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. 2017 Feb 14;12(2):e0172020. doi: 10.1371/journal.pone.0172020

Table 1. Phosphorylated amino acid residues identified by mass spectrometry.

In vitro phosphorylated HNF4α was subjected to mass spectrometry analysis. The fragments containing the phosphorylated amino acid residues correspond to phosphorylation sites on the HNF4α protein. Detected phosphorylation sites (serine/threonine residues) in the cryptic fragments are marked bold and underlined. Affected phosphorylation sites appear in the DNA binding domain (DBD), the hinge, the ligand-binding domain (LBD) and the C-terminus of HNF4α, as well.

Sequence Identified phosphorylation sites Part of HNF4α
KNHMYSCR S95 DBD
QNERDRISTRRSSYED S138/T139 hinge
QNERDRISTRRSSYED S142/S143 hinge
STRRSSYEDSSLPSINALLQ S147/S148 hinge
STRRSSYEDSSLPSIN S151 hinge
EVLSRQITSPVSGIN T166/S167 LBD
HCPELAEMSRVSIR S262, S265 LBD
GKIKRLRSQVQVSLED S313 C-terminus
SAIPQPTITKQE S451, T457, T549 C-terminus