Speckled Protein 140 (SP140) is an immune-specific chromatin reader that has previously been reported to control immune-related gene expression and has been linked to immune-mediated diseases such as multiple sclerosis, Crohn's disease, and chronic lymphocytic leukemia. The precise molecular mechanisms by which SP140 regulates gene expression remain unknown. SP140 contains multiple chromatin reader domains to interact with chromatin, such as the plant homeodomain (PHD), bromodomain (BRD) and a SAND domain. Although SP140 can bind directly to chromatin, there are conflicting reports about the specifics of its genomic occupancy or its influence on the transcription of occupied genes. We engineered a degron-tagged SP140 in a human B cell line, enabling rapid ablation of this protein. By using this dTAG model, we confidently mapped the genome binding sites of SP140. CUT&Tag profiling revealed that SP140 binds ubiquitously to non-methylated gene promoters, potentially via its SAND domain, and exhibits co-occupancy with other chromatin regulatory complexes. These findings provide new insights into the binding preferences and the potential regulatory role of SP140 in immune cells. By identifying SP140 specific genomic targets, this work offers a framework for further investigation into its gene regulatory function and its contribution to the development of immune-mediated diseases.