STAT3 typically binds to GAS-like elements located in the promoter region of various genes. In the present study, we identified two GAS-like elements in the promoter of miR-155, which suggested that STAT3 binds to the promoter of miR-155.EBP1 has been ascribed to its ability to translocate to the nucleolus. Deletion of EBP1 in mice results in subfertility with more than 50% decrease in the litter size than their wild type or heterozygous counterpart suggesting that EBP1 may potentially play an important role in ovarian function. However, virtually nothing is known about the role of EBP1 in ovarian follicular development, including primordial follicle formation or its regulation by E during primordial follicle formation in the hamster. Therefore, as a first step towards understanding the role of EBP1 in primordial folliculogenesis, the spatio-temporal expression of EBP1 transcript and protein in ovarian cells with respect to primordial follicle formation and its regulation by E were evaluated in the present study. The results of this study provide the first evidence that EBP1, an ERBB3 binding protein, is expressed in perinatal ovary cells and the expression is downregulated in ovarian somatic cells with their differentiation into early granulosa cells of primordial follicles. The presence of only one 48 kDa band in ovarian homogenate corroborates with the results furnished by the manufacturer and validates the specificity of the antibody in detecting EBP1 in the immunoblots. Therefore, it stands to reason that fluorescence generated by the EBP1 antibody in Disorder that frequently presents with co-morbid nonspecific killing reactions but was insufficient as regards specific predatory behavior immunolocalization reflects EBP1 antigen in ovarian cells. Because purified EBP1 protein is unavailable, additional validation of the antibody cannot be done. E regulates EBP1 turnover in developing ovary cells. The high degree of sequence similarity of hamster EBP1 cDNA and amino acid sequences with those of other mammals including the human suggests that this protein is highly conserved across species and also indicates its evolutionary functional importance. EBP1 amino acid sequence contains nucleolar localization sequence, which correlates with punctate EBP1 localization in the nucleolus of ovarian cells. EBP1 also contains a RNA binding site as well as the alpha10 helix sequence, which bind to the transcriptional coactivators or repressors. Potential serine, tyrosine and threonine phosphorylation sites suggest that specific phosphorylation of EBP1 may affect its function. It has been shown that phosphorylation of EBP1 at serine 363 results in its exclusive nuclear localization, and mutation of serine 363 to alanine significantly decreases the ability of EBP1 to repress transcription and suppress cell proliferation. Similarly, phosphorylation of EBP1 at threonine 261 by p21-regulated serine/threonine kinase, PAK1, in MCF-7 breast cancer cell line results in suppression of EBP1 transcriptional activity, reduction in ErbB2 protein levels and induction of tamoxifen resistance, but a threonine to alanine mutation reverses the effect.