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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 (show XPO1 Proteins), although Nup62 strongly interacted with Crm1 (show XPO1 Proteins) during mitosis. Moreover, depletion of Nup62 by small interference of RNA seriously induced the defects of chromosome alignment and spindle assembly
Knockdown of Nup62 (and CaMKK2 (show CAMKK2 Proteins)) reduced androgen receptor (show AR Proteins) transcriptional activity in castrate resistant prostate cancer cells.
The data presented here suggest that BGLF4 interferes with the normal functions of Nup62 and Nup153 (show NUP153 Proteins) and preferentially helps the nuclear import of viral proteins for viral DNA replication and assembly.
These data reveal an emergent Kap (show CDKN3 Proteins)-centric barrier mechanism that may underlie mechanistic and kinetic control in the nuclear pore complex.
Loss of presenilin (PS)1 function propagates tau accumulation through impairment of cargo-receptor protein p62-dependent tau degradation.
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.
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 (show NUP153 Proteins).
Nup62 and Nup88 protein levels were significantly decreased upon knockdown of O-GlcNAc transferase.
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.
Nucleoporin p62 (NUP62) and nucleoporin 214 (NUP214) are differentially distributed between nuclear pore complexes.
Role for NUP62 depletion and PYK2 (show PTK2B Proteins) redistribution in dendritic retraction resulting from chronic stress
ORP8 (show OSBPL8 Proteins) was shown to compete with Exo70 (show EXOC7 Proteins) for interaction with NUP62, and NUP62 knockdown abolished the migration enhancement of ORP8 (show OSBPL8 Proteins)-silenced cells, suggesting that the endogenous ORP8 (show OSBPL8 Proteins) suppresses migration via binding to NUP62.
Dtaa show that importin beta and the integral nuclear pore glycoprotein Nup62 interact with hsp90, hsp70, p23, and the TPR domain proteins FKBP52 and PP5 during nuclear transport.
Study analyzed genomic interactions of full-length nucleoporins Nup98 (show NUP98 Proteins), Nup50 (show NUP50 Proteins), and Nup62 and found that they predominantly interacted with active genes inside the nucleoplasm, particularly those involved in developmental regulation and the cell cycle.
The nuclear pore complex is a massive structure that extends across the nuclear envelope, forming a gateway that regulates the flow of macromolecules between the nucleus and the cytoplasm. Nucleoporins are the main components of the nuclear pore complex in eukaryotic cells. The protein encoded by this gene is a member of the FG-repeat containing nucleoporins and is localized to the nuclear pore central plug. This protein associates with the importin alpha/beta complex which is involved in the import of proteins containing nuclear localization signals. Multiple transcript variants of this gene encode a single protein isoform.
62 kDa nucleoporin
, nuclear pore glycoprotein p62
, nucleoporin Nup62
, nucleoporin 62kDa
, nuclear pore complex 1
, nucleoporin 62
, predicted protein
, Nup62 nuclear pore complex glycoprotein p62-related protein (IC)
, Nuclear pore glycoprotein p62
, nuclear pore glycoprotein 62