Detail Information for IndEnz0005000551
IED ID IndEnz0005000551
Enzyme Type ID lipase000551
Protein Name Calcium/calmodulin-dependent protein kinase type II subunit alpha
CaM kinase II subunit alpha
CaMK-II subunit alpha
EC 2.7.11.17
Gene Name Camk2a
Organism Mus musculus (Mouse)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MATITCTRFTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWISHRSTVASCMHRQETVDCLKKFNARRKLKGAILTTMLATRNFSGGKSGGNKKNDGVKESSESTNTTIEDEDTKVRKQEIIKVTEQLIEAISNGDFESYTKMCDPGMTAFEPEALGNLVEGLDFHRFYFENLWSRNSKPVHTTILNPHIHLMGDESACIAYIRITQYLDAGGIPRTAQSEETRVWHRRDGKWQIVHFHRSGAPSVLPH
Enzyme Length 478
Uniprot Accession Number P11798
Absorption
Active Site ACT_SITE 135; /note=Proton acceptor
Activity Regulation ACTIVITY REGULATION: Activated by Ca(2+)/calmodulin. Binding of calmodulin results in conformational change that relieves intrasteric autoinhibition and allows autophosphorylation of Thr-286 which turns the kinase in a constitutively active form and confers to the kinase a Ca(2+)-independent activity. {ECO:0000250|UniProtKB:Q9UQM7}.
Binding Site BINDING 42; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00159
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.17; Evidence={ECO:0000269|PubMed:23502535}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.17; Evidence={ECO:0000269|PubMed:23502535};
DNA Binding
EC Number 2.7.11.17
Enzyme Function FUNCTION: Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in synaptic plasticity, neurotransmitter release and long-term potentiation. Member of the NMDAR signaling complex in excitatory synapses, it regulates NMDAR-dependent potentiation of the AMPAR and therefore excitatory synaptic transmission (By similarity). Regulates dendritic spine development. Also regulates the migration of developing neurons (By similarity). Phosphorylates the transcription factor FOXO3 to activate its transcriptional activity (PubMed:23805378). Acts as a negative regulator of 2-arachidonoylglycerol (2-AG)-mediated synaptic signaling via modulation of DAGLA activity (PubMed:23502535). {ECO:0000250|UniProtKB:P11275, ECO:0000250|UniProtKB:Q9UQM7, ECO:0000269|PubMed:23502535, ECO:0000269|PubMed:23805378}.; FUNCTION: [Isoform Alpha KAP]: Has no kinase activity. {ECO:0000269|PubMed:8524307}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 19..27; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00159
Features Active site (1); Alternative sequence (3); Beta strand (7); Binding site (1); Chain (1); Compositional bias (1); Domain (1); Helix (5); Modified residue (9); Mutagenesis (3); Nucleotide binding (1); Region (3); Sequence conflict (3); Turn (1)
Keywords 3D-structure;ATP-binding;Alternative splicing;Calmodulin-binding;Cell junction;Cell projection;Cytoplasm;Direct protein sequencing;Kinase;Lipoprotein;Magnesium;Metal-binding;Nucleotide-binding;Palmitate;Phosphoprotein;Reference proteome;Serine/threonine-protein kinase;Synapse;Transferase
Interact With Q9JI91; Q62108; Q01097; Q00960; P70587; Q9Z1R2
Induction
Subcellular Location SUBCELLULAR LOCATION: [Isoform Alpha KAP]: Cytoplasm {ECO:0000305|PubMed:8524307}.; SUBCELLULAR LOCATION: Cell junction, synapse {ECO:0000269|PubMed:28642476}. Cell junction, synapse, postsynaptic density {ECO:0000250|UniProtKB:P11275}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q9UQM7}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9UQM7}. Note=Postsynaptic lipid rafts. {ECO:0000250|UniProtKB:P11275}.
Modified Residue MOD_RES 13; /note=Phosphotyrosine; /evidence=ECO:0007744|PubMed:18034455; MOD_RES 257; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P11275; MOD_RES 286; /note=Phosphothreonine; by autocatalysis; /evidence=ECO:0000269|PubMed:28130356; MOD_RES 330; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 331; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 333; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 336; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 337; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 404; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079
Post Translational Modification PTM: Autophosphorylation of Thr-286 following activation by Ca(2+)/calmodulin. Phosphorylation of Thr-286 locks the kinase into an activated state. {ECO:0000269|PubMed:28130356}.; PTM: Palmitoylated. Probably palmitoylated by ZDHHC3 and ZDHHC7. {ECO:0000250|UniProtKB:P11275}.
Signal Peptide
Structure 3D X-ray crystallography (3)
Cross Reference PDB 1HKX; 4X3I; 6TS3;
Mapped Pubmed ID 10087064; 10381553; 10454359; 10686608; 10767319; 10790881; 10862698; 10966622; 11042368; 11239428; 11264466; 11357133; 11713472; 11739749; 11889801; 11967152; 12147342; 12223541; 12231258; 12379661; 12408850; 12408851; 12408852; 12466851; 12554746; 12618516; 12629219; 12646704; 12660151; 12684449; 12693553; 12769848; 12798302; 12805283; 12824452; 12931786; 1319776; 1321493; 1339689; 1354644; 1378648; 14610273; 14725635; 14734049; 15073522; 15102471; 15131309; 15135664; 15140879; 15464294; 15582152; 15590632; 15778710; 15793582; 15927279; 15994560; 16091425; 16107656; 16120608; 16126302; 16157407; 16172120; 16186118; 16207525; 16253986; 16260731; 16260732; 16441656; 16512683; 16515554; 16519936; 16602821; 16615898; 16616897; 16630070; 16635246; 16651267; 16690036; 16710293; 16728448; 16776832; 16820363; 16824507; 16840718; 16861697; 16863646; 16875841; 16959763; 16982427; 17052727; 17114649; 17124502; 17184923; 17202430; 17259980; 17277773; 17292391; 17367784; 17445244; 17603011; 17610578; 17625814; 17634379; 17640289; 17660813; 17689560; 17884930; 17923476; 17923693; 17953618; 18045856; 18048055; 18054865; 18066053; 18077696; 18082335; 18178903; 18255058; 18305102; 18351675; 18413649; 18464936; 18480293; 18550767; 18551708; 18613116; 18622016; 18690039; 18703025; 18727829; 18799693; 18803808; 18809727; 18818394; 18948074; 18957226; 18984565; 19190753; 19208628; 19217379; 19233146; 19240035; 19245842; 19257910; 19276108; 19332541; 19339497; 19362146; 19439493; 19455133; 19457128; 19478130; 19485558; 19515929; 19562802; 19603549; 19605628; 19609731; 19654320; 19671701; 19735294; 19735476; 19750198; 19776387; 19799774; 19840220; 19934217; 19996366; 20141836; 20215576; 20237283; 20336626; 20371813; 20392935; 20461055; 20479240; 20538682; 20643921; 20877009; 20976158; 21068402; 21166200; 21187407; 21209221; 21252154; 21267068; 21276220; 21307321; 21343908; 21491429; 21516102; 21610080; 21614506; 21627991; 21677750; 21752990; 21785215; 21833587; 21925648; 21927594; 22025701; 22234183; 22348105; 22363696; 22427508; 22427672; 22454450; 22496563; 22503562; 22505582; 22560297; 22573680; 22647634; 22736516; 22768241; 22778257; 22796260; 22855824; 22952977; 22993434; 23028932; 23051746; 23063718; 23089915; 23173822; 23223335; 23227957; 23260144; 23313759; 23316062; 23386589; 23389689; 23402759; 23516528; 23632380; 23652597; 23660191; 23732653; 23753415; 23884469; 23958294; 24038144; 24095281; 24101510; 24136198; 24164423; 24193728; 24248603; 24336150; 24349346; 24374198; 24418021; 24448406; 24480420; 24485660; 24496615; 24498331; 24576293; 24627477; 24725413; 24806094; 24831007; 24831701; 24852843; 24949568; 24952961; 25042347; 25073061; 25097034; 25131634; 25143599; 25186740; 25246560; 25290264; 25297099; 25389288; 2550458; 25540577; 25560761; 25644714; 25650780; 25834039; 25834051; 25843407; 25864631; 25885040; 25922519; 26019340; 26095350; 26166359; 26247621; 26281891; 26292186; 26297240; 26300473; 26372002; 26415772; 26485287; 26490852; 26627310; 26670047; 26880306; 26932671; 27005420; 27028761; 27059140; 27158969; 27170659; 27496951; 27535377; 27648519; 27799554; 27918287; 28069946; 28137877; 28147268; 28230177; 28295333; 28344592; 28361052; 28521133; 28527717; 28548932; 28589927; 28636948; 28648815; 28662005; 28671696; 28714806; 29042611; 29056297; 29081444; 29107547; 29137928; 29146590; 29402414; 29518331; 29599132; 29602494; 29615706; 29786085; 29978952; 30104731; 30225347; 30232223; 30466882; 30504773; 30509490; 30675529; 30770570; 30814928; 30894537; 30992372; 31034488; 31064859; 31134625; 31151856; 31239443; 31445077; 31481791; 31530151; 31712124; 31800021; 31836540; 31914378; 31983435; 32001612; 32005752; 32005763; 32019829; 32407818; 32776935; 32887881; 33086056; 33497737; 33786818; 33804598; 33946543; 34062838; 34103655; 34297923; 34572045; 34587162; 34628110; 34932950; 7649368; 7775466; 7939668; 7953554; 8530541; 8602534; 8816712; 8939606; 8939850; 9096402; 9452387; 9452388; 9523577; 9882483;
Motif
Gene Encoded By
Mass 54,115
Kinetics
Metal Binding
Rhea ID RHEA:17989; RHEA:46608
Cross Reference Brenda 2.7.11.17;