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Gene Review

RANP1  -  RAN, member RAS oncogene family pseudogene 1

Homo sapiens

Synonyms: Em:AB014080.2, Ras-like, TC4
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Disease relevance of RANP1


Psychiatry related information on RANP1

  • In contrast to TC1, TC4 produced a stimulant effect in locomotor activity with the ED(50) estimated at 0.94 mg/kg [3].

High impact information on RANP1

  • G protein GAPs act allosterically on G subunits, in contrast to GAPs for the Ras-like monomeric GTP-binding proteins [4].
  • Members of the Rho family of small Ras-like GTPases--including RhoA, -B, and -C, Rac1 and -2, and Cdc42--exhibit guanine nucleotide-binding activity and function as molecular switches, cycling between an inactive GDP-bound state and an active GTP-bound state [5].
  • In the case of the Ras-like protein CDC42Hs, which is the human homolog of a Saccharomyces cerevisiae cell division cycle protein, the GDI protein also inhibited both the intrinsic and GAP-stimulated hydrolysis of GTP [6].
  • A GDP dissociation inhibitor that serves as a GTPase inhibitor for the Ras-like protein CDC42Hs [6].
  • These findings establish an additional role for the GDI protein--namely, as a guanosine triphosphatase (GTPase) inhibitory protein for a Ras-like GTP binding protein [6].

Chemical compound and disease context of RANP1

  • Trishomocubane analogues TC1 (N-(3'-fluorophenyl)ethyl-4-azahexacyclo [,6).0(3,10).0(5,9).0(8,11)]dodecan-3-ol) and TC4 (N-(3'-fluorophenyl)methyl-4-azahexacyclo [,6).0(3,10).0(5,9).0(8,11)]dodecan-3-ol) were evaluated for their modulatory effects on locomotor activity as well as interactions with cocaine-induced responses [3].

Biological context of RANP1

  • The Ras-like GTP-binding proteins comprise a large superfamily of proteins that play key roles in a wide variety of cellular activities, including cell growth, differentiation, secretion, and protein trafficking [7].
  • In this report we find distinct roles for TC4 in both nuclear assembly and cell cycle progression [8].
  • In a separate set of experiments using a cell-free extract of Xenopus eggs that cycles between S and M phases, the GDP-bound form of TC4 had dramatic effects, blocking entry into mitosis even in the complete absence of nuclei [8].
  • We found that a mutant TC4 protein defective in GTP binding (GDP-bound form) suppressed nuclear growth and prevented DNA replication [8].
  • Therefore, we provide direct biochemical evidence for a role of TC4 in both maintaining nuclear structure and in the signaling pathways that regulate entry into mitosis [8].

Anatomical context of RANP1

  • One of the most exciting recent discoveries in the area of intracellular protein transport is the finding that many organelles involved in exocytic and endocytic membrane traffic have one or more Ras-like GTP-binding proteins on their cytoplasmic face that are specific for each membranous compartment [9].
  • Rab is a family of small Ras-like GTPases regulating intracellular vesicle transport [10].
  • Costimulation through CD28 suppresses T cell receptor-dependent activation of the Ras-like small GTPase Rap1 in human T lymphocytes [11].
  • ADP-ribosylation factors (ARFs) are small Ras-like GTPases which play important roles in intracellular vesicle transport and in the remodeling of the actin cytoskeleton [12].
  • Northern blotting and reverse transcriptase-PCR assays with oligonucleotide probes and primers specific for each transcript demonstrated that the isoform identical to Ran/TC4 was expressed in both somatic tissues and testis, while the variant form was transcribed only in testis [13].

Associations of RANP1 with chemical compounds

  • Five years ago, Epac--a guanine nucleotide exchange factor for the Ras-like small GTPases Rap1 and Rap2--was found to be a new target of cyclic AMP, which opened up new avenues for cAMP research [14].
  • The effect of this mutant TC4 protein on cell cycle progression is mediated by phosphorylation of p34cdc2 on tyrosine and threonine residues, negatively regulating cdc2 kinase activity [8].
  • The Ras-like guanine-nucleotide-binding protein Rap1 controls integrin alpha(IIb)beta3 activity and platelet aggregation [15].
  • Expression of RasGRP3, a Ca(2+)/diacylglycerol-regulated guanine nucleotide exchange factor for Ras-like GTPases, but not expression of various other exchange factors enhanced GTP loading of Rap2B and PLC/Ca(2+) signaling by the EGF receptor [16].
  • Multiple tyrosine kinase substrates that facilitate EGF receptor trafficking between these various compartments, as well as the participation of phosphoinositides and Ras-like G proteins in the trafficking pathway are also described [17].

Physical interactions of RANP1

  • RRAG A (Rag A)/Gtr1p is a member of the Ras-like small G protein family that genetically interacts with RCC1, a guanine nucleotide exchange factor for RanGTPase [18].

Regulatory relationships of RANP1

  • From these results, we conclude that TC21 promotes Ras-like responses in diverse cell types due to the use of overlapping, if not identical, signaling elements of the Ras oncogenic pathway [19].

Other interactions of RANP1

  • Moreover, using purified proteins, we demonstrate the direct GTP-dependent interaction of the Ras-like GTPases with RalGDS-RBD and full-length RalGDS in vitro [20].
  • A small Ras-like G-protein, kappaB-Ras, participates with the IkappaBbeta insert to effectively mask the NF-kappaB nuclear localization potential [21].
  • NORE1, a noncatalytic polypeptide, binds specifically to Ras-GTP and to several other Ras-like GTPases [22].
  • cDNA cloning of a human RAB26-related gene encoding a Ras-like GTP-binding protein on chromosome 16p13.3 region [23].
  • Therefore, Rig and Noey2 may represent a new subfamily of Ras-like tumor suppressors [24].

Analytical, diagnostic and therapeutic context of RANP1


  1. Elimination of the vertebrate Escherichia coli Ras-like protein homologue leads to cell cycle arrest at G1 phase and apoptosis. Gohda, J., Nomura, Y., Suzuki, H., Arai, H., Akiyama, T., Inoue, J. Oncogene (2003) [Pubmed]
  2. GTP Binding Is Essential to the Protein Kinase Activity of LRRK2, a Causative Gene Product for Familial Parkinson's Disease. Ito, G., Okai, T., Fujino, G., Takeda, K., Ichijo, H., Katada, T., Iwatsubo, T. Biochemistry (2007) [Pubmed]
  3. Trishomocubanes: Novel sigma ligands modulate cocaine-induced behavioural effects. Liu, X., Banister, S.D., Christie, M.J., Banati, R., Meikle, S., Coster, M.J., Kassiou, M. Eur. J. Pharmacol. (2007) [Pubmed]
  4. GTPase-activating proteins for heterotrimeric G proteins: regulators of G protein signaling (RGS) and RGS-like proteins. Ross, E.M., Wilkie, T.M. Annu. Rev. Biochem. (2000) [Pubmed]
  5. Regulation of the cytoskeleton and cell adhesion by the Rho family GTPases in mammalian cells. Kaibuchi, K., Kuroda, S., Amano, M. Annu. Rev. Biochem. (1999) [Pubmed]
  6. A GDP dissociation inhibitor that serves as a GTPase inhibitor for the Ras-like protein CDC42Hs. Hart, M.J., Maru, Y., Leonard, D., Witte, O.N., Evans, T., Cerione, R.A. Science (1992) [Pubmed]
  7. The Ras superfamilies: regulatory proteins and post-translational modifications. Evans, T., Hart, M.J., Cerione, R.A. Curr. Opin. Cell Biol. (1991) [Pubmed]
  8. Evidence for a dual role for TC4 protein in regulating nuclear structure and cell cycle progression. Kornbluth, S., Dasso, M., Newport, J. J. Cell Biol. (1994) [Pubmed]
  9. GTP-binding proteins in intracellular transport. Pfeffer, S.R. Trends Cell Biol. (1992) [Pubmed]
  10. PRA1 inhibits the extraction of membrane-bound rab GTPase by GDI1. Hutt, D.M., Da-Silva, L.F., Chang, L.H., Prosser, D.C., Ngsee, J.K. J. Biol. Chem. (2000) [Pubmed]
  11. Costimulation through CD28 suppresses T cell receptor-dependent activation of the Ras-like small GTPase Rap1 in human T lymphocytes. Reedquist, K.A., Bos, J.L. J. Biol. Chem. (1998) [Pubmed]
  12. Phosphoinositides determine specificity of the guanine-nucleotide exchange activity of cytohesin-1 for ADP-ribosylation factors derived from a mammalian expression system. Knorr, T., Nagel, W., Kolanus, W. Eur. J. Biochem. (2000) [Pubmed]
  13. Tissue-specific expression of Ran isoforms in the mouse. Coutavas, E.E., Hsieh, C.M., Ren, M., Drivas, G.T., Rush, M.G., D'Eustachio, P.D. Mamm. Genome (1994) [Pubmed]
  14. Epac: a new cAMP target and new avenues in cAMP research. Bos, J.L. Nat. Rev. Mol. Cell Biol. (2003) [Pubmed]
  15. Rap1GAP2 is a new GTPase-activating protein of Rap1 expressed in human platelets. Schultess, J., Danielewski, O., Smolenski, A.P. Blood (2005) [Pubmed]
  16. Rap2B-dependent stimulation of phospholipase C-epsilon by epidermal growth factor receptor mediated by c-Src phosphorylation of RasGRP3. Stope, M.B., Vom Dorp, F., Szatkowski, D., Böhm, A., Keiper, M., Nolte, J., Oude Weernink, P.A., Rosskopf, D., Evellin, S., Jakobs, K.H., Schmidt, M. Mol. Cell. Biol. (2004) [Pubmed]
  17. The EGF receptor: a nexus for trafficking and signaling. Carpenter, G. Bioessays (2000) [Pubmed]
  18. A novel human nucleolar protein, Nop132, binds to the G proteins, RRAG A/C/D. Sekiguchi, T., Todaka, Y., Wang, Y., Hirose, E., Nakashima, N., Nishimoto, T. J. Biol. Chem. (2004) [Pubmed]
  19. Signal transduction elements of TC21, an oncogenic member of the R-Ras subfamily of GTP-binding proteins. Movilla, N., Crespo, P., Bustelo, X.R. Oncogene (1999) [Pubmed]
  20. Identification of the guanine nucleotide dissociation stimulator for Ral as a putative effector molecule of R-ras, H-ras, K-ras, and Rap. Spaargaren, M., Bischoff, J.R. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  21. KappaB-Ras binds to the unique insert within the ankyrin repeat domain of IkappaBbeta and regulates cytoplasmic retention of IkappaBbeta x NF-kappaB complexes. Chen, Y., Wu, J., Ghosh, G. J. Biol. Chem. (2003) [Pubmed]
  22. Identification of a novel Ras-regulated proapoptotic pathway. Khokhlatchev, A., Rabizadeh, S., Xavier, R., Nedwidek, M., Chen, T., Zhang, X.F., Seed, B., Avruch, J. Curr. Biol. (2002) [Pubmed]
  23. cDNA cloning of a human RAB26-related gene encoding a Ras-like GTP-binding protein on chromosome 16p13.3 region. Seki, N., Yoshikawa, T., Hattori, A., Miyajima, N., Muramatsu, M., Saito, T. J. Hum. Genet. (2000) [Pubmed]
  24. Rig is a novel Ras-related protein and potential neural tumor suppressor. Ellis, C.A., Vos, M.D., Howell, H., Vallecorsa, T., Fults, D.W., Clark, G.J. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  25. Use of a native affinity ligand for the detection of G proteins by capillary isoelectric focusing with laser-induced fluorescence detection. Cunliffe, J.M., Liu, Z., Pawliszyn, J., Kennedy, R.T. Electrophoresis (2004) [Pubmed]
  26. Evidence for expression of a Ras-like and a stage specific GTP binding homologous protein by Plasmodium falciparum. Thélu, J., Bracchi, V., Burnod, J., Ambroise-Thomas, P. Cell. Signal. (1994) [Pubmed]
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