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TEF1 (Transcriptional enhancer factor 1), a member of the TEA/ATTS domain family, 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.
2610024B07Rik; AA; B230114H05Rik; Gtrgeo5; mTEF-1; N TEAD1; NTEF1; NTEF-1; protein GT-IIC; REF1; Tcf13; TCF-13; TEA domain family member 1; TEA domain family member 1 (SV40 transcriptional enhancer factor); TEA domain transcription factor 1; TEAD1; TEAD-1; TEF1; TEF-1; Transcription factor 13; transcriptional enhancer factor 1; transcriptional enhancer factor TEF-1
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