FASEB J.
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Table 1. Post-translational modifications of Cx26 and Cx32

A.
Source m/z Calc m/z {Delta} Error (ppm) Sequence Domain Modification

Mouse 1650.816 1634.821 15.99 -0.28 MDWGTLQSILGGVNK (MSO: 1) 1–15 NT HYDR
HeLa 1714.810 1634.821 79.97 -13.45 MDWGTLQSILGGVNK (MSO: 1) 1–15 NT PHOS
Mouse 1308.656 1264.642 43.99 -18.54 NEFKDIEEIK 113–122 CL GGLU

B.
Source m/z Calc m/z {Delta} Error (ppm) Sequence Domain Modification

Mouse 1820.873 1740.874 79.97 -18.1 MNWTGLYTLLSGVNR (MSO: 1) 1–15 NT PHOS
HeLa 1756.867 1740.874 15.99 0.93 MNWTGLYTLLSGVNR (MSO: 1) 1–15 NT HYDR
HeLa 1820.865 1740.874 79.97 -13.71 MNWTGLYTLLSGVNR (MSO: 1) 1–15 NT PHOS
Mouse 1772.883 1728.903 43.99 5.37 LEGHGDPLHLEEVKR 108–122 CL GGLU
HeLa 1772.867 1728.903 43.99 14.40 LEGHGDPLHLEEVKR 108–122 CL GGLU
HeLa 925.397 845.438 79.97 7.48 KGSGFGHR 231–238 CT PHOS
HeLa 1514.668 1434.712 79.97 7.06 GSGFGHRLSPEYK 232–244 CT PHOS
Mouse 1036.524 798.287 238.23 -7.16 SDRCSAC (1xCys_CAM) 277–283 CT PALM

Differences in post-translational modification of mouse and HeLa Cx26 (A) and Cx32 (B) cytoplasmic domains are highlighted. Residues likely carrying the modifications are bolded and underlined. All modified peptides were also found unmodified in the same digest. See Text and Supplemental Data for further details. Modifications: GGLU, {gamma}-carboxyglutamate; HYDR, hydroxylation; PALM, palmitoylation; PHOS, phosphorylation.





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