The C terminus of the nuclear RAN/TC4 GTPase stabilizes the GDP-bound state and mediates interactions with RCC1, RAN-GAP, and HTF9A/RANBP1.

doi:10.1074/jbc.270.24.14405

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Article

The C terminus of the nuclear RAN/TC4 GTPase stabilizes the GDP-bound state and mediates interactions with RCC1, RAN-GAP, and HTF9A/RANBP1.

The Journal of biological chemistry - 16 Jun 1995

Richards S A, Lounsbury K M, Macara I G

Abstract excerpt

Ran/TC4 is a member of the Ras superfamily of GTPases. It is unusual in being predominantly nuclear and because it possesses an acidic -DEDDDL sequence instead of a consensus prenylation domain at the C terminus. Ran is required for nuclear protein import and cell cycle progression, and has been...

Topics

Amino Acid Sequence
Cell Cycle Proteins
Cell Nucleus
DNA-Binding Proteins
GTP-Binding Proteins
GTPase-Activating Proteins
Guanine Nucleotide Exchange Factors
Guanosine Diphosphate
Hydrolysis
Models, Chemical
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Nuclear Proteins

Protein Binding

Protein Conformation

Proteins

RNA-Binding Proteins

ran GTP-Binding Protein

Source

Open in PubMed

Identifiers

PMID: 7782302
DOI: 10.1074/jbc.270.24.14405

Genes

RAN
RANBP1
RCC1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-7782302-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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The C terminus of the nuclear RAN/TC4 GTPase stabilizes the GDP-bound state and mediates interactions with RCC1, RAN-GAP, and HTF9A/RANBP1.PMID 7782302Read ↗

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