Results for Q14011


Charge and fold propensity (Uversky et al 2000) scores are calculated over a sliding, 21 amino acid window.

Changes to charge and fold propensity upon phosphorylation are depicted in lighter shades.

The location of phosphorylation sites (as recorded in UniProt) and Pfam domains are displayed to assist in functional interpretation of IDPs.



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Plot Descriptions


  1. Windowed charge score per amino acid:

    Displays net charge per residue calculated over a sliding, overalpping 21 amino acid window. The dark blue and red colors represent the positive and negative charge scores per amino acid before phosphorylayion. Changes to the net charge upon phosphorylation are depicted in light blue and red shades.

  2. Windowed fold propensity per amino acid:

    Displays fold propensity per residue calculated over a sliding, overlapping 21 amino acid window. The dark yellow and blue colors represent the positive and negative fold propensity scores per amino acid before phosphorylation. Changes to the fold propensity upon phosphorylation are shown in light yellow and blue shades. An additional sawtooth window is included to smooth structured and intrinsically disordered regions displayed on the plot.

  3. Phosphorylation sites:

    Displays the location of phosphorylation sites in the sequence (if any). Phosphoserine is shown in blue, phosphothreonine in green, and phosphotyrosine in orange. For proteins with no phosphorylation, the plot will remain blank.

  4. Pfam domains:

    Displays Pfam domains across the sequence (if any). If there are none recorded in the Pfam database the plot will remain blank.