Curated Information
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Curated Information Page
PubMed Id: 22096607 
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.
Ye DZ, Jin S, Zhuo Y, Field J (2011) p21-Activated kinase 1 (Pak1) phosphorylates BAD directly at serine 111 in vitro and indirectly through Raf-1 at serine 112. PLoS One 6, e27637 22096607
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.
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S74-p - BAD (human)
Orthologous residues
BAD (human): S74‑p, BAD (mouse): S111‑p, BAD (rat): S112‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody, western blotting
 Disease tissue studied:  lung cancer, non-small cell lung cancer, neurofibromatosis type 1
 Relevant cell lines - cell types - tissues:  293T (epithelial), 90-8, NCI-H358 (pulmonary), RT4 (Schwann), ST88-14 (neuron), STS26
 Cellular systems studied:  cell lines
 Species studied:  human, rat
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE PAK1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PAK1 (human) transfection of inactive enzyme, transfection of constitutively active enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
GW 5074 no change compared to control
PD98059 no change compared to control
rapamycin no change compared to control
H-89 no change compared to control
BAY 43-9006 no change compared to control
IPA-3 decrease
Downstream Regulation
 Effect of modification (function):  molecular association, regulation, phosphorylation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
Bcl-2 (human) Disrupts pull-down assay
 Comments:  mutation of this site to Ala reduces S75 phosphorylation

S75-p - BAD (human)
Orthologous residues
BAD (human): S75‑p, BAD (mouse): S112‑p, BAD (rat): S113‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody, western blotting
 Relevant cell lines - cell types - tissues:  293T (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  human
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
GW 5074 decrease
PD98059 no change compared to control
rapamycin no change compared to control
H-89 no change compared to control
forskolin increase
H-89 forskolin inhibit treatment-induced increase
GW 5074 forskolin no effect upon treatment-induced increase
IPA-3 decrease
BAY 43-9006 decrease
PAK1 (human) increase
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
Bcl-2 (human) Disrupts pull-down assay

S99-p - BAD (human)
Orthologous residues
BAD (human): S99‑p, BAD (mouse): S136‑p, BAD (rat): S137‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody, western blotting
 Relevant cell lines - cell types - tissues:  293T (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  human
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
Bcl-2 (human) Disrupts pull-down assay
14-3-3 beta (human) Induces pull-down assay


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