RT Journal Article
SR Electronic
T1 Conservation and structural analysis of the Xenopus laevis phospho-proteome
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 009100
DO 10.1101/009100
A1 Jeffrey R. Johnson
A1 Silvia D. Santos
A1 Tasha Johnson
A1 Ursula Pieper
A1 Andrej Sali
A1 Nevan J. Krogan
A1 Pedro Beltrao
YR 2014
UL http://biorxiv.org/content/early/2014/09/14/009100.abstract
AB The African clawed frog Xenopus laevis is an important model organism for studies in developmental and cell biology, including cell-signaling. However, our knowledge of X. laevis protein post-translational modifications remains scarce. Here, we used a mass spectrometry-based approach to survey the phosphoproteome of this species, compiling a list of 3225 phosphosites. We used this resource to study the conservation between the phosphoproteomes of X. laevis and 13 other species. We found that the degree of conservation of phosphorylation across species is predictive of sites with known molecular function, kinase interactions and functionally relevant phospho-regulatory interactions. In addition, using comparative protein structure models, we find that phosphosites within structured domains tend to be located at positions with high conformational flexibility. A fraction of sites appear to occur in inaccessible positions and have the potential to regulate protein conformation.