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
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S56-p - Vimentin (human)
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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