RANBP1

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Protein-coding gene in the species Homo sapiens

title: "RANBP1" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public description: "Protein-coding gene in the species Homo sapiens" topic_path: "uncategorized" source: "https://en.wikipedia.org/wiki/RANBP1" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0

::summary Protein-coding gene in the species Homo sapiens ::

Ran-specific binding protein 1 is an enzyme that in humans is encoded by the RANBP1 gene.

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.

Interactions

RANBP1 has been shown to interact with XPO1, KPNB1 and Ran.

References

References

  1. (August 1995). "RanBP1, a Ras-like nuclear G protein binding to Ran/TC4, inhibits RCC1 via Ran/TC4". Mol Gen Genet.
  2. (July 1999). "A Role for RanBP1 in the Release of CRM1 from the Nuclear Pore Complex in a Terminal Step of Nuclear Export". J Cell Biol.
  3. "Entrez Gene: RANBP1 RAN binding protein 1".
  4. Singh, B B. (December 1999). "The zinc finger cluster domain of RanBP2 is a specific docking site for the nuclear export factor, exportin-1". J. Biol. Chem..
  5. Plafker, K. (May 2000). "Facilitated Nucleocytoplasmic Shuttling of the Ran Binding Protein RanBP1". Mol. Cell. Biol..
  6. Yaseen, N R. (September 1999). "GTP hydrolysis links initiation and termination of nuclear import on the nucleoporin nup358". J. Biol. Chem..
  7. Steggerda, S M. (July 2000). "The mammalian Mog1 protein is a guanine nucleotide release factor for Ran". J. Biol. Chem..

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