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First published online October 27, 2005
doi: 10.1242/10.1242/jcs.02696

Journal of Cell Science 118, 4931-4935 (2005)
Published by The Company of Biologists 2005
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FAK phosphorylation sites mapped by mass spectrometry

Pablo R. Grigera1,*, Erin D. Jeffery2,*, Karen H. Martin1, Jeffrey Shabanowitz2, Donald F. Hunt2,3 and J. Thomas Parsons1,{ddagger}

1 Department of Microbiology, University of Virginia, Charlottesville, VA 22908 USA
2 Department of Chemistry, University of Virginia, Charlottesville, VA 22908 USA
3 Department of Pathology, University of Virginia, Charlottesville, VA 22908 USA



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  		Fig. 1. Identified sites of serine, threonine and tyrosine phosphorylation in FAK. The sequence of chicken FAK (GenBank accession no. M86656) is shown with the amino acids that were identified by mass spectrometry (MS) shown in capital letters. The phosphorylated residues identified by the MS analysis are shown in red. There were two peptides in which the phosphorylated residue could not be distinguished (indicated by brackets). Because T394 was only observed within a peptide containing Y397, a known site of phosphorylation, the phosphorylation status of T394 is questionable.

 


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  		Fig. 2. Distribution of phosphorylation sites in FAK. The domain structure of FAK is shown with the mapped sites of serine (blue stars), threonine (green stars) and tyrosine (red stars) phosphorylation shown below. The sites of sumoylation ({diamondsuit}) and caspase cleavage (*) are indicated.

 




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