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NUP153
Nucleoporin 153 (Nup153) is a protein which in humans is encoded by the ''NUP153'' gene. It is an essential component of the basket of nuclear pore complexes (NPCs) in vertebrates, and is required for the anchoring of NPCs. It also acts as the docking site of an importing karyopherin. On the cytoplasmic side of the NPC, Nup358 fulfills an analogous role. Background Nuclear pore complexes are extremely elaborate structures that mediate the regulated movement of macromolecules between the nucleus and cytoplasm. These complexes are composed of at least 100 different polypeptide subunits, many of which belong to the nucleoporin family. Nucleoporins are pore complex-specific glycoproteins characterized by cytoplasmically oriented O-linked N-acetylglucosamine residues and numerous repeats of the pentapeptide sequence XFXFG. Structure Nucleoporin 153 has a mass of 153 kDA (hence its name). It is filamentous, and it contains three distinct domains: an N-terminal region within which a ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
SENP2
Sentrin-specific protease 2 is an enzyme that in humans is encoded by the ''SENP2'' gene. Function SUMO1 (UBL1; MIM 601912) is a small ubiquitin-like protein that can be covalently conjugated to other proteins. SENP2 is one of a group of protease enzymes that process newly synthesized SUMO1 into the conjugatable form and catalyze the deconjugation of SUMO1-containing species. upplied by OMIMref name="entrez"/> Interactions SENP2 has been shown to interact with NUP153 Nucleoporin 153 (Nup153) is a protein which in humans is encoded by the ''NUP153'' gene. It is an essential component of the basket of nuclear pore complexes (NPCs) in vertebrates, and is required for the anchoring of NPCs. It also acts as the doc .... References Further reading * * * * * * * * * * {{gene-3-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
KPNB1
Importin subunit beta-1 is a protein that in humans is encoded by the ''KPNB1'' gene. Function Nucleocytoplasmic transport, a signal- and energy-dependent process, takes place through nuclear pore complexes embedded in the nuclear envelope. The import of proteins containing a classical nuclear localization signal (NLS) requires the NLS import receptor, a heterodimer of importin alpha and beta subunits. Each of these subunits are part of the karyopherin family of proteins. Importin alpha binds the NLS-containing cargo in the cytoplasm and importin beta docks the complex at the cytoplasmic side of the nuclear pore complex. In the presence of nucleoside triphosphates and the small GTP binding protein Ran, the complex moves into the nuclear pore complex and the importin subunits dissociate. Importin alpha enters the nucleoplasm with its passenger protein and importin beta remains at the pore. Interactions between importin beta and the FG repeats of nucleoporins are essential in tra ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nuclear Pore Complexes
The nuclear pore complex (NPC), is a large protein complex giving rise to the nuclear pore. A great number of nuclear pores are studded throughout the nuclear envelope that surrounds the eukaryote cell nucleus. The pores enable the nuclear transport of macromolecules between the nucleoplasm of the nucleus and the cytoplasm of the cell. Small molecules can easily diffuse through the pores. Nuclear transport includes the transportation of RNA and ribosomal proteins from the nucleus to the cytoplasm, and the transport of proteins (such as DNA polymerase and lamins), carbohydrates, signaling molecules, and lipids into the nucleus. Each nuclear pore complex can actively mediate up to 1000 translocations per second. The nuclear pore complex consists predominantly of a family of proteins known as nucleoporins (Nups). Each pore complex in the human cell nucleus is composed of about 1,000 individual protein molecules, from an evolutionarily conserved set of 35 distinct nucleoporins. ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nup358
RAN binding protein 2 (RANBP2) is protein which in humans is encoded by the ''RANBP2'' gene. It is also known as nucleoporin 358 (Nup358) since it is a member nucleoporin family that makes up the nuclear pore complex. RanBP2 has a mass of 358 kDa. Function Ran (protein), RAN is a small G protein, GTP-binding protein of the ras (protein), RAS superfamily. Ran GTPase is a master regulatory switch, which among other functions, controls the shuttling of proteins between the nuclear and cytoplasm compartments of the cell. Ran GTPase controls a variety of cellular functions through its interactions with other proteins. The ''RanBP2'' gene encodes a very large RAN-binding protein that localizes to cytoplasmic filaments emanating from the nuclear pore complex. RanBP2/Nup358 is a giant scaffold and mosaic cyclophilin-related nucleoporin implicated in controlling selective processes of the Ran (protein)#Ran cycle, Ran-GTPase cycle. RanBP2 is composed of multiple domains. Each domain of R ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Zinc Finger
A zinc finger is a small protein structural motif that is characterized by the coordination of one or more zinc ions (Zn2+) which stabilizes the fold. The term ''zinc finger'' was originally coined to describe the finger-like appearance of a hypothesized structure from the African clawed frog (''Xenopus laevis'') transcription factor IIIA. However, it has been found to encompass a wide variety of differing protein structures in eukaryotic cells. '' Xenopus laevis'' TFIIIA was originally demonstrated to contain zinc and require the metal for function in 1983, the first such reported zinc requirement for a gene regulatory protein followed soon thereafter by the Krüppel factor in ''Drosophila''. It often appears as a metal-binding domain in multi-domain proteins. Proteins that contain zinc fingers (zinc finger proteins) are classified into several different structural families. Unlike many other clearly defined supersecondary structures such as Greek keys or β hairpins, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
