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Translocation of p53 (show TP53 ELISA Kits) is regulated by androgen-dependent sumoylation mediated by the G3BP2-interacting SUMO-E3 ligase (show PIAS1 ELISA Kits), RanBP2. G3BP2 knockdown results in reduced tumor growth and increased nuclear p53 (show TP53 ELISA Kits) accumulation in mouse xenograft models of prostate cancer with or without long-term androgen deprivation.
These our results reveal spatio-temporal regulation in the recruitment of nucleoporins and translation factors to cytoplasmic viral factories , and particularly the importance of Nup358 in vaccinia virus infection.
NUSAP1 (show NUSAP1 ELISA Kits) contributes to accurate chromosome segregation by acting as a co-factor for RanBP2-RanGAP1 (show RANGAP1 ELISA Kits)-UBC9 (show UBE2I ELISA Kits) during cell division.
Nup358-AGO interaction is important for miRNA-mediated gene silencing and identifies SIM (show SIM2 ELISA Kits) as a new interacting motif for the AGO family of proteins.
recurrent or familial ANE without the RANBP2 mutation has a more severe outcome and greater predilection for male sex than that with the RANBP2 mutation. This suggests that there are unknown gene mutations linked to ANE.
Based on the literature review of ANE1 with RANBP2 mutation, we propose a threshold for RANBP2 mutation tes (show TES ELISA Kits)
findings indicate that RanGDP and not RanGTP is the physiological target for the RanBP2 SUMO E3 ligase (show PIAS1 ELISA Kits) complex
Taken together, topographic and functional interactions between dynactin (show DCTN1 ELISA Kits), importin-beta (show KPNB1 ELISA Kits) and RanBP2 are involved in nuclear translocation of IGF-1R (show IGF1R ELISA Kits).
analysis of the RANBP2-ALK (show ALK ELISA Kits) gene fusion identified in ALK (show ALK ELISA Kits)-positive diffuse large B-cell lymphoma with a unique nuclear membrane staining of ALK (show ALK ELISA Kits) protein
Nup358, a nucleoporin that forms the cytoplasmic filaments of the nuclear pore complex, plays an important role in the nuclear import of hTERT.
reports identification of the cyclophilin-related protein (show PPID ELISA Kits), RanBP2 (note at the time the protein was not designated RanBP2), and the cis (show CISH ELISA Kits)-trans prolyl isomerase activity of its cyclophilin (show PPIE ELISA Kits) domain
reports interaction of the RBD4 and CY domains of RanBP2 with red/green opsin (show OPN1MW ELISA Kits) and the chaperone activity of these domains toward red/green opsin (show OPN1MW ELISA Kits).
reports identification of a binding domain in RanBP2, the cyclophilin (show PPIE ELISA Kits)-like domain, toward components of the 19S cap of the proteasome
reports identification of a binding domain in RanBP2, the zinc-finger rich domain, toward CRM1/exportin-1 (show XPO1 ELISA Kits)
reports identification of a novel domain in RanBP2 located between RBD2 and RBD3 with specific binding activity against the conventional heavy chain kinesins, KIF5B and KIF5C
reports the novel subcellular localizations of RanBP2 in retinal neurons of human and bovine
the cyclophilin-like domain of Ran-binding protein-2 modulates selectively the activity of the ubiquitin-proteasome system and protein biogenesis
Data (including data from studies in transgenic/knockout mice) suggest that Ranbp2 in photoreceptor neurons participates in coupling of photoreceptor degeneration (neural dysmorphology) and apoptosis (neural death) caused by toxic exposure to light.
These studies unravel selective roles of Ranbp2 and its RBD2 and RBD3 in retinal pigment epithelium survival and functions.
These results unveil distinct mechanistic and biological links between prolyl isomerase and chaperone activities of Ranbp2 cyclophilin (show PPIE ELISA Kits) toward proteostasis.
Novel roles in Ran GTPase (show RAN ELISA Kits)-independent subdomains of RBD2 and RBD3, and KBD of RanBP2, confer antagonizing and multi-modal mechanisms of kinesin-1 activation and regulation of mitochondrial motility.
Ranbp2 haploinsufficiency is associated with metabolic imbalances leading to parkinson's disease.
Knockdown of RANBP2 specifically affected the late step of nuclear entry, inducing cytoplasmic granules enriched with phosphorylated components. This suggests a novel regulatory mechanism for nuclear speckle formation involving RANBP2 and phosphorylation.
A critical function of RanBP2 is to capture recycling RanGTP-importin-beta (show KPNB1 ELISA Kits) complexes at cytoplasmic fibrils to allow for adequate classical nuclear localization signal-mediated cargo import.
findings indicate that the nuclear pore complex undergoes dynamic remodeling during muscle cell differentiation and that Nup358 is prominently involved in the remodeling process
These results provide a rationale for the neuroprotection from light damage of photosensory neurons by RANBP2 insufficiency.
RanBP2 associates in vitro and in vivo and colocalizes with the mitochondrial metallochaperone, Cox11, and the pacemaker of glycolysis, hexokinase type I (HKI (show HK1 ELISA Kits)) via its leucine-rich domain.
RAN is a small GTP-binding protein of the RAS superfamily that is associated with the nuclear membrane and is thought to control a variety of cellular functions through its interactions with other proteins. This gene encodes a very large RAN-binding protein that immunolocalizes to the nuclear pore complex. The protein is a giant scaffold and mosaic cyclophilin-related nucleoporin implicated in the Ran-GTPase cycle. The encoded protein directly interacts with the E2 enzyme UBC9 and strongly enhances SUMO1 transfer from UBC9 to the SUMO1 target SP100. These findings place sumoylation at the cytoplasmic filaments of the nuclear pore complex and suggest that, for some substrates, modification and nuclear import are linked events. This gene is partially duplicated in a gene cluster that lies in a hot spot for recombination on chromosome 2q.
RAN binding protein 1
, RAN binding protein 2
, e3 SUMO-protein ligase RanBP2-like
, 358 kDa nucleoporin
, E3 SUMO-protein ligase RanBP2
, nuclear pore complex protein Nup358
, nucleoporin 358
, nucleoporin Nup358
, ran-binding protein 2
, transformation-related protein 2