Curated Information

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Curated Information Page

PubMed Id: 15766329

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.

Tang DD, Bai Y, Gunst SJ (2005) Silencing of p21-activated kinase attenuates vimentin phosphorylation on Ser-56 and reorientation of the vimentin network during stimulation of smooth muscle cells by 5-hydroxytryptamine. Biochem J 388, 773-83 15766329

S56-p - vimentin (human)

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Orthologous residues

vimentin (human): S56‑p, vimentin (mouse): S56‑p, vimentin (rat): S56‑p, vimentin (hamster): S55‑p, vimentin (cow): S56‑p

Characterization

Methods used to characterize site in vivo: mutation of modification site, phospho-antibody

Relevant cell lines - cell types - tissues: 'muscle, skeletal'

Cellular systems studied: tissue

Species studied: dog

Upstream Regulation

Potential in vivo enzymes for site:

Type	Enzyme	Evidence	Notes
KINASE	PAK1 (human)	antisense inhibition of upstream enzyme

Treatments, proteins and their effect on site modification:

Treatments	Referenced Treatments	Manipulated Protein	Referenced Protein	Effect	Notes
5-HT				increase

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