Anti-NUP133 antibody [EPR10809]

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

NUP133 also known as nucleoporin 133 is a component of the nuclear pore complex. This protein weighs approximately 133 kDa. NUP133 localizes to the nuclear envelope and forms part of the structural scaffold of the nuclear pore. You will find expressions of this protein in a variety of cell types across different tissues. As an integral component of the nuclear pore complex NUP133 plays a role in transporting molecules between the nucleus and the cytoplasm.

Biological function summary

This protein is part of the Nup107-160 complex. This complex is essential for the assembly and maintenance of nuclear pores. NUP133 contributes to regulating the bidirectional transport of proteins and RNA across the nuclear envelope. It is involved in maintaining the structural integrity of the nuclear pore complex ensuring the selective exchange of substances between the nucleus and the cytoplasm. By doing so NUP133 influences various cellular processes like gene expression and DNA replication.

Pathways

The protein NUP133 engages primarily in the nucleocytoplasmic transport pathway. Within this framework it collaborates closely with other nucleoporins such as NUP107 and NUP160. The protein is also relevant in the regulation of the cell cycle as it ensures the proper formation and disassembly of nuclear pores during cell division. The interaction with other proteins within these pathways highlights the critical roles NUP133 fulfills in fundamental cellular activities.

Associated diseases and disorders

Studies link NUP133 to certain cancer types including ovarian cancer and glioblastoma. Mutations or misregulation of NUP133 can lead to disturbances in nuclear transport and cellular proliferation contributing to tumorigenesis. The protein interacts with other members of the nuclear pore complex such as NUP85 underlining its potential impact in cancer progression. Understanding these associations may inform therapeutic strategies targeting nuclear transport pathways in related diseases.