The myxoid/round cell liposarcoma oncogene TLS-CHOP belongs to a growing family of tumor type specific fusion genes generated by chromosome translocations. We have recently found that the TLS-CHOP fusion protein is localized to well-defined nuclear structures, a pattern distinct from normal TLS or CHOP cellular distribution. Since location and function are intimately coupled in the organized nucleus, the aberrant localization of the fusion protein most certainly reflects the oncogenic activities of TLS-CHOP. We have investigated the role of the functionally unknown, SYGQ-rich, TLS N-terminal in the localization of TLS-CHOP to nuclear structures. Here, we report the temperature-dependent localization of TLS-CHOP to splicing factor compartments and association with Cajal bodies. Further, mutational analysis of the N-terminal part of green fluorescent protein-tagged TLS-CHOP identifies a region within the N-terminal required for colocalization with the splicing factor SC-35.