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GenomicsNucleoporin Nup153 Regulates Stem Cell Pluripotency through Gene Silencing
Nucleoporins (Nups) are a family of proteins best known as the constituent building blocks of nuclear pore complexes (NPCs), the transport channels that mediate nuclear transport. Recent evidence suggest that several Nups have additional roles in controlling the activation and silencing of developme...
ORGANISM(S): Mus musculus 
2015-06-19 | E-GEOD-64008 | biostudies-arrayexpress
GenomicsCLIP-seq NUP153 TBEV
Investigating the interaction of NUP153 to TBEV viral RNA
PRJEB77840 | ENA
ProteomicsYildirim 4398 Nup153 Interactome
Identify Nup153 interacting proteins in Co-IP coupled with LC-MS/MS
ORGANISM(S): Homo sapiens (Human) 
2021-03-10 | PXD015441 | Pride
Nup153 interaction 
Genomics
Interaction of NUP153 with TBEV viral RNA using CLIP-seq
PRJNA1137903 | ENA
UnknownTwo distinct sites in Nup153 mediate interaction with the SUMO proteases SENP1 and SENP2.
Not available
S-EPMC3679279 | biostudies-literature
UnknownDirect interaction with nup153 mediates binding of Tpr to the periphery of the nuclear pore complex.
Not available
S-EPMC165087 | biostudies-literature
ProteomicsNup133 is required for proper nuclear pore basket assembly and dynamics in embryonic stem cells
Nup133 belongs to the Y-complex, a key component of the nuclear pore complex (NPC) scaffold. Studies on a null mutation in mice previously revealed that Nup133 is essential for embryonic development but not for mouse embryonic stem cells (mESCs) proliferation. Using single pore detection and average...
ORGANISM(S): Mus musculus (Mouse) 
2018-05-28 | PXD009466 | Pride
Mus musculus Embryonic stem cells Pulldown Nucleoporins 
UnknownCul3 substrate adaptor SPOP targets Nup153 for degradation.
Not available
S-EPMC10245568 | biostudies-literature
UnknownCul3 substrate adaptor SPOP targets Nup153 for degradation.
Not available
S-EPMC11974958 | biostudies-literature
UnknownNucleoporin NUP153 phenylalanine-glycine motifs engage a common binding pocket within the HIV-1 capsid protein to mediate lentiviral infectivity.
Not available
S-EPMC3795039 | biostudies-literature
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