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Tau Modifications v1.9.5

Tau Modifications Sections of NESTOR

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p(HGNC:SUMO1) increases p(HGNC:APP, pmod(Sumo, Lys, 595)) View Subject | View Object

Lysines 587 and 595 of APP, immediately adjacent to the site of beta-secretase cleavage, are covalently modified by SUMO proteins in vivo. Sumoylation of these lysine residues is associated with decreased levels of Abeta aggregates. The results demonstrate that the SUMO E2 enzyme (ubc9) is present within the endoplasmic reticulum, indicating how APP, and perhaps other proteins that enter this compartment, can be sumoylated. PubMed:18675254

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p(HGNC:SUMO2) increases p(HGNC:APP, pmod(Sumo, Lys, 595)) View Subject | View Object

Lysines 587 and 595 of APP, immediately adjacent to the site of beta-secretase cleavage, are covalently modified by SUMO proteins in vivo. Sumoylation of these lysine residues is associated with decreased levels of Abeta aggregates. The results demonstrate that the SUMO E2 enzyme (ubc9) is present within the endoplasmic reticulum, indicating how APP, and perhaps other proteins that enter this compartment, can be sumoylated. PubMed:18675254

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Out-Edges 1

p(HGNC:APP, pmod(Sumo, Lys, 595)) decreases a(CHEBI:"amyloid-beta") View Subject | View Object

Lysines 587 and 595 of APP, immediately adjacent to the site of beta-secretase cleavage, are covalently modified by SUMO proteins in vivo. Sumoylation of these lysine residues is associated with decreased levels of Abeta aggregates. The results demonstrate that the SUMO E2 enzyme (ubc9) is present within the endoplasmic reticulum, indicating how APP, and perhaps other proteins that enter this compartment, can be sumoylated. PubMed:18675254

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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.