Figure 2.
Relationship of human clinical genetic mutations and GATA2 posttranslational modification sites. (A) Multisite GATA2 phosphorylation model. Extracellular signal–regulated kinase (ERK)/p38α docks on the GATA2 DEF motif, S192 is phosphorylated, and other serine residues (S73, S119, S290, and S340) are phosphorylated subsequently. (B) Top, GATA2 protein structure. N- and C-zinc fingers, DEF motif, phosphorylated residues, and acetylated residues are indicated. Bottom, amino acid sequence from 165 aa to 200 aa of GATA2 protein. Phosphorylated residues, DEF motif, and mutations reported by ClinVar/ClinGen are indicated.

Relationship of human clinical genetic mutations and GATA2 posttranslational modification sites. (A) Multisite GATA2 phosphorylation model. Extracellular signal–regulated kinase (ERK)/p38α docks on the GATA2 DEF motif, S192 is phosphorylated, and other serine residues (S73, S119, S290, and S340) are phosphorylated subsequently. (B) Top, GATA2 protein structure. N- and C-zinc fingers, DEF motif, phosphorylated residues, and acetylated residues are indicated. Bottom, amino acid sequence from 165 aa to 200 aa of GATA2 protein. Phosphorylated residues, DEF motif, and mutations reported by ClinVar/ClinGen are indicated.

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