This work explores the surface properties of the transcription factor Fra-1 and compares them with those of two other immediate early proteins, c-Fos and c-Jun, to establish generalities and differences in the surface behavior and interaction with phospholipids of this type of proteins. We present several experimental clues of the flexible nature of Fra-1, c-Fos, and c-Jun that support sequence-based predictions of their intrinsical disorder. The values of surface parameters for Fra-1 are similar in general to those of c-Fos and c-Jun. However, we find differences in the interactions of the three proteins with phospholipids. The closely related Fra-1 and c-Fos share affinity for anionic lipids but the former has more affinity for a condensed phase and senses a change in DPPC phase, while the latter has more affinity for an expanded phase. These features are in contrast with our previous finding that c-Jun is not selective for phospholipid polar head group or charge. We show here that at least some immediate early transcription factors can interact with membrane phospholipids in a distinguishable manner, and this shall provide a basis for their potential capacity to regulate membrane-mediated cellular processes.