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Figure 1 | BMC Biochemistry

Figure 1

From: Identification of four novel phosphorylation sites in estrogen receptor α: impact on receptor-dependent gene expression and phosphorylation by protein kinase CK2

Figure 1

Estrogen receptor α (ERα) phosphorylation sites. The schematic in Figure 1 depicts both previously identified and novel ERα phosphorylation sites with relative locations within the ERα functional domains. Serines 104, 106, 118, and 167 constitute phosphorylation sites within the ligand-independent activation function-1 (AF-1) domain of ERα. S236 is the first phosphorylation site within the DNA binding domain of ERα. Serine 305, threonine 311 and tyrosine 537 are phosphorylation sites identified within the ligand-dependent activation function-2 (AF-2) domain. Indicated in bold italicized type are newly characterized phosphorylation sites of ERα: S46/47, S282, S294 and S559. S46/47 constitutes an additional site of phosphorylation within the AF-1 domain. Serines 282 and 294 are located in the hinge domain of ERα proximal to the DNA binding domain. Of note, S559 is the first phosphorylation site identified in the extreme C-terminal F domain of ERα and other steroid receptors. S154, S212, S294, S554, and S559 have been recently identified or independently confirmed by mass spectrophotometry (11).

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BMC Biochemistry

ISSN: 1471-2091

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