Curated Information
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PubMed Id: 15806160 
Sutherland BW, et al. (2005) Akt phosphorylates the Y-box binding protein 1 at Ser102 located in the cold shock domain and affects the anchorage-independent growth of breast cancer cells. Oncogene 24, 4281-92 15806160
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.
Information from this record has been curated, but not yet edited in PhosphoSitePlus® and may be incomplete.
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S473-p - Akt1 (human)
Orthologous residues
Akt1 (human): S473‑p, Akt1 (mouse): S473‑p, Akt1 (rat): S473‑p, Akt1 (fruit fly): S586‑p, Akt1 (cow): S473‑p
 Methods used to characterize site in vivo phospho-antibody, western blotting
 Disease tissue studied:  breast cancer
 Relevant cell lines - cell types - tissues:  breast, MDA-MB231 (breast cell)
 Cellular systems studied:  cell lines, tissue
 Species studied:  human
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
IGF-1 increase

S102-p - YB-1 (human)
Orthologous residues
YB‑1 (human): S102‑p, YB‑1 (mouse): S100‑p, YB‑1 (rat): S100‑p
 Methods used to characterize site in vivo mutation of modification site
 Disease tissue studied:  breast cancer
 Relevant cell lines - cell types - tissues:  MCF-7 (breast cell)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Akt1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Akt1 (human) modification site within consensus motif, co-immunoprecipitation
Downstream Regulation
 Effect of modification (function):  intracellular localization
 Effect of modification (process):  cell growth, altered

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