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A systematic comparative and structural analysis of protein phosphorylation sites based on the mtcPTM database

José L Jiménez1*, Björn Hegemann2, James RA Hutchins2, Jan-Michael Peters2 and Richard Durbin1

Author Affiliations

1 Wellcome Trust Sanger Institute, Genome Campus, Hinxton, Cambridge, CB10 1SA, UK

2 Research Institute of Molecular Pathology (IMP), Dr. Bohr-Gasse 7, 1030 Vienna, Austria

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Genome Biology 2007, 8:R90  doi:10.1186/gb-2007-8-5-r90

Published: 23 May 2007

Additional files

Additional data file 1:

The table provides further information about the modeling as well as mtcPTM links for each protein described in Figure 4. For each entry, the columns represent the corresponding Figure number (FIGURE), Ensembl identifier (PID), link to mtcPTM (mtcPTM link), start (Nt) and end (Ct) of the structure with respect to the full-length sequence, PDB template used for the modeling (PDBID) as well as the pair-wise sequence identity (IDENT), the position of the phosphosite (RESIDUE), experimental source (EXPERIMENT), the termini involved (TAIL), and the distance to the structured domain (DISTANCE).

Format: XLS Size: 11KB Download file

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Additional data file 2:

The table provides further information about the modelling as well as mtcPTM links for each protein described in Figures 8 to 10. For each entry, the columns represent the same fields described in Additional data file 1, along with the addition of two new columns containing the percentage of solvent accessibility for the whole side chain (SA-side) or only for its polar atoms (SA-polar).

Format: XLS Size: 21KB Download file

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