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Information on EC 2.7.11.17 - Ca2+/calmodulin-dependent protein kinase and Organism(s) Gallus gallus
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2.7.11.17 Ca2+/calmodulin-dependent protein kinaseIUBMB 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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Word Map
- 2.7.11.17
- synaptic
- actin
- hippocampal
- myosin
-
camks
- autophosphorylation
- cardiac
-
postsynaptic
-
ca2+-dependent
- nmda
- pkc
-
contractile
- agonist
- synapses
- dendritic
- n-methyl-d-aspartate
- tropomyosin
-
amp-activated
- calponin
-
calmodulin-binding
-
calcium-dependent
- calcineurin
-
excitatory
- myocytes
-
l-type
- desmin
-
signal-regulated
- actomyosin
-
activity-dependent
- sarcoplasmic
- gizzard
-
presynaptic
-
element-binding
-
glutamatergic
-
actin-binding
- phosphopeptide
-
ryanodine
-
cam-binding
- phospholamban
- ca2+-calmodulin
- calmidazolium
-
nonmuscle
-
actin-activated
-
ca2+-calmodulin-dependent
- mlck
- trifluoperazine
- meromyosin
-
myosin-binding
-
ampars
-
actin-myosin
- medicine
The taxonomic range for the selected organisms is: Gallus gallus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CAKI
-
-
-
-
caldesmon
-
-
-
-
Calspermin
-
-
-
-
CAM kinase-GR
-
-
-
-
CMPK
-
-
-
-
kinase, caldesmon (phosphorylating)
-
-
-
-
kinase, microtubule-associated protein 2 (phosphorylating)
-
-
-
-
MAP kinase
-
-
-
-
MAP-2 kinase
-
-
-
-
MAP-2 protein serine kinase
-
-
-
-
microtubule associated protein kinase
-
-
-
-
microtubule-associated protein 2 kinase
-
-
-
-
peripheral plasma membrane protein CaMGUK
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate
the reaction is an intramolecular autophosphorylation which is site-specific: predominantly serine with some threonine and no tyrosine residues are phosphorylated
-
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate
enzyme appears to be identical with caldesmon
-
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate
p42/p44erk mitogen-activated protein kinase appears to be the major caldesmon kinase, but a yet unidentified kinase, rather than mitogen-activated protein kinase, may be involved in regulation of the caldesmon function in vivo
-
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate
not identical but with strong binding affinity for caldesmon
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
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
141467-21-2
-
93229-57-3
-
97350-82-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + cAMP response element binding protein
ADP + phosphorylated cAMP response element binding protein
-
-
-
-
?
ATP + myosin
ADP + phosphomyosin
-
isolated light chain of smooth-muscle myosin, phosphorylated at 80% the rate of caldesmon
-
-
?
ATP + phosphatidylinositol 3-kinase
ADP + phosphorylated phosphatidylinositol 3-kinase
-
-
-
-
?
ATP + caldesmon
ADP + caldesmon phosphate
-
less efficient than synapsin
-
?
ATP + caldesmon
ADP + caldesmon phosphate
-
caldesmon plays a role in the regulation of smooth muscle contraction
-
?
ATP + caldesmon
ADP + caldesmon phosphate
-
caldesmon plays a role in the regulation of smooth muscle contraction
-
-
?
ATP + casein
ADP + phosphocasein
-
phosphorylation at about 60% the rate of caldesmon
-
-
?
ATP + histone
ADP + phosphohistone
-
calf thymus histone II-S, poor substrate
-
-
?
ATP + synapsin
ADP + phosphosynapsin
-
brain synapsin best substrate of chicken gizzard caldesmon kinase
-
-
?
ATP + synapsin
ADP + phosphosynapsin
-
brain synapsin best substrate, phosphorylated at 950% the rate of caldesmon
-
-
?
additional information
?
-
-
no substrates are bovine cardiac C-protein, bovine brain fodrin, rabbit skeletal muscle glycogen synthase, phosphorylase B, troponon (I + T + C), actin, tropomyosin, smooth muscle actin, filamin, vinculin, alpha-actinin, protamine or phosvitin
-
-
?
additional information
?
-
-
caldesmon is not a substrate of smooth-muscle myosin light-chain kinase
-
-
?
additional information
?
-
-
isozyme of calmodulin-dependent multifunctional protein kinase II in smooth-muscle
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + caldesmon
ADP + caldesmon phosphate
-
caldesmon plays a role in the regulation of smooth muscle contraction
-
?
ATP + caldesmon
ADP + caldesmon phosphate
-
caldesmon plays a role in the regulation of smooth muscle contraction
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Calmodulin
-
after autophosphorylation, the enzyme is active in the absence of Ca2+/calmodulin and even in the presence of EGTA
Calmodulin
-
dependent on, 2 mM CaCl2 plus 0.001 mM calmodulin induce 69.2% activation of CaMKIV activity
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Ca2+
-
after autophosphorylation, the enzyme is active in the absence of Ca2+/calmodulin and even in the presence of EGTA
Ca2+
-
dependent on, 2 mM CaCl2 plus 0.001 mM calmodulin induce 69.2% activation of CaMKIV activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phorbol 12,13-dibutyrate
-
induces an about 2fold maximum increase in caldesmon phosphorylation
additional information
-
after autophosphorylation the enzyme is active in the absence of Ca2+/calmodulin and even in the presence of EGTA
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic parameters, association with caldesmon does not alter enzymatic properties
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). KCC2D_CHICK
479
0
54203
Swiss-Prot
other Location (Reliability: 1)
A0A3Q2UFJ3_CHICK
551
0
62116
TrEMBL
other Location (Reliability: 1)
E1BZ86_CHICK
454
1
51550
TrEMBL
Mitochondrion (Reliability: 3)
A0A1D5NZU2_CHICK
523
0
59122
TrEMBL
other Location (Reliability: 1)
F1P1J7_CHICK
477
1
53978
TrEMBL
Mitochondrion (Reliability: 3)
F1P011_CHICK
478
0
54077
TrEMBL
other Location (Reliability: 2)
Q9YHB8_CHICK
478
0
54097
TrEMBL
other Location (Reliability: 2)
A0A1D5NYA6_CHICK
540
0
60195
TrEMBL
other Location (Reliability: 1)
A0A1D5NZG7_CHICK
489
0
55442
TrEMBL
other Location (Reliability: 1)
O93559_CHICK
489
0
55329
TrEMBL
other Location (Reliability: 2)
O93560_CHICK
540
0
60181
TrEMBL
other Location (Reliability: 1)
A0A3Q2UMD3_CHICK
512
0
57870
TrEMBL
other Location (Reliability: 1)
A0A1D5PNB0_CHICK
478
0
54206
TrEMBL
other Location (Reliability: 1)
F1NGS8_CHICK
489
0
55309
TrEMBL
other Location (Reliability: 2)
A0A3Q2U2C3_CHICK
503
0
56974
TrEMBL
other Location (Reliability: 1)
A0A1D5PDX2_CHICK
1043
0
112857
TrEMBL
other Location (Reliability: 1)
A0A1D5PXX2_CHICK
1020
0
110623
TrEMBL
other Location (Reliability: 1)
A0A3Q2UPU8_CHICK
492
0
55724
TrEMBL
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
purified enzyme binds tightly to caldesmon, binding is abolished by high concentrations of Mg2+
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
CaMKII is an essential component of intracellular signaling pathways regulating chondrocyte maturation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Scott-Woo, G.C.; Walsh, M.P.
Autophosphorylation of smooth-muscle caldesmon
Biochem. J.
252
463-472
1988
Bos taurus, Gallus gallus
Ngai, P.K.; Walsh, M.P.
Inhibition of smooth muscle actin-activated myosin Mg2+-ATPase activity by caldesmon
J. Biol. Chem.
259
13656-13659
1984
Gallus gallus
Ngai, P.K.; Walsh, M.P.
Properties of caldesmon isolated from chicken gizzard
Biochem. J.
230
695-707
1985
Gallus gallus
Ikebe, M.; Reardon, S.; Scott-Woo, G.C.; Zhou, Z.; Koda, Y.
Purification and characterization of calmodulin-dependent multifunctional protein kinase from smooth muscle: isolation of caldesmon kinase
Biochemistry
29
11242-11248
1990
Gallus gallus
Krymsky, M.A.; Chibalina, M.V.; Shirinsky, V.P.; Marston, S.B.; Vorotnikov, A.V.
Evidence against the regulation of caldesmon inhibitory activity by p42/p44erk mitogen-activated protein kinase in vitro and demonstration of another caldesmon kinase in intact gizzard smooth muscle
FEBS Lett.
452
254-258
1999
Gallus gallus
Taschner, M.J.; Rafigh, M.; Lampert, F.; Schnaiter, S.; Hartmann, C.
Ca2+/calmodulin-dependent kinase II signaling causes skeletal overgrowth and premature chondrocyte maturation
Dev. Biol.
317
132-146
2008
Gallus gallus
EXTERNAL LINKS (specific for EC-Number 2.7.11.17)
Transporter Classification Database (TCDB): 8.A.104.1.12, 8.A.24.1.11
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