Table I Identification of O-GlcNAc modification, phosphorylation, and methylation sites on human Runx2
PeptideResiduesModificationSiteObserved (m/z)ΔM [ppm]ChargeMS/MS ModePreviously described?
RFSPPSSSLQPGK26–38Phospho28489.900.36+3HCD, ETDYes (17, 21, 58, 59, 88)
RFSPPSSSLQPGK26–38Phospho/HexNAcp28/g32557.600.41+3HCD, ETDNo
FSPPSSSLQPGK27–38HexNAc32717.861.52+2HCD, ETDNo
FSPPSSSLQPGK27–38HexNAc33717.861.52+2HCD, ETDNo
IPHPSMR252–258Methyl258426.23−0.56*+2HCDNo
VGVPPQNPRPSLNSAPSPFNPQGQSQITDPR259–289Methyl2671099.89−5.63*+3HCDNo
VGVPPQNPRPSLNSAPSPFNPQGQSQITDPR259–289Dimethyl2671104.90−6.72*+3HCDYes (62)
RISDDDTATSDFC[Cam] LWPSTLSK338–358Phospho3401248.55−0.99+2HCDYes (17, 21)
KSQAGASELGPFSDPR359–374HexNAc371617.640.01+3HCD, ETDNo
QFPSISSLTESR375–386Methyl386683.35−1.48+2HCDNo
QFPSISSLTESRFSNPR375–391Methyl386984.010.15+2HCDNo
QFPSISSLTESRFSNPR375–391Dimethyl386991.521.57+2HCDNo
  • Bold residues denote localization of PTMs either by HCD or ETD MS/MS. [Cam] = carbamidomethyl. Peptide precursor masses were recalibrated in MaxQuant. Mass errors of peptides only detected by Proteome Discoverer are indicated with an asterisk.