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p(HGNC:PIN1, pmod(Ph, Ser, 65))

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Entity

Name
PIN1
Namespace
hgnc
Namespace Version
20180906
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/hgnc-names.belns

Appears in Networks 1

Tau Modifications v1.9.5

Tau Modifications Sections of NESTOR

In-Edges 2

p(HGNC:MAPT) negativeCorrelation p(HGNC:PIN1, pmod(Ph, Ser, 65)) View Subject | View Object

Because Pin1 has at least 4 major isovariants in addition to the native polypeptide, this means that Pin1 has 4 (possibly more) posttranslational modifications including phosphorylation at 3 sites (Ser16 and Ser65/Ser71), N-acetylation (amino-terminus and Lys46) and oxidation (Met130 and 146). In all experimental conditions, including tau-overexpressing cells, tau transgenic mice and AD brains, global levels of Pin1 posttranslational modifications were decreased compared with control conditions. PubMed:22926167

Appears in Networks:

p(HGNC:PIN1) hasVariant p(HGNC:PIN1, pmod(Ph, Ser, 65)) View Subject | View Object

Appears in Networks:

Out-Edges 2

p(HGNC:PIN1, pmod(Ph, Ser, 65)) negativeCorrelation p(HGNC:MAPT) View Subject | View Object

Because Pin1 has at least 4 major isovariants in addition to the native polypeptide, this means that Pin1 has 4 (possibly more) posttranslational modifications including phosphorylation at 3 sites (Ser16 and Ser65/Ser71), N-acetylation (amino-terminus and Lys46) and oxidation (Met130 and 146). In all experimental conditions, including tau-overexpressing cells, tau transgenic mice and AD brains, global levels of Pin1 posttranslational modifications were decreased compared with control conditions. PubMed:22926167

Appears in Networks:

p(HGNC:PIN1, pmod(Ph, Ser, 65)) increases act(p(HGNC:PIN1)) View Subject | View Object

In fact, phosphorylation of Pin1 at Ser16 inhibits its nuclear localization possibly through inhibition of Pin1 substrate-binding property (Lu et al., 2002) while phosphorylation at Ser65 does not change activity of localization but stabilizes Pin1 by preventing its ubiquitination PubMed:22926167

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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.