3SOA

Full-length human CaMKII

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000082	biological_process	G1/S transition of mitotic cell cycle
A	0000166	molecular_function	nucleotide binding
A	0002931	biological_process	response to ischemia
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0004683	molecular_function	calcium/calmodulin-dependent protein kinase activity
A	0005515	molecular_function	protein binding
A	0005516	molecular_function	calmodulin binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0005954	cellular_component	calcium- and calmodulin-dependent protein kinase complex
A	0006468	biological_process	protein phosphorylation
A	0006816	biological_process	calcium ion transport
A	0007259	biological_process	cell surface receptor signaling pathway via JAK-STAT
A	0010666	biological_process	positive regulation of cardiac muscle cell apoptotic process
A	0014069	cellular_component	postsynaptic density
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0030425	cellular_component	dendrite
A	0030666	cellular_component	endocytic vesicle membrane
A	0035254	molecular_function	glutamate receptor binding
A	0035458	biological_process	cellular response to interferon-beta
A	0038166	biological_process	angiotensin-activated signaling pathway
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0042995	cellular_component	cell projection
A	0043005	cellular_component	neuron projection
A	0043197	cellular_component	dendritic spine
A	0045202	cellular_component	synapse
A	0046427	biological_process	positive regulation of receptor signaling pathway via JAK-STAT
A	0046872	molecular_function	metal ion binding
A	0046928	biological_process	regulation of neurotransmitter secretion
A	0048168	biological_process	regulation of neuronal synaptic plasticity
A	0051092	biological_process	positive regulation of NF-kappaB transcription factor activity
A	0051346	biological_process	negative regulation of hydrolase activity
A	0051928	biological_process	positive regulation of calcium ion transport
A	0060291	biological_process	long-term synaptic potentiation
A	0060996	biological_process	dendritic spine development
A	0071346	biological_process	cellular response to type II interferon
A	0106310	molecular_function	protein serine kinase activity
A	1902108	biological_process	regulation of mitochondrial membrane permeability involved in apoptotic process
A	1903076	biological_process	regulation of protein localization to plasma membrane
A	1990443	biological_process	peptidyl-threonine autophosphorylation
A	2000124	biological_process	regulation of endocannabinoid signaling pathway
A	2001222	biological_process	regulation of neuron migration

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DB8 A 445

Chain	Residue
A	LEU19
A	VAL27
A	MET42
A	PHE89
A	VAL92
A	PHE157

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	10
Details	Region: {"description":"Calmodulin-binding"}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P11798","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P11275","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"UniProtKB","id":"P11275","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P11798","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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