1. Catalog
  2. Nodes
  3. p(HGNC:CAMK2A)

p(HGNC:CAMK2A)

Equivalencies: 0 | Classes: 0 | Children: 0 | Explore

Entity

Name
CAMK2A
Namespace
hgnc
Namespace Version
20180906
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/hgnc-names.belns

Appears in Networks 3

Proteolytic processing of Alzeimer's beta-amyloid precursor protein v1.0.1

Tau in physiology and pathology v1.0.0

Nuclear Factor Kappa-light-chain-enhancer of Activated B Cells (NF-κB) - a Friend, a Foe, or a Bystander - in the Neurodegenerative Cascade and Pathogenesis of Alzheimer's Disease v1.0.0

In-Edges 2

a(MESH:"Receptors, N-Methyl-D-Aspartate") regulates act(p(HGNC:CAMK2A)) View Subject | View Object

The molecular mechanism underlying constitutive activation of NF-κB by glutamate-induced excitatory synaptic neurotransmission has been ascribed to NMDA receptor mediated Ca2+ influx and subsequent activation of CaMKII PubMed:28745240

Appears in Networks:
Annotations
MeSH
Alzheimer Disease

bp(GO:"calcium ion import") increases act(p(HGNC:CAMK2A)) View Subject | View Object

In addition to CamKII, other kinases activated in response to a rise in cytosolic Ca2+ such as protein kinase C (PKC), phosphatidylinositol-3-kinase (PI3K), and Akt, also activate NF-κB signaling pathway by increasing the phosphorylation and activation of IKK PubMed:28745240

Appears in Networks:
Annotations
MeSH
Alzheimer Disease

Out-Edges 9

p(HGNC:CAMK2A) increases p(HBP:HBP00071, pmod(Ph, Thr, 654)) View Subject | View Object

AICD also contains three phosphorylation sites, including two threonine residues at 654 and 668 and a serine residue at 665. AICD has been found to be phosphorylated by PKC, calcium-calmodulin dependent-kinase II, GSK3-b, Cdk5 and c-Jun N-terminal kinase (JNK) at the Ser/Thr sites mentioned above PubMed:22122372

Appears in Networks:
Annotations
Confidence
High
MeSH
Neurons

p(HGNC:CAMK2A) increases p(HBP:HBP00071, pmod(Ph, Thr, 668)) View Subject | View Object

AICD also contains three phosphorylation sites, including two threonine residues at 654 and 668 and a serine residue at 665. AICD has been found to be phosphorylated by PKC, calcium-calmodulin dependent-kinase II, GSK3-b, Cdk5 and c-Jun N-terminal kinase (JNK) at the Ser/Thr sites mentioned above PubMed:22122372

Appears in Networks:
Annotations
Confidence
High
MeSH
Neurons

p(HGNC:CAMK2A) increases p(HBP:HBP00071, pmod(Ph, Ser, 665)) View Subject | View Object

AICD also contains three phosphorylation sites, including two threonine residues at 654 and 668 and a serine residue at 665. AICD has been found to be phosphorylated by PKC, calcium-calmodulin dependent-kinase II, GSK3-b, Cdk5 and c-Jun N-terminal kinase (JNK) at the Ser/Thr sites mentioned above PubMed:22122372

Appears in Networks:
Annotations
Confidence
High
MeSH
Neurons

p(HGNC:CAMK2A) directlyIncreases p(HGNC:MAPT, pmod(Ph)) View Subject | View Object

Other phosphorylation sites in or near the repeat domain are phosphorylated by microtubule affinity-regulating kinases (MARKs; also known as PAR1 kinases), cyclic AMP-dependent protein kinase (PKA) and Ca2+- or calmodulin-dependent protein kinase II (CaMKII), among others PubMed:26631930

Appears in Networks:

p(HGNC:CAMK2A) directlyIncreases p(HGNC:MAPT, pmod(Ph, Ser, 262)) View Subject | View Object

For example,the phosphorylation of KXGS motifs (particularly Ser262) in the repeat domain of tau by MARK, PKA or CaMKII can reduce the affinity of tau to microtubules PubMed:26631930

Appears in Networks:

act(p(HGNC:CAMK2A)) increases act(complex(GO:"NF-kappaB complex")) View Subject | View Object

The molecular mechanism underlying constitutive activation of NF-κB by glutamate-induced excitatory synaptic neurotransmission has been ascribed to NMDA receptor mediated Ca2+ influx and subsequent activation of CaMKII PubMed:28745240

Appears in Networks:
Annotations
MeSH
Alzheimer Disease

act(p(HGNC:CAMK2A)) increases act(complex(GO:"NF-kappaB complex")) View Subject | View Object

The three well characterized sensors of intracellular calcium – calmodulin/CamKII pathway, PI3K/ Akt pathway, and protein kinase C (PKC) pathway – are known to induce NF-κB activation and couple upstream signal transduction pathways that induce calcium dyshomeostasis to NF-κB activation PubMed:28745240

Appears in Networks:
Annotations
MeSH
Alzheimer Disease

act(p(HGNC:CAMK2A)) increases act(complex(GO:"IkappaB kinase complex")) View Subject | View Object

In addition to CamKII, other kinases activated in response to a rise in cytosolic Ca2+ such as protein kinase C (PKC), phosphatidylinositol-3-kinase (PI3K), and Akt, also activate NF-κB signaling pathway by increasing the phosphorylation and activation of IKK PubMed:28745240

Appears in Networks:
Annotations
MeSH
Alzheimer Disease

act(p(HGNC:CAMK2A)) increases p(MESH:"I-kappa B Kinase", pmod(Ph)) View Subject | View Object

In addition to CamKII, other kinases activated in response to a rise in cytosolic Ca2+ such as protein kinase C (PKC), phosphatidylinositol-3-kinase (PI3K), and Akt, also activate NF-κB signaling pathway by increasing the phosphorylation and activation of IKK PubMed:28745240

Appears in Networks:
Annotations
MeSH
Alzheimer Disease

About

BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.

If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.