Structure of the human GATA1 protein. GATA1 mutations found in patients with congenital red blood cell disorders and thrombocytopenias are indicated, with their clinical manifestation and the possible molecular mechanisms underpinning them.^1,9,10 TAD, N-terminal activation domain deleted by missense mutations resulting in expression of GATA1short associated with DBA and transient myeloproliferative disease in Down syndrome. Amino acids 300 to 320 located C-terminally to the second DNA binding ZF are shown, with R307 shown in red and phosphorylatable S310 shown in green. The AKT phosphorylation consensus sequence is underlined. The acetylatable lysine cluster is shown in bold. Amino acids 300 to 320 largely overlap the IDR described by Ludwig et al. aa, amino acids; DBA, Diamond-Blackfan anemia; DS-TMD, transient myeloproliferative disease associated with Down syndrome.