A member of the TEA/ATTS domain family, Transcriptional enhancer factor 1 (TEF-1) is a nuclear protein that is expressed in numerous cell types and plays a role in controlling the expression of numerous genes. TEF family members have a highly conserved DNA-binding domain; TEF-1 binds to GT-IIC, SphI/II and M-CAT. TEF-1 also binds to the proximal regulatory element (PRE) of transforming growth factor-alpha, a member of the EGF family that is overexpressed in many types of cancer. Furthermore, TEF-1 represses transcription in placental cells. In vitro, TEF-1 is phosphorylated by several PKC isozymes. TEF-1 is phosphorylated in vivo at serine and threonine residues. Phosphorylation of TEF-1, both in vivo and in vitro, results in a reduction in its DNA-binding capability, which suggests a potential role for TEF-1 in PKC inhibition. TEF-1 also complexes with larger tumor antigen (TAg), and may thus have a role in tumorigenesis. Dimerization of TEF-1 may be important for TEF-1 to function as a regulator of gene transcription.
NTEF-1; NTEF1; Protein GT-IIC; TCF-13; TCF13; TEA domain family member 1; TEA domain family member 1 (SV40 transcriptional enhancer factor); TEAD-1; TEAD1; TEF1; Transcription factor 13; transcriptional enhancer factor 1; Transcriptional enhancer factor TEF-1