NUP153 Antibody, Biotin conjugated

1. Nup153 is essential for the HIV-1 nuclear import in nondividing cells, and CPSF6 is important for HIV-1 integration. PMID: 29997211
2. Despite the requirement of all three nucleoporins for accurate NHEJ, only Nup153 is needed for proper nuclear import of 53BP1 and SENP1-dependent sumoylation of 53BP1. Our data support the role of Nup153 as an important regulator of 53BP1 activity and efficient NHEJ. PMID: 28576968
3. results further highlight the antagonistic relationship between 53BP1 and BRCA1, and place Nup153 and Nup50 in a molecular pathway that regulates 53BP1 function by counteracting BRCA1-mediated events. PMID: 28751496
4. Nup153 is an epigenetic regulator which, upon altered NO signalling, mediates the activation of genes potentially associated with early dystrophic cardiac remodelling. PMID: 28513807
5. NUP153 and CPSF6 have overlapping binding sites, but each makes unique capsid monomers (CA) interactions. Multiple ligands share an overlapping interface in HIV-1 capsid that is lost upon viral disassembly. PMID: 25356722
6. Study assessed the extent of collapse of a Nup153 fragment in molecular dynamics simulations and compared the results to single molecule FRET and small-angle X-ray scattering experiments of this peptide PMID: 26030189
7. Our data indicate a central function of Nup153 in the organization of the nucleus, not only at the periphery, but throughout the entire nuclear interior. PMID: 25485891
8. Nucleoporin Nup153 is required for NPC assembly during interphase but not during mitotic exit. It functions in interphasic NPC formation by binding directly to the inner nuclear membrane via an N-terminal amphipathic helix. PMID: 26051542
9. The data presented here suggest that BGLF4 interferes with the normal functions of Nup62 and Nup153 and preferentially helps the nuclear import of viral proteins for viral DNA replication and assembly. PMID: 25410863
10. These data reveal an emergent Kap-centric barrier mechanism that may underlie mechanistic and kinetic control in the nuclear pore complex. PMID: 24739174
11. a subset of lentiviral CA proteins directly engage FG-motifs present on NUP153 to affect viral nuclear import. PMID: 24130490
12. The Nup153 binds to both SENP1 and SENP2 and does so by interacting with the unique N-terminal domain of Nup153 as well as a specific region within the C-terminal FG-rich region. PMID: 22688647
13. A hydrophobic patch 65LRLFV69 within the zinc-binding domain is essential for the nuclear import and localization of HPV8 E7 via hydrophobic interactions with Nup62 and Nup153. PMID: 24418548
14. The roles of NUP153 and nup98 in the integration and replication of HIV-1 in human Jurkat lymphocytes are reported. PMID: 23523133
15. analysis of the Nup153-Nup50 protein interface and its role in nuclear import PMID: 23007389
16. human nucleoporin 153 (NUP153) has a role in repair of DSBs and in the activation of DNA damage checkpoints. PMID: 22249246
17. Nup153 binds to importin alpha PMID: 22510057
18. Data show that the C-terminal part of NUP153 is required for effective 53BP1 nuclear import, and that 53BP1 is imported to the nucleus through the NUP153-importin-beta interplay. PMID: 22075984
19. Nup153 levels regulate the localization of Mad1 during the metaphase/anaphase transition thereby affecting its phoshorylation status and in turn spindle checkpoint activity and mitotic exit. PMID: 21327106
20. The N-terminal domain of Nup153 and its C terminus associate with the Ig-fold domain of A- and B-type lamins. PMID: 21983083
21. Data suggest NUP153 plays a crucial role in the nuclear localization of the DICER1 protein. PMID: 21858095
22. A significant association of a polymorphic marker (rs2328136) near the NUP153 gene (which produces a 153 kDa nucleoporin) was obtained PMID: 22118420
23. results suggest that capsid, likely by the qualities of its uncoating, determines whether HIV-1 requires cellular NUP153 for PIC nuclear import PMID: 21593146
24. NUP153 is a target gene of the BACH1 transcription factor according to ChIP-seq analysis in HEK 293 cells. PMID: 21555518
25. Relocation of cellular proteins and inhibition of nuclear import in Hela cells during rhinovirus type 14 infection correlated with the degradation of Nup153 PMID: 12163599
26. Smad2 nucleocytoplasmic shuttling by nucleoporins CAN/Nup214 and Nup153 feeds TGFbeta signaling complexes in the cytoplasm and nucleus. PMID: 12191473
27. Nup153 and Nup98 have distinct domains to mediate transcription-dependent mobility PMID: 14718558
28. nuclear import of the transcription factor PU.1 occurs via RanGTP-stimulated binding to Nup153 PMID: 15632149
29. in vitro-translated Nup153 coimmunoprecipitate HIV-1 Vpr; Nup153 shares a unique N-terminal domain with Nup124 that is absolutely essential for Tf1 transposition PMID: 15659641
30. MSL complex interacts with components of the nuclear pore, in particular Mtor/TPR and Nup153. Knockdown of Mtor or Nup153 results in loss of the typical MSL X-chromosomal staining and dosage compensation in Drosophila male cells but not in female cells. PMID: 16543150
31. Nup153 zinc fingers bound GDP and GTP forms of Ran with similar affinities, indicating that this interaction is not influenced by a nucleotide-dependent conformational switch PMID: 17426026
32. Although full-length Nup1p or Nup153 does not complement Nup124p, the functionality of their conserved domains with reference to Tf1 activity suggests that these three proteins evolved from a common ancestor. PMID: 17615301
33. study found binding interactions with karyopherin-beta1 caused FG domains of nucleoporin Nup153 to collapse into compact molecular conformations; reversible collapse of the FG domains may play an important role in regulating nucleocytoplasmic transport PMID: 17916694
34. The formation of high molecular mass complexes containing importin-alpha, Nup153 and Nup88 is increased upon oxidant treatment. PMID: 18068677
35. FG-rich region of Nup153 was required to rescue defects in late mitosis PMID: 19158386
36. HIV-1 integrase binds directly to nucleoporin NUP153 to mediate active nuclear import. PMID: 19369352

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HGNC: 8062

OMIM: 603948

KEGG: hsa:9972

STRING: 9606.ENSP00000262077

UniGene: Hs.601591