RAT:KCC2A

Species (Taxon ID)	Rattus norvegicus (Rat). (10116)
Gene Name(s)	Camk2a
Protein Name(s)	Calcium/calmodulin-dependent protein kinase type II subunit alpha CaM kinase II subunit alpha CaMK-II subunit alpha
External Links
UniProt	P11275
EMBL	J02942 M16960 M29699
PIR	A30355
RefSeq	NP_037052.1
UniGene	Rn.107499
PDB	1CDM 1CM1 1CM4
PDBsum	1CDM 1CM1 1CM4
ProteinModelPortal	P11275
SMR	P11275
BioGrid	247435
DIP	DIP-29639N
IntAct	P11275
MINT	MINT-153011
STRING	10116.ENSRNOP00000025283
BindingDB	P11275
ChEMBL	CHEMBL2359
GuidetoPHARMACOLOGY	1555
PhosphoSite	P11275
PaxDb	P11275
PRIDE	P11275
GeneID	25400
KEGG	rno:25400
UCSC	RGD:2261
CTD	815
RGD	2261
eggNOG	COG0515
HOVERGEN	HBG108055
InParanoid	P11275
KO	K04515
PhylomeDB	P11275
BRENDA	2.7.11.17
EvolutionaryTrace	P11275
NextBio	606489
PMAP-CutDB	P11275
Proteomes	UP000002494
Genevestigator	P11275
GO	GO:0030054 GO:0030425 GO:0032839 GO:0005739 GO:0042734 GO:0005524 GO:0004683 GO:0035254 GO:0032794 GO:0004674 GO:0006816 GO:0000082 GO:0035235 GO:0018105 GO:0051928 GO:0010666 GO:0046777 GO:0006468 GO:1902108 GO:0048168 GO:0046928 GO:0002931
InterPro	IPR020636 IPR013543 IPR011009 IPR000719 IPR017441 IPR002290 IPR008271
PANTHER	PTHR24347
Pfam	PF08332 PF00069
SMART	SM00220
SUPFAM	SSF56112
PROSITE	PS00107 PS50011 PS00108

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
involved_in	GO:2001222	regulation of neuron migration	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9UQM7	P		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P11798	C	part_of:(UBERON:0000948)	Seeded From UniProt	complete
involved_in	GO:1903076	regulation of protein localization to plasma membrane	PMID:19188609^[1]	ECO:0000316	genetic interaction evidence used in manual assertion	ComplexPortal:CPX-1134,UniProtKB:P08413,UniProtKB:P11730,UniProtKB:P15791	P	occurs_in:(CL:0002608) has_target_start_location:(GO:0032590) transports_or_maintains_localization_of:(UniProtKB:P06213) has_target_end_location:(GO:0032809)\|occurs_in(CL:0002608) has_target_start_location:(GO:0032590) transports_or_maintains_localization_of:(GO:0017146) has_target_end_location:(GO:0032809)	Seeded From UniProt	complete
involved_in	GO:0099004	calmodulin dependent kinase signaling pathway	PMID:20670832^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(GO:0043197) occurs_in:(CL:0002608)	Seeded From UniProt	complete
involved_in	GO:0098989	NMDA selective glutamate receptor signaling pathway	PMID:20670832^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(GO:0043197) occurs_in:(CL:0002608)	Seeded From UniProt	complete
part_of	GO:0099573	glutamatergic postsynaptic density	PMID:10102820^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0002608)	Seeded From UniProt	complete
part_of	GO:0099524	postsynaptic cytosol	PMID:10102820^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0002608)	Seeded From UniProt	complete
involved_in	GO:0098970	postsynaptic neurotransmitter receptor diffusion trapping	PMID:24894704^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(GO:0060077) occurs_in:(CL:0002608) transports_or_maintains_localization_of:(GO:1902711)	Seeded From UniProt	complete
involved_in	GO:0046928	regulation of neurotransmitter secretion	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P11798	P		Seeded From UniProt	complete
enables	GO:0035254	glutamate receptor binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P11798	F		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P11798	F	has_direct_input:(MGI:MGI:1347359)	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P11798	F		Seeded From UniProt	complete
involved_in	GO:1902108	regulation of mitochondrial membrane permeability involved in apoptotic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P11798	P		Seeded From UniProt	complete
involved_in	GO:0051928	positive regulation of calcium ion transport	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P11798	P		Seeded From UniProt	complete
involved_in	GO:0048168	regulation of neuronal synaptic plasticity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P11798	P		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:22514276^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004683	calmodulin-dependent protein kinase activity	PMID:22514276^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0010666	positive regulation of cardiac muscle cell apoptotic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P11798	P		Seeded From UniProt	complete
involved_in	GO:0006816	calcium ion transport	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P11798	P		Seeded From UniProt	complete
involved_in	GO:0002931	response to ischemia	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P11798	P		Seeded From UniProt	complete
involved_in	GO:0000082	G1/S transition of mitotic cell cycle	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P11798	P		Seeded From UniProt	complete
part_of	GO:0043197	dendritic spine	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9UQM7	C		Seeded From UniProt	complete
part_of	GO:0005954	calcium- and calmodulin-dependent protein kinase complex	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9UQM7	C		Seeded From UniProt	complete
involved_in	GO:1990443	peptidyl-threonine autophosphorylation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9UQM7	P		Seeded From UniProt	complete
involved_in	GO:0060996	dendritic spine development	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9UQM7	P		Seeded From UniProt	complete
part_of	GO:0032839	dendrite cytoplasm	PMID:1419001^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0035235	ionotropic glutamate receptor signaling pathway	PMID:12223541^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0030425	dendrite	PMID:12223541^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0099524	postsynaptic cytosol	PMID:17957478^[8]	ECO:0006003	electron microscopy evidence used in manual assertion		C	part_of:(GO:0098978) part_of:(UBERON:0000061) part_of:(UBERON:0002421)	Seeded From UniProt	complete
part_of	GO:0099523	presynaptic cytosol	PMID:17957478^[8]	ECO:0006003	electron microscopy evidence used in manual assertion		C	part_of:(GO:0098978) part_of:(UBERON:0000061) part_of:(UBERON:0002421)	Seeded From UniProt	complete
part_of	GO:0098978	glutamatergic synapse	PMID:12202034^[9]	ECO:0006063	over expression analysis evidence used in manual assertion		C	part_of:(UBERON:0002421)	Seeded From UniProt	complete
part_of	GO:0098978	glutamatergic synapse	PMID:12202034^[9]	ECO:0006013	patch-clamp recording evidence used in manual assertion		C	part_of:(UBERON:0002421)	Seeded From UniProt	complete
part_of	GO:0098978	glutamatergic synapse	PMID:17957478^[8]	ECO:0006003	electron microscopy evidence used in manual assertion		C	part_of:(UBERON:0002421)	Seeded From UniProt	complete
involved_in	GO:0098696	regulation of neurotransmitter receptor localization to postsynaptic specialization membrane	PMID:12202034^[9]	ECO:0006063	over expression analysis evidence used in manual assertion		P	occurs_in:(GO:0098978) occurs_in:(UBERON:0000061) occurs_in:(UBERON:0002421)	Seeded From UniProt	complete
involved_in	GO:0098696	regulation of neurotransmitter receptor localization to postsynaptic specialization membrane	PMID:12202034^[9]	ECO:0006013	patch-clamp recording evidence used in manual assertion		P	occurs_in:(GO:0098978) occurs_in:(UBERON:0000061) occurs_in:(UBERON:0002421)	Seeded From UniProt	complete
part_of	GO:0014069	postsynaptic density	PMID:20878786^[10]	ECO:0006042	cell fractionation evidence used in manual assertion		C	part_of:(UBERON:0001890)	Seeded From UniProt	complete
part_of	GO:0014069	postsynaptic density	PMID:20878786^[10]	ECO:0006003	electron microscopy evidence used in manual assertion		C	part_of:(UBERON:0001890)	Seeded From UniProt	complete
involved_in	GO:0046777	protein autophosphorylation	PMID:16095822^[11]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0043025	neuronal cell body	PMID:7820660^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0032794	GTPase activating protein binding	PMID:12951199^[13]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:621090	F		Seeded From UniProt	complete
part_of	GO:0030425	dendrite	PMID:7820660^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0030424	axon	PMID:12176168^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0018105	peptidyl-serine phosphorylation	PMID:12951199^[13]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:12951199^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0014069	postsynaptic density	PMID:7820660^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:12401560^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:14688616^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:7820660^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004683	calmodulin-dependent protein kinase activity	PMID:16095822^[11]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004683	calmodulin-dependent protein kinase activity	PMID:12951199^[13]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004683	calmodulin-dependent protein kinase activity	PMID:12401560^[15]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0043005	neuron projection	PMID:21873635^[17]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002389359 WB:WBGene00006779	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[17]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1341265 PANTHER:PTN002389359 RGD:2263	C		Seeded From UniProt	complete
enables	GO:0005516	calmodulin binding	PMID:21873635^[17]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:88256 PANTHER:PTN002389359 UniProtKB:Q13557 UniProtKB:Q9UQM7	F		Seeded From UniProt	complete
enables	GO:0004683	calmodulin-dependent protein kinase activity	PMID:21873635^[17]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0264607 MGI:MGI:88256 MGI:MGI:88257 PANTHER:PTN002389359 RGD:2261 RGD:2262 RGD:2263 RGD:621802 UniProtKB:Q13557 UniProtKB:Q9UQM7 WB:WBGene00006779	F		Seeded From UniProt	complete
part_of	GO:0099634	postsynaptic specialization membrane	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0098970	C		Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR008271	F		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR039071	F		Seeded From UniProt	complete
enables	GO:0004683	calmodulin-dependent protein kinase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR013543 InterPro:IPR039071	F		Seeded From UniProt	complete
enables	GO:0005516	calmodulin binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR013543	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR017441	F		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR008271 InterPro:IPR013543	P		Seeded From UniProt	complete
enables	GO:0004683	calmodulin-dependent protein kinase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.7.11.17	F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-RNO-9620437 Reactome:R-RNO-9619459 Reactome:R-RNO-9618659 Reactome:R-RNO-9618616 Reactome:R-RNO-9618605 Reactome:R-RNO-9617322	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0016301	kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	F		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F		Seeded From UniProt	complete
part_of	GO:0045202	synapse	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0770 UniProtKB-SubCell:SL-0258	C		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
involved_in	GO:0016310	phosphorylation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	P		Seeded From UniProt	complete
part_of	GO:0042995	cell projection	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0966	C		Seeded From UniProt	complete
part_of	GO:0045211	postsynaptic membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0628	C		Seeded From UniProt	complete
enables	GO:0005516	calmodulin binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0112	F		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003	C		Seeded From UniProt	complete
part_of	GO:0030054	cell junction	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0965	C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0723	F		Seeded From UniProt	complete
part_of	GO:0043197	dendritic spine	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0284	C		Seeded From UniProt	complete
part_of	GO:0014069	postsynaptic density	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0297	C		Seeded From UniProt	complete
part_of	GO:0030425	dendrite	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0283	C		Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ De Felice, FG et al. (2009) Protection of synapses against Alzheimer's-linked toxins: insulin signaling prevents the pathogenic binding of Abeta oligomers. Proc. Natl. Acad. Sci. U.S.A. 106 1971-6 PubMed GONUTS page
↑ ^2.0 ^2.1 Opazo, P et al. (2010) CaMKII triggers the diffusional trapping of surface AMPARs through phosphorylation of stargazin. Neuron 67 239-52 PubMed GONUTS page
↑ ^3.0 ^3.1 Shen, K & Meyer, T (1999) Dynamic control of CaMKII translocation and localization in hippocampal neurons by NMDA receptor stimulation. Science 284 162-6 PubMed GONUTS page
↑ Petrini, EM et al. (2014) Synaptic recruitment of gephyrin regulates surface GABAA receptor dynamics for the expression of inhibitory LTP. Nat Commun 5 3921 PubMed GONUTS page
↑ ^5.0 ^5.1 Ashpole, NM et al. (2012) Ca2+/calmodulin-dependent protein kinase II (CaMKII) regulates cardiac sodium channel NaV1.5 gating by multiple phosphorylation sites. J. Biol. Chem. 287 19856-69 PubMed GONUTS page
↑ Cho, KO et al. (1992) The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein. Neuron 9 929-42 PubMed GONUTS page
↑ ^7.0 ^7.1 Dhavan, R et al. (2002) The cyclin-dependent kinase 5 activators p35 and p39 interact with the alpha-subunit of Ca2+/calmodulin-dependent protein kinase II and alpha-actinin-1 in a calcium-dependent manner. J. Neurosci. 22 7879-91 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 Tao-Cheng, JH et al. (2006) Changes in the distribution of calcium calmodulin-dependent protein kinase II at the presynaptic bouton after depolarization. Brain Cell Biol 35 117-24 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 ^9.3 Zhu, JJ et al. (2002) Ras and Rap control AMPA receptor trafficking during synaptic plasticity. Cell 110 443-55 PubMed GONUTS page
↑ ^10.0 ^10.1 Swulius, MT et al. (2010) Structure and composition of the postsynaptic density during development. J. Comp. Neurol. 518 4243-60 PubMed GONUTS page
↑ ^11.0 ^11.1 Price, TJ et al. (2005) Pharmacological interactions between calcium/calmodulin-dependent kinase II alpha and TRPV1 receptors in rat trigeminal sensory neurons. Neurosci. Lett. 389 94-8 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 ^12.3 Ochiishi, T et al. (1994) Specific distribution of Ca2+/calmodulin-dependent protein kinase II alpha and beta isoforms in some structures of the rat forebrain. Brain Res. 659 179-93 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 ^13.3 Song, B et al. (2003) Cerebral ischemia immediately increases serine phosphorylation of the synaptic RAS-GTPase activating protein SynGAP by calcium/calmodulin-dependent protein kinase II alpha in hippocampus of rats. Neurosci. Lett. 349 183-6 PubMed GONUTS page
↑ Carlton, SM (2002) Localization of CaMKIIalpha in rat primary sensory neurons: increase in inflammation. Brain Res. 947 252-9 PubMed GONUTS page
↑ ^15.0 ^15.1 Meng, F & Zhang, G (2002) Autophosphorylated calcium/calmodulin-dependent protein kinase II alpha induced by cerebral ischemia immediately targets and phosphorylates N-methyl-D-aspartate receptor subunit 2B (NR2B) in hippocampus of rats. Neurosci. Lett. 333 59-63 PubMed GONUTS page
↑ Matsumoto, S et al. (2004) Protein kinase C-gamma and calcium/calmodulin-dependent protein kinase II-alpha are persistently translocated to cell membranes of the rat brain during and after middle cerebral artery occlusion. J. Cereb. Blood Flow Metab. 24 54-61 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 ^17.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:19188609-1] De Felice, FG et al. (2009) Protection of synapses against Alzheimer's-linked toxins: insulin signaling prevents the pathogenic binding of Abeta oligomers. Proc. Natl. Acad. Sci. U.S.A. 106 1971-6 PubMed GONUTS page

[PMID:20670832-2] 2.0 ^2.1 Opazo, P et al. (2010) CaMKII triggers the diffusional trapping of surface AMPARs through phosphorylation of stargazin. Neuron 67 239-52 PubMed GONUTS page

[PMID:10102820-3] 3.0 ^3.1 Shen, K & Meyer, T (1999) Dynamic control of CaMKII translocation and localization in hippocampal neurons by NMDA receptor stimulation. Science 284 162-6 PubMed GONUTS page

[PMID:24894704-4] Petrini, EM et al. (2014) Synaptic recruitment of gephyrin regulates surface GABAA receptor dynamics for the expression of inhibitory LTP. Nat Commun 5 3921 PubMed GONUTS page

[PMID:22514276-5] 5.0 ^5.1 Ashpole, NM et al. (2012) Ca2+/calmodulin-dependent protein kinase II (CaMKII) regulates cardiac sodium channel NaV1.5 gating by multiple phosphorylation sites. J. Biol. Chem. 287 19856-69 PubMed GONUTS page

[PMID:1419001-6] Cho, KO et al. (1992) The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein. Neuron 9 929-42 PubMed GONUTS page

[PMID:12223541-7] 7.0 ^7.1 Dhavan, R et al. (2002) The cyclin-dependent kinase 5 activators p35 and p39 interact with the alpha-subunit of Ca2+/calmodulin-dependent protein kinase II and alpha-actinin-1 in a calcium-dependent manner. J. Neurosci. 22 7879-91 PubMed GONUTS page

[PMID:17957478-8] 8.0 ^8.1 ^8.2 Tao-Cheng, JH et al. (2006) Changes in the distribution of calcium calmodulin-dependent protein kinase II at the presynaptic bouton after depolarization. Brain Cell Biol 35 117-24 PubMed GONUTS page

[PMID:12202034-9] 9.0 ^9.1 ^9.2 ^9.3 Zhu, JJ et al. (2002) Ras and Rap control AMPA receptor trafficking during synaptic plasticity. Cell 110 443-55 PubMed GONUTS page

[PMID:20878786-10] 10.0 ^10.1 Swulius, MT et al. (2010) Structure and composition of the postsynaptic density during development. J. Comp. Neurol. 518 4243-60 PubMed GONUTS page

[PMID:16095822-11] 11.0 ^11.1 Price, TJ et al. (2005) Pharmacological interactions between calcium/calmodulin-dependent kinase II alpha and TRPV1 receptors in rat trigeminal sensory neurons. Neurosci. Lett. 389 94-8 PubMed GONUTS page

[PMID:7820660-12] 12.0 ^12.1 ^12.2 ^12.3 Ochiishi, T et al. (1994) Specific distribution of Ca2+/calmodulin-dependent protein kinase II alpha and beta isoforms in some structures of the rat forebrain. Brain Res. 659 179-93 PubMed GONUTS page

[PMID:12951199-13] 13.0 ^13.1 ^13.2 ^13.3 Song, B et al. (2003) Cerebral ischemia immediately increases serine phosphorylation of the synaptic RAS-GTPase activating protein SynGAP by calcium/calmodulin-dependent protein kinase II alpha in hippocampus of rats. Neurosci. Lett. 349 183-6 PubMed GONUTS page

[PMID:12176168-14] Carlton, SM (2002) Localization of CaMKIIalpha in rat primary sensory neurons: increase in inflammation. Brain Res. 947 252-9 PubMed GONUTS page

[PMID:12401560-15] 15.0 ^15.1 Meng, F & Zhang, G (2002) Autophosphorylated calcium/calmodulin-dependent protein kinase II alpha induced by cerebral ischemia immediately targets and phosphorylates N-methyl-D-aspartate receptor subunit 2B (NR2B) in hippocampus of rats. Neurosci. Lett. 333 59-63 PubMed GONUTS page

[PMID:14688616-16] Matsumoto, S et al. (2004) Protein kinase C-gamma and calcium/calmodulin-dependent protein kinase II-alpha are persistently translocated to cell membranes of the rat brain during and after middle cerebral artery occlusion. J. Cereb. Blood Flow Metab. 24 54-61 PubMed GONUTS page

[PMID:21873635-17] 17.0 ^17.1 ^17.2 ^17.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

[12]

[13]

[14]

[15]

[16]

[17]

RAT:KCC2A

Contents

Annotations

Notes

References

a

c

d

e

g

i

k

m

n

o

p

r

s

t

v

Navigation menu

Personal tools

Namespaces

Variants

Views

More

Search

Navigation

Cacao

Links

Tools