Transmembrane Protein 48 (TMEM48)

NDC1 has a role in the assembly of nuclear pore complexes and the nuclear envelope in vivo and in vitro. Rat Ndc1 interacted with Nup53 in vitro. NDC1 depletion by RNA interference reduced binding of the Nup53-Nup93 subcomplex to the assembling nuclear pore complex in HeLa cells.

The deduced 611-amino acid protein has 6 transmembrane domains and several putative phosphorylation sites. Immunohistochemical analysis detected NDC1 along the nuclear envelope, where it colocalized with p62 (NUP62) at the nuclear rim. In HeLa cells, the apparent molecular mass of endogenous NDC1 was reduced following phosphatase treatment.