Nucleoporin 153

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.

NUP153
Available structures PDB Human UniProt search: PDBe RCSB List of PDB id codes 2EBQ, 2EBR, 2EBV, 2GQE, 4U0C, 4U0D
Identifiers
Aliases	NUP153, HN153, nucleoporin 153kDa, nucleoporin 153
External IDs	OMIM: 603948; MGI: 2385621; HomoloGene: 68442; GeneCards: NUP153; OMA:NUP153 - orthologs
Gene location (Human) Chr. Chromosome 6 (human) Band 6p22.3 Start 17,615,035 bp End 17,706,925 bp
Gene location (Mouse) Chr. Chromosome 13 (mouse) Band 13|13 A5 Start 46,833,381 bp End 46,881,416 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in secondary oocyte epithelium of nasopharynx cartilage tissue tibia germinal epithelium Epithelium of choroid plexus amniotic fluid skin of thigh parietal pleura Skeletal muscle tissue of rectus abdominis Top expressed in tail of embryo primitive streak genital tubercle Gonadal ridge ciliary body Paneth cell abdominal wall medial ganglionic eminence mandibular prominence spermatid More reference expression data BioGPS More reference expression data
Gene ontology Molecular function DNA binding protein-membrane adaptor activity metal ion binding protein binding identical protein binding nuclear localization sequence binding structural constituent of nuclear pore Cellular component nuclear membrane nuclear periphery membrane nuclear pore nucleoplasm nucleolus nuclear inclusion body nuclear pore nuclear basket nucleus nuclear pore central transport channel cytosol host cell Biological process mRNA transport nuclear pore complex assembly viral penetration into host nucleus protein transport viral entry into host cell viral process negative regulation of RNA export from nucleus mRNA export from nucleus protein import into nucleus regulation of glycolytic process tRNA export from nucleus protein sumoylation viral transcription regulation of gene silencing by miRNA intracellular transport of virus regulation of cellular response to heat Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 9972 218210 Ensembl ENSG00000124789 ENSMUSG00000021374 UniProt P49790 n/a RefSeq (mRNA) NM_001278209 NM_001278210 NM_005124 NM_175749 RefSeq (protein) NP_001265138 NP_001265139 NP_005115 n/a Location (UCSC) Chr 6: 17.62 – 17.71 Mb Chr 13: 46.83 – 46.88 Mb PubMed search
Wikidata
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Background

Main article: Nuclear pore

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 pore targeting domain has been identified, a central region containing multiple zinc finger motifs, and a C-terminal region containing multiple XFXFG repeats.

Interactions

NUP153 has been shown to interact with SENP2 and KPNB1.

Further reading

• Moroianu J (2000). "Nuclear import and export pathways". J. Cell. Biochem. Suppl 32-33 (S32): 76–83. doi:10.1002/(SICI)1097-4644(1999)75:32+<76::AID-JCB10>3.0.CO;2-Q. PMID 10629106. S2CID 45613755.
• Adam SA (2002). "The nuclear pore complex". Genome Biol. 2 (9): REVIEWS0007. doi:10.1186/gb-2001-2-9-reviews0007. PMC 138961. PMID 11574060.
• McMorrow I, Bastos R, Horton H, Burke B (1994). "Sequence analysis of a cDNA encoding a human nuclear pore complex protein, hnup153". Biochim. Biophys. Acta. 1217 (2): 219–23. doi:10.1016/0167-4781(94)90040-X. PMID 8110839.
• Yaseen NR, Blobel G (1997). "Cloning and characterization of human karyopherin beta3". Proc. Natl. Acad. Sci. U.S.A. 94 (9): 4451–6. Bibcode:1997PNAS...94.4451Y. doi:10.1073/pnas.94.9.4451. PMC 20743. PMID 9114010.
• Zolotukhin AS, Felber BK (1999). "Nucleoporins nup98 and nup214 participate in nuclear export of human immunodeficiency virus type 1 Rev". J. Virol. 73 (1): 120–7. doi:10.1128/JVI.73.1.120-127.1999. PMC 103815. PMID 9847314.
• Ullman KS, Shah S, Powers MA, Forbes DJ (1999). "The nucleoporin nup153 plays a critical role in multiple types of nuclear export". Mol. Biol. Cell. 10 (3): 649–64. doi:10.1091/mbc.10.3.649. PMC 25193. PMID 10069809.
• Nakielny S, Shaikh S, Burke B, Dreyfuss G (1999). "Nup153 is an M9-containing mobile nucleoporin with a novel Ran-binding domain". EMBO J. 18 (7): 1982–95. doi:10.1093/emboj/18.7.1982. PMC 1171283. PMID 10202161.
• Bachi A, Braun IC, Rodrigues JP, et al. (2000). "The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substrates". RNA. 6 (1): 136–58. doi:10.1017/S1355838200991994. PMC 1369901. PMID 10668806.
• Kehlenbach RH, Gerace L (2000). "Phosphorylation of the nuclear transport machinery down-regulates nuclear protein import in vitro". J. Biol. Chem. 275 (23): 17848–56. doi:10.1074/jbc.M001455200. PMID 10749866.
• Kutay U, Hartmann E, Treichel N, et al. (2001). "Identification of two novel RanGTP-binding proteins belonging to the importin beta superfamily". J. Biol. Chem. 275 (51): 40163–8. doi:10.1074/jbc.M006242200. hdl:11858/00-001M-0000-0015-3D4E-B. PMID 11024021.
• Herold A, Suyama M, Rodrigues JP, et al. (2000). "TAP (NXF1) belongs to a multigene family of putative RNA export factors with a conserved modular architecture". Mol. Cell. Biol. 20 (23): 8996–9008. doi:10.1128/MCB.20.23.8996-9008.2000. PMC 86553. PMID 11073998.
• Hofmann W, Reichart B, Ewald A, et al. (2001). "Cofactor requirements for nuclear export of Rev response element (RRE)- and constitutive transport element (CTE)-containing retroviral RNAs. An unexpected role for actin". J. Cell Biol. 152 (5): 895–910. doi:10.1083/jcb.152.5.895. PMC 2198816. PMID 11238447.
• Ben-Efraim I, Gerace L (2001). "Gradient of increasing affinity of importin beta for nucleoporins along the pathway of nuclear import". J. Cell Biol. 152 (2): 411–7. doi:10.1083/jcb.152.2.411. PMC 2199621. PMID 11266456.
• Dimaano C, Ball JR, Prunuske AJ, Ullman KS (2002). "RNA association defines a functionally conserved domain in the nuclear pore protein Nup153". J. Biol. Chem. 276 (48): 45349–57. doi:10.1074/jbc.M102592200. PMID 11567018.
• Walther TC, Fornerod M, Pickersgill H, et al. (2001). "The nucleoporin Nup153 is required for nuclear pore basket formation, nuclear pore complex anchoring and import of a subset of nuclear proteins". EMBO J. 20 (20): 5703–14. doi:10.1093/emboj/20.20.5703. PMC 125666. PMID 11598013.
• Brownawell AM, Macara IG (2002). "Exportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding proteins". J. Cell Biol. 156 (1): 53–64. doi:10.1083/jcb.200110082. PMC 2173575. PMID 11777942.
• Hang J, Dasso M (2002). "Association of the human SUMO-1 protease SENP2 with the nuclear pore". J. Biol. Chem. 277 (22): 19961–6. doi:10.1074/jbc.M201799200. PMID 11896061.