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Mouse (Murine) Monoclonal RANGAP1 Primary Antibody für ICC, IF - ABIN1042672
Xia, Lee, Altieri: Tumor cell dependence on Ran-GTP-directed mitosis. in Cancer research 2008
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Cow (Bovine) Polyclonal RANGAP1 Primary Antibody für WB - ABIN2786743
Ewing, Chu, Elisma, Li, Taylor, Climie, McBroom-Cerajewski, Robinson, OConnor, Li, Taylor, Dharsee, Ho, Heilbut, Moore, Zhang, Ornatsky, Bukhman, Ethier, Sheng, Vasilescu, Abu-Farha, Lambert, Duewel et al.: Large-scale mapping of human protein-protein interactions by mass spectrometry. ... in Molecular systems biology 2007
Human Polyclonal RANGAP1 Primary Antibody für IHC (p), IHC - ABIN250151
Bischoff, Krebber, Kempf, Hermes, Ponstingl: Human RanGTPase-activating protein RanGAP1 is a homologue of yeast Rna1p involved in mRNA processing and transport. in Proceedings of the National Academy of Sciences of the United States of America 1995
NUSAP1 contributes to accurate chromosome segregation by acting as a co-factor for RanBP2-RanGAP1-UBC9 during cell division.
RanGAP1 upregulation is associated with drug resistance in Chronic Myeloid Leukemia.
Abnormal localization of RanGAP1 was found in cortex of Huntington's disease patients.
our results elucidate that RanGAP1 is actively transported between the nuclear and cytoplasmic compartments, and that the cytoplasmic and NPC localization of RanGAP1 is dependent on CRM1-mediated nuclear export.
immune cell adaptor SLP-76 binds directly to SUMO-RanGAP1 of cytoplasmic fibrils of the nuclear pore complex, and this interaction is needed for optimal NFATc1 and NF-kappaB p65 nuclear entry in T cells
Differentiation of human coronary artery smooth muscle cell to a contractile phenotype by stepwise serum depletion leads to significant reduction of RanGAP1 protein levels.
Determinants of small ubiquitin-like modifier 1 (SUMO1) protein specificity, E3 ligase, and SUMO-RanGAP1 binding activities of nucleoporin RanBP2.
Analysis of the dynamics of E2(Ubc9)-SUMO-Target(RanGAP1) in the absence and presence of E3(RanBP2) revealed that two different allosteric sites regulate the ligase activity.
the RanGAP1 consensus sumoylation site and SUMO-1 C terminus are both conformationally flexible
the 3.0-A crystal structure of a four-protein complex of Ubc9, a Nup358/RanBP2 E3 ligase domain (IR1-M) and SUMO-1 conjugated to the carboxy-terminal domain of RanGAP1
RanGAP1 is phosphorylated on Ser-358 in vivo & in vitro. Phosphorylated RanGAP1, but not a mutant at 358S, formed a stable ternary complex with Ran and RanBP1 in vivo, suggesting that its 358S phosphorylation affects the Ran system.
The results of this study strengthen the conclusion that mel-18 functions as an anti-SUMO E3 factor, and extend its targets to include regulation of the sumoylation of the important cellular protein RanGAP1.
The data show that plant development is differentially affected by RanGAP mutant allele combinations of increasing severity and requires the GAP activity of RanGAP, while the subcellular positioning of RanGAP is dispensable.
These results show that the two RanGAPs are redundant and indispensable for female gametophyte development in Arabidopsis but dispensable for pollen development.
AtRanGAP1 has a mitotic trafficking pattern uniquely different from that of vertebrate RanGAP.
In a wip1-1/wip2-1/wip3-1 triple mutant, RanGAP1 is dislocated from the nuclear envelope in undifferentiated root-tip cells, whereas nuclear envelope targeting in differentiated root cells and targeting to the cell plate remain intact.
Data suggest that an unanticipated complexity of RanGAP nuclear envelope targeting and at least one member of each NE-associated coiled-coil and transmembrane domains protein family is required for RanGAP targeting in root tip cells.
propose that Arabidopsis RanGAP, a continuous positive protein marker of the plant division plane, has a role in spatial signaling during plant cell division
These data suggest that both HSC70-1 and the WPP-domain proteins play a role in facilitating WIT1 nuclear envelope targeting; this may be the first described in planta activity for the WPP-domain proteins.
data suggest that remodeling of the RanGAP-mediated nuclear transport system plays a key role in cell cycle exit for terminal differentiation of cortical neurons
nuclear localization of Ran was strongly increased in MYCBP2-deficient DRGs
These data suggest a dual function of the Nup358-RanGAP1 complex as a coordinator of importin beta recycling and reformation of novel import complexes.
Protection from isopeptidase-mediated deconjugation regulates paralog-selective sumoylation of RanGAP1.
molecular and evolutionary genetics of Segregation Distorter
Sd, the primary gene responsible for segregation distortion, encodes a mutant RanGAP, a key protein in the Ran signaling pathway required for nuclear transport and other nuclear functions.
RanGAP1, is a homodimeric 65-kD polypeptide that specifically induces the GTPase activity of RAN, but not of RAS by over 1,000-fold. RanGAP1 is the immediate antagonist of RCC1, a regulator molecule that keeps RAN in the active, GTP-bound state. The RANGAP1 gene encodes a 587-amino acid polypeptide. The sequence is unrelated to that of GTPase activators for other RAS-related proteins, but is 88% identical to Fug1, the murine homolog of yeast Rna1p. RanGAP1 and RCC1 control RAN-dependent transport between the nucleus and cytoplasm. RanGAP1 is a key regulator of the RAN GTP/GDP cycle.
ran GTPase-activating protein 1
, segregation distorter homolog
, segregation distortion
, ran GTPase activating protein 1
, Ran GTPase activating protein 1 b
, Ran GTPase activating protein 1
, RAN GTPase activating protein 1
, RAN GTPase activating protein 1 a
, CG9999 gene product from transcript CG9999-RA
, Protein segregation distorter
, Ran-GTPase activating protein
, segregation distorter