| POM121 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Aliases | POM121 , P145, POM121A, POM121 transmembrane nucleoporin | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 615753 MGI: 2137624 HomoloGene: 70878 GeneCards: POM121 | ||||||||||||||||||||||||||||||||||||||||||||||||||
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| Wikidata | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Nuclear envelope pore membrane protein POM 121 is a protein that in humans is encoded by the POM121 gene. [5] [6] [7] Alternatively spliced variants that encode different protein isoforms have been described but the full-length nature of only one has been determined. [8]
The nuclear envelope creates distinct nuclear and cytoplasmic compartments in eukaryotic cells. It consists of two concentric membranes perforated by nuclear pores, large protein complexes that form aqueous channels to regulate the flow of macromolecules between the nucleus and the cytoplasm. These complexes are composed of at least 100 different polypeptide subunits, many of which belong to the nucleoporin family. This gene encodes a member of the FG-repeat-containing nucleoporins. The protein encoded by this gene is an integral membrane protein that localizes to the central spoke ring complex and participates in anchoring the nuclear pore complex to the nuclear envelope. [8]
Antibodies against this protein can be used to identify the nuclear envelope in immunofluorescence experiments. [9]
A nuclear pore is a part of a large complex of proteins, known as a nuclear pore complex that spans the nuclear envelope, which is the double membrane surrounding the eukaryotic cell nucleus. There are approximately 1,000 nuclear pore complexes (NPCs) in the nuclear envelope of a vertebrate cell, but this number varies depending on cell type and the stage in the life cycle. The human nuclear pore complex (hNPC) is a 110 megadalton (MDa) structure. The proteins that make up the nuclear pore complex are known as nucleoporins; each NPC contains at least 456 individual protein molecules and is composed of 34 distinct nucleoporin proteins. About half of the nucleoporins typically contain solenoid protein domains—either an alpha solenoid or a beta-propeller fold, or in some cases both as separate structural domains. The other half show structural characteristics typical of "natively unfolded" or intrinsically disordered proteins, i.e. they are highly flexible proteins that lack ordered tertiary structure. These disordered proteins are the FG nucleoporins, so called because their amino-acid sequence contains many phenylalanine–glycine repeats.
Nuclear pore glycoprotein-210 (gp210) is an essential trafficking regulator in the eukaryotic nuclear pore complex. Gp-210 anchors the pore complex to the nuclear membrane. and protein tagging reveals its primarily located on the luminal side of double layer membrane at the pore. A single polypeptide motif of gp210 is responsible for sorting to nuclear membrane, and indicate the carboxyl tail of the protein is oriented toward the cytoplasmic side of the membrane.
Nuclear pore glycoprotein p62 is a protein complex associated with the nuclear envelope. The p62 protein remains associated with the nuclear pore complex-lamina fraction. p62 is synthesized as a soluble cytoplasmic precursor of 61 kDa followed by modification that involve addition of N-acetylglucosamine residues, followed by association with other complex proteins. In humans it is encoded by the NUP62 gene.
The nuclear envelope, also known as the nuclear membrane, is made up of two lipid bilayer membranes that in eukaryotic cells surround the nucleus, which encloses the genetic material.
Nucleoporins are a family of proteins which are the constituent building blocks of the nuclear pore complex (NPC). The nuclear pore complex is a massive structure embedded in the nuclear envelope at sites where the inner and outer nuclear membranes fuse, forming a gateway that regulates the flow of macromolecules between the cell nucleus and the cytoplasm. Nuclear pores enable the passive and facilitated transport of molecules across the nuclear envelope. Nucleoporins, a family of around 30 proteins, are the main components of the nuclear pore complex in eukaryotic cells. Nucleoporin 62 is the most abundant member of this family. Nucleoporins are able to transport molecules across the nuclear envelope at a very high rate. A single NPC is able to transport 60,000 protein molecules across the nuclear envelope every minute.
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 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.
Nucleoporin 88 (Nup88) is a protein that in humans is encoded by the NUP88 gene.
Nucleoporin 50 (Nup50) is a protein that in humans is encoded by the NUP50 gene.
NTF2-related export protein 1 is a protein that in humans is encoded by the NXT1 gene.
Nucleoporin 54 (Nup54) is a protein that in humans is encoded by the NUP54 gene.
Nuclear pore complex protein Nup133, or Nucleoporin Nup133, is a protein that in humans is encoded by the NUP133 gene.
Nucleoporin-like 2 is a protein that in humans is encoded by the NUPL2 gene.
Nucleoporin 160 (Nup160) is a protein that in humans is encoded by the NUP160 gene.
Nucleoporin 155 (Nup155) is a protein that in humans is encoded by the NUP155 gene.
Nucleoporin NDC1 is a protein that in humans is encoded by the TMEM48 gene. It anchors aladin to the nuclear pore complex.
Nucleoporin 43 (Nup43) is a protein that in humans is encoded by the NUP43 gene.
Nucleoporin 93 (Nup93) is a protein that in humans is encoded by the NUP93 gene.
Nucleoporin p58/p45 is a protein that in humans is encoded by the NUPL1 gene.
Nucleoporin 35 (Nup35) is a protein that in humans is encoded by the NUP35 gene.
Nucleoporin 205 (Nup205) is a protein that in humans is encoded by the NUP205 gene.
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