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Table 1 The 3 phosphorylated proteins (HuR, Chain B and p38p) and the 6 phosphopeptides identified and validated (amino acid sequences below the identified proteins) when using SIMAC coupled to MAS by the LTQ ion Trap mass spectrometer are shown in this table.

From: Discovering and validating unknown phospho-sites from p38 and HuR protein kinases in vitroby Phosphoproteomic and Bioinformatic tools

Proteins Phosphopeptides
HuR RNA binding protein gi/1022961 DVEDMFSphR (*)
  VLVDQTTphGLSR
  DANLYSphGLPR (*)
  SLFSSIGEVESphAK (*)
Chain B, Structure Of Appbp-1-Uba3-nedd8-Mgatp-Ubc 12 (c111a), A Trapped Ubiquitin-Like Protein Activation Complex gi/126031226 TphAVINAASGR (*)
P38 MAP Kinase gi/1469306 DLSphSIFR (*)
  1. Around ≥ 3 μg of complex peptides mixture were loaded into SIMAC micro-columns and analyzed by nano-LC-ESI-LTQ ion Trap (Thermo).
  2. In addition when using SIMAC coupled to DDNLMS3 3 proteins were identified: (a) HuR RNA binding protein gi/1022961, (b) P38 MAP Kinase gi/1469306 and (c) Change B, A Trapped Ubiquitin like-protein activation gi/126031226.
  3. (a) From the phosphorylated protein HuR RNA binding protein gi/1022961, 3 phosphopeptides were isolated and validated (K.DVEDMFSR.F, K.DANLYISGLPR.T, R.SLFSSIGEVESAK.L).
  4. (b) From the phosphorylated protein p38 MAP Kinase gi/1469306, one phosphopeptide was isolated and validated (K.DLSSIFR.G).
  5. (c) From the phosphorylated protein Change B, A Trapped Ubiquitin like-protein activation gi/126031226, one phosphopeptide was isolated and validated (R.TAVINAASGR.Q).
  6. [Identified and validated phosphopeptides using SIMAC coupled to DDNLMS3 are distinguished by the symbol (*)]