Ran-specific binding protein 1 is an enzyme that in humans is encoded by the RANBP1gene.[1][2][3]
Ran/TC4-binding protein, RanBP1, interacts specifically with GTP-charged RAN. RANBP1 encodes a 23-kD protein that binds to RAN complexed with GTP but not GDP. RANBP1 does not activate GTPase activity of RAN but does markedly increase GTP hydrolysis by the RanGTPase-activating protein (RanGAP1). The RANBP1 cDNA encodes a 201-amino acid protein that is 92% similar to its mouse homolog. In both mammalian cells and in yeast, RANBP1 acts as a negative regulator of RCC1 by inhibiting RCC1-stimulated guanine nucleotide release from RAN.[3]
↑Hayashi N, Yokoyama N, Seki T, Azuma Y, Ohba T, Nishimoto T (August 1995). "RanBP1, a Ras-like nuclear G protein binding to Ran/TC4, inhibits RCC1 via Ran/TC4". Mol Gen Genet. 247 (6): 661–9. doi:10.1007/BF00290397. PMID7616957.
↑Singh, B B; Patel H H; Roepman R; Schick D; Ferreira P A (December 1999). "The zinc finger cluster domain of RanBP2 is a specific docking site for the nuclear export factor, exportin-1". J. Biol. Chem. United States. 274 (52): 37370–8. doi:10.1074/jbc.274.52.37370. ISSN0021-9258. PMID10601307.
↑Yaseen, N R; Blobel G (September 1999). "GTP hydrolysis links initiation and termination of nuclear import on the nucleoporin nup358". J. Biol. Chem. United States. 274 (37): 26493–502. doi:10.1074/jbc.274.37.26493. ISSN0021-9258. PMID10473610.
↑Steggerda, S M; Paschal B M (July 2000). "The mammalian Mog1 protein is a guanine nucleotide release factor for Ran". J. Biol. Chem. United States. 275 (30): 23175–80. doi:10.1074/jbc.C000252200. ISSN0021-9258. PMID10811801.
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