-L-seryl-L-valyl-L-alanylglycyl-L-leucyl-L-prolylglycyl-L-lysyl-L-lysine
-
-
?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
the unphosphorylated CaMK1 is dependent on Ca2+ and calmodulin, while the autophosphorylated enzyme is not
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Calmodulin
the binding site comprises residues 913-932 with a basic amphiphilic alpha-helix structure, maximal binding at 105 nM, three different isoforms of calmodulin, CaM1, CaM3, and CaM13, differentially regulate CaMK1, overview, the unphosphorylated CaMK1 is dependent on Ca2+ and calmodulin, while the autophosphorylated enzyme is not
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0445
histone IIIS
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-
0.0221
syntide-2 peptide
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-
additional information
additional information
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CaMK1
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q84ZT8_TOBAC
1415
0
158879
TrEMBL
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
the enzyme performs Ca2+/calmodulin-dependent autophosphorylation, which renders the enzyme independent on Ca2+ and calmodulin
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L916R
site-directed mutagenesis, mutation in the calmodulin binding site residue abolishes the calmodulin binding
R924E/K925E/K926E/K927E
site-directed mutagenesis, mutations break the basic amphiphilic alpha-helix structure of the calmodulin binding site, the mutant is not capable of calmodulin binding
W919R
site-directed mutagenesis, mutation in the calmodulin binding site residue abolishes the calmodulin binding
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
construction of a cDNA library, CaMK1 DNA and amino acid sequence determination and analysis, genetic organization, expression of wild-type and mutant CaMK1s in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ma, L.; Liang, S.; Jones, R.L.; Lu, Y.T.
Characterization of a novel calcium/calmodulin-dependent protein kinase from tobacco
Plant Physiol.
135
1280-1293
2004
Nicotiana tabacum (Q84ZT8), Nicotiana tabacum
Manually annotated by BRENDA team