Curated Information

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Curated Information Page

PubMed Id: 16629905

This page summarizes selected information from the article referenced above and curated into PhosphoSitePlus^®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus^®, click here.

Oguri T, et al. (2006) Vimentin-Ser82 as a memory phosphorylation site in astrocytes. Genes Cells 11, 531-40 16629905

Only sites from this record are displayed on this page. Click on the protein name to open the protein page, and on the RSD number to open the site page. For the complete dataset, click the download button, on the right.

S39-p - vimentin (rat)

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Orthologous residues

vimentin (human): S39‑p, vimentin (mouse): S39‑p, vimentin (rat): S39‑p, vimentin (hamster): S39‑p, vimentin (cow): S39‑p

Characterization

Methods used to characterize site in vivo: phospho-antibody

Relevant cell lines - cell types - tissues: astrocyte-'brain, cerebrum'

Cellular systems studied: primary cultured cells

Species studied: rat

Enzymes shown to modify site in vitro:

Type	Enzyme
PHOSPHATASE	PPP1CA (human)
KINASE	CaMK2-alpha (human)

Upstream Regulation

Treatments, proteins and their effect on site modification:

Treatments	Referenced Treatments	Effect
PGE2a		increase
ionomycin		increase
EGTA	ionomycin	inhibit treatment-induced increase
EGTA, calyculin A	ionomycin	augment treatment-induced increase
okadaic acid, EGTA	ionomycin	inhibit treatment-induced increase

S83-p - vimentin (rat)

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