Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. NUP98 and NUP96 are involved in the bidirectional transport across the NPC. May anchor NUP153 and TPR to the NPC. In cooperation with DHX9, plays a role in transcription and alternative splicing activation of a subset of genes. Involved in the localization of DHX9 in discrete intranuclear foci (GLFG-body). Part of the nuclear pore complex (NPC). Interacts directly with NUP96. Part of the Nup160 subcomplex in the nuclear pore which is composed of NUP160, NUP133, NUP107 and NUP96; this complex plays a role in RNA export and in tethering NUP98 and NUP153 to the nucleus. Interacts with RAE1. Does not interact with TPR (By similarity). Interacts directly with NUP88 and NUP214, subunits of the cytoplasmic filaments of the NPC (PubMed:22480613). Interacts (via N-terminus) with DHX9 (via DRBM, OB-fold and RGG domains); this interaction occurs in a RNA-dependent manner and stimulates DHX9-mediated ATPase activity (By similarity). Localized to the nucleoplasmic side of the nuclear pore complex (NPC), at or near the nucleoplasmic basket. Dissociates from the dissasembled NPC structure early during prophase of mitosis. Colocalized with NUP153 and TPR to the nuclear basket of NPC. Colocalized with DHX9 in diffuse and discrete intranuclear foci (GLFG-body). Remains localized to the nuclear membrane after poliovirus (PV) infection. Contains G-L-F-G repeats. The FG repeat domains have a direct role in the transport (By similarity). Autoproteolytically cleaved to yield Nup98 and Nup96 or Nup98 only, respectively. Cleaved Nup98 is necessary for the targeting of Nup98 to the nuclear pore and the interaction with Nup96. Belongs to the nucleoporin GLFG family. Contaminating sequence. Potential poly-A sequence. Contaminating sequence. Potential poly-A sequence. Contaminating sequence. Potential poly-A sequence.