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Calcium/calmodulin-dependent protein kinase type II (CaM kinase II) (EC 2.7.11.17) (Uncoordinated protein 43)

 KCC2D_CAEEL             Reviewed;         720 AA.
O62305; A5JYT0; A7LPH2; B3GWC8; O62304; Q21431; Q7JLT8; Q9NG91;
Q9NH55; Q9NH56; Q9NH57; Q9NH58; Q9NH59; Q9NH60; Q9U6Q0;
10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
01-OCT-2001, sequence version 2.
05-JUL-2017, entry version 150.
RecName: Full=Calcium/calmodulin-dependent protein kinase type II {ECO:0000303|PubMed:10647014};
Short=CaM kinase II {ECO:0000303|PubMed:10647014};
EC=2.7.11.17;
AltName: Full=Uncoordinated protein 43;
Name=unc-43; ORFNames=K11E8.1;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1] {ECO:0000305, ECO:0000312|EMBL:AAD53949.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D), TISSUE SPECIFICITY, DISRUPTION
PHENOTYPE, AND MUTAGENESIS OF GLU-108.
PubMed=10647014; DOI=10.1038/46072;
Reiner D.J., Newton E.M., Tian H., Thomas J.H.;
"Diverse behavioural defects caused by mutations in Caenorhabditis
elegans unc-43 CaM kinase II.";
Nature 402:199-203(1999).
[2] {ECO:0000305, ECO:0000312|EMBL:AAF63321.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS E; F; G; H; I; K AND L).
Guarin E., Hernandez M.C., Gomez M., Schulman H., Nef P.;
"Biochemical properties of calcium/calmodulin-pependent protein kinase
II (UNC-43) Isoforms in Caernohabditis elegans.";
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000305, ECO:0000312|EMBL:CAO82047.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
SPLICING.
STRAIN=Bristol N2 {ECO:0000312|EMBL:CAO82047.1};
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[4]
FUNCTION.
PubMed=10571181; DOI=10.1016/S0092-8674(00)81525-1;
Troemel E.R., Sagasti A., Bargmann C.I.;
"Lateral signaling mediated by axon contact and calcium entry
regulates asymmetric odorant receptor expression in C. elegans.";
Cell 99:387-398(1999).
[5]
INTERACTION WITH NSY-1.
PubMed=11336672; DOI=10.1016/S0092-8674(01)00313-0;
Sagasti A., Hisamoto N., Hyodo J., Tanaka-Hino M., Matsumoto K.,
Bargmann C.I.;
"The CaMKII UNC-43 activates the MAPKKK NSY-1 to execute a lateral
signaling decision required for asymmetric olfactory neuron fates.";
Cell 105:221-232(2001).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12221132; DOI=10.1091/mbc.E02-01-0005;
Bandyopadhyay J., Lee J., Lee J., Lee J.I., Yu J.-R., Jee C.,
Cho J.-H., Jung S., Lee M.H., Zannoni S., Singson A., Kim D.,
Koo H.-S., Ahnn J.;
"Calcineurin, a calcium/calmodulin-dependent protein phosphatase, is
involved in movement, fertility, egg laying, and growth in
Caenorhabditis elegans.";
Mol. Biol. Cell 13:3281-3293(2002).
[7]
FUNCTION.
PubMed=15166144; DOI=10.1534/genetics.167.1.161;
Solomon A., Bandhakavi S., Jabbar S., Shah R., Beitel G.J.,
Morimoto R.I.;
"Caenorhabditis elegans OSR-1 regulates behavioral and physiological
responses to hyperosmotic environments.";
Genetics 167:161-170(2004).
[8]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=16267094; DOI=10.1242/dev.02083;
Corrigan C., Subramanian R., Miller M.A.;
"Eph and NMDA receptors control Ca2+/calmodulin-dependent protein
kinase II activation during C. elegans oocyte meiotic maturation.";
Development 132:5225-5237(2005).
[9]
INTERACTION WITH TIR-1, AND SUBCELLULAR LOCATION.
PubMed=15625192; DOI=10.1101/gad.1276505;
Chuang C.-F., Bargmann C.I.;
"A Toll-interleukin 1 repeat protein at the synapse specifies
asymmetric odorant receptor expression via ASK1 MAPKKK signaling.";
Genes Dev. 19:270-281(2005).
[10]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
PHE-97; GLU-108; LYS-147; ASP-236; HIS-280; ARG-281 AND THR-284.
PubMed=16079277; DOI=10.1242/jcs.02457;
Umemura T., Rapp P., Rongo C.;
"The role of regulatory domain interactions in UNC-43 CaMKII
localization and trafficking.";
J. Cell Sci. 118:3327-3338(2005).
[11]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17898212; DOI=10.1523/JNEUROSCI.5634-06.2007;
Liu Q., Chen B., Ge Q., Wang Z.W.;
"Presynaptic Ca2+/calmodulin-dependent protein kinase II modulates
neurotransmitter release by activating BK channels at Caenorhabditis
elegans neuromuscular junction.";
J. Neurosci. 27:10404-10413(2007).
[12]
FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-170; SER-179
AND ALA-665.
PubMed=17941711; DOI=10.1371/journal.pgen.0030156;
LeBoeuf B., Gruninger T.R., Garcia L.R.;
"Food deprivation attenuates seizures through CaMKII and EAG K+
channels.";
PLoS Genet. 3:1622-1632(2007).
[13]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17942636; DOI=10.1152/ajpcell.00303.2007;
Nehrke K., Denton J., Mowrey W.;
"Intestinal Ca2+ wave dynamics in freely moving C. elegans coordinate
execution of a rhythmic motor program.";
Am. J. Physiol. 294:C333-344(2008).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=21771813; DOI=10.1242/dev.069740;
Chang C., Hsieh Y.W., Lesch B.J., Bargmann C.I., Chuang C.F.;
"Microtubule-based localization of a synaptic calcium-signaling
complex is required for left-right neuronal asymmetry in C. elegans.";
Development 138:3509-3518(2011).
[15]
FUNCTION, AND INTERACTION WITH EGL-2.
PubMed=21145946; DOI=10.1016/j.neuroscience.2010.12.002;
LeBoeuf B., Guo X., Garcia L.R.;
"The effects of transient starvation persist through direct
interactions between CaMKII and ether-a-go-go K+ channels in C.
elegans males.";
Neuroscience 175:1-17(2011).
[16]
FUNCTION.
PubMed=22629462; DOI=10.1371/journal.pone.0037831;
Wani K.A., Catanese M., Normantowicz R., Herd M., Maher K.N.,
Chase D.L.;
"D1 dopamine receptor signaling is modulated by the R7 RGS protein
EAT-16 and the R7 binding protein RSBP-1 in Caenoerhabditis elegans
motor neurons.";
PLoS ONE 7:E37831-E37831(2012).
[17]
FUNCTION, AND MUTAGENESIS OF GLU-108.
PubMed=23805378; DOI=10.7554/eLife.00518;
Tao L., Xie Q., Ding Y.H., Li S.T., Peng S., Zhang Y.P., Tan D.,
Yuan Z., Dong M.Q.;
"CAMKII and Calcineurin regulate the lifespan of Caenorhabditis
elegans through the FOXO transcription factor DAF-16.";
Elife 2:E00518-E00518(2013).
[18]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=23325232; DOI=10.1523/JNEUROSCI.2355-12.2013;
Qin Y., Zhang X., Zhang Y.;
"A neuronal signaling pathway of CaMKII and Gqalpha regulates
experience-dependent transcription of tph-1.";
J. Neurosci. 33:925-935(2013).
[19]
FUNCTION.
PubMed=23663262; DOI=10.1186/1749-8104-8-10;
Caylor R.C., Jin Y., Ackley B.D.;
"The Caenorhabditis elegans voltage-gated calcium channel subunits
UNC-2 and UNC-36 and the calcium-dependent kinase UNC-43/CaMKII
regulate neuromuscular junction morphology.";
Neural Dev. 8:10-10(2013).
[20]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-343 OF ISOFORM I, ENZYME
REGULATION, PHOSPHORYLATION AT THR-284, AND MUTAGENESIS OF ASP-134.
PubMed=16325579; DOI=10.1016/j.cell.2005.10.029;
Rosenberg O.S., Deindl S., Sung R.J., Nairn A.C., Kuriyan J.;
"Structure of the autoinhibited kinase domain of CaMKII and SAXS
analysis of the holoenzyme.";
Cell 123:849-860(2005).
[21]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 340-482 OF ISOFORM D, AND
SUBUNIT.
PubMed=16441656; DOI=10.1111/j.1742-4658.2005.05088.x;
Rosenberg O.S., Deindl S., Comolli L.R., Hoelz A., Downing K.H.,
Nairn A.C., Kuriyan J.;
"Oligomerization states of the association domain and the holoenyzme
of Ca2+/CaM kinase II.";
FEBS J. 273:682-694(2006).
[22]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 5-288 OF ISOFORM E,
INTERACTION WITH CALMODULIN, ENZYME REGULATION, SUBUNIT, AND
MUTAGENESIS OF LYS-41; PHE-97; ILE-100; ASP-134; ILE-200 AND
278-ALA-ILE-279.
PubMed=20139983; DOI=10.1038/nsmb.1751;
Chao L.H., Pellicena P., Deindl S., Barclay L.A., Schulman H.,
Kuriyan J.;
"Intersubunit capture of regulatory segments is a component of
cooperative CaMKII activation.";
Nat. Struct. Mol. Biol. 17:264-272(2010).
-!- FUNCTION: Acts in the signaling of a variety of pathways and
processes. Phosphorylates 'Ser-319' of daf-16 in response to
stress signals, such as heat, starvation and oxidation, which
plays a role in prolonging lifespan. Required for viability under
chronic osmotic stress in which it acts downstream of osr-1. Has
roles in locomotion, oocyte maturation, brood size, egg laying,
defecation, meiotic maturation and neuronal cell fate
specification. Required for the regulation of synaptic density and
neuromuscular junction morphology. Regulates the synaptic
trafficking of glr-1. Bidirectional modulator of neurotransmitter
release with negative modulatory effects mainly mediated via slo-1
activation. Involved in activation of ADF neurons and increased
tph-1 transcription following exposure to pathogenic bacteria
which leads to learned olfactory aversion to the bacteria.
Implicated in the muscle regulation of spicule protraction. In
conjunction with egl-2 has a role in the suppression of mating
behavior under food deprivation to encourage foraging. Involved in
restricting str-2 expression to only one of the two AWC neurons.
May suppress the functional response to an internal pacemaker,
perhaps by modulating the activity of the IP3 receptor.
{ECO:0000269|PubMed:10571181, ECO:0000269|PubMed:12221132,
ECO:0000269|PubMed:15166144, ECO:0000269|PubMed:16079277,
ECO:0000269|PubMed:16267094, ECO:0000269|PubMed:17898212,
ECO:0000269|PubMed:17941711, ECO:0000269|PubMed:17942636,
ECO:0000269|PubMed:21145946, ECO:0000269|PubMed:21771813,
ECO:0000269|PubMed:22629462, ECO:0000269|PubMed:23325232,
ECO:0000269|PubMed:23663262, ECO:0000269|PubMed:23805378}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:16079277}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:16079277};
-!- ENZYME REGULATION: Ca2(+)/calmodulin binding removes an
autoinhibitory regulatory segment located C-terminal to the kinase
domain. This releases the catalytic activity of the enzyme and
makes accessible a regulatory residue Thr-284. Phosphorylation of
Thr-284 by another kinase domain within the oligomeric holoenzyme
keeps CaMKII active in the absence of Ca(2+)/calmodulin by
preventing the rebinding of the regulatory segment to the kinase
domain and by increasing the affinity of calmodulin for the
enzyme. Can respond to high-frequency Ca(2+) pulses to become
Ca(2+) independent. {ECO:0000269|PubMed:16325579,
ECO:0000269|PubMed:20139983}.
-!- SUBUNIT: Dodecamer. Subunits are tightly packed around a central
ring-shaped scaffold with extensive contacts between the
regulatory segment of one kinase and the catalytic domain of
another enabling cooperative activation of a subunit by the
adjacent molecule (PubMed:16441656, PubMed:20139983). Interacts
with and phosphorylates daf-16; the interaction promotes daf-16
nuclear localization. Interacts with egl-2 and tir-1
(PubMed:15625192, PubMed:21145946). Interacts with nsy-1
(PubMed:11336672). {ECO:0000269|PubMed:11336672,
ECO:0000269|PubMed:15625192, ECO:0000269|PubMed:16441656,
ECO:0000269|PubMed:20139983, ECO:0000269|PubMed:21145946}.
-!- INTERACTION:
P91409:syx-4; NbExp=3; IntAct=EBI-313095, EBI-326499;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16079277}.
Cell projection, axon {ECO:0000269|PubMed:15625192}. Perikaryon
{ECO:0000269|PubMed:15625192, ECO:0000269|PubMed:16079277}.
Note=Localizes at or near the Golgi apparatus (PubMed:16079277).
Localizes to post-synaptic regions and is enriched in punctate
structures in axons of AWC neurons where it co-localizes with tir-
1. Localization is regulated by tir-1 (PubMed:15625192).
{ECO:0000269|PubMed:15625192, ECO:0000269|PubMed:16079277}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=15;
Name=c {ECO:0000269|PubMed:9851916};
IsoId=O62305-1; Sequence=Displayed;
Note=No experimental confirmation available. {ECO:0000305};
Name=a {ECO:0000269|PubMed:9851916};
IsoId=O62305-2; Sequence=VSP_039592, VSP_039608;
Note=No experimental confirmation available. {ECO:0000305};
Name=b {ECO:0000269|PubMed:9851916};
IsoId=O62305-3; Sequence=VSP_039595, VSP_039596;
Note=No experimental confirmation available. {ECO:0000305};
Name=d {ECO:0000269|PubMed:10647014, ECO:0000269|PubMed:9851916};
IsoId=O62305-4; Sequence=VSP_039597, VSP_039603, VSP_039611;
Name=e {ECO:0000269|PubMed:9851916, ECO:0000269|Ref.2}; Synonyms=C
{ECO:0000269|Ref.2};
IsoId=O62305-5; Sequence=VSP_039604, VSP_039605, VSP_039611;
Name=f {ECO:0000269|PubMed:9851916, ECO:0000269|Ref.2}; Synonyms=E
{ECO:0000269|Ref.2};
IsoId=O62305-6; Sequence=VSP_039598, VSP_039602;
Name=g {ECO:0000269|PubMed:9851916, ECO:0000269|Ref.2}; Synonyms=B
{ECO:0000269|Ref.2};
IsoId=O62305-7; Sequence=VSP_039597, VSP_039603;
Name=h {ECO:0000269|PubMed:9851916, ECO:0000269|Ref.2}; Synonyms=D
{ECO:0000269|Ref.2};
IsoId=O62305-8; Sequence=VSP_039604, VSP_039605;
Name=i {ECO:0000269|PubMed:9851916, ECO:0000269|Ref.2}; Synonyms=H
{ECO:0000269|Ref.2};
IsoId=O62305-9; Sequence=VSP_039597, VSP_039603, VSP_039612,
VSP_039613;
Name=k {ECO:0000269|PubMed:9851916, ECO:0000269|Ref.2}; Synonyms=F
{ECO:0000269|Ref.2};
IsoId=O62305-10; Sequence=VSP_039599, VSP_039601;
Name=l {ECO:0000269|PubMed:9851916, ECO:0000269|Ref.2}; Synonyms=G
{ECO:0000269|Ref.2};
IsoId=O62305-11; Sequence=VSP_039600, VSP_039601;
Name=m {ECO:0000269|PubMed:9851916};
IsoId=O62305-12; Sequence=VSP_039594, VSP_039606;
Note=No experimental confirmation available. {ECO:0000305};
Name=n {ECO:0000269|PubMed:9851916};
IsoId=O62305-13; Sequence=VSP_039590, VSP_039610;
Note=No experimental confirmation available. {ECO:0000305};
Name=o {ECO:0000269|PubMed:9851916};
IsoId=O62305-14; Sequence=VSP_039593, VSP_039607, VSP_039611;
Note=No experimental confirmation available. {ECO:0000305};
Name=p {ECO:0000269|PubMed:9851916};
IsoId=O62305-15; Sequence=VSP_039591, VSP_039609;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed in the nervous system. Observed in
the ADF and AWC neurons. Position in AWC neurons is regulated by
microtubules. Localized to clusters in ventral cord neurites which
appear to be required for glr-1 trafficking. Also present in
oocytes. {ECO:0000269|PubMed:10647014,
ECO:0000269|PubMed:16079277, ECO:0000269|PubMed:16267094,
ECO:0000269|PubMed:23325232}.
-!- DISRUPTION PHENOTYPE: Increased frequency of defecation, typified
by a weaker repetition of the defecation motor program, an echo,
10 s after the primary motor program. Abnormal spicule
protraction. Lack of tph-1 transcriptional up-regulation during
learned olfactory aversion to bacteria. Reduced brood size, body
length and width. Lethargic movement. A gain-of function mutation
reduces locomotory activity, alters excitation of three muscle
types and lengthens the period of the motor output of a behavioral
clock. Both classes of mutation inhibit neurotransmitter release.
{ECO:0000269|PubMed:10647014, ECO:0000269|PubMed:12221132,
ECO:0000269|PubMed:17898212, ECO:0000269|PubMed:17941711,
ECO:0000269|PubMed:17942636, ECO:0000269|PubMed:23325232}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. CaMK subfamily. {ECO:0000255}.
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EMBL; AF180735; AAD53949.1; -; mRNA.
EMBL; AF233262; AAF63320.1; -; mRNA.
EMBL; AF233263; AAF63321.1; -; mRNA.
EMBL; AF233264; AAF63322.1; -; mRNA.
EMBL; AF233265; AAF63323.1; -; mRNA.
EMBL; AF233266; AAF63324.1; -; mRNA.
EMBL; AF233267; AAF63325.1; -; mRNA.
EMBL; AF255956; AAF71543.1; -; mRNA.
EMBL; Z70279; CAA94242.3; -; Genomic_DNA.
EMBL; Z70279; CAA94243.3; -; Genomic_DNA.
EMBL; AL023841; CAA94243.3; JOINED; Genomic_DNA.
EMBL; Z70279; CAC42322.1; -; Genomic_DNA.
EMBL; AL023841; CAC42322.1; JOINED; Genomic_DNA.
EMBL; Z70279; CAC42323.1; -; Genomic_DNA.
EMBL; AL023841; CAC42323.1; JOINED; Genomic_DNA.
EMBL; Z70279; CAC42324.1; -; Genomic_DNA.
EMBL; AL023841; CAC42324.1; JOINED; Genomic_DNA.
EMBL; Z70279; CAC42325.1; -; Genomic_DNA.
EMBL; AL023841; CAC42325.1; JOINED; Genomic_DNA.
EMBL; Z70279; CAC42326.1; -; Genomic_DNA.
EMBL; AL023841; CAC42326.1; JOINED; Genomic_DNA.
EMBL; Z70279; CAC42327.1; -; Genomic_DNA.
EMBL; AL023841; CAC42327.1; JOINED; Genomic_DNA.
EMBL; Z70279; CAC42328.1; -; Genomic_DNA.
EMBL; AL023841; CAC42328.1; JOINED; Genomic_DNA.
EMBL; Z70279; CAC42329.1; -; Genomic_DNA.
EMBL; AL023841; CAC42329.1; JOINED; Genomic_DNA.
EMBL; Z70279; CAE46679.1; -; Genomic_DNA.
EMBL; Z70279; CAN86910.1; -; Genomic_DNA.
EMBL; Z70279; CAO82047.1; -; Genomic_DNA.
EMBL; Z70279; CAQ58116.1; -; Genomic_DNA.
PIR; B88809; B88809.
PIR; T23616; T23616.
RefSeq; NP_001023293.2; NM_001028122.4. [O62305-2]
RefSeq; NP_001023294.1; NM_001028123.3. [O62305-3]
RefSeq; NP_001023296.1; NM_001028125.3. [O62305-4]
RefSeq; NP_001023297.1; NM_001028126.3. [O62305-5]
RefSeq; NP_001023298.1; NM_001028127.3. [O62305-6]
RefSeq; NP_001023299.1; NM_001028128.3. [O62305-7]
RefSeq; NP_001023300.1; NM_001028129.3. [O62305-8]
RefSeq; NP_001023301.1; NM_001028130.3. [O62305-9]
RefSeq; NP_001023302.1; NM_001028131.3. [O62305-10]
RefSeq; NP_001023303.1; NM_001028132.3. [O62305-11]
RefSeq; NP_001023304.1; NM_001028133.4. [O62305-12]
RefSeq; NP_001122788.1; NM_001129316.2. [O62305-13]
RefSeq; NP_001122789.1; NM_001129317.2. [O62305-14]
RefSeq; NP_001129863.1; NM_001136391.2. [O62305-15]
UniGene; Cel.22903; -.
PDB; 2BDW; X-ray; 1.80 A; A/B=1-543.
PDB; 2F86; X-ray; 2.64 A; B/D/F/H/J/L/N=540-720.
PDB; 3KK8; X-ray; 1.72 A; A=5-288.
PDB; 3KK9; X-ray; 3.21 A; A=6-287.
PDB; 3KL8; X-ray; 3.37 A; A/C/E/G/I=5-273.
PDBsum; 2BDW; -.
PDBsum; 2F86; -.
PDBsum; 3KK8; -.
PDBsum; 3KK9; -.
PDBsum; 3KL8; -.
ProteinModelPortal; O62305; -.
SMR; O62305; -.
BioGrid; 43023; 8.
DIP; DIP-25971N; -.
DIP; DIP-58986N; -.
IntAct; O62305; 8.
MINT; MINT-115321; -.
iPTMnet; O62305; -.
EPD; O62305; -.
PeptideAtlas; O62305; -.
PRIDE; O62305; -.
GeneID; 177921; -.
UCSC; K11E8.1a.1; c. elegans.
CTD; 177921; -.
WormBase; K11E8.1a; CE42693; WBGene00006779; unc-43. [O62305-2]
WormBase; K11E8.1b; CE28052; WBGene00006779; unc-43. [O62305-3]
WormBase; K11E8.1d; CE28054; WBGene00006779; unc-43. [O62305-4]
WormBase; K11E8.1e; CE28055; WBGene00006779; unc-43. [O62305-5]
WormBase; K11E8.1f; CE28056; WBGene00006779; unc-43. [O62305-6]
WormBase; K11E8.1g; CE28057; WBGene00006779; unc-43. [O62305-7]
WormBase; K11E8.1h; CE28058; WBGene00006779; unc-43. [O62305-8]
WormBase; K11E8.1i; CE28059; WBGene00006779; unc-43. [O62305-9]
WormBase; K11E8.1k; CE28060; WBGene00006779; unc-43. [O62305-10]
WormBase; K11E8.1l; CE28061; WBGene00006779; unc-43. [O62305-11]
WormBase; K11E8.1m; CE35590; WBGene00006779; unc-43. [O62305-12]
WormBase; K11E8.1n; CE40979; WBGene00006779; unc-43. [O62305-13]
WormBase; K11E8.1o; CE41430; WBGene00006779; unc-43. [O62305-14]
WormBase; K11E8.1p; CE42670; WBGene00006779; unc-43. [O62305-15]
InParanoid; O62305; -.
PhylomeDB; O62305; -.
BRENDA; 2.7.11.17; 1045.
SignaLink; O62305; -.
EvolutionaryTrace; O62305; -.
PRO; PR:O62305; -.
Proteomes; UP000001940; Chromosome IV.
GO; GO:1904115; C:axon cytoplasm; IDA:WormBase.
GO; GO:0043005; C:neuron projection; IDA:WormBase.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IDA:WormBase.
GO; GO:0044325; F:ion channel binding; IPI:WormBase.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0000165; P:MAPK cascade; IMP:WormBase.
GO; GO:0072375; P:medium-term memory; IMP:WormBase.
GO; GO:0007399; P:nervous system development; IBA:GO_Central.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:WormBase.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:WormBase.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:WormBase.
InterPro; IPR020636; Ca/CaM-dep_Ca-dep_prot_Kinase.
InterPro; IPR013543; Ca/CaM-dep_prot_kinase-assoc.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR032710; NTF2-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR24347; PTHR24347; 1.
Pfam; PF08332; CaMKII_AD; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF54427; SSF54427; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Calmodulin-binding;
Cell projection; Complete proteome; Cytoplasm; Kinase; Magnesium;
Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Stress response; Transferase.
CHAIN 1 720 Calcium/calmodulin-dependent protein
kinase type II.
/FTId=PRO_0000396645.
DOMAIN 12 269 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 18 26 ATP. {ECO:0000250|UniProtKB:P28523,
ECO:0000255|PROSITE-ProRule:PRU00159}.
ACT_SITE 134 134 Proton acceptor. {ECO:0000305}.
BINDING 41 41 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:20139983}.
MOD_RES 284 284 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:16325579}.
VAR_SEQ 1 505 Missing (in isoform n).
{ECO:0000303|PubMed:9851916}.
/FTId=VSP_039590.
VAR_SEQ 1 504 Missing (in isoform p).
{ECO:0000303|PubMed:9851916}.
/FTId=VSP_039591.
VAR_SEQ 1 490 Missing (in isoform a).
{ECO:0000303|PubMed:9851916}.
/FTId=VSP_039592.
VAR_SEQ 1 416 Missing (in isoform o).
{ECO:0000303|PubMed:9851916}.
/FTId=VSP_039593.
VAR_SEQ 1 414 Missing (in isoform m).
{ECO:0000303|PubMed:9851916}.
/FTId=VSP_039594.
VAR_SEQ 113 138 HCIQQILESIAYCHSNGIVHRDLKPE -> CCIMQILDGVN
YCHQRGIVHRDMKV (in isoform b).
{ECO:0000303|PubMed:9851916}.
/FTId=VSP_039595.
VAR_SEQ 139 720 Missing (in isoform b).
{ECO:0000303|PubMed:9851916}.
/FTId=VSP_039596.
VAR_SEQ 299 314 AAISAVKMVTRMSGVL -> GAILTTMIATRNLSNL (in
isoform d, isoform g and isoform i).
{ECO:0000303|PubMed:10647014,
ECO:0000303|PubMed:9851916,
ECO:0000303|Ref.2}.
/FTId=VSP_039597.
VAR_SEQ 299 313 AAISAVKMVTRMSGV -> GAILTTMIATRNLSS (in
isoform f). {ECO:0000303|PubMed:9851916,
ECO:0000303|Ref.2}.
/FTId=VSP_039598.
VAR_SEQ 299 302 AAIS -> VVDS (in isoform k).
{ECO:0000303|PubMed:9851916,
ECO:0000303|Ref.2}.
/FTId=VSP_039599.
VAR_SEQ 299 302 AAIS -> VAIC (in isoform l).
{ECO:0000303|PubMed:9851916,
ECO:0000303|Ref.2}.
/FTId=VSP_039600.
VAR_SEQ 303 720 Missing (in isoform k and isoform l).
{ECO:0000303|PubMed:9851916,
ECO:0000303|Ref.2}.
/FTId=VSP_039601.
VAR_SEQ 314 515 Missing (in isoform f).
{ECO:0000303|PubMed:9851916,
ECO:0000303|Ref.2}.
/FTId=VSP_039602.
VAR_SEQ 315 514 Missing (in isoform d, isoform g and
isoform i). {ECO:0000303|PubMed:10647014,
ECO:0000303|PubMed:9851916,
ECO:0000303|Ref.2}.
/FTId=VSP_039603.
VAR_SEQ 350 364 VYPNVLLFNPQKFPR -> GAILTTMIATRNLSN (in
isoform e and isoform h).
{ECO:0000303|PubMed:10647014,
ECO:0000303|PubMed:9851916,
ECO:0000303|Ref.2}.
/FTId=VSP_039604.
VAR_SEQ 365 513 Missing (in isoform e and isoform h).
{ECO:0000303|PubMed:10647014,
ECO:0000303|PubMed:9851916,
ECO:0000303|Ref.2}.
/FTId=VSP_039605.
VAR_SEQ 415 512 PYHCFTNKMSNYERAAPSSHGSSTTKKIANAIADLVIRRSS
PSIRRKTEADVHNSNRNRKVSAPANLQHALVPVIDVVVATG
ALASSSVDNLSASTSS -> MDGLLARLKLGSKRKKKTSSS
VKRSSRPESARQAPRDTTGSLYSNLTASSSTVSACSAPEIV
VLKKEQVVLAVDHKDQVDEQKKKNEQVVKKPEKLEVEAD
(in isoform m).
{ECO:0000303|PubMed:9851916}.
/FTId=VSP_039606.
VAR_SEQ 417 514 HCFTNKMSNYERAAPSSHGSSTTKKIANAIADLVIRRSSPS
IRRKTEADVHNSNRNRKVSAPANLQHALVPVIDVVVATGAL
ASSSVDNLSASTSSDL -> MDGLLARLKLGSKRKKKTSSS
VKRSSRPESARQAPRDTTGSLYSNLTASSSTVSACSAPEIV
VLKKEQVVLAVDHKDQVDEQKKKNEQVVKKPEKLEVEAD
(in isoform o).
{ECO:0000303|PubMed:9851916}.
/FTId=VSP_039607.
VAR_SEQ 491 515 VVVATGALASSSVDNLSASTSSDLG -> MKNIEYWQVLLN
KIFATYKIKMKQC (in isoform a).
{ECO:0000303|PubMed:9851916}.
/FTId=VSP_039608.
VAR_SEQ 505 513 NLSASTSSD -> MIATRNLSN (in isoform p).
{ECO:0000303|PubMed:9851916}.
/FTId=VSP_039609.
VAR_SEQ 506 515 LSASTSSDLG -> MNFLRFSGKC (in isoform n).
{ECO:0000303|PubMed:9851916}.
/FTId=VSP_039610.
VAR_SEQ 548 585 Missing (in isoform d, isoform e and
isoform o). {ECO:0000303|PubMed:10647014,
ECO:0000303|PubMed:9851916,
ECO:0000303|Ref.2}.
/FTId=VSP_039611.
VAR_SEQ 549 550 GG -> NE (in isoform i).
{ECO:0000303|PubMed:9851916,
ECO:0000303|Ref.2}.
/FTId=VSP_039612.
VAR_SEQ 551 720 Missing (in isoform i).
{ECO:0000303|PubMed:9851916,
ECO:0000303|Ref.2}.
/FTId=VSP_039613.
MUTAGEN 41 41 K->M: Loss of kinase activity.
{ECO:0000269|PubMed:20139983}.
MUTAGEN 97 97 F->E: Loss of cooperative activation of
adjacent holoenzyme subunits.
{ECO:0000269|PubMed:16079277,
ECO:0000269|PubMed:20139983}.
MUTAGEN 97 97 F->K: Increase in calcium independent
kinase activity, no effect on
translocation to the neurite.
{ECO:0000269|PubMed:16079277,
ECO:0000269|PubMed:20139983}.
MUTAGEN 100 100 I->K: Loss of cooperative activation of
adjacent holoenzyme subunits.
{ECO:0000269|PubMed:20139983}.
MUTAGEN 108 108 E->K: In n498gf; slight increase in
calcium independent kinase activity, no
effect on translocation to the neurite.
Nuclear translocation of daf-16 resulting
in lifespan extension.
{ECO:0000269|PubMed:10647014,
ECO:0000269|PubMed:16079277,
ECO:0000269|PubMed:23805378}.
MUTAGEN 134 134 D->N: Loss of autoinhibition and increase
in binding of Ca2+/calmodulin.
{ECO:0000269|PubMed:16325579,
ECO:0000269|PubMed:20139983}.
MUTAGEN 147 147 K->E: Slight increase in calcium
independent kinase activity, no effect on
translocation to the neurite.
{ECO:0000269|PubMed:16079277}.
MUTAGEN 170 170 G->E: In sy574; abnormal spicule
protraction; when associated with V-665.
{ECO:0000269|PubMed:17941711}.
MUTAGEN 179 179 S->L: In e408; males display locomotor
and muscle seizure defects and egg laying
defects. {ECO:0000269|PubMed:17941711}.
MUTAGEN 200 200 I->K: Loss of cooperative activation of
adjacent holoenzyme subunits.
{ECO:0000269|PubMed:20139983}.
MUTAGEN 236 236 D->R: Increase in calcium independent
kinase activity, loss of translocation to
neurites and glr-1 trafficking.
{ECO:0000269|PubMed:16079277}.
MUTAGEN 278 279 AI->DD: Decrease in binding of
Ca2+/calmodulin.
{ECO:0000269|PubMed:20139983}.
MUTAGEN 280 280 H->K: Increase in calcium independent
kinase activity, no effect on
translocation to the neurite.
{ECO:0000269|PubMed:16079277}.
MUTAGEN 281 281 R->E: Increase in calcium independent
kinase activity and translocation to an
unlocalized pool in the neurite. Small
decrease in glr-1 trafficking.
{ECO:0000269|PubMed:16079277}.
MUTAGEN 284 284 T->D: Constitutively activate kinase
activity, increase in translocation to
the neurites.
{ECO:0000269|PubMed:16079277}.
MUTAGEN 665 665 A->V: In sy574; abnormal spicule
protraction; when associated with E-170.
{ECO:0000269|PubMed:17941711}.
TURN 7 11 {ECO:0000244|PDB:3KK8}.
STRAND 12 21 {ECO:0000244|PDB:3KK8}.
STRAND 24 31 {ECO:0000244|PDB:3KK8}.
TURN 32 34 {ECO:0000244|PDB:3KK8}.
STRAND 37 44 {ECO:0000244|PDB:3KK8}.
HELIX 45 47 {ECO:0000244|PDB:3KK8}.
HELIX 50 65 {ECO:0000244|PDB:3KK8}.
STRAND 74 79 {ECO:0000244|PDB:3KK8}.
STRAND 81 88 {ECO:0000244|PDB:3KK8}.
HELIX 96 103 {ECO:0000244|PDB:3KK8}.
HELIX 108 127 {ECO:0000244|PDB:3KK8}.
HELIX 137 139 {ECO:0000244|PDB:3KK8}.
STRAND 140 146 {ECO:0000244|PDB:3KK8}.
STRAND 151 153 {ECO:0000244|PDB:3KK8}.
HELIX 175 177 {ECO:0000244|PDB:3KK8}.
HELIX 180 183 {ECO:0000244|PDB:3KK8}.
HELIX 191 206 {ECO:0000244|PDB:3KK8}.
HELIX 216 225 {ECO:0000244|PDB:3KK8}.
TURN 232 237 {ECO:0000244|PDB:3KK8}.
HELIX 240 249 {ECO:0000244|PDB:3KK8}.
TURN 254 256 {ECO:0000244|PDB:3KK8}.
HELIX 260 263 {ECO:0000244|PDB:3KK8}.
HELIX 267 270 {ECO:0000244|PDB:3KK8}.
HELIX 275 277 {ECO:0000244|PDB:3KK8}.
HELIX 282 309 {ECO:0000244|PDB:2BDW}.
HELIX 585 604 {ECO:0000244|PDB:2F86}.
HELIX 607 613 {ECO:0000244|PDB:2F86}.
STRAND 614 621 {ECO:0000244|PDB:2F86}.
HELIX 623 625 {ECO:0000244|PDB:2F86}.
HELIX 634 637 {ECO:0000244|PDB:2F86}.
STRAND 640 642 {ECO:0000244|PDB:2F86}.
STRAND 649 660 {ECO:0000244|PDB:2F86}.
TURN 661 663 {ECO:0000244|PDB:2F86}.
STRAND 664 676 {ECO:0000244|PDB:2F86}.
STRAND 682 696 {ECO:0000244|PDB:2F86}.
STRAND 699 708 {ECO:0000244|PDB:2F86}.
SEQUENCE 720 AA; 79927 MW; 3231366FFF81A695 CRC64;
MMNASTKFSD NYDVKEELGK GAFSVVRRCV HKTTGLEFAA KIINTKKLSA RDFQKLEREA
RICRKLQHPN IVRLHDSIQE ESFHYLVFDL VTGGELFEDI VAREFYSEAD ASHCIQQILE
SIAYCHSNGI VHRDLKPENL LLASKAKGAA VKLADFGLAI EVNDSEAWHG FAGTPGYLSP
EVLKKDPYSK PVDIWACGVI LYILLVGYPP FWDEDQHRLY AQIKAGAYDY PSPEWDTVTP
EAKSLIDSML TVNPKKRITA DQALKVPWIC NRERVASAIH RQDTVDCLKK FNARRKLKAA
ISAVKMVTRM SGVLRTSDST GSVASNGSTT HDASQVAGTS SQPTSPAAEV YPNVLLFNPQ
KFPRNCVHPF TTHPYYSPKE SSKKKLFFTL LFEVCPHTSR SHILLRDNTK NIYHPYHCFT
NKMSNYERAA PSSHGSSTTK KIANAIADLV IRRSSPSIRR KTEADVHNSN RNRKVSAPAN
LQHALVPVID VVVATGALAS SSVDNLSAST SSDLGRNLLN KKEQGPPSTI KESSESSQTI
DDNDSEKGGG QLKHENTVVR ADGATGIVSS SNSSTASKSS STNLSAQKQD IVRVTQTLLD
AISCKDFETY TRLCDTSMTC FEPEALGNLI EGIEFHRFYF DGNRKNQVHT TMLNPNVHII
GEDAACVAYV KLTQFLDRNG EAHTRQSQES RVWSKKQGRW VCVHVHRSTQ PSTNTTVSEF


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