Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.7.11.17 - Ca2+/calmodulin-dependent protein kinase and Organism(s) Caenorhabditis elegans and UniProt Accession O62305

for references in articles please use BRENDA:EC2.7.11.17
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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).
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Caenorhabditis elegans
UNIPROT: O62305
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Caenorhabditis elegans
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
hide
ATP
+
a [protein]-(L-serine/L-threonine)
=
ADP
+
a [protein]-(L-serine/L-threonine) phosphate
+
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
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 TYPE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
141467-21-2
-
93229-57-3
-
97350-82-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + autocamtide-2
ADP + phosphorylated autocamtide-2
show the reaction diagram
highly selective peptide substrate for calcium/calmodulin-dependent protein kinase II
-
-
?
ATP + syntide-2
ADP + phosphorylated syntide-2
show the reaction diagram
a peptide containing the R-X-X-S/T consensus phosphorylation site 2 of glycogen synthase within the sequence
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
autoinhibition and activation of the kinase domain of CaMKII. Autoinhibition involves a conformeric equilibrium of the regulatory domain, modulating substrate and nucleotide access. Binding of calmodulin to the regulatory domain induces conformational changes that release the catalytic cleft, activating the kinase and exposing an otherwise inaccessible phosphorylation site, threonine 286. Autophosphorylation at Thr286 further disrupts the interactions between the catalytic and regulatory domains, enhancing the interaction with calmodulin, but maintains the regulatory domain in a dynamic unstructured conformation following dissociation of calmodulin, sustaining activation
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
autoinhibition and activation of the kinase domain of CaMKII. Autoinhibition involves a conformeric equilibrium of the regulatory domain, modulating substrate and nucleotide access. Binding of calmodulin to the regulatory domain induces conformational changes that release the catalytic cleft, activating the kinase and exposing an otherwise inaccessible phosphorylation site, threonine 286. Autophosphorylation at Thr286 further disrupts the interactions between the catalytic and regulatory domains, enhancing the interaction with calmodulin, but maintains the regulatory domain in a dynamic unstructured conformation following dissociation of calmodulin, sustaining activation
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KCC2D_CAEEL
720
0
79927
Swiss-Prot
other Location (Reliability: 3)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
T286E/D135N
phosphomimic mutant, lower melting temperature. Distinct changes in backbone order upon binding of Ca2+/CaM to the T286E/D135N mutant
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hoffman, L.; Stein, R.A.; Colbran, R.J.; Mchaourab, H.S.
Conformational changes underlying calcium/calmodulin-dependent protein kinase II activation
EMBO J.
30
1251-1262
2011
Caenorhabditis elegans (O62305), Mus musculus (P11798)
Manually annotated by BRENDA team