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Figure 6 | Biology Direct

Figure 6

From: Cooperativity within proximal phosphorylation sites is revealed from large-scale proteomics data

Figure 6

Structural and biochemical features of pS/pT sites. (A) The tendency of pS/pT sites to be inside/outside a domain. The proportions of being inside or outside a Pfam domain are measured for: (i) all amino acids, (ii) all S/T phosphosites, (iii) only S/T phosphosites with a near neighbor, (iv) all Y phosphosites and (v) only Y phosphosites with a near neighbor. (B) Distribution of secondary structure elements. The proportions of being coiled, in α-Helix or β-sheet for: (i) S/T positions that are not phosphosites (~12,000 random positions) (ii) all S/T phosphosites (~18,300 sites) where these are divided to: (iii) only S/T phosphosites with a near neighbor (~8400 sites) (iv) only S/T phosphosites without a near neighbor (~9900 sites). (C) Distribution of ordered and disordered elements. The proportions of being in disordered regions: (i) S/T positions that are not phosphosites (~36,700 random positions) (ii) all S/T phosphosites (~36,000 sites) where these are divided to: (iii) only S/T phosphosites with a near neighbor (~16,700 sites) (iv) only S/T phosphosites without a near neighbor (~19,200 sites).

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