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Calcium/calmodulin-dependent protein kinase type II alpha chain (CaM-kinase II alpha chain) (EC 2.7.11.17)

 KCC2A_DROME             Reviewed;         530 AA.
Q00168; Q59DP1; Q59DP2; Q9V495;
26-APR-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 154.
RecName: Full=Calcium/calmodulin-dependent protein kinase type II alpha chain;
Short=CaM-kinase II alpha chain;
EC=2.7.11.17;
Name=CaMKII; Synonyms=CaM; ORFNames=CG18069;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), AND TISSUE
SPECIFICITY.
TISSUE=Head;
PubMed=8380587;
Ohsako S., Nishida Y., Ryo H., Yamauchi T.;
"Molecular characterization and expression of the Drosophila
Ca2+/calmodulin-dependent protein kinase II gene. Identification of
four forms of the enzyme generated from a single gene by alternative
splicing.";
J. Biol. Chem. 268:2052-2062(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND TISSUE SPECIFICITY.
TISSUE=Head;
PubMed=1910789; DOI=10.1016/0896-6273(91)90296-C;
Cho K.O., Wall J.B., Pugh P.C., Ito M., Mueller S.A., Kennedy M.B.;
"The alpha subunit of type II Ca2+/calmodulin-dependent protein kinase
is highly conserved in Drosophila.";
Neuron 7:439-450(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 347-388.
PubMed=8397298; DOI=10.1111/j.1471-4159.1993.tb13650.x;
Griffith L.C., Greenspan R.J.;
"The diversity of calcium/calmodulin-dependent protein kinase II
isoforms in Drosophila is generated by alternative splicing of a
single gene.";
J. Neurochem. 61:1534-1537(1993).
[6]
FUNCTION.
PubMed=11980904; DOI=10.1074/jbc.M201949200;
Wang Z., Wilson G.F., Griffith L.C.;
"Calcium/calmodulin-dependent protein kinase II phosphorylates and
regulates the Drosophila eag potassium channel.";
J. Biol. Chem. 277:24022-24029(2002).
[7]
FUNCTION, INTERACTION WITH CASK, PHOSPHORYLATION AT THR-287; THR-306
AND THR-307, AND MUTAGENESIS OF THR-306 AND THR-307.
PubMed=14687552; DOI=10.1016/S0896-6273(03)00786-4;
Lu C.S., Hodge J.J., Mehren J., Sun X.X., Griffith L.C.;
"Regulation of the Ca2+/CaM-responsive pool of CaMKII by scaffold-
dependent autophosphorylation.";
Neuron 40:1185-1197(2003).
[8]
PHOSPHORYLATION AT THR-287, AND ENZYME REGULATION.
PubMed=16880127; DOI=10.1016/j.neuron.2006.06.020;
Hodge J.J., Mullasseril P., Griffith L.C.;
"Activity-dependent gating of CaMKII autonomous activity by Drosophila
CASK.";
Neuron 51:327-337(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327, AND IDENTIFICATION
BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
-!- FUNCTION: A key regulator of plasticity in synaptic physiology and
behavior, alterations in its activity produce pleiotrophic effects
that involve synaptic transmission and development as well as
various aspects of behavior. Directly modulates eag potassium
channels. {ECO:0000269|PubMed:11980904,
ECO:0000269|PubMed:14687552}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: CASK plays a role in regulation of CaMKII
autophosphorylation. When complexed with CASK and in the presence
Ca[2+]/CaM, autophosphorylation of Thr-287 causes constitutive
activation of the kinase. In the absence of Ca[2+]/CaM,
autophosphorylation of Thr-306 causes inactivation of the kinase.
{ECO:0000269|PubMed:16880127}.
-!- SUBUNIT: Interacts with CASK. {ECO:0000269|PubMed:14687552}.
-!- INTERACTION:
Q24210:CASK; NbExp=5; IntAct=EBI-124595, EBI-214423;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=530aa, D;
IsoId=Q00168-1; Sequence=Displayed;
Name=2; Synonyms=516aa, G;
IsoId=Q00168-2; Sequence=VSP_050262;
Name=3; Synonyms=509aa, B, E;
IsoId=Q00168-3; Sequence=VSP_050263;
Name=4; Synonyms=490aa, A, C;
IsoId=Q00168-4; Sequence=VSP_050261, VSP_050264;
-!- TISSUE SPECIFICITY: Expressed at a high level in the central
nervous system during the late embryonic stage. In adults,
expression is more abundant in the head than in the body.
{ECO:0000269|PubMed:1910789, ECO:0000269|PubMed:8380587}.
-!- PTM: Autophosphorylation at Thr-287 is independent of
autophosphorylation at Thr-306 and Thr-307.
{ECO:0000269|PubMed:14687552, ECO:0000269|PubMed:16880127,
ECO:0000269|PubMed:18327897}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. CaMK subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Calmodulin-dependent kinase
entry;
URL="https://en.wikipedia.org/wiki/Calmodulin_dependent_kinase";
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EMBL; D13330; BAA02593.1; -; mRNA.
EMBL; D13331; BAA02594.1; -; mRNA.
EMBL; D13332; BAA02595.1; -; mRNA.
EMBL; D13333; BAA02596.1; -; mRNA.
EMBL; M74583; AAA51459.1; -; mRNA.
EMBL; AE014135; AAF59388.3; -; Genomic_DNA.
EMBL; AE014135; AAF59390.2; -; Genomic_DNA.
EMBL; AE014135; AAN06568.2; -; Genomic_DNA.
EMBL; AE014135; AAX53595.1; -; Genomic_DNA.
EMBL; S65712; AAB28244.1; -; mRNA.
EMBL; S65716; AAB28245.1; -; mRNA.
EMBL; S65717; AAB28246.2; -; mRNA.
EMBL; S65719; AAB28247.1; -; mRNA.
EMBL; S65724; AAB28248.2; -; mRNA.
PIR; B44412; B44412.
PIR; C44412; JU0270.
PIR; D44412; D44412.
RefSeq; NP_001014696.1; NM_001014696.2. [Q00168-2]
RefSeq; NP_001162831.1; NM_001169360.2. [Q00168-4]
RefSeq; NP_001162832.1; NM_001169361.2. [Q00168-1]
RefSeq; NP_524635.3; NM_079896.4. [Q00168-4]
RefSeq; NP_726633.2; NM_166810.5. [Q00168-4]
RefSeq; NP_726634.1; NM_166811.2. [Q00168-3]
RefSeq; NP_726635.2; NM_166812.3. [Q00168-1]
RefSeq; NP_726636.2; NM_166813.3. [Q00168-3]
UniGene; Dm.1709; -.
PDB; 5FG8; X-ray; 1.96 A; A=1-283.
PDB; 5H9B; X-ray; 2.25 A; A=1-283.
PDB; 5HU3; X-ray; 1.89 A; A=1-283.
PDBsum; 5FG8; -.
PDBsum; 5H9B; -.
PDBsum; 5HU3; -.
ProteinModelPortal; Q00168; -.
SMR; Q00168; -.
BioGrid; 68654; 24.
IntAct; Q00168; 5.
MINT; MINT-1561551; -.
STRING; 7227.FBpp0289608; -.
iPTMnet; Q00168; -.
PaxDb; Q00168; -.
PRIDE; Q00168; -.
EnsemblMetazoa; FBtr0089217; FBpp0088281; FBgn0264607. [Q00168-4]
EnsemblMetazoa; FBtr0089218; FBpp0088282; FBgn0264607. [Q00168-4]
EnsemblMetazoa; FBtr0089219; FBpp0088283; FBgn0264607. [Q00168-3]
EnsemblMetazoa; FBtr0100146; FBpp0099496; FBgn0264607. [Q00168-1]
EnsemblMetazoa; FBtr0100147; FBpp0099497; FBgn0264607. [Q00168-3]
EnsemblMetazoa; FBtr0100148; FBpp0099498; FBgn0264607. [Q00168-2]
EnsemblMetazoa; FBtr0300377; FBpp0289606; FBgn0264607. [Q00168-4]
EnsemblMetazoa; FBtr0300378; FBpp0289607; FBgn0264607. [Q00168-1]
GeneID; 43828; -.
KEGG; dme:Dmel_CG18069; -.
CTD; 43828; -.
FlyBase; FBgn0264607; CaMKII.
eggNOG; KOG0033; Eukaryota.
eggNOG; ENOG410XNRX; LUCA.
GeneTree; ENSGT00760000118944; -.
InParanoid; Q00168; -.
KO; K04515; -.
OrthoDB; EOG091G0SCS; -.
PhylomeDB; Q00168; -.
BRENDA; 2.7.11.17; 1994.
Reactome; R-DME-3371571; HSF1-dependent transactivation.
Reactome; R-DME-4086398; Ca2+ pathway.
Reactome; R-DME-438066; Unblocking of NMDA receptor, glutamate binding and activation.
Reactome; R-DME-442729; CREB phosphorylation through the activation of CaMKII.
Reactome; R-DME-442742; CREB phosphorylation through the activation of Ras.
SignaLink; Q00168; -.
GenomeRNAi; 43828; -.
PRO; PR:Q00168; -.
Proteomes; UP000000803; Chromosome 4.
Bgee; FBgn0264607; -.
ExpressionAtlas; Q00168; differential.
Genevisible; Q00168; DM.
GO; GO:0030424; C:axon; IDA:FlyBase.
GO; GO:0005954; C:calcium- and calmodulin-dependent protein kinase complex; ISS:FlyBase.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0030425; C:dendrite; IDA:FlyBase.
GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
GO; GO:0045211; C:postsynaptic membrane; IDA:FlyBase.
GO; GO:0048786; C:presynaptic active zone; IDA:FlyBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005516; F:calmodulin binding; TAS:FlyBase.
GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IDA:FlyBase.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:FlyBase.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0007268; P:chemical synaptic transmission; IMP:FlyBase.
GO; GO:0007619; P:courtship behavior; TAS:FlyBase.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0007611; P:learning or memory; IMP:FlyBase.
GO; GO:0007616; P:long-term memory; IMP:FlyBase.
GO; GO:0008049; P:male courtship behavior; IMP:FlyBase.
GO; GO:0007528; P:neuromuscular junction development; NAS:FlyBase.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
GO; GO:0006468; P:protein phosphorylation; TAS:FlyBase.
GO; GO:0051489; P:regulation of filopodium assembly; IMP:FlyBase.
GO; GO:0060278; P:regulation of ovulation; IGI:FlyBase.
GO; GO:0008582; P:regulation of synaptic growth at neuromuscular junction; IMP:FlyBase.
InterPro; IPR013543; Ca/CaM-dep_prot_kinase-assoc.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR032710; NTF2-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
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;
Complete proteome; Kinase; Nucleotide-binding; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Transferase.
CHAIN 1 530 Calcium/calmodulin-dependent protein
kinase type II alpha chain.
/FTId=PRO_0000086095.
DOMAIN 12 272 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 20 28 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 291 301 Calmodulin-binding.
ACT_SITE 136 136 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 43 43 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 287 287 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:14687552,
ECO:0000269|PubMed:16880127}.
MOD_RES 306 306 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:14687552}.
MOD_RES 307 307 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:14687552}.
MOD_RES 327 327 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
VAR_SEQ 347 386 Missing (in isoform 4).
{ECO:0000303|PubMed:1910789,
ECO:0000303|PubMed:8380587}.
/FTId=VSP_050261.
VAR_SEQ 366 387 DIRILCPAKTYQQNIGNSQCSS -> VNLFTNKA (in
isoform 2). {ECO:0000303|PubMed:8380587}.
/FTId=VSP_050262.
VAR_SEQ 366 387 DIRILCPAKTYQQNIGNSQCSS -> A (in isoform
3). {ECO:0000303|PubMed:8380587}.
/FTId=VSP_050263.
VAR_SEQ 387 387 S -> A (in isoform 4).
{ECO:0000303|PubMed:1910789,
ECO:0000303|PubMed:8380587}.
/FTId=VSP_050264.
MUTAGEN 306 306 T->A: Fails to interact with CASK,
catalytically active but fails to
autophosphorylate, when associated with
A-307. {ECO:0000269|PubMed:14687552}.
MUTAGEN 306 306 T->D: Fails to interact with CASK, kinase
inactive, when associated with D-307.
{ECO:0000269|PubMed:14687552}.
MUTAGEN 306 306 T->S: Fails to interact with CASK,
catalytically active and can
autophosphorylate, when associated with
S-307. {ECO:0000269|PubMed:14687552}.
MUTAGEN 307 307 T->A: Fails to interact with CASK,
catalytically active but fails to
autophosphorylate, when associated with
A-306. {ECO:0000269|PubMed:14687552}.
MUTAGEN 307 307 T->D: Fails to interact with CASK, kinase
inactive, when associated with D-306.
{ECO:0000269|PubMed:14687552}.
MUTAGEN 307 307 T->S: Fails to interact with CASK,
catalytically active and can
autophosphorylate, when associated with
S-306. {ECO:0000269|PubMed:14687552}.
CONFLICT 388 388 A -> S (in Ref. 2; AAB28246/AAB28248).
{ECO:0000305}.
HELIX 9 13 {ECO:0000244|PDB:5HU3}.
STRAND 14 23 {ECO:0000244|PDB:5HU3}.
STRAND 26 33 {ECO:0000244|PDB:5HU3}.
TURN 34 36 {ECO:0000244|PDB:5HU3}.
STRAND 39 46 {ECO:0000244|PDB:5HU3}.
HELIX 52 67 {ECO:0000244|PDB:5HU3}.
STRAND 76 81 {ECO:0000244|PDB:5HU3}.
STRAND 83 91 {ECO:0000244|PDB:5HU3}.
HELIX 98 105 {ECO:0000244|PDB:5HU3}.
HELIX 110 128 {ECO:0000244|PDB:5HU3}.
TURN 129 131 {ECO:0000244|PDB:5HU3}.
HELIX 139 141 {ECO:0000244|PDB:5HU3}.
STRAND 142 145 {ECO:0000244|PDB:5HU3}.
STRAND 153 155 {ECO:0000244|PDB:5HU3}.
STRAND 174 176 {ECO:0000244|PDB:5HU3}.
HELIX 178 180 {ECO:0000244|PDB:5HU3}.
HELIX 183 186 {ECO:0000244|PDB:5HU3}.
HELIX 194 209 {ECO:0000244|PDB:5HU3}.
HELIX 219 228 {ECO:0000244|PDB:5HU3}.
TURN 235 240 {ECO:0000244|PDB:5HU3}.
HELIX 243 252 {ECO:0000244|PDB:5HU3}.
TURN 257 259 {ECO:0000244|PDB:5FG8}.
HELIX 263 266 {ECO:0000244|PDB:5HU3}.
HELIX 270 273 {ECO:0000244|PDB:5FG8}.
SEQUENCE 530 AA; 59920 MW; 4F3D83582ABDFCFD CRC64;
MAAPAACTRF SDNYDIKEEL GKGAFSIVKR CVQKSTGFEF AAKIINTKKL TARDFQKLER
EARICRKLHH PNIVRLHDSI QEENYHYLVF DLVTGGELFE DIVAREFYSE ADASHCIQQI
LESVNHCHQN GVVHRDLKPE NLLLASKAKG AAVKLADFGL AIEVQGDHQA WFGFAGTPGY
LSPEVLKKEP YGKSVDIWAC GVILYILLVG YPPFWDEDQH RLYSQIKAGA YDYPSPEWDT
VTPEAKNLIN QMLTVNPNKR ITAAEALKHP WICQRERVAS VVHRQETVDC LKKFNARRKL
KGAILTTMLA TRNFSSRSMI TKKGEGSQVK ESTDSSSTTL EDDDIKEDKK GTVDRSTTVV
SKEPEDIRIL CPAKTYQQNI GNSQCSSARR QEIIKITEQL IEAINSGDFD GYTKICDPHL
TAFEPEALGN LVEGIDFHKF YFENVLGKNC KAINTTILNP HVHLLGEEAA CIAYVRLTQY
IDKQGHAHTH QSEETRVWHK RDNKWQNVHF HRSASAKISG ATTFDFIPQK


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CG94 Calcium calmodulin-dependent protein kinase type 1D CAMK1D lmg
KCC1B_RAT Rat ELISA Kit FOR Calcium per calmodulin-dependent protein kinase type 1B 96T
CG94 Calcium calmodulin-dependent protein kinase type 1D CAMK1D 500
KKCC1_HUMAN Human ELISA Kit FOR Calcium per calmodulin-dependent protein kinase kinase 1 96T
E0670b Mouse ELISA Kit FOR Calcium per calmodulin-dependent protein kinase kinase 1 96T
TA2R7_MOUSE Mouse ELISA Kit FOR Calcium per calmodulin-dependent protein kinase kinase 1 96T
ZNF26_HUMAN Rat ELISA Kit FOR Calcium per calmodulin-dependent protein kinase kinase 1 96T
E0160h Rat ELISA Kit FOR Calcium per calmodulin-dependent protein kinase kinase 1 96T


 

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