RANGAP1

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Protein-coding gene in the species Homo sapiens

title: "RANGAP1" 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/RANGAP1" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0

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

Ran GTPase-activating protein 1 is an enzyme that in humans is encoded by the RANGAP1 gene.

Function

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 Rangap1 (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.

Interactions

RanGAP1 is a trafficking protein which helps transport other proteins from the cytoplasm to the nucleus. Small ubiquitin-related modifier needs to be associated with it before it can be localized at the nuclear pore.

RANGAP1 has been shown to interact with:

References

References

  1. (Apr 1995). "Human RanGTPase-activating protein RanGAP1 is a homologue of yeast Rna1p involved in mRNA processing and transport". Proc Natl Acad Sci U S A.
  2. "Entrez Gene: RANGAP1 Ran GTPase activating protein 1".
  3. (2000). "Biochemistry. All in the ubiquitin family". Science.
  4. (Jun 1999). "The crystal structure of rna1p: a new fold for a GTPase-activating protein". Mol. Cell.
  5. (May 1995). "RNA1 encodes a GTPase-activating protein specific for Gsp1p, the Ran/TC4 homologue of Saccharomyces cerevisiae". J. Biol. Chem..
  6. (Mar 1994). "RanGAP1 induces GTPase activity of nuclear Ras-related Ran". Proc. Natl. Acad. Sci. U.S.A..
  7. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol..
  8. (Aug 2003). "Role of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and conjugation". Biochemistry.
  9. (Aug 2008). "Ubc9 sumoylation regulates SUMO target discrimination". Mol. Cell.

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