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Essential component of the nuclear pore complex. The N-terminal is probably involved in nucleocytoplasmic transport. The C-terminal is involved in protein-protein interaction probably via coiled-coil formation, promotes its association with centrosomes and may function in anchorage of p62 to the pore complex. Plays a role in mitotic cell cycle progression by regulating centrosome segregation, centriole maturation and spindle orientation. It might be involved in protein recruitment to the centrosome after nuclear breakdown.
Gene References into Functions
it was revealed that a fraction of Nup62 was associated with mitotic spindle microtubule instead of spindle matrix, and the localization of Nup62 in the mitotic spindle depended on its three coiled-coil domains rather than Crm1, although Nup62 strongly interacted with Crm1 during mitosis. Moreover, depletion of Nup62 by small interference of RNA seriously induced the defects of chromosome alignment and spindle assembly PMID: 27298184
Knockdown of Nup62 (and CaMKK2) reduced androgen receptor transcriptional activity in castrate resistant prostate cancer cells. PMID: 26552607
Loss of presenilin (PS)1 function propagates tau accumulation through impairment of cargo-receptor protein p62-dependent tau degradation. PMID: 23794287
Nup62 depletion leads to the appearance of multinucleated cells and induces the formation of multipolar centrosomes, centriole synthesis defects, dramatic spindle orientation defects, and centrosome component rearrangements that impair cell bi-polarity. PMID: 24107630
Nup62 and Nup88 protein levels were significantly decreased upon knockdown of O-GlcNAc transferase. PMID: 23777819
that a patch of hydrophobic residues, 65LRLCV69, within the zinc-binding domain of HPV16 E7 mediates its nuclear import via hydrophobic interactions with the FG domain of the central channel nucleoporin Nup62. PMID: 24074597
Nucleoporin p62 (NUP62) and nucleoporin 214 (NUP214) are differentially distributed between nuclear pore complexes. PMID: 22558357
Nup62 protein intact and properly localized in HSV-1-infected cells, and an ICP27 mutant deficient for Nup62 binding failed to inhibit cellular nucleocytoplasmic transport pathways. PMID: 22334672
the cellular Nup62 is specifically recruited by HIV-1 IN and contribute to an efficient viral DNA integration. PMID: 22308026
impact of overexpressed ORP8 on nSREBPs and their target mRNAs was inhibited in cells depleted of Nup62 PMID: 21698267
Site-directed mutagenesis of putative cleavage sites in Nup62 identified six different positions that are cleaved by 2A(pro) in vitro. This analysis revealed that 2A(pro) cleavage sites were located between amino acids 103 and 298 in Nup62 PMID: 20622012
Oxidative stress up-regulated the binding of Crm1 to Ran and affected multiple repeat-containing nucleoporins by changing their localization, phosphorylation, O-glycosylation, or interaction with other transport components. PMID: 19828735
Relocation of cellular proteins and inhibition of nuclear import in HeLa cells during rhinovirus type 14 infections correlated with the degradation of p62 PMID: 12163599
The formation of Nup358/p62 and p62/Nup153 complexes was restricted to interphase cells, whereas Nup214/p62 binding was detected in interphase as well as during mitosis. PMID: 16730000
p62 has a cell type-specific role and is important in the degeneration of the basal ganglia in humans PMID: 16786527
autoantibodies reacting with the 60 kDa component of NPCs target p62 nucleoporin PMID: 17960595
Nuclear envelope permeabilization was accompanied by hyperphosphorylation of Nup62 in cells infected with wild-type mengovirus, whereas both of these alterations were suppressed in L-deficient virus mutants. PMID: 19144712
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Involvement in disease
Infantile striatonigral degeneration (SNDI)
Subcellular Location
Nucleus, nuclear pore complex. Cytoplasm, cytoskeleton, spindle pole. Nucleus envelope. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.