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. 2007 Jun 20;2(6):e536. doi: 10.1371/journal.pone.0000536

Table 1. Tau phosphorylation sites identified in sod2 null mouse brain tissue.

residues Detected by Antibody % change a mass spec ID b phospho peptide observed by mass spectrometry P site ID
Thr-205 Yes 728 +/− c MS c
Ser-404 Yes 309 +/− S396PVVSGDTpS404PR406 MS/MS d
Ser-396 Yes 210 +/− T386DHGAEIVYKpS396PVVSGDTpS404PR406 MS e
Ser-214 Yes 63 + T212PpS214LPTPPTREPK224 MS/MS
Thr-231 Yes 147 + V226AVVRpT231PPKSPSASK240 MS/MS
Ser-202 Yes NS + S195GYSSPGpS202PGTPGSR209 MS/MS
Thr-181 No + T175TPSPKpT181PPGSGEPPK190 MS/MS f
Ser-159 ND + G156AApS159PAQKGTSNATRIPAK174 MS/MS

a: Percent changes of listed residue in sod2 null mice relative to sod2wild-types (normalized to 100%, see Figure 1), both treated with EUK189 at 1 mg/kg quantitated by Western blotting with monoclonal antibodies for the indicated tau residues, NS– not significant, ND – not done.

b: identifications were positive (+) if a MS/MS spectrum could be unambiguously interpreted to identify a unique phosphorylation site. In three cases (+/−) assignments were based on MS or MS/MS data and alternative sites were possible.

c: several matching phospho peptides observed by ESI-MS (i.e., peptides: mono-/di-phosph. S195-R209 and mono-/di-phosph. S181-R209);

d: Phosphorylate site possibly on Ser-404, Thr-403 or Ser-400;

e: peptide observed with 1P and 2P groups;

f: differences in peptide sequence (human vs. mouse) likely accounting for negative antibody result (homologous human peptide: TPPAPKTPPSSGEPPK);

g: no antibody available for Ser-159.