Curated Information
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Curated Information Page
PubMed Id: 12851456 
Xie J, et al. (2003) Protein kinase A phosphorylation modulates transport of the polypyrimidine tract-binding protein. Proc Natl Acad Sci U S A 100, 8776-81 12851456
This page summarizes selected information from the record 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.
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S16-p - hnRNP I (human)
Orthologous residues
hnRNP I (human): S16‑p, hnRNP I (mouse): S16‑p, hnRNP I iso2 (mouse): S16‑p, hnRNP I (rat): S16‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site, phospho-antibody, phosphoamino acid analysis, phosphopeptide mapping
 Relevant cell lines - cell types - tissues:  293 (epithelial), 3T3 (fibroblast) [SHP-2 (mouse), homozygous knockout], oocyte [CPEB (mouse)], PC-12 (chromaffin)
 Cellular systems studied:  cell lines, primary cells
 Species studied:  frog, human, mouse, rat
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE PKACA (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKACA (human) pharmacological activator of upstream enzyme, genetic transfer of constitutively active upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
cAMP analog increase
forskolin increase
Downstream Regulation
 Effect of modification (function):  intracellular localization


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