RANGAP1 Antibody

1. RanGAP1 upregulation is associated with drug resistance in Chronic Myeloid Leukemia. PMID: 27228340
2. Abnormal localization of RanGAP1 was found in cortex of Huntington's disease patients. PMID: 28384474
3. 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. PMID: 26506250
4. 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 PMID: 26321253
5. Differentiation of human coronary artery smooth muscle cell to a contractile phenotype by stepwise serum depletion leads to significant reduction of RanGAP1 protein levels. PMID: 24988324
6. 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. PMID: 21216249
7. the RanGAP1 consensus sumoylation site and SUMO-1 C terminus are both conformationally flexible PMID: 15355965
8. 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 PMID: 15931224
9. 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. PMID: 16428860
10. 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. PMID: 18706886

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HGNC: 9854

OMIM: 602362

KEGG: hsa:5905

STRING: 9606.ENSP00000348577

UniGene: Hs.183800