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

Appears in Networks 1

In-Edges 8

a(MESH:"JNK Mitogen-Activated Protein Kinases") 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

bp(HBP:HBP00073) association p(HBP:HBP00071, pmod(Ph, Thr, 654)) View Subject | View Object

Such phosphorylation may affect APP processing or the binding of AICD-interacting proteins, thus affecting the function of AICD (Gandy et al. 1988; Suzuki et al. 1994; Iijima et al. 2000; Inomata et al. 2003) PubMed:22122372

act(p(HBP:HBP00071)) association p(HBP:HBP00071, pmod(Ph, Thr, 654)) View Subject | View Object

Such phosphorylation may affect APP processing or the binding of AICD-interacting proteins, thus affecting the function of AICD (Gandy et al. 1988; Suzuki et al. 1994; Iijima et al. 2000; Inomata et al. 2003) PubMed:22122372

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

p(HGNC:CDK5) 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

p(HGNC:GSK3B) 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

p(HGNC:PRKCA) 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

Out-Edges 2

p(HBP:HBP00071, pmod(Ph, Thr, 654)) association bp(HBP:HBP00073) View Subject | View Object

Such phosphorylation may affect APP processing or the binding of AICD-interacting proteins, thus affecting the function of AICD (Gandy et al. 1988; Suzuki et al. 1994; Iijima et al. 2000; Inomata et al. 2003) PubMed:22122372

p(HBP:HBP00071, pmod(Ph, Thr, 654)) association act(p(HBP:HBP00071)) View Subject | View Object

Such phosphorylation may affect APP processing or the binding of AICD-interacting proteins, thus affecting the function of AICD (Gandy et al. 1988; Suzuki et al. 1994; Iijima et al. 2000; Inomata et al. 2003) PubMed:22122372

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.